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Conserved domains on  [gi|2462561112|ref|XP_054174912|]
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receptor-type tyrosine-protein phosphatase mu isoform X39 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 879-1151 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


:

Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 582.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  879 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYH 958
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  959 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 1038
Cdd:cd14633     81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1039 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 1118
Cdd:cd14633    161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462561112 1119 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1151
Cdd:cd14633    241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1237-1442 1.61e-147

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


:

Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 446.83  E-value: 1.61e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1316
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1317 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1396
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1397 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 20-177 2.73e-58

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 197.95  E-value: 2.73e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112    20 GGCLFDEPySTCGYSQSEGDDFNWEQVNTLTK---PTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 95
Cdd:smart00137    4 GNCDFEEG-STCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTFW 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112    96 YFvssKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTfWPNFYQVIFEVITS-GHQGYLAIDEVKVLG 174
Cdd:smart00137   83 YY---MYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGkGHSGYIALDDILLSN 158


                    ...
gi 2462561112   175 HPC 177
Cdd:smart00137  159 GPC 161
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 187-269 3.92e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


:

Pssm-ID: 395002  Cd Length: 86  Bit Score: 66.45  E-value: 3.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  187 QNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKeIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 266
Cdd:pfam00047    4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82


                   ...
gi 2462561112  267 NYA 269
Cdd:pfam00047   83 STS 85
fn3 pfam00041
Fibronectin type III domain;
494-569 2.83e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 2.83e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112  494 IFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNqsgrvskLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPP 569
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
150-633 4.33e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  150 YQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFqcSAIGRTVAGDRLWlqGIDVRDAPLKEIK 229
Cdd:COG3401     21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG--GRAGTTSGVAAVA--VAAAPPTATGLTT 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  230 VTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYlwiqlnANSINGDGPIV 309
Cdd:COG3401     97 LTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTT------ASSVAGAGVVV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  310 AREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTrpGEGGTGSPGPALRTRTKCADPMRgPRKLEVVEVKSR 389
Cdd:COG3401    171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT--DTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  390 QITIRWEP-FGYNVTrchSYNLtvhycYQVGGQEQVREEVSWDTENSHpqhTITNLSPYTNVSVKLILMNPEGRK--ESQ 466
Cdd:COG3401    248 SVTLSWDPvTESDAT---GYRV-----YRSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTAVDAAGNEsaPSN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  467 ELIVQTDEDLPGAvPTESIQGSTFEEKIFLQWREPTQTYgvITLYEITYKAVSSFDPEidlsnqsgRVSKLGNETHFLFF 546
Cdd:COG3401    317 VVSVTTDLTPPAA-PSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGGTYT--------KIAETVTTTSYTDT 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  547 GLYPGTTYSFTIRASTAKGFGPPATNQFT-TKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERP 625
Cdd:COG3401    386 GLTPGTTYYYKVTAVDAAGNESAPSEEVSaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465


                   ....*...
gi 2462561112  626 RRTKKTTE 633
Cdd:COG3401    466 NAVPFTTT 473
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 879-1151 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 582.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  879 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYH 958
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  959 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 1038
Cdd:cd14633     81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1039 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 1118
Cdd:cd14633    161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462561112 1119 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1151
Cdd:cd14633    241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1237-1442 1.61e-147

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 446.83  E-value: 1.61e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1316
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1317 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1396
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1397 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
894-1148 9.08e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 374.69  E-value: 9.08e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   894 GFKEEYESFFEGQSA--PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDtNSDYINGNYIDGYHRPNHYIATQGPMQ 971
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   972 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREI 1048
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1049 RQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 1128
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 2462561112  1129 RVNMVQTEEQYVFIHDAILE 1148
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
918-1148 2.41e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 356.17  E-value: 2.41e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEGDtnSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 997
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  998 VGRVKCCKYWP---DDTEIYKDIKVTLI-ETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 1073
Cdd:pfam00102   79 KGREKCAQYWPeeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1074 QV-KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:pfam00102  159 KVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1180-1442 6.83e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 283.78  E-value: 6.83e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1180 QIKEEFRTLNMVTPTlrVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPL 1259
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1260 PNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgy 1335
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1336 RMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHA 1415
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 2462561112  1416 VKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1208-1442 1.10e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 279.13  E-value: 1.10e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLiTIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA 1287
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1288 --QLCPQYWPE--NGVHRHGPIQVEFVSA-DLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPmYRDTPVSKRSFLKL 1362
Cdd:pfam00102   80 grEKCAQYWPEeeGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEE--TRTVKHFHYTGWP-DHGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1363 IRQVDKWQEeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 20-177 2.73e-58

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 197.95  E-value: 2.73e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112    20 GGCLFDEPySTCGYSQSEGDDFNWEQVNTLTK---PTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 95
Cdd:smart00137    4 GNCDFEEG-STCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTFW 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112    96 YFvssKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTfWPNFYQVIFEVITS-GHQGYLAIDEVKVLG 174
Cdd:smart00137   83 YY---MYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGkGHSGYIALDDILLSN 158


                    ...
gi 2462561112   175 HPC 177
Cdd:smart00137  159 GPC 161
PHA02738 PHA02738
hypothetical protein; Provisional
 918-1146 1.89e-49

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 178.97  E-value: 1.89e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEgdTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 997
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAER--NRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  998 VGRVKCCKYWPD---DTEIYKDIKVTLIETELLAEYVIRTFAVEKrGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 1074
Cdd:PHA02738   127 NGREKCFPYWSDveqGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1075 VKS----------------KSPPsagPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 1138
Cdd:PHA02738   206 VRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282


                   ....*...
gi 2462561112 1139 YVFIHDAI 1146
Cdd:PHA02738   283 YFFCYRAV 290
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 22-177 9.26e-48

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.94  E-value: 9.26e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   22 CLFDEPysTCGYSQSEGDDFNWEQVNTLTKPTSDP-----WMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 95
Cdd:cd06263      1 CDFEDG--LCGWTQDSTDDFDWTRVSGSTPSPGTPpdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   96 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWpNFYQVIFEVIT-SGHQGYLAIDEVKVLG 174
Cdd:cd06263     79 YHMYG---SGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRgSGSRGDIALDDISLSP 154


                   ...
gi 2462561112  175 HPC 177
Cdd:cd06263    155 GPC 157
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
917-1142 4.97e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.58  E-value: 4.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  917 ENRMKNRYGNIIAYDHSRVRlqtiegdTNSDYINGNYIDGYhRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 996
Cdd:COG5599     41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  997 EVG--RVKCCKYWPDDTEIYK-DIKVTLIETELLAEYV-IRTFAVEKRGV-HEIREIRQFHFTGWPDHGVP----YHAtg 1067
Cdd:COG5599    113 EISkpKVKMPVYFRQDGEYGKyEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAIsaeaLKN-- 190

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1068 LLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDM--AEREGVVDIYNCVRELR-SRRVNMVQTEEQYVFI 1142
Cdd:COG5599    191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDVL 268
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 22-177 2.03e-45

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 160.99  E-value: 2.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   22 CLFDEPySTCGYSQSEGDDFNWEQVNTL---TKPTSDPWM--PSGSFMLVNASGRPEGQRAHLLLPQLKENDT-HCIDFH 95
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPsvkTGPSSDHTQgtGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   96 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFwPNFYQVIFEVI-TSGHQGYLAIDEVKVLG 174
Cdd:pfam00629   80 YHMSG---SGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIrGGGSRGGIALDDISLSS 155


                   ...
gi 2462561112  175 HPC 177
Cdd:pfam00629  156 GPC 158
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1206-1444 4.32e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 128.20  E-value: 4.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1206 PRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN--- 1282
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1283 DVDPAQLCPQYW--PENGVHRHGPIQVEFVSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFL 1360
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1361 KLIRQVD----KWQEEYNGGEG---RTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:PHA02747   206 KFIKIIDinrkKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                          250
                   ....*....|....
gi 2462561112 1434 KF---CYEVALEYL 1444
Cdd:PHA02747   286 LFiqpGYEVLHYFL 299
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 187-269 3.92e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 66.45  E-value: 3.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  187 QNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKeIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 266
Cdd:pfam00047    4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82


                   ...
gi 2462561112  267 NYA 269
Cdd:pfam00047   83 STS 85
fn3 pfam00041
Fibronectin type III domain;
494-569 2.83e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 2.83e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112  494 IFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNqsgrvskLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPP 569
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
150-633 4.33e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  150 YQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFqcSAIGRTVAGDRLWlqGIDVRDAPLKEIK 229
Cdd:COG3401     21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG--GRAGTTSGVAAVA--VAAAPPTATGLTT 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  230 VTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYlwiqlnANSINGDGPIV 309
Cdd:COG3401     97 LTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTT------ASSVAGAGVVV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  310 AREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTrpGEGGTGSPGPALRTRTKCADPMRgPRKLEVVEVKSR 389
Cdd:COG3401    171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT--DTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  390 QITIRWEP-FGYNVTrchSYNLtvhycYQVGGQEQVREEVSWDTENSHpqhTITNLSPYTNVSVKLILMNPEGRK--ESQ 466
Cdd:COG3401    248 SVTLSWDPvTESDAT---GYRV-----YRSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTAVDAAGNEsaPSN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  467 ELIVQTDEDLPGAvPTESIQGSTFEEKIFLQWREPTQTYgvITLYEITYKAVSSFDPEidlsnqsgRVSKLGNETHFLFF 546
Cdd:COG3401    317 VVSVTTDLTPPAA-PSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGGTYT--------KIAETVTTTSYTDT 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  547 GLYPGTTYSFTIRASTAKGFGPPATNQFT-TKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERP 625
Cdd:COG3401    386 GLTPGTTYYYKVTAVDAAGNESAPSEEVSaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465


                   ....*...
gi 2462561112  626 RRTKKTTE 633
Cdd:COG3401    466 NAVPFTTT 473
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 494-576 1.47e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 59.05  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  494 IFLQWREPTQTYGVITLYEITYKAVSSfdpeidlsNQSGRVSK-LGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATN 572
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS--------GDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSES 88


                   ....*
gi 2462561112  573 -QFTT 576
Cdd:cd00063     89 vTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 378-472 5.45e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  378 PRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLtvhYCYQVGGQEQVREEVSWDTENShpqHTITNLSPYTNVSVKLILM 457
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV---EYREKGSGDWKEVEVTPGSETS---YTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 2462561112  458 NPEGR-KESQELIVQT 472
Cdd:cd00063     78 NGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 378-462 5.90e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.76  E-value: 5.90e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   378 PRKLEVVEVKSRQITIRWEPFGYNVTRchSYNLTvhycYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILM 457
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVG----YRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*
gi 2462561112   458 NPEGR 462
Cdd:smart00060   78 NGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 477-567 1.44e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.44e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   477 PGAVPTESIQGSTfEEKIFLQWREPTqtYGVITLYEITYKAVSSfdpeiDLSNQSGRVSKLGNETHFLFFGLYPGTTYSF 556
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPP--DDGITGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72

                            90
                    ....*....|.
gi 2462561112   557 TIRASTAKGFG 567
Cdd:smart00060   73 RVRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 187-273 1.81e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 1.81e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   187 QNVEVNAGQFATFQCSAIGRTVAgDRLWLQGIDVRDAPLKEIKVTSSRrFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 266
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ....*..
gi 2462561112   267 NyAELVV 273
Cdd:smart00410   80 G-TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
279-356 1.21e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  279 PIAPPQLASVGATYLWIQLNANSiNGDGPIVAREVEYCTASGSWNDRQ---PVDSTSYKIGHLDPDTEYEISVlLTRPGE 355
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEitvPGTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 2462561112  356 G 356
Cdd:pfam00041   80 G 80
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1341-1435 1.88e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1341 FQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSGTFCAisivCEMLRHQRTVDvfHAVKTLR 1420
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA----AYLVLLGLSAE--EALARVR 117

                           90
                   ....*....|....*
gi 2462561112 1421 NNKPNMVDLLDQYKF 1435
Cdd:COG2453    118 AARPGAVETPAQRAF 132
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 879-1151 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 582.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  879 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYH 958
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  959 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 1038
Cdd:cd14633     81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1039 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 1118
Cdd:cd14633    161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462561112 1119 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1151
Cdd:cd14633    241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 948-1151 2.28e-150

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 454.37  E-value: 2.28e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELL 1027
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1028 AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIML 1107
Cdd:cd14555     81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIML 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462561112 1108 DMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1151
Cdd:cd14555    161 DMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 916-1152 9.60e-150

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 454.10  E-value: 9.60e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  916 DENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNL 995
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  996 VEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV 1075
Cdd:cd14630     81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1076 KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1152
Cdd:cd14630    161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1237-1442 1.61e-147

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 446.83  E-value: 1.61e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1316
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1317 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1396
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1397 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 934-1151 1.04e-131

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 405.17  E-value: 1.04e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  934 RVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI 1013
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1014 YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAG 1093
Cdd:cd14631     81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1094 AGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1151
Cdd:cd14631    161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 948-1152 6.86e-129

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 397.11  E-value: 6.86e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELL 1027
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1028 AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIML 1107
Cdd:cd14632     81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462561112 1108 DMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1152
Cdd:cd14632    161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1237-1442 3.14e-127

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 392.85  E-value: 3.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1316
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1317 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1396
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1397 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1237-1438 1.49e-126

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 390.61  E-value: 1.49e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP-AQLCPQYWPENGVHRHGPIQVEFVSADLE 1315
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPkDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1316 EDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYngGEGRTVVHCLNGGGRSGTFC 1395
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462561112 1396 AISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 918-1152 2.07e-125

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 389.06  E-value: 2.07e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 997
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  998 VGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVK 1076
Cdd:cd14553     83 RSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1077 SKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1152
Cdd:cd14553    163 ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
894-1148 9.08e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 374.69  E-value: 9.08e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   894 GFKEEYESFFEGQSA--PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDtNSDYINGNYIDGYHRPNHYIATQGPMQ 971
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   972 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREI 1048
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1049 RQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 1128
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 2462561112  1129 RVNMVQTEEQYVFIHDAILE 1148
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1237-1442 9.32e-116

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 361.65  E-value: 9.32e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1316
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1317 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1396
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1397 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
918-1148 2.41e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 356.17  E-value: 2.41e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEGDtnSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 997
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  998 VGRVKCCKYWP---DDTEIYKDIKVTLI-ETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 1073
Cdd:pfam00102   79 KGREKCAQYWPeeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1074 QV-KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:pfam00102  159 KVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 878-1152 2.56e-112

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 355.11  E-value: 2.56e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  878 ADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGY 957
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  958 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFA 1036
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATYSVRTFA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1037 VEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVV 1116
Cdd:cd14626    161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462561112 1117 DIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1152
Cdd:cd14626    241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 872-1154 4.43e-107

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 341.33  E-value: 4.43e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  872 HPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYING 951
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  952 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEY 1030
Cdd:cd14624     81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSrGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1031 VIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMA 1110
Cdd:cd14624    161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462561112 1111 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGD 1154
Cdd:cd14624    241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 872-1152 1.42e-106

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 339.76  E-value: 1.42e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  872 HPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYING 951
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  952 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEY 1030
Cdd:cd14625     81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSrGTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1031 VIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMA 1110
Cdd:cd14625    161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462561112 1111 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1152
Cdd:cd14625    241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1237-1442 8.53e-101

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 320.70  E-value: 8.53e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVD---PAQLCPQYWPENGVHRHGPIQVEFVSAD 1313
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNqsnSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1314 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 1393
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462561112 1394 FCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 948-1144 1.30e-96

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 308.45  E-value: 1.30e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKDIKVTLIET 1024
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1025 ELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVID 1104
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462561112 1105 IMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd00047    161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 948-1144 4.14e-95

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 304.66  E-value: 4.14e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETEL 1026
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAV------EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14549     81 LATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd14549    161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 923-1143 8.17e-93

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 298.88  E-value: 8.17e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  923 RYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVK 1002
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1003 CCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP 1080
Cdd:cd14548     81 CDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1081 PSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14548    159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1180-1442 6.83e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 283.78  E-value: 6.83e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1180 QIKEEFRTLNMVTPTlrVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPL 1259
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1260 PNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgy 1335
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1336 RMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHA 1415
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 2462561112  1416 VKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 868-1157 2.03e-86

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 283.84  E-value: 2.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  868 TGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQ-SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNS 946
Cdd:cd14621      1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  947 DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETE 1025
Cdd:cd14621     81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQgCWTYGNIRVSVEDVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LLAEYVIRTFAVEKRG----VHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFI 1101
Cdd:cd14621    161 VLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFI 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1102 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSV 1157
Cdd:cd14621    241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 917-1151 7.25e-86

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 281.54  E-value: 7.25e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  917 ENRMKNRYGNIIAYDHSRVRLQTIEG--DTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN 994
Cdd:cd17667     26 DNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  995 LVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVEK-----------RGVHEIREIRQFHFTGWPDHGVP 1062
Cdd:cd17667    106 LVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVP 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1063 YHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 1142
Cdd:cd17667    186 EYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 265


                   ....*....
gi 2462561112 1143 HDAILEACL 1151
Cdd:cd17667    266 HDALLEAIL 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1208-1442 1.10e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 279.13  E-value: 1.10e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLiTIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA 1287
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1288 --QLCPQYWPE--NGVHRHGPIQVEFVSA-DLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPmYRDTPVSKRSFLKL 1362
Cdd:pfam00102   80 grEKCAQYWPEeeGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEE--TRTVKHFHYTGWP-DHGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1363 IRQVDKWQEeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 894-1143 2.00e-83

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 274.63  E-value: 2.00e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  894 GFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQE 972
Cdd:cd14543      4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  973 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIR 1049
Cdd:cd14543     84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1050 QFHFTGWPDHGVPYHATGLLGF---VRQ-----VKSKSPPSAG-----PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVV 1116
Cdd:cd14543    164 HFQFTSWPDFGVPSSAAALLDFlgeVRQqqalaVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                          250       260
                   ....*....|....*....|....*..
gi 2462561112 1117 DIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14543    244 NVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 922-1148 2.85e-82

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 269.38  E-value: 2.85e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  922 NRYGNIIAYDHSRVRLqTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1001
Cdd:cd14615      1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1002 KCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF---VRQVKS 1077
Cdd:cd14615     80 KCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVREYMK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1078 KSPPSaGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14615    160 QNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 918-1146 1.75e-78

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 259.70  E-value: 1.75e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEGD-TNSDYINGNYI-----DGYHRPNH--YIATQGPMQETIYDFWRMVWHENTASI 989
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrneneGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  990 IMVTNLVEVGRVKCCKYWPDD--TEIYKDIKVTLIETELLAEYVIRTFAVEKRG-VHEIREIRQFHFTGWPDHGVPYHAT 1066
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1067 GLLGFVRQV--KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVF 1141
Cdd:cd14544    161 GVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 2462561112 1142 IHDAI 1146
Cdd:cd14544    241 IYVAV 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 924-1148 2.22e-78

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 258.33  E-value: 2.22e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  924 YGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKC 1003
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1004 CKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKR---GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKS 1079
Cdd:cd14620     81 YQYWPDQgCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1080 PPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14620    161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 922-1148 7.97e-77

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 254.04  E-value: 7.97e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  922 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1001
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1002 KCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 1077
Cdd:cd14619     81 KCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQwl 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1078 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14619    161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 922-1143 1.27e-76

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 253.30  E-value: 1.27e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  922 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1001
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1002 KCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAV-EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS- 1077
Cdd:cd14617     81 KCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDy 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1078 -KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14617    161 iNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 918-1147 1.39e-75

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 250.90  E-value: 1.39e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 997
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  998 VGRVKCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV- 1075
Cdd:cd14554     86 MGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVh 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1076 KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1147
Cdd:cd14554    166 KTKEQfGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 948-1143 6.97e-75

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 247.13  E-value: 6.97e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE-IYKDIKVTLIETEL 1026
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAVEKR----GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIV 1102
Cdd:cd14551     81 LVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462561112 1103 IDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14551    161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 909-1147 1.45e-73

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 245.18  E-value: 1.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  909 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 988
Cdd:cd14614      3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  989 IIMVTNLVEVGRVKCCKYWP--DDTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIREIRQFHFTGWPDHGVPY--H 1064
Cdd:cd14614     83 IVMLTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSY--ADEVQDVMHFNYTAWPDHGVPTanA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1065 ATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ...
gi 2462561112 1145 AIL 1147
Cdd:cd14614    241 CVQ 243
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 922-1143 3.52e-73

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 243.46  E-value: 3.52e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  922 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvGR 1000
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1001 VKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 1077
Cdd:cd14547     80 EKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEar 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1078 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14547    158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 922-1147 8.24e-72

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 239.84  E-value: 8.24e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  922 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1001
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1002 KCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 1077
Cdd:cd14618     81 LCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREhv 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1078 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1147
Cdd:cd14618    161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 948-1147 3.52e-70

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 234.10  E-value: 3.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETEL 1026
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAVE--------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTG 1098
Cdd:cd17668     81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462561112 1099 CFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1147
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 948-1144 1.13e-69

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 232.91  E-value: 1.13e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYID-GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVTLIET 1024
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgeYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1025 ELLAE--YVIRTFAVeKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR--QVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd18533     81 EENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1101 IVIDIMLDMAER--------EGVVD-IYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd18533    160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 917-1146 1.36e-68

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 231.45  E-value: 1.36e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  917 ENRMKNRYGNIIAYDHSRVRLQtiEGDTN---SDYINGNYIDGYH-------RPNH-YIATQGPMQETIYDFWRMVWHEN 985
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIIMPEFetkcnnsKPKKsYIATQGCLQNTVNDFWRMVFQEN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  986 TASIIMVTNLVEVGRVKCCKYWPDDTEI--YKDIKVTLIETELLAEYVIRTFAVEKRGVHEI-REIRQFHFTGWPDHGVP 1062
Cdd:cd14605     79 SRVIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1063 YHATGLLGFVRQV--KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEE 1137
Cdd:cd14605    159 SDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238


                   ....*....
gi 2462561112 1138 QYVFIHDAI 1146
Cdd:cd14605    239 QYRFIYMAV 247
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 873-1148 4.69e-67

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 228.46  E-value: 4.69e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  873 PAIRVADLLQHITQMKCAEGY-GFKEEYESFF--EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYI 949
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLAssKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  950 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 1028
Cdd:cd14628     84 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMP 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1029 EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV-KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIM 1106
Cdd:cd14628    164 QYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVhKTKEQfGQDGPISVHCSAGVGRTGVFITLSIV 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462561112 1107 LDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14628    244 LERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 948-1143 1.84e-66

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 223.17  E-value: 1.84e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIET 1024
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1025 ELLAEYVIRTFAV----EKRGVHEIREIRqfhFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14557     81 KICPDYIIRKLNInnkkEKGSGREVTHIQ---FTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14557    158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 922-1143 2.74e-66

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 223.63  E-value: 2.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  922 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1001
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1002 KCCKYWPDDTE---IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIreIRQFHFTGWPDHGVPYHATGLLGFVRQVKSK 1078
Cdd:cd14616     81 RCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462561112 1079 SPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14616    159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1237-1438 3.74e-66

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 222.16  E-value: 3.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENG--VHRHGPIQVEFVSA 1312
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgREKCERYWPEEGgkPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1313 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGgegRTVVHCLNGGGRSG 1392
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES--REVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEARKPNG---PIVVHCSAGVGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1393 TFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd00047    155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 911-1148 8.20e-66

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 223.99  E-value: 8.20e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  911 DSAKKDENRMKNRYGNIIAYDHSRVRLQTieGDTN---SDYINGNYIDGY-----HRPNHYIATQGPMQETIYDFWRMVW 982
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVILQG--RDSNipgSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAW 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  983 HENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHE-IREIRQFHFTGWPDH 1059
Cdd:cd14606     89 QENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1060 GVPYHATGLLGFVRQV--KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQ 1134
Cdd:cd14606    169 GVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQ 248

                          250
                   ....*....|....
gi 2462561112 1135 TEEQYVFIHDAILE 1148
Cdd:cd14606    249 TEAQYKFIYVAIAQ 262
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 873-1148 1.36e-65

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 224.23  E-value: 1.36e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  873 PAIRVADLLQHITQMKCAEGY-GFKEEYESFF--EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYI 949
Cdd:cd14627      5 PARNLYSYIQKLAQVEVGEHVtGMELEFKRLAnsKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  950 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 1028
Cdd:cd14627     85 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1029 EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV-KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIM 1106
Cdd:cd14627    165 QYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVhKTKEQfGQDGPISVHCSAGVGRTGVFITLSIV 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462561112 1107 LDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14627    245 LERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 948-1146 9.04e-64

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 215.60  E-value: 9.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI-YKDIKVTLIETEL 1026
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSA-GPLVVHCSAGAGRTGCFIVIDI 1105
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGTFCALST 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462561112 1106 MLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1146
Cdd:cd14552    161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 912-1148 1.36e-63

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 218.44  E-value: 1.36e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  912 SAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 991
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  992 VTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLG 1070
Cdd:cd14629    127 LTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1071 FVRQV-KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14629    207 FIGQVhKTKEQfGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 923-1148 3.35e-63

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 214.91  E-value: 3.35e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  923 RYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVK 1002
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1003 CCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPP 1081
Cdd:cd14623     81 CAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1082 SAG-PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14623    161 SGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 948-1149 7.96e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 213.00  E-value: 7.96e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYI------DGYHrpnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE----IYKDI 1017
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1018 KVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSppSAGPLVVHCSAGAGRT 1097
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1098 GCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 1149
Cdd:cd14538    155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 909-1146 6.40e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 214.03  E-value: 6.40e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  909 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 988
Cdd:cd14604     48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  989 IIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHA 1065
Cdd:cd14604    128 IVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDVPSSF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1066 TGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAeREGVV----DIYNCVRELRSRRVNMVQTEEQYVF 1141
Cdd:cd14604    206 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAVQTKEQYEL 284


                   ....*
gi 2462561112 1142 IHDAI 1146
Cdd:cd14604    285 VHRAI 289
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 921-1146 1.17e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 211.64  E-value: 1.17e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  921 KNRYGNIIAYDHSRVRLQTIE-GDTNSDYINGNYIDGY-HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 998
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  999 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV--- 1075
Cdd:cd14613    108 NE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVeea 184

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1076 KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1146
Cdd:cd14613    185 RQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 921-1141 3.22e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 209.17  E-value: 3.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  921 KNRYGNIIAYDHSRVRLQTIEGDtnSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGR 1000
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1001 VKCCKYWP---DDTEIYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF---V 1072
Cdd:cd14545     79 IKCAQYWPqgeGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFlqkV 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1073 RQVKSKSpPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV--VDIYNCVRELRSRRVNMVQTEEQYVF 1141
Cdd:cd14545    159 RESGSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 947-1149 1.49e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 206.80  E-value: 1.49e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  947 DYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVT 1020
Cdd:cd14541      1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1021 LIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 1149
Cdd:cd14541    161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 921-1148 1.80e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 207.39  E-value: 1.80e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  921 KNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGR 1000
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1001 VKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS 1077
Cdd:cd14602     81 KKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462561112 1078 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAeREGVV----DIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14602    159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 917-1147 2.69e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 206.99  E-value: 2.69e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  917 ENRMKNRYGNIIAYDHSRVRLqtieGDTNsDYINGNYID-GYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTN 994
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKmPVGDEEFvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  995 LVEVGRVKCCKYWPDD----TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLG 1070
Cdd:cd14597     77 EVEGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1071 FVRQVKSKSppSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1147
Cdd:cd14597    157 FISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 917-1148 4.63e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 207.37  E-value: 4.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  917 ENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 996
Cdd:cd14603     29 ENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  997 EVGRVKCCKYWP--DDTEIYKDIKVTLI-ETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 1073
Cdd:cd14603    109 EMGKKKCERYWAqeQEPLQTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1074 QVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVD---IYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14603    187 LARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 948-1144 4.85e-60

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 204.93  E-value: 4.85e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELL 1027
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1028 AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP------PSAGPLVVHCSAGAGRTGCFI 1101
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSSRTGIFC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462561112 1102 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd14558    161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 921-1143 2.46e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 201.60  E-value: 2.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  921 KNRYGNIIAYDHSRVRLQTIEG-DTNSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEv 998
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  999 GRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS- 1077
Cdd:cd14612     97 KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEEs 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1078 -KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14612    175 rQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 20-177 2.73e-58

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 197.95  E-value: 2.73e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112    20 GGCLFDEPySTCGYSQSEGDDFNWEQVNTLTK---PTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 95
Cdd:smart00137    4 GNCDFEEG-STCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTFW 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112    96 YFvssKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTfWPNFYQVIFEVITS-GHQGYLAIDEVKVLG 174
Cdd:smart00137   83 YY---MYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGkGHSGYIALDDILLSN 158


                    ...
gi 2462561112   175 HPC 177
Cdd:smart00137  159 GPC 161
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 895-1148 4.96e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 202.21  E-value: 4.96e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  895 FKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYI-DGYHRPNHYIATQGPMQ 971
Cdd:cd14610     19 LEKEWEALCAYQAEPNATnvAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  972 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIR 1049
Cdd:cd14610     99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1050 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSR 1128
Cdd:cd14610    179 QFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQ 258

                          250       260
                   ....*....|....*....|
gi 2462561112 1129 RVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14610    259 RPGMVQTKEQFEFALTAVAE 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 904-1157 1.44e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 200.64  E-value: 1.44e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  904 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTiegdTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 983
Cdd:cd14608     11 EASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  984 ENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPD 1058
Cdd:cd14608     87 QKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1059 HGVPYHATGLLGFVRQVKSKSP--PSAGPLVVHCSAGAGRTGCFIVID---IMLDMAEREGVVDIYNCVRELRSRRVNMV 1133
Cdd:cd14608    167 FGVPESPASFLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLI 246

                          250       260
                   ....*....|....*....|....*.
gi 2462561112 1134 QTEEQYVFIHDAILEAC--LCGDTSV 1157
Cdd:cd14608    247 QTADQLRFSYLAVIEGAkfIMGDSSV 272
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 897-1148 3.44e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 199.88  E-value: 3.44e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  897 EEYESFFEGQSAP--WDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGN-YIDGYHRPNHYIATQGPMQET 973
Cdd:cd14609     19 KEWQALCAYQAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  974 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIRQF 1051
Cdd:cd14609     99 IADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQF 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1052 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRV 1130
Cdd:cd14609    179 HFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRP 258

                          250
                   ....*....|....*...
gi 2462561112 1131 NMVQTEEQYVFIHDAILE 1148
Cdd:cd14609    259 GMVRTKDQFEFALTAVAE 276
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 921-1143 5.39e-57

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 197.06  E-value: 5.39e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  921 KNRYGNIIAYDHSRVRLQTIE-GDTNSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 998
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  999 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVeKRGVHEiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS- 1077
Cdd:cd14611     82 NE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTL-KQGSQS-RSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEd 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1078 -KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14611    159 rLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 948-1143 1.03e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 195.33  E-value: 1.03e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIET 1024
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPeegEEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1025 ELLAE-YVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVI 1103
Cdd:cd14542     81 KRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462561112 1104 DIMLDMAEREGVVD---IYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd14542    159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 947-1146 1.73e-56

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 194.84  E-value: 1.73e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  947 DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI-YKDIKVTLIETE 1025
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAG-PLVVHCSAGAGRTGCFIVID 1104
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTFIALS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462561112 1105 IMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1146
Cdd:cd14622    161 NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1203-1441 1.06e-55

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 193.89  E-value: 1.06e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1203 ALLPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML 1281
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1282 NDVDPA--QLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSF 1359
Cdd:cd14554     81 TKLREMgrEKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1360 LKLIRQVDKWQEEYnGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1439
Cdd:cd14554    158 IDFIGQVHKTKEQF-GQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                   ..
gi 2462561112 1440 AL 1441
Cdd:cd14554    237 AL 238
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 913-1147 1.48e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 191.99  E-value: 1.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  913 AKKDENRMKNRYGNIIAYDHSRVRLQTiegdtNSDYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 988
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  989 IIMVTNLVEVGRVKCCKYWPDDTEI--YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHAT 1066
Cdd:cd14600    110 IVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1067 GLLGFVRQVKSKSPPSAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1146
Cdd:cd14600    190 DFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268


                   .
gi 2462561112 1147 L 1147
Cdd:cd14600    269 L 269
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 904-1146 2.59e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 190.56  E-value: 2.59e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  904 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQtiegDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 983
Cdd:cd14607     10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  984 ENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPD 1058
Cdd:cd14607     86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPD 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1059 HGVPYHATGLLGF---VRQVKSKSPPSaGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG--VVDIYNCVRELRSRRVNMV 1133
Cdd:cd14607    166 FGVPESPASFLNFlfkVRESGSLSPEH-GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244

                          250
                   ....*....|...
gi 2462561112 1134 QTEEQYVFIHDAI 1146
Cdd:cd14607    245 QTPDQLRFSYMAV 257
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1237-1439 2.39e-53

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 185.55  E-value: 2.39e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENGVHRHGPIQVEFVSADL 1314
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErsQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGTF 1394
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGST--RTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAGAGRTGTF 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462561112 1395 CAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1439
Cdd:cd14552    156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1154-1446 3.56e-53

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 188.40  E-value: 3.56e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1154 DTSVPAsqvRSLYYDMNKL---DPQTNSSQIKEEFRTL-NMVTPTLRVEDcsiALLPRNHEKNRCMDILPPDRCLPFLIT 1229
Cdd:cd14627      1 NTEVPA---RNLYSYIQKLaqvEVGEHVTGMELEFKRLaNSKAHTSRFIS---ANLPCNKFKNRLVNIMPYETTRVCLQP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1230 IDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPengVHRHGPIQ 1306
Cdd:cd14627     75 IRGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMgrEKCHQYWP---AERSARYQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1307 VEFVSADLEEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCL 1385
Cdd:cd14627    152 YFVVDPMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCS 229

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1386 NGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNS 1446
Cdd:cd14627    230 AGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1155-1446 1.16e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 184.16  E-value: 1.16e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1155 TSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLnmVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDG-E 1233
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRL--ASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1234 SSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPengVHRHGPIQVEFVS 1311
Cdd:cd14628     79 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWP---AERSARYQYFVVD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1312 ADLEEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCLNGGGR 1390
Cdd:cd14628    156 PMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1391 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNS 1446
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1155-1446 1.97e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 183.39  E-value: 1.97e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1155 TSVPAsqvRSLYYDMNKLD---PQTNSSQIKEEFRTLnmVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITID 1231
Cdd:cd14629      2 TEVPA---RNLYAHIQKLTqvpPGESVTAMELEFKLL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1232 G-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPengVHRHGPIQVE 1308
Cdd:cd14629     77 GvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWP---AERSARYQYF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1309 FVSADLEEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCLNG 1387
Cdd:cd14629    154 VVDPMAEYNMPQYILREFKVTDARDGQsRTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAG 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1388 GGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNS 1446
Cdd:cd14629    232 VGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1236-1443 1.03e-50

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 178.28  E-value: 1.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1236 NYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVHRHGPIQVEFVSAD 1313
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQekCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1314 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 1393
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSAGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1394 FCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEY 1443
Cdd:cd14622    156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 948-1148 5.04e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 176.88  E-value: 5.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYI----DGYHRpnHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIK 1018
Cdd:cd14540      1 YINASHItatvGGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggehDALTFGEYK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1019 VTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-----------KSPPSagPLV 1087
Cdd:cd14540     79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqdvagHNRNP--PTL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1088 VHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14540    157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 948-1149 1.10e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 175.32  E-value: 1.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYI-----DGYHRpnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD---DTEIYKDIKV 1019
Cdd:cd14596      1 YINASYItmpvgEEELF---YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqEPMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1020 TLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSppSAGPLVVHCSAGAGRTGC 1099
Cdd:cd14596     78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1100 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 1149
Cdd:cd14596    156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1179-1437 1.57e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 177.17  E-value: 1.57e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1179 SQIKEEFRTLNMVTPTLRVEdCSiaLLPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQH 1257
Cdd:cd14543      3 RGIYEEYEDIRREPPAGTFL-CS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1258 PLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWP--ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAArpQD 1333
Cdd:cd14543     80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERgrVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE--TD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1334 GYRMVQQFQFLGWPMYrDTPVSKRS---FLKLIRQ---------VDKWQEEYNGGEgrTVVHCLNGGGRSGTFCAISIVC 1401
Cdd:cd14543    158 ESRQVTHFQFTSWPDF-GVPSSAAAlldFLGEVRQqqalavkamGDRWKGHPPGPP--IVVHCSAGIGRTGTFCTLDICL 234

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462561112 1402 EMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14543    235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PHA02738 PHA02738
hypothetical protein; Provisional
 918-1146 1.89e-49

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 178.97  E-value: 1.89e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  918 NRMKNRYGNIIAYDHSRVRLQTIEgdTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 997
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAER--NRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  998 VGRVKCCKYWPD---DTEIYKDIKVTLIETELLAEYVIRTFAVEKrGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 1074
Cdd:PHA02738   127 NGREKCFPYWSDveqGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1075 VKS----------------KSPPsagPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 1138
Cdd:PHA02738   206 VRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282


                   ....*...
gi 2462561112 1139 YVFIHDAI 1146
Cdd:PHA02738   283 YFFCYRAV 290
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 948-1148 9.55e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 172.63  E-value: 9.55e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYI-DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLI-ET 1024
Cdd:cd14546      1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVsEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1025 ELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVID 1104
Cdd:cd14546     81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462561112 1105 IMLD-MAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14546    161 MVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 947-1148 7.61e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 170.13  E-value: 7.61e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  947 DYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVT 1020
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1021 LIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14601    161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 22-177 9.26e-48

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.94  E-value: 9.26e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   22 CLFDEPysTCGYSQSEGDDFNWEQVNTLTKPTSDP-----WMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 95
Cdd:cd06263      1 CDFEDG--LCGWTQDSTDDFDWTRVSGSTPSPGTPpdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   96 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWpNFYQVIFEVIT-SGHQGYLAIDEVKVLG 174
Cdd:cd06263     79 YHMYG---SGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRgSGSRGDIALDDISLSP 154


                   ...
gi 2462561112  175 HPC 177
Cdd:cd06263    155 GPC 157
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 875-1143 1.12e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 173.26  E-value: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  875 IRVADLLQHITQMKCAeGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTnSDYINGNYI 954
Cdd:PHA02747     9 CRAIDFLKRRNQLNCF-GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  955 DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV-GRVKCCKYW---PDDTEIYKDIKVTLIETELLAEY 1030
Cdd:PHA02747    87 DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKY 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1031 VIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF------VRQVKSK--SPPSA--GPLVVHCSAGAGRTGCF 1100
Cdd:PHA02747   167 ILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFikiidiNRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIF 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:PHA02747   247 CAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1237-1438 1.96e-47

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 168.73  E-value: 1.96e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQLCPQYWPENGvHRHGPIQVEFVSADL 1314
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkeGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT---VVHCLNGGGRS 1391
Cdd:cd14558     80 SPTYTVRVFEITHLKRKDS--RTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462561112 1392 GTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 948-1144 2.67e-46

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 165.27  E-value: 2.67e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVEVGRVKCCKYWPDDTE-IYKDIKVTLIETEL 1026
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAVE--KRGVHEIREIRQFHFTGWPDHG-VPYHATGLLGFVRQV-KSKSPPSAGPLVVHCSAGAGRTGCFIV 1102
Cdd:cd14556     80 DEDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFCA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462561112 1103 IDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd14556    160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1233-1442 3.52e-46

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 165.99  E-value: 3.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1233 ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENGVHRHGPIQVEFV 1310
Cdd:cd14623     22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYWPSDGSVSYGDITIELK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1311 SADLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGR 1390
Cdd:cd14623    102 KEEECESYTVRDLLVTNTR--ENKSRQIRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHCSAGAGR 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1391 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14623    177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
917-1142 4.97e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.58  E-value: 4.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  917 ENRMKNRYGNIIAYDHSRVRlqtiegdTNSDYINGNYIDGYhRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 996
Cdd:COG5599     41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  997 EVG--RVKCCKYWPDDTEIYK-DIKVTLIETELLAEYV-IRTFAVEKRGV-HEIREIRQFHFTGWPDHGVP----YHAtg 1067
Cdd:COG5599    113 EISkpKVKMPVYFRQDGEYGKyEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAIsaeaLKN-- 190

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1068 LLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDM--AEREGVVDIYNCVRELR-SRRVNMVQTEEQYVFI 1142
Cdd:COG5599    191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDVL 268
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 22-177 2.03e-45

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 160.99  E-value: 2.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   22 CLFDEPySTCGYSQSEGDDFNWEQVNTL---TKPTSDPWM--PSGSFMLVNASGRPEGQRAHLLLPQLKENDT-HCIDFH 95
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPsvkTGPSSDHTQgtGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   96 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFwPNFYQVIFEVI-TSGHQGYLAIDEVKVLG 174
Cdd:pfam00629   80 YHMSG---SGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIrGGGSRGGIALDDISLSS 155


                   ...
gi 2462561112  175 HPC 177
Cdd:pfam00629  156 GPC 158
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 895-1148 1.76e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 164.02  E-value: 1.76e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  895 FKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGdtNSDYINGNYIDGYHRPNHYIATQGPMQET 973
Cdd:PHA02742    28 LKEEHEHIMQEIVAfSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEET 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  974 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYW---PDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 1050
Cdd:PHA02742   106 ALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1051 FHFTGWPDHGVPYHATGLLGFVRQV-----------KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIY 1119
Cdd:PHA02742   186 FAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLL 265

                          250       260
                   ....*....|....*....|....*....
gi 2462561112 1120 NCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:PHA02742   266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1208-1446 1.49e-43

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 158.71  E-value: 1.49e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP 1286
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1287 AQL--CPQYWPENGVHRHGPIQVEFV-SADLEEDIIsRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLI 1363
Cdd:cd14553     83 RSRvkCDQYWPTRGTETYGLIQVTLLdTVELATYTV-RTFALHKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLAFL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1364 RQVdkwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEY 1443
Cdd:cd14553    159 RRV---KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235


                   ...
gi 2462561112 1444 LNS 1446
Cdd:cd14553    236 VTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1213-1435 2.51e-43

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 157.52  E-value: 2.51e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1213 RCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QL 1289
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgrVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1290 CPQYWPENGVHR-HGPIQVEFVSADLEEDIISRIFRIYNAarpqDGYRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQv 1366
Cdd:cd14548     81 CDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERG----DEVRSVRQFHFTAWPDHGvpEAPDSLLRFVRLVRD- 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1367 dkwqeEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKF 1435
Cdd:cd14548    156 -----YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 948-1144 6.14e-43

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 156.00  E-value: 6.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGY--HRPNhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLI 1022
Cdd:cd14539      1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1023 ETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS---KSPPSAGPLVVHCSAGAGRTGC 1099
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1100 F-IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd14539    160 FcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 897-1148 3.25e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 156.70  E-value: 3.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  897 EEYESFFEGQSAP-------WDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEgDTNSDYINGNYIDGYHRPN--HYIATQ 967
Cdd:cd14599     10 EEGMVFTEYEQIPkkkadgvFTTATLPENAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEewHYIATQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  968 GPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGV 1042
Cdd:cd14599     89 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLS 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1043 HEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS----------KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 1112
Cdd:cd14599    169 GQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmldSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEH 248

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462561112 1113 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14599    249 NEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1237-1438 1.18e-41

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 152.09  E-value: 1.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRH-GPIQVEFVSADL- 1314
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLEcETFKVTLSGEDHs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 ----EEDIISRIFRIYNAarpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVDKWQEEYNGGegrTVVHCLNGGG 1389
Cdd:cd14550     81 clsnEIRLIVRDFILEST---QDDYVLeVRQFQCPSWP-NPCSPIH--TVFELINTVQEWAQQRDGP---IVVHDRYGGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462561112 1390 RSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14550    152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 948-1143 1.40e-40

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 149.15  E-value: 1.40e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNH--YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE-VGRVKCCKYWPD---DTEIYKDIKVTl 1021
Cdd:cd17658      1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAeenESREFGRISVT- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1022 IETELLAEYVI--RTFAVEKRGVHE-IREIRQFHFTGWPDHGVPyHATgllGFVRQVKSKS---PPSAGPLVVHCSAGAG 1095
Cdd:cd17658     80 NKKLKHSQHSItlRVLEVQYIESEEpPLSVLHIQYPEWPDHGVP-KDT---RSVRELLKRLygiPPSAGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462561112 1096 RTGCFIVID-----IML-DMAeregVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1143
Cdd:cd17658    156 RTGAYCTIHntirrILEgDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1200-1446 2.03e-40

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 151.36  E-value: 2.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1200 CSIALLPRNHEKNRCMDILPPDRCLPFLITIDGES-SNYINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTS 1277
Cdd:cd14610     36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVV 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1278 VVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADLE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWpMYRDTPV 1354
Cdd:cd14610    116 IVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWcEDFLVRSFYLKNLQTNET--RTVTQFHFLSW-NDQGVPA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1355 SKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSGTFCAISIVC-EMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:cd14610    193 STRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSGTYILIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQF 269

                          250
                   ....*....|...
gi 2462561112 1434 KFCYEVALEYLNS 1446
Cdd:cd14610    270 EFALTAVAEEVNA 282
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1047-1148 2.76e-40

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 144.42  E-value: 2.76e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1047 EIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSA--GPLVVHCSAGAGRTGCFIVIDIMLDMAERE-GVVDIYNCVR 1123
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2462561112  1124 ELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1047-1148 2.76e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 144.42  E-value: 2.76e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1047 EIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSA--GPLVVHCSAGAGRTGCFIVIDIMLDMAERE-GVVDIYNCVR 1123
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2462561112  1124 ELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1208-1442 3.89e-40

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 150.19  E-value: 3.89e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP 1286
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1287 AQL--CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKL 1362
Cdd:cd14626    121 KSRvkCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDHgvPEYPTPILAFLRR 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1363 IRQVDKwqeeynGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14626    199 VKACNP------PDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 915-1146 1.55e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 147.10  E-value: 1.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  915 KDENRMKNRYGNIIAYDHSRV-------------------RLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIY 975
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  976 DFWRMVWHENTASIIMVTNlVEVGRVKCCKYW--PDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFH 1052
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1053 FTGWPDHGVPYHATGLLGFVRQVKSK----------SPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCV 1122
Cdd:PHA02746   207 FPDWPDNGIPTGMAEFLELINKVNEEqaelikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                          250       260
                   ....*....|....*....|....
gi 2462561112 1123 RELRSRRVNMVQTEEQYVFIHDAI 1146
Cdd:PHA02746   287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1216-1442 3.85e-38

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 143.16  E-value: 3.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1216 DILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVD--PAQLCPQ 1292
Cdd:cd14620      3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1293 YWPENGVHRHGPIQVEFVSADLEEDIISRIFRI-YNAARPQDGYRMVQQFQFLGWPMYRD--TPVSKRSFLKLIRQVDKW 1369
Cdd:cd14620     83 YWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIqPQLPDGCKAPRLVTQLHFTSWPDFGVpfTPIGMLKFLKKVKSVNPV 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1370 QEeynggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14620    163 HA------GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1212-1441 5.87e-38

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 142.39  E-value: 5.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1212 NRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQ 1288
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGmeNGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1289 LCPQYWPENGVH-RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQ 1365
Cdd:cd14618     81 LCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE--RRVKHLHYTAWPDHGipESTSSLMAFRELVRE 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1366 vdkwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd14618    159 ----HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1158-1443 1.00e-37

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 144.01  E-value: 1.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1158 PASQVRSLYYDMNKLDPQTNSsQIKEEFRTLnmvtPTLRVE-DCSIALLPRNHEKNRCMDILPPDRCLPFLITIDG-ESS 1235
Cdd:cd14621      6 PPLPVDKLEEEINRRMADDNK-LFREEFNAL----PACPIQaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1236 NYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQ--LCPQYWPENGVHRHGPIQVEFVSAD 1313
Cdd:cd14621     81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1314 LEEDIISRIFRIYNAA-----RPQdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGegrTVVHCLNGG 1388
Cdd:cd14621    161 VLVDYTVRKFCIQQVGdvtnkKPQ---RLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYAGA---IVVHCSAGV 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462561112 1389 GRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEY 1443
Cdd:cd14621    234 GRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1200-1446 1.14e-37

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 143.25  E-value: 1.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1200 CSIALLPRNHEKNRCMDILPPDRC-LPFLITIDGESSNYINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTS 1277
Cdd:cd14609     34 CSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTV 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1278 VVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADLE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPV 1354
Cdd:cd14609    114 IVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWcEDFLVRSFYLKNVQTQET--RTLTQFHFLSWPA-EGIPS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1355 SKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSGTFCAISIVC-EMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:cd14609    191 STRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267

                          250
                   ....*....|...
gi 2462561112 1434 KFCYEVALEYLNS 1446
Cdd:cd14609    268 EFALTAVAEEVNA 280
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 948-1148 2.09e-37

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 140.50  E-value: 2.09e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNH--YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-----DDTEIYKDIKVT 1020
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1021 LIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-----------KSPPSagPLVVH 1089
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstidpKSPNP--PVLVH 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1090 CSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14598    159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1205-1447 4.91e-37

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 141.79  E-value: 4.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1205 LPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND 1283
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1284 VDPAQL--CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLK 1361
Cdd:cd14624    124 LEERSRvkCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1362 LIRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd14624    201 FLRRVKTCNPP---DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                   ....*.
gi 2462561112 1442 EYLNSG 1447
Cdd:cd14624    278 EAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1205-1442 6.56e-37

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 141.38  E-value: 6.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1205 LPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND 1283
Cdd:cd14625     44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1284 VDPAQL--CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLK 1361
Cdd:cd14625    124 LEEKSRikCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQFTAWPDH-GVPEYPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1362 LIRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd14625    201 FLRRVKTCNPP---DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277


                   .
gi 2462561112 1442 E 1442
Cdd:cd14625    278 E 278
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1237-1445 1.16e-36

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 137.96  E-value: 1.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-----NDVDpaqLCPQYWPENGVHRHGPIQVEFV 1310
Cdd:cd14546      1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlqeNGVK---QCARYWPEEGSEVYHIYEVHLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1311 SADL-EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKwqeEYNGGEGRTVVHCLNGGG 1389
Cdd:cd14546     78 SEHIwCDDYLVRSFYLKNLQTSET--RTVTQFHFLSWP-DEGIPASAKPLLEFRRKVNK---SYRGRSCPIVVHCSDGAG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1390 RSGTFCAISIVCE-MLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLN 1445
Cdd:cd14546    152 RTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1237-1438 1.63e-36

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 137.48  E-value: 1.63e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 1314
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMItNLVERGRRkCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIFRIYNA----ARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGGGR 1390
Cdd:cd14549     81 LATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRKSSAAN---PPGAGPIVVHCSAGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1391 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14549    157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1237-1438 5.40e-36

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 136.22  E-value: 5.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMD-SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVH-RHGPIQVEFVSA 1312
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGRekCDQYWPSGEYEgEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1313 DLEED--IISRIFRIynaARPQDGYRMVQQFQFLGWPmyrD--TPVSKRSFLKLIRQVDKWQEEyNGGEGRTVVHCLNGG 1388
Cdd:cd18533     81 EENDDggFIVREFEL---SKEDGKVKKVYHIQYKSWP---DfgVPDSPEDLLTLIKLKRELNDS-ASLDPPIIVHCSAGV 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1389 GRSGTFCAISIVCEMLRHQRTVD---------VFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd18533    154 GRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1237-1442 1.50e-35

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 134.66  E-value: 1.50e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENgVHRHGPIQVEFVSADL 1314
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRVkCSRYWPDD-TEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRSGTF 1394
Cdd:cd14555     80 LAEYVVRTFAL--ERRGYHEIREVRQFHFTGWPDH-GVPYHATGLLGFIRRV---KASNPPSAGPIVVHCSAGAGRTGCY 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1395 CAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14555    154 IVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1212-1435 6.85e-35

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 133.29  E-value: 6.85e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1212 NRCMDILPPDR---CLPflITIDGESSNYINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDP 1286
Cdd:cd14547      1 NRYKTILPNEHsrvCLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMItNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1287 AQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQV 1366
Cdd:cd14547     79 KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY----GGEKRYLKHYWYTSWPDHK-TPEAAQPLLSLVQEV 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1367 DKWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKF 1435
Cdd:cd14547    154 EEARQTEPH-RGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1212-1442 6.94e-35

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 133.40  E-value: 6.94e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1212 NRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQL- 1289
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcVEQGRTk 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1290 CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPmyrDTPVSKRS-----FLKLIR 1364
Cdd:cd14615     81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNES--RTVRHFHFTSWP---DHGVPETTdllinFRHLVR 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1365 QVDKwqeeYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14615    156 EYMK----QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1237-1438 9.78e-35

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 132.34  E-value: 9.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENGVHRHGPIQVEFVSADL 1314
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIF------RIYNAARPqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGegrTVVHCLNGG 1388
Cdd:cd14551     81 LVDYTTRKFciqkvnRGIGEKRV----RLVTQFHFTSWPDF-GVPFTPIGMLKFLKKVKSANPPRAGP---IVVHCSAGV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1389 GRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14551    153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1208-1442 1.90e-34

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 132.46  E-value: 1.90e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVD 1285
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1286 PAQL-CPQYWPENgVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1364
Cdd:cd14630     83 VGRVkCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHE--IREIRQFHFTSWPDH-GVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1365 QVdKWQEEYNGGEgrTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14630    159 QV-KFLNPPDAGP--IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1203-1438 2.16e-34

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 132.70  E-value: 2.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1203 ALLPRNHEKNRCMDILPPDRCLPFLITI-DGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML 1281
Cdd:cd14614      7 ADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1282 NDVDPAQL--CPQYWP--ENGVHrHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMY----RDTP 1353
Cdd:cd14614     87 TQCNEKRRvkCDHYWPftEEPVA-YGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHgvptANAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1354 VSKRSFLKLIRQvdkwqeEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:cd14614    162 ESILQFVQMVRQ------QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                   ....*
gi 2462561112 1434 KFCYE 1438
Cdd:cd14614    236 IFIHQ 240
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 948-1148 2.83e-34

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 130.91  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVEVGRVkCCKYWPDDTE-IYKDIKVTLIETEL 1026
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVRQV---KSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14634     79 DEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14634    159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1212-1444 3.18e-34

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 131.93  E-value: 3.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1212 NRCMDILPPDRCLPFLITIDGE-SSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL- 1289
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1290 -CPQYWPENGVH-RHGPIQVEFVSADLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 1367
Cdd:cd14619     81 kCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE--EQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLLR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1368 KWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1444
Cdd:cd14619    158 QWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 948-1148 1.33e-33

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 128.99  E-value: 1.33e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMvtnLVEVGRVKCC-KYWPDDTEI-YKDIKVTLIETE 1025
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQGCpQYWPEEGMLrYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVRQV---KSKSPPSAGPLVVHCSAGAGRTGC 1099
Cdd:cd14636     78 MDCDVISRIFRIcnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRSGM 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462561112 1100 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14636    158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1231-1442 1.84e-33

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 128.98  E-value: 1.84e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1231 DGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENgVHRHGPIQVE 1308
Cdd:cd14631      9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDD-TEVYGDFKVT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1309 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 1388
Cdd:cd14631     88 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHCSAGA 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462561112 1389 GRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14631    162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1206-1442 3.63e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 129.95  E-value: 3.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1206 PRNHEKNRCMDILPPDR---CLPFLItiDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM-L 1281
Cdd:cd14603     28 KENVKKNRYKDILPYDQtrvILSLLQ--EEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaC 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1282 NDVDPA-QLCPQYWP-ENGVHRHGPIQVEFVSAD-LEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPmYRDTPVSKRS 1358
Cdd:cd14603    106 REIEMGkKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKV----TFQKESRSVSHFQYMAWP-DHGIPDSPDC 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1359 FLKLIRQVDKWQeeyngGEGRT--VVHCLNGGGRSGTFCAISIVCEMLRHQRTVD---VFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:cd14603    181 MLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQY 255


                   ....*....
gi 2462561112 1434 KFCYEVALE 1442
Cdd:cd14603    256 EFLYHTVAQ 264
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 948-1142 1.65e-32

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 125.51  E-value: 1.65e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGrvKCCKYWPD-DTEIYKD-IKVTLIETE 1025
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTkEKPLECEtFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LL-----AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14550     79 HSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 1142
Cdd:cd14550    157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1208-1442 1.67e-32

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 128.24  E-value: 1.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVD 1285
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1286 PAQL-CPQYWPENgVHRHGPIQVEFVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1364
Cdd:cd14633    120 VGRVkCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1365 QVdkwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14633    196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1237-1442 2.10e-32

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 125.55  E-value: 2.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQL-CPQYWPENGvHRHGPIQVEFVSADL 1314
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKlVEVGRVkCSKYWPDDS-DTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIFriynaARPQDGYRM---VQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRS 1391
Cdd:cd14632     80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1392 GTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1206-1444 4.32e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 128.20  E-value: 4.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1206 PRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN--- 1282
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1283 DVDPAQLCPQYW--PENGVHRHGPIQVEFVSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFL 1360
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1361 KLIRQVD----KWQEEYNGGEG---RTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:PHA02747   206 KFIKIIDinrkKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                          250
                   ....*....|....
gi 2462561112 1434 KF---CYEVALEYL 1444
Cdd:PHA02747   286 LFiqpGYEVLHYFL 299
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1211-1439 1.53e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 124.97  E-value: 1.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1211 KNRCMDILPPDRCLPFLITIDGES--SNYINAALMDSY-KQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA 1287
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1288 -QLCPQYWPENGVHRHGpIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQV 1366
Cdd:cd14613    108 nEKCTEYWPEEQVTYEG-IEITVKQVIHADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK-TPDNAPPLLQLVQEV 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1367 DKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1439
Cdd:cd14613    182 EEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1200-1442 1.78e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 125.14  E-value: 1.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1200 CSIALLPRNHEKNRCMDILPPDRCLpflITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVV 1279
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1280 MLNDV--DPAQLCPQYWPEN----GVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RD 1351
Cdd:cd14608     94 MLNRVmeKGSLKCAQYWPQKeekeMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1352 TPVSKRSFLKLIRQVDKWQEEYnggeGRTVVHCLNGGGRSGTFCAISiVCEMLRHQR----TVDVFHAVKTLRNNKPNMV 1427
Cdd:cd14608    172 SPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGIGRSGTFCLAD-TCLLLMDKRkdpsSVDIKKVLLEMRKFRMGLI 246

                          250
                   ....*....|....*
gi 2462561112 1428 DLLDQYKFCYEVALE 1442
Cdd:cd14608    247 QTADQLRFSYLAVIE 261
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1237-1438 2.83e-31

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 122.49  E-value: 2.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSA-FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLndVDPAQLCPQ----YWPEN-GVH-RHGPIQVEF 1309
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML--VSEQENEKQkvhrYWPTErGQAlVYGAITVSL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1310 VSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGG 1389
Cdd:cd14539     79 QSVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1390 RSGTFC-AISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14539    156 RTGAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 948-1148 6.51e-31

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 121.33  E-value: 6.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVEVGRVkCCKYWPDD-TEIYKDIKVTLIETEL 1026
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENgVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1027 LAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVRQV---KSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd14635     79 EEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRSGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14635    159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1237-1437 6.57e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 120.99  E-value: 6.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENG--VHRHGPIQVEFVSA 1312
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKkCERYWPEEGeeQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1313 D-LEEDIISRIFRiynaARPQDGYRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRS 1391
Cdd:cd14542     81 KrVGPDFLIRTLK----VTFQKESRTVYQFHYTAWP-DHGVPSSVDPILDLVRLVRDYQGS---EDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462561112 1392 GTFCAISIVCEMLRHQRTVD---VFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1237-1444 1.61e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 120.17  E-value: 1.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAalmdSY------KQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN-DVDPAQL-CPQYWPEN---GVHRHGPI 1305
Cdd:cd14538      1 YINA----SHiripvgGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVkCHRYWPDSlnkPLICGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1306 QVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCL 1385
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEV--HHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHNS-----GPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1386 NGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1444
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1237-1441 2.36e-30

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 119.71  E-value: 2.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV-DPAQLCPQYWPengvHRHGPIQVEFVSADL- 1314
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWP----NKDEPINCETFKVTLi 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 1384
Cdd:cd17669     77 aeehkclsnEEKLIIQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII---KEEAANRDGPMIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1385 LNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd17669    148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1211-1437 4.47e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 119.80  E-value: 4.47e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1211 KNRCMDILPPDRCLpflITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQ 1288
Cdd:cd14545      3 RYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLmeKGQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1289 LCPQYWPENGVH----RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1364
Cdd:cd14545     80 KCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462561112 1365 QVdKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT--VDVFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14545    157 KV-RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1205-1437 5.48e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 119.94  E-value: 5.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1205 LPRNHEKNRCMDILP-PDR--CLPFLITIDgESSNYINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM 1280
Cdd:cd14612     12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1281 LNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSF 1359
Cdd:cd14612     91 ITKLkEKKEKCVHYWPEKE-GTYGRFEIRVQDMKECDGYTIRDLTI----QLEEESRSVKHYWFSSWPDHQ-TPESAGPL 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1360 LKLIRQVDKwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14612    165 LRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1237-1433 1.96e-29

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 116.85  E-value: 1.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 1312
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnkCAQYWPsmEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1313 DLEEDIISRIFRIYNaARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGGGRSG 1392
Cdd:cd14557     81 KICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN---NFFSGPIVVHCSAGVGRTG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462561112 1393 TFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1433
Cdd:cd14557    156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 948-1147 2.06e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 117.02  E-value: 2.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCkYWPDDTE--IYKDIKVTLIETE 1025
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LLA-----EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1100
Cdd:cd17669     80 HKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462561112 1101 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1147
Cdd:cd17669    158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1206-1442 3.01e-29

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 118.60  E-value: 3.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1206 PRNHEKNRCMDILPPDRC---LPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML- 1281
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIt 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1282 NDVDPAQL-CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAA--RPQDG-------YRMVQQFQFLGWPmyrD 1351
Cdd:cd17667    105 NLVEKGRRkCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkKGQKGnpkgrqnERTVIQYHYTQWP---D 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1352 TPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLD 1431
Cdd:cd17667    182 MGVPEYA-LPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 260

                          250
                   ....*....|.
gi 2462561112 1432 QYKFCYEVALE 1442
Cdd:cd17667    261 QYIFIHDALLE 271
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1235-1438 5.79e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 116.16  E-value: 5.79e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1235 SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV-DPAQL-CPQYWPENG--VHRHGPIQVEFV 1310
Cdd:cd14616     25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCfEKGRIrCHQYWPEDNkpVTVFGDIVITKL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1311 SADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGR 1390
Cdd:cd14616    105 MEDVQIDWTIRDLKI----ERHGDYMMVRQCNFTSWPEH-GVPESSAPLIHFVKLVRASRAHDN---TPMIVHCSAGVGR 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1391 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14616    177 TGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 948-1148 6.23e-29

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 115.78  E-value: 6.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV-KCCKYWPDD-TEIYKDIKVTLIETE 1025
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPgLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LLAEYVIRTFAVEK--RGVHEIREIRQFHFTGW-PDHGVPYHATGLLGFVRQV-KSKSPPSAGPLVVHCSAGAGRTGCFI 1101
Cdd:cd14637     81 ADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSGTYC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462561112 1102 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1148
Cdd:cd14637    161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1237-1441 1.83e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 114.39  E-value: 1.83e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQLCPQYWPEngvhRHGPIQVEFVSADL- 1314
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnQGLAEDEFVYWPS----REESMNCEAFTVTLi 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVdkwQEEYNGGEGRTVVHC 1384
Cdd:cd17670     77 skdrlclsnEEQIIIHDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDAPIS--STFELINVI---KEEALTRDGPTIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1385 LNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd17670    148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1212-1438 2.02e-28

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 115.02  E-value: 2.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1212 NRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQL 1289
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1290 -CPQYWP-ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 1367
Cdd:cd14617     81 kCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQ-LDAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462561112 1368 KWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd14617    159 DYINRTPG-SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1211-1442 4.30e-28

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 114.17  E-value: 4.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1211 KNRCMDILPPDRCLP--FLITIDgESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM--LNDVDP 1286
Cdd:cd14602      1 KNRYKDILPYDHSRVelSLITSD-EDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacMEFEMG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1287 AQLCPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRiynaARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1364
Cdd:cd14602     80 KKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLK----VKFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1365 QVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQ---RTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd14602    155 DVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                   .
gi 2462561112 1442 E 1442
Cdd:cd14602    232 E 232
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 948-1147 4.57e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 113.23  E-value: 4.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  948 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN---LVEVGRVkcckYWPDDTEIY--KDIKVTLI 1022
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPSREESMncEAFTVTLI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1023 ETELLA-----EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPSAGPLVVHCSAGAGRT 1097
Cdd:cd17670     77 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGAVSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1098 GCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1147
Cdd:cd17670    155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1337-1442 2.28e-27

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 107.44  E-value: 2.28e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1337 MVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRH-QRTVDVFHA 1415
Cdd:smart00012    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 2462561112  1416 VKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1337-1442 2.28e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 107.44  E-value: 2.28e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  1337 MVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRH-QRTVDVFHA 1415
Cdd:smart00404    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 2462561112  1416 VKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1211-1437 3.83e-27

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 111.16  E-value: 3.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1211 KNRCMDILPPDRCLPFLIT--IDGESSNYINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV-DP 1286
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1287 AQLCPQYWPEN-GVHrhGPIQVEFVSADLEEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQ 1365
Cdd:cd14611     82 NEKCVLYWPEKrGIY--GKVEVLVNSVKECDNYTIRNLTLKQGSQS----RSVKHYWYTSWPDHK-TPDSAQPLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1366 VDKWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14611    155 VEEDRLASPG-RGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1208-1446 4.01e-27

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 112.03  E-value: 4.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLpfLITIDGE----SSNYINAALM--------DSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHC 1275
Cdd:cd14605      2 NKNKNRYKNILPFDHTR--VVLHDGDpnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1276 TSVVMLN-DVDPAQL-CPQYWP-ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDT 1352
Cdd:cd14605     80 RVIVMTTkEVERGKSkCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQ-GNTERTVWQYHFRTWPDH-GV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1353 PVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT---VDVFHAVKTLRNNKPNMVDL 1429
Cdd:cd14605    158 PSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236

                          250
                   ....*....|....*..
gi 2462561112 1430 LDQYKFCYEVALEYLNS 1446
Cdd:cd14605    237 EAQYRFIYMAVQHYIET 253
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1228-1439 1.71e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 112.04  E-value: 1.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1228 ITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVD-PAQLCPQYW--PENGVHRHGP 1304
Cdd:PHA02746    91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDdDDEKCFELWtkEEDSELAFGR 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1305 IQVEFVSADLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEY-------NGGE 1377
Cdd:PHA02746   171 FVAKILDIIEELSFTKTRLMITDKI--SDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAELikqadndPQTL 247

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1378 GRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1439
Cdd:PHA02746   248 GPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKA 309
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1237-1444 2.49e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 108.30  E-value: 2.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAA--LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN-DVDPAQL-CPQYWPENgvhRHGPIQVEFVSA 1312
Cdd:cd14596      1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVkCHRYWPET---LQEPMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1313 DLE-----EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNG 1387
Cdd:cd14596     78 RLEnyqalQYFIIRIIKLVEKETGEN--RLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHCSAG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462561112 1388 GGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1444
Cdd:cd14596    150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1237-1438 2.71e-26

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 108.14  E-value: 2.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 1314
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRkCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1315 EEDIISRIFRIYNA--------ARPQDgyRMVQQFQFLGWPmyrDTPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLN 1386
Cdd:cd17668     81 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWP---DMGVPEYT-LPVLTFVRKASYAKRHAVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1387 GGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1208-1437 3.53e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 110.41  E-value: 3.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRC-LPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM-LNDVD 1285
Cdd:cd14604     57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMaCREFE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1286 PA-QLCPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKL 1362
Cdd:cd14604    137 MGrKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----EFQNETRRLYQFHYVNWPDH-DVPSSFDSILDM 211

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462561112 1363 IRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT---VDVFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14604    212 ISLMRKYQEH---EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 286
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1202-1437 4.35e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 108.90  E-value: 4.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1202 IALLPRNHEKNRCMDILPPDRCLpflITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML 1281
Cdd:cd14607     18 VAKYPENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1282 NDV--DPAQLCPQYWPENG----VHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVS 1355
Cdd:cd14607     95 NRIveKDSVKCAQYWPTDEeevlSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDF-GVPES 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1356 KRSFLKLIRQVdKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISiVCEMLRHQR---TVDVFHAVKTLRNNKPNMVDLLDQ 1432
Cdd:cd14607    172 PASFLNFLFKV-RESGSLSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKdpdSVDIKQVLLDMRKYRMGLIQTPDQ 249


                   ....*
gi 2462561112 1433 YKFCY 1437
Cdd:cd14607    250 LRFSY 254
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1237-1438 8.55e-26

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 106.78  E-value: 8.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALM--DSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL---CPQYWP--ENGVHRHGPIQVEF 1309
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1310 VSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKwqeeyngGEGRTVVHCLNG 1387
Cdd:cd17658     81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDHgvPKDTRSVRELLKRLYGIPP-------SAGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1388 GGRSGTFCAISIVCE--MLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1438
Cdd:cd17658    154 IGRTGAYCTIHNTIRriLEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1237-1435 1.36e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 106.26  E-value: 1.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1237 YINAALMDSYKQPSA----FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQLCPQYWPE-NGVHRHGPIQVEF 1309
Cdd:cd14541      2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLveRGRVKCHQYWPDlGETMQFGNLQITC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1310 VSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEeynGGEGRTVVHCLNGGG 1389
Cdd:cd14541     82 VSEEVTPSFAFREFILTNTNTGEE--RHITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRV---GMVEPTVVHCSAGIG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1390 RSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKF 1435
Cdd:cd14541    156 RTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1252-1444 1.53e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 106.39  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1252 FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND--VDPAQLCPQYWPENGVHRH----GPIQVEFVSADLEEDIISRIFRI 1325
Cdd:cd14540     18 YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAeeEGGREKCFRYWPTLGGEHDaltfGEYKVSTKFSVSSGCYTTTGLRV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1326 YNAarPQDGYRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQVDKWQEEYNGGEGR---TVVHCLNGGGRSGT--FCAIS 1398
Cdd:cd14540     98 KHT--LSGQSRTVWHLQYTDWPDHGcpEDVSGFLDFLEEINSVRRHTNQDVAGHNRnppTLVHCSAGVGRTGVviLADLM 175

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462561112 1399 IVCemLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1444
Cdd:cd14540    176 LYC--LDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1208-1444 2.50e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 106.07  E-value: 2.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLitidGESSNYINAAL--MDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDV 1284
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1285 DPAQL-CPQYWPE---NGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFL 1360
Cdd:cd14597     79 EGGKIkCQRYWPEilgKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTRE--VRHITHLNFTAWPDH-DTPSQPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1361 KLI---RQVDKwqeeynggEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1437
Cdd:cd14597    156 TFIsymRHIHK--------SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCY 227


                   ....*..
gi 2462561112 1438 EVALEYL 1444
Cdd:cd14597    228 QVILYVL 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1208-1444 1.67e-24

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 104.08  E-value: 1.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMDILPPDRCLPFLITIDGE--SSNYINA----------ALMDSYKqpsAFIVTQHPLPNTVKDFWRLVLDYHC 1275
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirnenegpTTDENAK---TYIATQGCLENTVSDFWSMVWQENS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1276 TSVVML-NDVDPAQ-LCPQYWP-ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDT 1352
Cdd:cd14544     78 RVIVMTtKEVERGKnKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPI-REIWHYQYLSWPDH-GV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1353 PVSKRSFLKLIRQVDKWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQR---TVDVFHAVKTLRNNKPNMVDL 1429
Cdd:cd14544    156 PSDPGGVLNFLEDVNQRQESLPH-AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQT 234

                          250
                   ....*....|....*
gi 2462561112 1430 LDQYKFCYEVALEYL 1444
Cdd:cd14544    235 EAQYKFIYVAVAQYI 249
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1200-1443 1.46e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 102.77  E-value: 1.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1200 CSIALLPRNHEKNRCMDILPPDRCLPFLITIDGeSSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVV 1279
Cdd:PHA02742    44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1280 MLNDV--DPAQLCPQYW--PENGVHRHGPIQVEFVSAdleediisRIFRIYNAARPQ-----DGYRM-VQQFQFLGWPmY 1349
Cdd:PHA02742   123 MITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKI--------KSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP-H 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1350 RDTPVSKRSFLKLI---RQVDKWQEEYNGGEGRT-----VVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRN 1421
Cdd:PHA02742   194 GGLPRDPNKFLDFVlavREADLKADVDIKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRK 273

                          250       260
                   ....*....|....*....|..
gi 2462561112 1422 NKPNMVDLLDQYKFCYEVALEY 1443
Cdd:PHA02742   274 QRHNCLSLPQQYIFCYFIVLIF 295
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1206-1446 1.51e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 101.88  E-value: 1.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1206 PRNHEKNRCMDILPPDRCLPFLITIDGE-------SSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSV 1278
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1279 VMLN-DVDPAQ-LCPQYWPENGVHR-HGPIQVEFVSadlEEDIISRIFRIYNAARPQDG--YRMVQQFQFLGWPMYrDTP 1353
Cdd:cd14606     96 VMTTrEVEKGRnKCVPYWPEVGMQRaYGPYSVTNCG---EHDTTEYKLRTLQVSPLDNGelIREIWHYQYLSWPDH-GVP 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1354 VSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT---VDVFHAVKTLRNNKPNMVDLL 1430
Cdd:cd14606    172 SEPGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTE 250

                          250
                   ....*....|....*.
gi 2462561112 1431 DQYKFCYEVALEYLNS 1446
Cdd:cd14606    251 AQYKFIYVAIAQFIET 266
PHA02738 PHA02738
hypothetical protein; Provisional
 1207-1446 2.64e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 99.61  E-value: 2.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1207 RNHEKNR-----CMD----ILPPDRclpflitidgESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTS 1277
Cdd:PHA02738    48 KNRKLNRyldavCFDhsrvILPAER----------NRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQI 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1278 VVML--NDVDPAQLCPQYWP--ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAArpqDGYRMVQQFQFLGWPMYrDTP 1353
Cdd:PHA02738   118 IVMLckKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGT---SATQTVTHFNFTAWPDH-DVP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1354 VSKRSFLKLIRQV-----DKWQEEYNGGEGRT-----VVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNK 1423
Cdd:PHA02738   194 KNTSEFLNFVLEVrqcqkELAQESLQIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQR 273

                          250       260
                   ....*....|....*....|...
gi 2462561112 1424 PNMVDLLDQYKFCYEVALEYLNS 1446
Cdd:PHA02738   274 YYSLFIPFQYFFCYRAVKRYVNL 296
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1169-1441 3.67e-21

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 95.30  E-value: 3.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1169 MNKLDPQTNSSQIKEEFRTLNMVTPTLRVedcSIALLPRNHEKNRCMDILPPDRCLPFLitidGESSNYINAALMDSyKQ 1248
Cdd:cd14600      4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1249 PSA-----FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPE-NGVHRHGPIQVEFVSADLEEDIIS 1320
Cdd:cd14600     76 PSAnivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERgrTKCHQYWPDpPDVMEYGGFRVQCHSEDCTIAYVF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1321 RIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSGTFCAISIV 1400
Cdd:cd14600    156 REMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVE----NEPVLVHCSAGIGRTGVLVTMETA 228

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2462561112 1401 CEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1441
Cdd:cd14600    229 MCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1234-1442 4.90e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 90.00  E-value: 4.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1234 SSNYINAALmDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPE-NGVHRHGPIQVEFV 1310
Cdd:cd14601      4 NANYINMEI-PSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVkCHQYWPEpSGSSSYGGFQVTCH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1311 SADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGR 1390
Cdd:cd14601     83 SEEGNPAYVFREMTLTNLEKNES--RPLTQIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1391 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1442
Cdd:cd14601    157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1201-1444 9.61e-19

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 88.52  E-value: 9.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1201 SIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSA--FIVTQHPLPNTVKDFWRLVLDYHCTSV 1278
Cdd:cd14599     31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1279 VMLNDVDPA--QLCPQYWPENGVHRHGPIQVEF-VSADLEED---IISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDT 1352
Cdd:cd14599    111 AMVTAEEEGgrSKSHRYWPKLGSKHSSATYGKFkVTTKFRTDsgcYATTGLKVKHLLSGQE--RTVWHLQYTDWPDH-GC 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1353 PVSKRSFLKLIRQVDKWQEEYNGGEGRT-------VVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPN 1425
Cdd:cd14599    188 PEEVQGFLSYLEEIQSVRRHTNSMLDSTkncnppiVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMF 267

                          250
                   ....*....|....*....
gi 2462561112 1426 MVDLLDQYKFCYEVALEYL 1444
Cdd:cd14599    268 MIQTIAQYKFVYQVLIQFL 286
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 875-1146 3.33e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 81.17  E-value: 3.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  875 IRVADLLQHITQmkcaEGYGFKEEYESffEGQSapwdSAKKDENRMKNRYG--NIIAYDHSRVRLQTIEgdtnsDYINGN 952
Cdd:PHA02740    18 INKPDLLSCIIK----EYRAIVPEHED--EANK----ACAQAENKAKDENLalHITRLLHRRIKLFNDE-----KVLDAR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  953 YIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvgrvKCC--KYWPDD---TEIYKDIKVTLIETELL 1027
Cdd:PHA02740    83 FVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD----KKCfnQFWSLKegcVITSDKFQIETLEIIIK 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1028 AEYVIRTFAV-EKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--------KSPPSAGPLVVHCSAGAGRTG 1098
Cdd:PHA02740   159 PHFNLTLLSLtDKFG--QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlekhKADGKIAPIIIDCIDGISSSA 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462561112 1099 CFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1146
Cdd:PHA02740   237 VFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1252-1444 3.58e-14

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 73.47  E-value: 3.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1252 FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPENGvHRHGPIQV-EFvsadleeDIISRiFRIYNA 1328
Cdd:cd14598     18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgrEKSFRYWPRLG-SRHNTVTYgRF-------KITTR-FRTDSG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1329 ARPQDGY----------RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYN------GGEGRTVVHCLNGGGRSG 1392
Cdd:cd14598     89 CYATTGLkikhlltgqeRTVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRRHTNstidpkSPNPPVLVHCSAGVGRTG 167

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1393 TFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1444
Cdd:cd14598    168 VVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 187-269 3.92e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 66.45  E-value: 3.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  187 QNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKeIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 266
Cdd:pfam00047    4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82


                   ...
gi 2462561112  267 NYA 269
Cdd:pfam00047   83 STS 85
fn3 pfam00041
Fibronectin type III domain;
494-569 2.83e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 2.83e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112  494 IFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNqsgrvskLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPP 569
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
150-633 4.33e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  150 YQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFqcSAIGRTVAGDRLWlqGIDVRDAPLKEIK 229
Cdd:COG3401     21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG--GRAGTTSGVAAVA--VAAAPPTATGLTT 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  230 VTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYlwiqlnANSINGDGPIV 309
Cdd:COG3401     97 LTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTT------ASSVAGAGVVV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  310 AREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTrpGEGGTGSPGPALRTRTKCADPMRgPRKLEVVEVKSR 389
Cdd:COG3401    171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT--DTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  390 QITIRWEP-FGYNVTrchSYNLtvhycYQVGGQEQVREEVSWDTENSHpqhTITNLSPYTNVSVKLILMNPEGRK--ESQ 466
Cdd:COG3401    248 SVTLSWDPvTESDAT---GYRV-----YRSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTAVDAAGNEsaPSN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  467 ELIVQTDEDLPGAvPTESIQGSTFEEKIFLQWREPTQTYgvITLYEITYKAVSSFDPEidlsnqsgRVSKLGNETHFLFF 546
Cdd:COG3401    317 VVSVTTDLTPPAA-PSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGGTYT--------KIAETVTTTSYTDT 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  547 GLYPGTTYSFTIRASTAKGFGPPATNQFT-TKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERP 625
Cdd:COG3401    386 GLTPGTTYYYKVTAVDAAGNESAPSEEVSaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465


                   ....*...
gi 2462561112  626 RRTKKTTE 633
Cdd:COG3401    466 NAVPFTTT 473
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 494-576 1.47e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 59.05  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  494 IFLQWREPTQTYGVITLYEITYKAVSSfdpeidlsNQSGRVSK-LGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATN 572
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS--------GDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSES 88


                   ....*
gi 2462561112  573 -QFTT 576
Cdd:cd00063     89 vTVTT 93
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 949-1140 4.21e-10

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 61.65  E-value: 4.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  949 INGNY--IDGYHRpnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYW-PDDTeiYKDIKVT----- 1020
Cdd:cd14559     18 LNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT--YGSVTVKskktg 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1021 ---LIETELLAEYVIRTFAVEKRgvheiREIRQFHFTGWPDHG-VPYHAT----GLLGFVRQVKSKSPPSAGPL------ 1086
Cdd:cd14559     93 kdeLVDGLKADMYNLKITDGNKT-----ITIPVVHVTNWPDHTaISSEGLkelaDLVNKSAEEKRNFYKSKGSSaindkn 167

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462561112 1087 ----VVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIyncVRELR-SRRVNMVQTEEQYV 1140
Cdd:cd14559    168 kllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRtSRNGKMVQKDEQLD 223
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1208-1444 2.63e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 60.37  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1208 NHEKNRCMD---ILPPDRCLPFLITIDGESsNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV 1284
Cdd:PHA02740    47 AQAENKAKDenlALHITRLLHRRIKLFNDE-KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1285 DPAQLCPQYWP--ENGVHRHGPIQVEFVsadleeDIISRIFRIYNAARPQDGY---RMVQQFQFLGWPM--YRDTPvskR 1357
Cdd:PHA02740   126 ADKKCFNQFWSlkEGCVITSDKFQIETL------EIIIKPHFNLTLLSLTDKFgqaQKISHFQYTAWPAdgFSHDP---D 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1358 SFLKLIRQVDKW-----QEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQ 1432
Cdd:PHA02740   197 AFIDFFCNIDDLcadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDD 276

                          250
                   ....*....|..
gi 2462561112 1433 YKFCYEVALEYL 1444
Cdd:PHA02740   277 YVFCYHLIAAYL 288
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1046-1144 1.43e-07

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 53.51  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1046 REIRQFHFtGWPDHGVPYHATgLLGFVrQVKSKSPPSAGPLVVHCSAGAGRTG----CFIVidIMLDMAEREgvvdiynC 1121
Cdd:cd14506     75 AGIYFYNF-GWKDYGVPSLTT-ILDIV-KVMAFALQEGGKVAVHCHAGLGRTGvliaCYLV--YALRMSADQ-------A 142

                           90       100
                   ....*....|....*....|...
gi 2462561112 1122 VRELRSRRVNMVQTEEQYVFIHD 1144
Cdd:cd14506    143 IRLVRSKRPNSIQTRGQVLCVRE 165
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1071-1144 4.06e-07

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 50.04  E-value: 4.06e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462561112 1071 FVRQVKSKSPPSaGPLVVHCSAGAGRTGCFIVIDIMLDMaeREGVVDIyncVRELRSRRVN-MVQTEEQYVFIHD 1144
Cdd:cd14494     45 FLEVLDQAEKPG-EPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEA---VRIVRLIRPGgIPQTIEQLDFLIK 113
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 378-472 5.45e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  378 PRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLtvhYCYQVGGQEQVREEVSWDTENShpqHTITNLSPYTNVSVKLILM 457
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV---EYREKGSGDWKEVEVTPGSETS---YTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 2462561112  458 NPEGR-KESQELIVQT 472
Cdd:cd00063     78 NGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 378-462 5.90e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.76  E-value: 5.90e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   378 PRKLEVVEVKSRQITIRWEPFGYNVTRchSYNLTvhycYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILM 457
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVG----YRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*
gi 2462561112   458 NPEGR 462
Cdd:smart00060   78 NGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 477-567 1.44e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.44e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   477 PGAVPTESIQGSTfEEKIFLQWREPTqtYGVITLYEITYKAVSSfdpeiDLSNQSGRVSKLGNETHFLFFGLYPGTTYSF 556
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPP--DDGITGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72

                            90
                    ....*....|.
gi 2462561112   557 TIRASTAKGFG 567
Cdd:smart00060   73 RVRAVNGAGEG 83
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1026-1144 2.71e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.43  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1026 LLAEYVIRTFAVEKRGVheireirQFHFTGWPDHGVPyHATGLLGFVRQVKSKSPPSaGPLVVHCSAGAGRTGCFIvidI 1105
Cdd:COG2453     32 LTEEEELLLGLLEEAGL-------EYLHLPIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVA---A 99

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462561112 1106 MLDMAEREGVVDIYNCVRELRSRRvnmVQTEEQYVFIHD 1144
Cdd:COG2453    100 AYLVLLGLSAEEALARVRAARPGA---VETPAQRAFLER 135
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 187-273 1.81e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 1.81e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   187 QNVEVNAGQFATFQCSAIGRTVAgDRLWLQGIDVRDAPLKEIKVTSSRrFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 266
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ....*..
gi 2462561112   267 NyAELVV 273
Cdd:smart00410   80 G-TTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 277-356 1.90e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 1.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112   277 PVPIAPPQLASVGATYLWIQ-LNANSINGDGPIVAREVEYCTASGSWND-RQPVDSTSYKIGHLDPDTEYEISVL-LTRP 353
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 2462561112   354 GEG 356
Cdd:smart00060   81 GEG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1352-1438 2.23e-05

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 45.03  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1352 TPVSKRSFLKLIRQVDKwqeeyngGEGRTVVHCLNGGGRSGTFCAisivCEMLRHQRTvDVFHAVKTLRNNKPN-MVDLL 1430
Cdd:cd14494     38 TLAMVDRFLEVLDQAEK-------PGEPVLVHCKAGVGRTGTLVA----CYLVLLGGM-SAEEAVRIVRLIRPGgIPQTI 105


                   ....*...
gi 2462561112 1431 DQYKFCYE 1438
Cdd:cd14494    106 EQLDFLIK 113
I-set pfam07679
Immunoglobulin I-set domain;
181-262 1.41e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.86  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  181 PHFLR-IQNVEVNAGQFATFQCSAIGR---TVAgdrlWLQGidvrDAPLKeikvtSSRRF-------IASFNVVNTTKRD 249
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTGTpdpEVS----WFKD----GQPLR-----SSDRFkvtyeggTYTLTISNVQPDD 67

                           90
                   ....*....|...
gi 2462561112  250 AGKYRCMIRTEGG 262
Cdd:pfam07679   68 SGKYTCVATNSAG 80
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1071-1142 1.45e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.42  E-value: 1.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462561112 1071 FVRQVKsKSPPSAGPLVVHCSAGAGRTG----CFIVIDIMLDMAEregvvdiynCVRELRSRRVNMVQTEEQYVFI 1142
Cdd:cd14504     71 FLDIVE-EANAKNEAVLVHCLAGKGRTGtmlaCYLVKTGKISAVD---------AINEIRRIRPGSIETSEQEKFV 136
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 277-369 1.83e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  277 PVPIAPPQLASVGATYLWIQLNANSINGdGPIVAREVEYCTA-SGSWN--DRQPVDSTSYKIGHLDPDTEYEISVLLTRp 353
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKgSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78

                           90
                   ....*....|....*.
gi 2462561112  354 gEGGTGSPGPALRTRT 369
Cdd:cd00063     79 -GGGESPPSESVTVTT 93
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1252-1434 1.92e-04

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 44.70  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1252 FIVTQHPLPNTVKDFWRLVLDYHCTSVVML--NDVDPAQLCPQYWPENGvhRHGPIQV--EFVSADLEEDIISriFRIYN 1327
Cdd:cd14559     31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLasNKDIQRKGLPPYFRQSG--TYGSVTVksKKTGKDELVDGLK--ADMYN 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1328 AARPQDGYRM-VQQFQFLGWPmyrD-TPVSKRSFLKLIRQVDKWQEEYNGG-------------EGRTVVHCLNGGGRSG 1392
Cdd:cd14559    107 LKITDGNKTItIPVVHVTNWP---DhTAISSEGLKELADLVNKSAEEKRNFykskgssaindknKLLPVIHCRAGVGRTG 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462561112 1393 TFCAisiVCEMLRHQRTV---DVFHAVKTLRNNKpnMVDLLDQYK 1434
Cdd:cd14559    184 QLAA---AMELNKSPNNLsveDIVSDMRTSRNGK--MVQKDEQLD 223
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1019-1144 4.22e-04

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 42.64  E-value: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1019 VTLIETELLAEYVIRTF--AVEKRGvheireIRQFHFTgWPDHGVP----YHATgLLGFVRQVKSKSppsaGPLVVHCSA 1092
Cdd:cd14505     48 VTLCTDGELEELGVPDLleQYQQAG------ITWHHLP-IPDGGVPsdiaQWQE-LLEELLSALENG----KKVLIHCKG 115

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462561112 1093 GAGRTGcFIVIDIMLDMAEREGVVDIYNCVRELRSRrvnMVQTEEQYVFIHD 1144
Cdd:cd14505    116 GLGRTG-LIAACLLLELGDTLDPEQAIAAVRALRPG---AIQTPKQENFLHQ 163
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1005-1109 6.79e-04

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 43.13  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1005 KYWPDDTEIYKDIKVTLIETEllaEYVirtfaVEKRGVHEIREIRQFHFtgWPDhgvPYHATGLLGFVRQVksksPPSAG 1084
Cdd:cd14495    126 KDKKKSPSQPKTVKVESVRTE---EEL-----VKKKGAHYVRIAATDHV--WPD---DEEIDAFVAFYRSL----PADAW 188

                           90       100
                   ....*....|....*....|....*
gi 2462561112 1085 pLVVHCSAGAGRTGCFIVidiMLDM 1109
Cdd:cd14495    189 -LHFHCRAGKGRTTTFMV---MYDM 209
fn3 pfam00041
Fibronectin type III domain;
279-356 1.21e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  279 PIAPPQLASVGATYLWIQLNANSiNGDGPIVAREVEYCTASGSWNDRQ---PVDSTSYKIGHLDPDTEYEISVlLTRPGE 355
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEitvPGTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 2462561112  356 G 356
Cdd:pfam00041   80 G 80
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1352-1438 1.80e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 40.71  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1352 TPVSKRSFLKLIRQVdkwQEEYNGGEgRTVVHCLNGGGRSGTFCAisivCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLD 1431
Cdd:cd14505     85 VPSDIAQWQELLEEL---LSALENGK-KVLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQTPK 156


                   ....*..
gi 2462561112 1432 QYKFCYE 1438
Cdd:cd14505    157 QENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1341-1435 1.88e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112 1341 FQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSGTFCAisivCEMLRHQRTVDvfHAVKTLR 1420
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA----AYLVLLGLSAE--EALARVR 117

                           90
                   ....*....|....*
gi 2462561112 1421 NNKPNMVDLLDQYKF 1435
Cdd:COG2453    118 AARPGAVETPAQRAF 132
fn3 pfam00041
Fibronectin type III domain;
378-458 2.40e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561112  378 PRKLEVVEVKSRQITIRWEP--------FGYNVTrchsynltvhyCYQVGGQEQVREEvswDTENSHPQHTITNLSPYTN 449
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgngpiTGYEVE-----------YRPKNSGEPWNEI---TVPGTTTSVTLTGLKPGTE 68


                   ....*....
gi 2462561112  450 VSVKLILMN 458
Cdd:pfam00041   69 YEVRVQAVN 77
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 1364-1425 3.68e-03

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 39.07  E-value: 3.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462561112 1364 RQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCemLRHQRTVDVFHAVKTLRNN-KPN 1425
Cdd:cd14514     65 EVADKIHQVKRRG-GRTLVHCVAGVSRSATLCLAYLMK--YEGMTLREAYKHVKAARPIiRPN 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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