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Conserved domains on  [gi|503774431|ref|NP_001265167|]
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tyrosine-protein phosphatase non-receptor type 5 isoform c [Homo sapiens]

Protein Classification

tyrosine-protein phosphatase non-receptor type 5( domain architecture ID 12998696)

tyrosine-protein phosphatase non-receptor type 5 (PTPN5/STEP) is a tyrosine-specific protein-tyrosine phosphatase (PTP) that may regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors

EC:  3.1.3.48
Gene Symbol:  PTPN5
Gene Ontology:  GO:0004725|GO:0016791
PubMed:  27514797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 274-531 0e+00

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: 573.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 274 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIV 353
Cdd:cd14613    1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 354 STVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFT 433
Cdd:cd14613   81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 434 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGG 513
Cdd:cd14613  161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                        250
                 ....*....|....*...
gi 503774431 514 MIQTCEQYQFVHHVMSLY 531
Cdd:cd14613  241 MIQTCEQYQFVHHVLSLY 258
 
Name Accession Description Interval E-value
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 274-531 0e+00

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: 573.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 274 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIV 353
Cdd:cd14613    1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 354 STVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFT 433
Cdd:cd14613   81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 434 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGG 513
Cdd:cd14613  161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                        250
                 ....*....|....*...
gi 503774431 514 MIQTCEQYQFVHHVMSLY 531
Cdd:cd14613  241 MIQTCEQYQFVHHVLSLY 258
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
275-528 7.59e-105

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.98  E-value: 7.59e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   275 LLQAEFFEIPMNFVDPKEYDI---PGLVRKNRYKTILPNPHSRVCLTspDPDDPLSSYINANYIRGYGgEEKVYIATQGP 351
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLK--PPPGEGSDYINASYIDGPN-GPKAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   352 IVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEEQ---VAYDGVEITVQKVIHTEDYRLRLISLKSGT--EER 425
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   426 GLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTC 505
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTG---PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                          250       260
                   ....*....|....*....|...
gi 503774431   506 QLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
300-528 3.61e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 302.24  E-value: 3.61e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431  300 RKNRYKTILPNPHSRVCLTSPDPDdplSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE 379
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKP-KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431  380 MN-EKCTEYWP---EEQVAYDGVEITVQK-VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:pfam00102  79 KGrEKCAQYWPeeeGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431  453 EVEEaaQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:pfam00102 159 KVRK--SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 265-525 2.01e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.09  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 265 ELHEKALDPFLLQAEFFEIPMNfvdpkeydipglVRKNRYKTILPNPHSRVCLTSPDpdDPLSSYINANYIRGYGgEEKV 344
Cdd:PHA02747  30 EHHQIILKPFDGLIANFEKPEN------------QPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFE-DDKK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 345 YIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN--EKCTEYW-PEEQVAYD--GVEITVQKVIHTEDYRLRLISL- 418
Cdd:PHA02747  95 FIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgeEKCYQYWcLNEDGNIDmeDFRIETLKTSVRAKYILTLIEIt 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 419 -KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH-------CAPIIVHCSAGIGRTGCFIATSICCQ 490
Cdd:PHA02747 175 dKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLN 254

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 503774431 491 QLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:PHA02747 255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
286-523 2.89e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 144.46  E-value: 2.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 286 NFVDPKEYDIPGLVRKNRYKTILPNPHSRVclTSPDPddplssYINANYIRGygGEEKVYIATQGPIVSTVADFWRMVWQ 365
Cdd:COG5599   30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL--RANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 366 EHTPIIVMITNIEEM---NEKCTEYWPE-EQVAYDGVEITVQKVIHTED---YRLRLISLK-SGTEERGLKHYWFTSWPD 437
Cdd:COG5599  100 NNTPVLVVLASDDEIskpKVKMPVYFRQdGEYGKYEVSSELTESIQLRDgieARTYVLTIKgTGQKKIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 438 QKTPDrAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATsICCQQLRQEGV---VDILKTTCQLRQDRG-G 513
Cdd:COG5599  180 HGAIS-AEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRNgG 257

                        250
                 ....*....|
gi 503774431 514 MIQTCEQYQF 523
Cdd:COG5599  258 MVQTSEQLDV 267
 
Name Accession Description Interval E-value
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 274-531 0e+00

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: 573.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 274 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIV 353
Cdd:cd14613    1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 354 STVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFT 433
Cdd:cd14613   81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 434 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGG 513
Cdd:cd14613  161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                        250
                 ....*....|....*...
gi 503774431 514 MIQTCEQYQFVHHVMSLY 531
Cdd:cd14613  241 MIQTCEQYQFVHHVLSLY 258
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 302-526 2.99e-159

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: 452.24  E-value: 2.99e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTSpDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN 381
Cdd:cd14547    1 NRYKTILPNEHSRVCLPS-VDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 382 EKCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQ 460
Cdd:cd14547   80 EKCAQYWPEEENeTYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 461 EgPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14547  160 E-PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 284-531 2.32e-131

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: 382.26  E-value: 2.32e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 284 PMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMV 363
Cdd:cd14612    1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 364 WQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDR 443
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 444 APPLLHLVREVEEaAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14612  161 AGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                 ....*...
gi 503774431 524 VHHVMSLY 531
Cdd:cd14612  240 LHHTLALY 247
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 301-526 1.22e-122

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: 359.23  E-value: 1.22e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEaAQQ 460
Cdd:cd14611   82 NEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE-DRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 461 EGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14611  161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
275-528 7.59e-105

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.98  E-value: 7.59e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   275 LLQAEFFEIPMNFVDPKEYDI---PGLVRKNRYKTILPNPHSRVCLTspDPDDPLSSYINANYIRGYGgEEKVYIATQGP 351
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLK--PPPGEGSDYINASYIDGPN-GPKAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   352 IVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEEQ---VAYDGVEITVQKVIHTEDYRLRLISLKSGT--EER 425
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   426 GLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTC 505
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTG---PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                          250       260
                   ....*....|....*....|...
gi 503774431   506 QLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
300-528 3.61e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 302.24  E-value: 3.61e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431  300 RKNRYKTILPNPHSRVCLTSPDPDdplSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE 379
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKP-KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431  380 MN-EKCTEYWP---EEQVAYDGVEITVQK-VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:pfam00102  79 KGrEKCAQYWPeeeGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431  453 EVEEaaQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:pfam00102 159 KVRK--SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 329-526 4.78e-81

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: 251.82  E-value: 4.78e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEEQ---VAYDGVEITVQK 404
Cdd:cd00047    1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrEKCERYWPEEGgkpLEYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 405 VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHCSAGIGRTGCF 482
Cdd:cd00047   80 EEELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG---PIVVHCSAGVGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503774431 483 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd00047  157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 301-531 9.87e-74

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: 234.66  E-value: 9.87e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIR------GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMI 374
Cdd:cd14544    4 KNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 375 TN-IEEMNEKCTEYWPEE--QVAYDGVEITVQKVIHTEDYRLRLISLK---SGTEERGLKHYWFTSWPDQKTPDRAPPLL 448
Cdd:cd14544   84 TKeVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDPGGVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 449 HLVREVEEaAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14544  164 NFLEDVNQ-RQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242


                 ....*.
gi 503774431 526 HVMSLY 531
Cdd:cd14544  243 VAVAQY 248
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 301-525 3.32e-71

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: 227.66  E-value: 3.32e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14553    6 KNRYANVIAYDHSRVIL-QPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEE-QVAYDGVEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14553   84 SRvKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503774431 457 AAQqegPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14553  164 CNP---PDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 296-525 3.41e-70

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: 226.09  E-value: 3.41e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 296 PGLVRKNRYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMIT 375
Cdd:cd14543   27 PANQEKNRYGDVLCLDQSRVKLPKRNGDER-TDYINANFMDGYK-QKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 376 NIEEMNE-KCTEYWPEE---QVAYDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLH 449
Cdd:cd14543  105 RVVERGRvKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 450 LVREVEE----AAQQEGP----HCA--PIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCE 519
Cdd:cd14543  185 FLGEVRQqqalAVKAMGDrwkgHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPD 264


                 ....*.
gi 503774431 520 QYQFVH 525
Cdd:cd14543  265 QYYFCY 270
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 303-525 4.60e-70

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: 224.16  E-value: 4.60e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 303 RYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMN 381
Cdd:cd14548    1 RYTNILPYDHSRVKL-IPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcMEKGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 382 EKCTEYWPEEQVAYDGVEITVQKV--IHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQ 459
Cdd:cd14548   79 VKCDHYWPFDQDPVYYGDITVTMLseSVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 460 QEGphcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14548  159 QEK---GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 329-525 2.64e-64

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: 208.36  E-value: 2.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWPEEQV-AYDGVEITVQKVI 406
Cdd:cd14549    1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgRRKCDQYWPKEGTeTYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 407 HTEDYRLRLISLK--------SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCAPIIVHCSAGIGR 478
Cdd:cd14549   80 VLATYTVRTFSLKnlklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA---NPPGAGPIVVHCSAGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 479 TGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14549  157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 302-524 8.21e-61

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: 200.04  E-value: 8.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTSPDpdDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEM 380
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQS--HSTDDYINANYMPGYN-SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcVEQG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NEKCTEYWPEEQ-VAYDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLL---HLVREV 454
Cdd:cd14615   78 RTKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLInfrHLVREY 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 455 eeaaQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14615  158 ----MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 301-531 1.72e-60

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: 200.24  E-value: 1.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYI-------RGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVM 373
Cdd:cd14605    5 KNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 374 ITN-IEEMNEKCTEYWPEEQV--AYDGVEITVQKVIHTEDYRLRLISLK---SGTEERGLKHYWFTSWPDQKTPDRAPPL 447
Cdd:cd14605   85 TTKeVERGKSKCVKYWPDEYAlkEYGVMRVRNVKESAAHDYILRELKLSkvgQGNTERTVWQYHFRTWPDHGVPSDPGGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 448 LHLVREVEEaaQQEG-PHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14605  165 LDFLEEVHH--KQESiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRF 242


                 ....*...
gi 503774431 524 VHHVMSLY 531
Cdd:cd14605  243 IYMAVQHY 250
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 301-525 2.49e-60

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: 199.10  E-value: 2.49e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14630    6 KNRYGNIISYDHSRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEA 457
Cdd:cd14630   84 GRvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVqKKGYHEiREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503774431 458 aqqEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14630  164 ---NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVH 228
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 301-525 3.66e-60

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: 198.90  E-value: 3.66e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14554    9 KNRLVNILPYESTRVCL-QPIRGVEGSDYINASFIDGYR-QRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 N-EKCTEYWPEE---QVAYDGVEITVQKviHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREV 454
Cdd:cd14554   87 GrEKCHQYWPAErsaRYQYFVVDPMAEY--NMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQV 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503774431 455 EEAAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14554  165 HKTKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 329-526 1.56e-59

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: 196.32  E-value: 1.56e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMNEKCTEYWPEE--QVAYDGVEITVQKV 405
Cdd:cd18533    1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPlVENGREKCDQYWPSGeyEGEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 406 IHTEDYRL--RLISLKSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEgPHCAPIIVHCSAGIGRTGCF 482
Cdd:cd18533   81 EENDDGGFivREFELSKEDgKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSA-SLDPPIIVHCSAGVGRTGTF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503774431 483 IATSICCQQLRQ--------EGVVD-ILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd18533  160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 301-528 1.64e-59

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: 198.34  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTS-PDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IE 378
Cdd:cd17667   30 KNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNlVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 379 EMNEKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGTEERGLK-------------HYWFTSWPDQKTPDRA 444
Cdd:cd17667  109 KGRRKCDQYWPTENSEeYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnpkgrqnertviQYHYTQWPDMGVPEYA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 445 PPLLHLVREvEEAAQQegPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd17667  189 LPVLTFVRR-SSAART--PEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 265


                 ....
gi 503774431 525 HHVM 528
Cdd:cd17667  266 HDAL 269
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 301-528 2.15e-59

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: 198.34  E-value: 2.15e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14626   44 KNRYANVIAYDHSRVILTSVD-GVPGSDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14626  122 SRvKCDQYWPIRGTeTYGMIQVTLLDTVELATYSVRTFALyKNGSsEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 457 AaqqEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14626  202 C---NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 284-525 1.23e-57

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: 193.17  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 284 PMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIR----GYGGEEKVYIATQGPIVSTVADF 359
Cdd:cd14606    4 VKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 360 WRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPE--EQVAYDGVEITVQKVIHTEDYRLRLISL---KSGTEERGLKHYWFT 433
Cdd:cd14606   84 WQMAWQENSRVIVMTTrEVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELIREIWHYQYL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 434 SWPDQKTPDRAPPLLHLVREVEEaAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQD 510
Cdd:cd14606  164 SWPDHGVPSEPGGVLSFLDQINQ-RQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQ 242

                        250
                 ....*....|....*
gi 503774431 511 RGGMIQTCEQYQFVH 525
Cdd:cd14606  243 RSGMVQTEAQYKFIY 257
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 294-530 1.58e-57

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: 192.03  E-value: 1.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 294 DIPGLVRKNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVM 373
Cdd:cd14614    8 DLPVNRCKNRYTNILPYDFSRVKLVSMH-EEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 374 ITNIEEMNE-KCTEYWP--EEQVAYDgvEITVQKVIHTE--DYRLRLISLKSGTEERGLKHYWFTSWPDQKTP--DRAPP 446
Cdd:cd14614   86 LTQCNEKRRvKCDHYWPftEEPVAYG--DITVEMLSEEEqpDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAES 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 447 LLHLVREVEeaaQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14614  164 ILQFVQMVR---QQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                 ....
gi 503774431 527 VMSL 530
Cdd:cd14614  241 CVQL 244
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 329-525 2.80e-56

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: 187.43  E-value: 2.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQVAYDGVEITVQKVIH 407
Cdd:cd14555    1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvKCSRYWPDDTEVYGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 TEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCAPIIVHCSAGIGRTGCFIAT 485
Cdd:cd14555   80 LAEYVVRTFALeRRGYHEiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP---PSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 503774431 486 SICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14555  157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 314-525 5.82e-56

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: 187.15  E-value: 5.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 314 RVCLtSPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQ 392
Cdd:cd14631    1 RVIL-QPVEDDPSSDYINANYIDGYQRPSH-YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvKCYKYWPDDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 393 VAYDGVEITVQKVIHTEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCAPIIV 470
Cdd:cd14631   79 EVYGDFKVTCVEMEPLAEYVVRTFTLeRRGYNEiREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLS---NPPSAGPIVV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503774431 471 HCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14631  156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 210
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 329-528 9.71e-56

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: 185.94  E-value: 9.71e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEE-QVAYDGVEITVQKVI 406
Cdd:cd14552    1 YINASFIDGYR-QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqNKCAQYWPEDgSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 407 HTEDYRLR--LISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcaPIIVHCSAGIGRTGCFIA 484
Cdd:cd14552   80 DYEDYTLRdfLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH--PITVHCSAGAGRTGTFCA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503774431 485 TSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14552  158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 302-525 7.99e-55

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: 184.38  E-value: 7.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTSPdPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEM 380
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQL-GGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NEKCTEYWPEEQ--VAYDGVEITVQKVIHTEDYRLRLISLKSGTE--ERGLKHYWFTSWPDQKTPDRAPPLL---HLVRE 453
Cdd:cd14618   79 RVLCDHYWPSEStpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMafrELVRE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 454 VEEAAQQEGPhcapIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14618  159 HVQATKGKGP----TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLH 226
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 301-525 1.50e-54

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: 185.25  E-value: 1.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14633   43 KNRYGNIIAYDHSRVRL-QPIEGETSSDYINGNYIDGYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEea 457
Cdd:cd14633  121 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVeKRGVHEiREIRQFHFTGWPDHGVPYHATGLLGFVRQVK-- 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503774431 458 aQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14633  199 -SKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 265
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 301-537 3.34e-54

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: 184.93  E-value: 3.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14628   55 KNRLVNIMPYESTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 N-EKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14628  133 GrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 457 AAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLS 536
Cdd:cd14628  213 TKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291


                 .
gi 503774431 537 H 537
Cdd:cd14628  292 H 292
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 329-525 6.63e-54

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: 181.33  E-value: 6.63e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMNEKCTEYWPEEQVAYDGVEITVQKVIH 407
Cdd:cd17668    1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 T------EDYRLRLISLKSGTE-----ERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEgphCAPIIVHCSAGI 476
Cdd:cd17668   80 VlayytvRNFTLRNTKIKKGSQkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHA---VGPVVVHCSAGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503774431 477 GRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd17668  157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 301-531 3.45e-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: 182.24  E-value: 3.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14627   56 KNRLVNIMPYETTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREM 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 N-EKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14627  134 GrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503774431 457 AAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY 531
Cdd:cd14627  214 TKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 301-528 4.58e-53

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: 181.83  E-value: 4.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14625   50 KNRYANVIAYDHSRVILQ-PIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEK 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14625  128 SRiKCDQYWPSRGTeTYGMIQVTLLDTIELATFCVRTFSLhKNGSsEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 457 AaqqEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14625  208 C---NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 329-525 6.30e-53

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: 178.48  E-value: 6.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWP---EEQVAYDGVEITVQK 404
Cdd:cd14557    1 YINASYIDGFK-EPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnKCAQYWPsmeEGSRAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 405 VIHTEDYRLRLISL---KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCAPIIVHCSAGIGRTGC 481
Cdd:cd14557   80 EKICPDYIIRKLNInnkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF---NNFFSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503774431 482 FIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14557  157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 302-528 7.45e-53

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: 179.31  E-value: 7.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN 381
Cdd:cd14619    1 NRFRNVLPYDWSRVPLK-PIHEEPGSDYINANYMPGYWSSQE-FIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 382 E-KCTEYWPEEQV--AYDGVEITVQKVIHTEDYRLRLISLKSGTEE--RGLKHYWFTSWPDQKTPDRAPPLL---HLVRE 453
Cdd:cd14619   79 RvKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQktLSVRHFHFTAWPDHGVPSSTDTLLafrRLLRQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503774431 454 VEEAAQQEGPhcapIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14619  159 WLDQTMSGGP----TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 301-528 1.11e-52

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: 180.70  E-value: 1.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14624   50 KNRYANVIAYDHSRVLLSAIE-GIPGSDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEER 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQVAYDG-VEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14624  128 SRvKCDQYWPSRGTETYGlIQVTLLDTVELATYCVRTFALyKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 457 AaqqEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14624  208 C---NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 329-525 1.14e-52

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: 177.94  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQVAYDGVEITVQKVIH 407
Cdd:cd14632    1 YINANYIDGYHRSNH-FIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSKYWPDDSDTYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 TEDYRLRLISLksgtEERG------LKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCAPIIVHCSAGIGRTGC 481
Cdd:cd14632   80 LAEYSVRTFAL----ERRGysarheVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP---PDAGPVVVHCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 482 FIATSICCQQLRQEGVVDI---LKTTCQLRQDrggMIQTCEQYQFVH 525
Cdd:cd14632  153 YIVLDVMLDMAECEGVVDIyncVKTLCSRRIN---MIQTEEQYIFIH 196
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 329-523 9.06e-52

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: 175.64  E-value: 9.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPEE----QVAYDGVEITV 402
Cdd:cd14538    1 YINASHIRiPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVKCHRYWPDSlnkpLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 403 QKVIHTEDYRLRLISL--KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQegphcAPIIVHCSAGIGRTG 480
Cdd:cd14538   81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS-----GPIVVHCSAGIGRTG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 503774431 481 CFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14538  156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIF 198
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 299-526 9.09e-52

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: 177.71  E-value: 9.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 299 VRKNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVM-ITNI 377
Cdd:cd14603   31 VKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGS-RAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 378 EEMNEKCTEYWPEEQVAYDGVEITVQKVIH---TEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREV 454
Cdd:cd14603  109 EMGKKKCERYWAQEQEPLQTGPFTITLVKEkrlNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503774431 455 EEaAQQEGPhcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVD---ILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14603  189 RR-LQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYH 260
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 304-528 3.20e-51

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: 175.13  E-value: 3.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 304 YKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE- 382
Cdd:cd14620    1 YPNILPYDHSRVILSQLD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 383 KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLKSGTEE-----RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14620   79 KCYQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDgckapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 457 AaqqEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14620  159 V---NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 301-525 5.22e-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: 176.45  E-value: 5.22e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14629   56 KNRLVNIMPYELTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 N-EKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14629  134 GrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHK 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503774431 457 AAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14629  214 TKEQFGQD-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 300-531 3.52e-50

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: 172.32  E-value: 3.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 300 RKNRYKTILPNPHSRVCLTSPdpddplSSYINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-I 377
Cdd:cd14597    5 KKNRYKNILPYDTTRVPLGDE------GGYINASFIKmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQeV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 378 EEMNEKCTEYWPEE----QVAYDGVEITVQKVIHTEDYRLRLISLK--SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLV 451
Cdd:cd14597   79 EGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 452 ---REVEEAaqqegphcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14597  159 symRHIHKS--------GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                 ...
gi 503774431 529 sLY 531
Cdd:cd14597  231 -LY 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 302-525 5.75e-50

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: 171.64  E-value: 5.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEM 380
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVD-DDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEE-----RGLKHYWFTSWPDQKTPDRAPPLLHLVREVE 455
Cdd:cd14617   79 RVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEqldapRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 456 EAAQQEgPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14617  159 DYINRT-PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 329-531 2.56e-49

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: 169.03  E-value: 2.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWPEEQVAYDG---VEITVQK 404
Cdd:cd14622    2 YINASFIDGYR-QKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReQEKCVQYWPSEGSVTHGeitIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 405 VIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcaPIIVHCSAGIGRTGCFIA 484
Cdd:cd14622   81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH--PIVVHCSAGAGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 485 TSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY 531
Cdd:cd14622  159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 299-535 6.08e-49

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: 171.27  E-value: 6.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 299 VRKNRYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIE 378
Cdd:cd14604   58 VKKNRYKDILPFDHSRVKLTLKTSSQD-SDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 379 EMN-EKCTEYWP---EEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREV 454
Cdd:cd14604  136 EMGrKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 455 EEAAQQEGphcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQDRGGMIQTCEQYQFVHHVMS-L 530
Cdd:cd14604  216 RKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqL 292


                 ....*
gi 503774431 531 YEKQL 535
Cdd:cd14604  293 FEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 329-526 9.68e-49

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: 167.21  E-value: 9.68e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWP---EEQVAYDGVEITVQK 404
Cdd:cd14542    1 YINANFIKGVSGS-KAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKkKCERYWPeegEEQLQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 405 V-IHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHCSAGIGRTGCFI 483
Cdd:cd14542   80 EkRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV---PICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503774431 484 ATSICCQQLRQEG------VVDILKttcQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14542  157 AIDYVWNLLKTGKipeefsLFDLVR---EMRKQRPAMVQTKEQYELVYR 202
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 302-525 1.90e-48

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: 167.39  E-value: 1.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN 381
Cdd:cd14616    1 NRFPNIKPYNNNRVKLI-ADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 382 E-KCTEYWPEEQ--VAYDGvEITVQKVIH--TEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14616   79 RiRCHQYWPEDNkpVTVFG-DIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503774431 457 AAQQEGphcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14616  158 SRAHDN---TPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 329-532 1.06e-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: 164.49  E-value: 1.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMNEKCTEYWPEEQVAYDGVEITVQKVIH 407
Cdd:cd14558    1 YINASFIDGYWGP-KSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 TEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAA---QQEGPHCAPIIVHCSAGIGRTGCF 482
Cdd:cd14558   80 SPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpykNSKHGRSVPIVVHCSDGSSRTGIF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503774431 483 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFvhhvmsLYE 532
Cdd:cd14558  160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQF------LYD 203
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 303-528 2.28e-47

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: 164.83  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 303 RYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-N 381
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEEN-TDYVNASFIDGYR-QKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 382 EKCTEYWPEE-QVAYDGVEITVQKVIHTEDYRLR--LISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAA 458
Cdd:cd14623   79 EKCAQYWPSDgSVSYGDITIELKKEEECESYTVRdlLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 459 QQEGPHcaPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14623  159 QQSGNH--PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 301-528 3.19e-47

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: 166.35  E-value: 3.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14621   55 KNRYVNILPYDHSRVHLT-PVEGVPDSDYINASFINGYQEKNK-FIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKER 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLK------SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14621  133 KEcKCAQYWPDQGCwTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLK 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 453 EVEEAAQQegpHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14621  213 KVKNCNPQ---YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 329-524 2.19e-46

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: 161.34  E-value: 2.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANY----IRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPE--EQVAYDGVEIT 401
Cdd:cd14541    2 YINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTtLVERGRVKCHQYWPDlgETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 402 VQKVIHTEDYRLRLISLK--SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEeaAQQEGPhCAPIIVHCSAGIGRT 479
Cdd:cd14541   81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGM-VEPTVVHCSAGIGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 480 GCFIA--TSICCQQLRQEgvVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14541  158 GVLITmeTAMCLIEANEP--VYPLDIVRTMRDQRAMLIQTPSQYRFV 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 301-523 2.25e-46

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: 162.18  E-value: 2.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDPDdplSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 380
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NE-KCTEYWPEEQVA-----YDGVEITVQKVIHTEDYRLRLISL--KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14545   77 GQiKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503774431 453 EVEEAAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQEGV--VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14545  157 KVRESGSLSSDV-GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 329-525 3.58e-46

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: 160.63  E-value: 3.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEE---QVAYDGVEITVQK 404
Cdd:cd14539    1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKqKVHRYWPTErgqALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 405 VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCF 482
Cdd:cd14539   81 VRTTPTHVERIISIQHKDtrLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503774431 483 IATSICCQQLRQE-GVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14539  161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 299-523 4.54e-46

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: 162.92  E-value: 4.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 299 VRKNRYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIE 378
Cdd:cd14610   45 VQKNRSLAVLPYDHSRIILKAENSHSH-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 379 EMN-EKCTEYWPEE-QVAYDGVEIT-VQKVIHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVRE 453
Cdd:cd14610  124 ENGvKQCYHYWPDEgSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNlqTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRK 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503774431 454 VEEAAQqeGPHCaPIIVHCSAGIGRTGCFIATSICCQQLRQEGV-VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14610  204 VNKCYR--GRSC-PIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 329-525 9.56e-46

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: 159.31  E-value: 9.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQVAYDG-VEITVQKVI 406
Cdd:cd14551    1 YINASYIDGYQ-EKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEkKCSQYWPDQGCWTYGnLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 407 HTEDYRLRLISLKSGTEERGLK------HYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCAPIIVHCSAGIGRTG 480
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIGEKrvrlvtQFHFTSWPDFGVPFTPIGMLKFLKKVKSANP---PRAGPIVVHCSAGVGRTG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503774431 481 CFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14551  157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 329-528 1.90e-45

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: 158.76  E-value: 1.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPEeqvaydgveiTVQKVI 406
Cdd:cd14596    1 YINASYITmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVKCHRYWPE----------TLQEPM 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 407 HTEDYRLRL----------ISL-----KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEeAAQQEGPhcapIIVH 471
Cdd:cd14596   71 ELENYQLRLenyqalqyfiIRIiklveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-KVHNTGP----IVVH 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503774431 472 CSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14596  146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 265-525 2.01e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.09  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 265 ELHEKALDPFLLQAEFFEIPMNfvdpkeydipglVRKNRYKTILPNPHSRVCLTSPDpdDPLSSYINANYIRGYGgEEKV 344
Cdd:PHA02747  30 EHHQIILKPFDGLIANFEKPEN------------QPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFE-DDKK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 345 YIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN--EKCTEYW-PEEQVAYD--GVEITVQKVIHTEDYRLRLISL- 418
Cdd:PHA02747  95 FIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgeEKCYQYWcLNEDGNIDmeDFRIETLKTSVRAKYILTLIEIt 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 419 -KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH-------CAPIIVHCSAGIGRTGCFIATSICCQ 490
Cdd:PHA02747 175 dKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLN 254

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 503774431 491 QLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:PHA02747 255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 301-525 4.73e-45

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: 158.85  E-value: 4.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLT--SPDPDdplSSYINANYIRG-YGgeEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNI 377
Cdd:cd14602    1 KNRYKDILPYDHSRVELSliTSDED---SDYINANFIKGvYG--PRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACME 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 378 EEM-NEKCTEYWP---EEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVRE 453
Cdd:cd14602   76 FEMgKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWD 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 454 VEEAAQQEGPhcaPIIVHCSAGIGRTGCFIATSICCQQLRqEGVV----DILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14602  156 VRCYQEDDSV---PICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 299-523 2.15e-44

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: 158.28  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 299 VRKNRYKTILPNPHSRVCLTSpDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIE 378
Cdd:cd14609   43 VKKNRNPDFVPYDHARIKLKA-ESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 379 EMNEK-CTEYWPEEQVA-YDGVEIT-VQKVIHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVRE 453
Cdd:cd14609  122 EDGVKqCDRYWPDEGSSlYHIYEVNlVSEHIWCEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRK 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 454 VEEAAQqeGPHCaPIIVHCSAGIGRTGCFIATSICCQQLrQEGV--VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14609  202 VNKCYR--GRSC-PIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 329-524 1.19e-43

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: 154.14  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWPEE-QVAYDGVEIT-VQKV 405
Cdd:cd14546    1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENgVKQCARYWPEEgSEVYHIYEVHlVSEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 406 IHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqQEGPHCaPIIVHCSAGIGRTGCFI 483
Cdd:cd14546   81 IWCDDYLVRSFYLKNlqTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS--YRGRSC-PIVVHCSDGAGRTGTYI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 503774431 484 ATSICCQQL-RQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14546  158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFV 199
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 329-525 3.13e-43

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: 152.56  E-value: 3.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVeITVQKVIHT 408
Cdd:cd14556    1 YINAALLDSYK-QPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGP-IQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 409 EDYRL-----RLISLKSGTEE-RGLKHYWFTSWP-DQKTPDRAPPLLHLVREVEEAAQQEGPhcAPIIVHCSAGIGRTGC 481
Cdd:cd14556   79 IDEDVisrifRLQNTTRPQEGyRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWQEQSGE--GPIVVHCLNGVGRSGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503774431 482 FIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14556  157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 329-531 1.24e-42

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: 151.84  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE-MNEKCTEYWPEEQVAYDGV-----EIT 401
Cdd:cd14540    1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLGGEHDALtfgeyKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 402 VQKVIHTEDY---RLRLISLKSGTEeRGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE----AAQQEGPHC--APIIVHC 472
Cdd:cd14540   81 TKFSVSSGCYtttGLRVKHTLSGQS-RTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhTNQDVAGHNrnPPTLVHC 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503774431 473 SAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY 531
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 259-528 7.58e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 152.88  E-value: 7.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 259 RVLQAEELHEKALDP----FLLQ--AEFFEIPM-----NFVDPKEydipglVRKNRYKTILPNPHSRVCLTS-------- 319
Cdd:PHA02746   7 EIFNAFDFFDKTNHAkfceFVLLehAEVMDIPIrgttnHFLKKEN------LKKNRFHDIPCWDHSRVVINAheslkmfd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 320 ---PDP-------DDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWP 389
Cdd:PHA02746  81 vgdSDGkkievtsEDNAENYIHANFVDGFK-EANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 390 EE---QVAYDGVEITVQKVIHTEDY---RLRLISLKSGTEeRGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE------- 456
Cdd:PHA02746 160 KEedsELAFGRFVAKILDIIEELSFtktRLMITDKISDTS-REIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelik 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 457 AAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:PHA02746 239 QADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 301-523 2.27e-41

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: 150.18  E-value: 2.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDPDdplssYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEE 379
Cdd:cd14608   28 RNRYRDVSPFDHSRIKLHQEDND-----YINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 380 MNEKCTEYWP---EEQVAYDGVEITVQKVihTED----YRLRLISLK--SGTEERGLKHYWFTSWPDQKTPDRAPPLLHL 450
Cdd:cd14608  102 GSLKCAQYWPqkeEKEMIFEDTNLKLTLI--SEDiksyYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNF 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 451 VREVEEAAQQEgPHCAPIIVHCSAGIGRTGCFIATSICC---QQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14608  180 LFKVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 254
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 268-528 2.77e-40

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: 147.45  E-value: 2.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 268 EKALDPFLLQAEFFEIPMNFVDP--KEYDIPGLVRKNRYKTILPNPHSRVCLTsPDPDDPlSSYINANYIR-GYGGEEKV 344
Cdd:cd14599    6 ERKLEEGMVFTEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVELV-PTKENN-TGYINASHIKvTVGGEEWH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 345 YIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPE-----EQVAYDGVEITVQKVIHTEDYR---LRL 415
Cdd:cd14599   84 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRsKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYAttgLKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 416 ISLKSGtEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHC-------APIIVHCSAGIGRTGCFIATSIC 488
Cdd:cd14599  164 KHLLSG-QERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLdstkncnPPIVVHCSAGVGRTGVVILTELM 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 503774431 489 CQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14599  243 IGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 301-524 8.89e-40

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: 145.76  E-value: 8.89e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDpddplsSYINANY----IRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN 376
Cdd:cd14600   43 KNRYKDVLPYDATRVVLQGNE------DYINASYvnmeIPSANIVNK-YIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 377 IEEMNE-KCTEYWPE--EQVAYDGVEITVqkviHTEDY-------RLRLISLKSGtEERGLKHYWFTSWPDQKTPDRAPP 446
Cdd:cd14600  116 LTERGRtKCHQYWPDppDVMEYGGFRVQC----HSEDCtiayvfrEMLLTNTQTG-EERTVTHLQYVAWPDHGVPDDSSD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 447 LLHLVREVEEAAQQEgphcAPIIVHCSAGIGRTGCFIA--TSICCQQLRQEgvVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14600  191 FLEFVNYVRSKRVEN----EPVLVHCSAGIGRTGVLVTmeTAMCLTERNQP--VYPLDIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 329-528 2.06e-39

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: 143.19  E-value: 2.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWP-----EEQVAYDGVEIT 401
Cdd:cd14598    1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgREKSFRYWPrlgsrHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 402 VQKVIHTEDYR---LRLISLKSGtEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE-------AAQQEGPHcAPIIVH 471
Cdd:cd14598   81 TRFRTDSGCYAttgLKIKHLLTG-QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnsTIDPKSPN-PPVLVH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503774431 472 CSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd14598  159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
286-523 2.89e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 144.46  E-value: 2.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 286 NFVDPKEYDIPGLVRKNRYKTILPNPHSRVclTSPDPddplssYINANYIRGygGEEKVYIATQGPIVSTVADFWRMVWQ 365
Cdd:COG5599   30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL--RANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 366 EHTPIIVMITNIEEM---NEKCTEYWPE-EQVAYDGVEITVQKVIHTED---YRLRLISLK-SGTEERGLKHYWFTSWPD 437
Cdd:COG5599  100 NNTPVLVVLASDDEIskpKVKMPVYFRQdGEYGKYEVSSELTESIQLRDgieARTYVLTIKgTGQKKIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 438 QKTPDrAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATsICCQQLRQEGV---VDILKTTCQLRQDRG-G 513
Cdd:COG5599  180 HGAIS-AEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRNgG 257

                        250
                 ....*....|
gi 503774431 514 MIQTCEQYQF 523
Cdd:COG5599  258 MVQTSEQLDV 267
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 301-523 3.20e-39

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: 143.57  E-value: 3.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 301 KNRYKTILPNPHSRVCLTSPDPDdplssYINANYIRgYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNI-EE 379
Cdd:cd14607   27 RNRYRDVSPYDHSRVKLQNTEND-----YINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIvEK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 380 MNEKCTEYWP---EEQVAYDGVEITVQKVihTED----YRLRLISL---KSGtEERGLKHYWFTSWPDQKTPDRAPPLLH 449
Cdd:cd14607  101 DSVKCAQYWPtdeEEVLSFKETGFSVKLL--SEDvksyYTVHLLQLeniNSG-ETRTISHFHYTTWPDFGVPESPASFLN 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503774431 450 LVREVEEAAQQeGPHCAPIIVHCSAGIGRTGCF--IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14607  178 FLFKVRESGSL-SPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRF 252
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 329-523 1.06e-37

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: 137.98  E-value: 1.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEE-KVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE--KCTEYWP---EEQVAYDGVEITV 402
Cdd:cd17658    1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStaKCADYFPaeeNESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 403 QKVIHTED-YRLRLISLKSGTEE---RGLKHYWFTSWPDQKTPDRAPPllhlVREVEEAAQQEGPHCAPIIVHCSAGIGR 478
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIESEeppLSVLHIQYPEWPDHGVPKDTRS----VRELLKRLYGIPPSAGPIVVHCSAGIGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 479 TGCFIATSICCQQLRQEGV--VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd17658  157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PHA02738 PHA02738
hypothetical protein; Provisional
 302-531 1.33e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 141.22  E-value: 1.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 302 NRYKTILPNPHSRVCLTSpdpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE-M 380
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPA---ERNRGDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 381 NEKCTEYWPE-EQ--VAYDGVEITVQKVIHTEDYRLRLISLKSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:PHA02738 129 REKCFPYWSDvEQgsIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQ 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 457 AAQQ----------EGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:PHA02738 209 CQKElaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYR 288


                 ....*
gi 503774431 527 VMSLY 531
Cdd:PHA02738 289 AVKRY 293
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
427-528 7.87e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 132.10  E-value: 7.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   427 LKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQE-GVVDILKTTC 505
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|...
gi 503774431   506 QLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 427-528 7.87e-37

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: 132.10  E-value: 7.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431   427 LKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcAPIIVHCSAGIGRTGCFIATSICCQQLRQE-GVVDILKTTC 505
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|...
gi 503774431   506 QLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 329-533 9.23e-37

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: 135.46  E-value: 9.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIR---GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMI-TNIEEMNEKCTEYWPE--EQVAYDGVEITV 402
Cdd:cd14601    2 YINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 403 QKVIHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEeaaQQEGPHCAPIIVHCSAGIGRTG 480
Cdd:cd14601   82 HSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR---NKRAGKDEPVVVHCSAGIGRTG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503774431 481 CFIA--TSICCQQLRQEGV-VDILKTtcqLRQDRGGMIQTCEQYQFV-HHVMSLYEK 533
Cdd:cd14601  159 VLITmeTAMCLIECNQPVYpLDIVRT---MRDQRAMMIQTPSQYRFVcEAILKVYEE 212
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 300-536 5.59e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 127.81  E-value: 5.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 300 RKNRYKTILPNPHSRVCLTSpdpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE 379
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVILKI---EDGGDDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 380 MN-EKCTEYW-PEEQ--VAYDGVEITVQKVIHTEDYR---LRLISLKSGTEeRGLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:PHA02742 130 DGkEACYPYWmPHERgkATHGEFKIKTKKIKSFRNYAvtnLCLTDTNTGAS-LDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 453 EVEEA--------AQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:PHA02742 209 AVREAdlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFC 288

                        250
                 ....*....|..
gi 503774431 525 HHVMSLYEKQLS 536
Cdd:PHA02742 289 YFIVLIFAKLMA 300
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 329-523 1.03e-31

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: 121.27  E-value: 1.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEmNEKCTEYWPEEQVAYDGVEITV------ 402
Cdd:cd14550    1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL-NEDEPIYWPTKEKPLECETFKVtlsged 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 403 -QKVIHTEDYRLRLISLKSGTEERGL--KHYWFTSWPDQKTPDRAppLLHLVREV-EEAAQQEGphcaPIIVHCSAGIGR 478
Cdd:cd14550   79 hSCLSNEIRLIVRDFILESTQDDYVLevRQFQCPSWPNPCSPIHT--VFELINTVqEWAQQRDG----PIVVHDRYGGVQ 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503774431 479 TGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14550  153 AATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 329-527 2.40e-29

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: 114.73  E-value: 2.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMnEKCTEYWPEE-QVAYDGVEITVQKVIH 407
Cdd:cd14634    1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA-QLCMQYWPEKtSCCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 TEDYRLRLISL----KSGTEERGLKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCF 482
Cdd:cd14634   79 DEDIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503774431 483 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHV 527
Cdd:cd14634  159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 329-528 9.97e-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: 113.17  E-value: 9.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWP--EEQVAYDGVEITVQKVI 406
Cdd:cd17669    1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPnkDEPINCETFKVTLIAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 407 HT-----EDYRLRLISLKSGTEERGL--KHYWFTSWPDQKTP-DRAPPLLHLVRevEEAAQQEGphcaPIIVHCSAGIGR 478
Cdd:cd17669   80 HKclsneEKLIIQDFILEATQDDYVLevRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRDG----PMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503774431 479 TGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd17669  154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 329-527 1.52e-25

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: 104.38  E-value: 1.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMnEKCTEYWPEEQVAYDG-VEITVQKVIH 407
Cdd:cd14635    1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA-QLCPQYWPENGVHRHGpIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 TEDYRLRLISLKSGTEE----RGLKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCF 482
Cdd:cd14635   79 EEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503774431 483 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHV 527
Cdd:cd14635  159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 329-528 6.06e-25

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: 102.45  E-value: 6.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITV------ 402
Cdd:cd17670    1 YINASYIMGYYRSNE-FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVtliskd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 403 --------QKVIHteDYRLRLISLKSGTEERglkHYWFTSWPDQKTPDRAP-PLLHLVRevEEAAQQEGphcaPIIVHCS 473
Cdd:cd17670   80 rlclsneeQIIIH--DFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTfELINVIK--EEALTRDG----PTIVHDE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503774431 474 AGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 528
Cdd:cd17670  149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 329-527 3.55e-24

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: 100.37  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEK--CTEYWPEEQVA-YDGVEITVQKV 405
Cdd:cd14637    1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPGLQqYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 406 IHTEDYRLRLISLKSGT----EERGLKHYWFTSW-PDQKTPDRAPPLLHLVREVEEAAQQEGPHcaPIIVHCSAGIGRTG 480
Cdd:cd14637   80 SADEDIVTRLFRVQNITrlqeGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEG--RTVVHCLNGGGRSG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 481 CFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHV 527
Cdd:cd14637  158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 329-529 1.99e-23

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: 98.17  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 329 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEeMNEKCTEYWPEE-QVAYDGVEITVQKVIH 407
Cdd:cd14636    1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVD-LAQGCPQYWPEEgMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 408 TEDYRLRLISLKSGTEERG----LKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCF 482
Cdd:cd14636   79 DCDVISRIFRICNLTRPQEgylmVQQFQYLGWASHReVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503774431 483 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMS 529
Cdd:cd14636  159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 312-534 2.03e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.79  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 312 HSRVCLTSPDpddplsSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEmnEKC-TEYWPE 390
Cdd:PHA02740  67 HRRIKLFNDE------KVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCfNQFWSL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 391 EQ---VAYDGVEITVQKVIHTEDYRLRLISL--KSGtEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH- 464
Cdd:PHA02740 138 KEgcvITSDKFQIETLEIIIKPHFNLTLLSLtdKFG-QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHk 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503774431 465 ----CAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQ 534
Cdd:PHA02740 217 adgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKE 290
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 310-522 2.67e-13

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: 69.35  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 310 NPHSRVCLTSPDPDDPLssyINANYIRGygGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEK-CTEYW 388
Cdd:cd14559    1 NRFTNIQTRVSTPVGKN---LNANRVQI--GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKgLPPYF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 389 -PEEQvaYDGVEITVQKV--------IHTEDYRLRLislKSGTEERGLKHYWFTSWPDQKTPDrAPPLLHLVREVEEAAQ 459
Cdd:cd14559   76 rQSGT--YGSVTVKSKKTgkdelvdgLKADMYNLKI---TDGNKTITIPVVHVTNWPDHTAIS-SEGLKELADLVNKSAE 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503774431 460 Q-----EGPHCAPI--------IVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKttcQLRQDRGG-MIQTCEQYQ 522
Cdd:cd14559  150 EkrnfyKSKGSSAIndknkllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVS---DMRTSRNGkMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 448-526 1.72e-11

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: 61.21  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 448 LHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRqeGVVDILkttCQLRQDRGGMI-QTCEQYQFVHH 526
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM--SAEEAV---RIVRLIRPGGIpQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
423-526 4.27e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 52.28  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 423 EERGLKHYWFTsWPDQKTPDRAPpLLHLVREVEEAAQQEGPhcapIIVHCSAGIGRTGCFIAtsiccQQLRQEGV--VDI 500
Cdd:COG2453   44 EEAGLEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREGKK----VLVHCRGGIGRTGTVAA-----AYLVLLGLsaEEA 112

                         90       100
                 ....*....|....*....|....*.
gi 503774431 501 LKttcQLRQDRGGMIQTCEQYQFVHH 526
Cdd:COG2453  113 LA---RVRAARPGAVETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 412-525 2.12e-06

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: 47.64  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 412 RLRLISLKSGTEERGLKHYWFtSWPDQKTPDRAPPLLHLVREVEEAAQQeGPHcapIIVHCSAGIGRTGCFIAtsicCQQ 491
Cdd:cd14505   58 ELGVPDLLEQYQQAGITWHHL-PIPDGGVPSDIAQWQELLEELLSALEN-GKK---VLIHCKGGLGRTGLIAA----CLL 128

                         90       100       110
                 ....*....|....*....|....*....|....
gi 503774431 492 LRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14505  129 LELGDTLDPEQAIAAVRALRPGAIQTPKQENFLH 162
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 424-525 9.18e-06

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: 46.57  E-value: 9.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 424 ERGLKHYWFtSWPDQKTPDRAPpLLHLVReVEEAAQQEGphcAPIIVHCSAGIGRTGCFIATS-ICCQQLRQEGVVDIlk 502
Cdd:cd14506   74 RAGIYFYNF-GWKDYGVPSLTT-ILDIVK-VMAFALQEG---GKVAVHCHAGLGRTGVLIACYlVYALRMSADQAIRL-- 145

                         90       100
                 ....*....|....*....|...
gi 503774431 503 ttcqLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14506  146 ----VRSKRPNSIQTRGQVLCVR 164
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 423-534 2.52e-05

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: 44.19  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503774431 423 EERGLKHYWFtswpdqKTPDRAPPLLHLVRE----VEEA-AQQEgphcaPIIVHCSAGIGRTGCFIAtsiCcqQLRQEGV 497
Cdd:cd14504   46 TCPGLRYHHI------PIEDYTPPTLEQIDEfldiVEEAnAKNE-----AVLVHCLAGKGRTGTMLA---C--YLVKTGK 109

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503774431 498 VDILKTTCQLRQDRGGMIQTCEQYQFVhhvmSLYEKQ 534
Cdd:cd14504  110 ISAVDAINEIRRIRPGSIETSEQEKFV----IQFAKT 142
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 423-484 1.28e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 39.74  E-value: 1.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503774431 423 EERGLKHY--WFtswPDQKTPDRappllHLVREVEEAAQQEGphcAPIIVHCSAGIGRTGCFIA 484
Cdd:cd14499   76 TDAGIRHYdlYF---PDGSTPSD-----DIVKKFLDICENEK---GAIAVHCKAGLGRTGTLIA 128
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 423-484 3.10e-03

unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases.


Pssm-ID: 350514 [Multi-domain]  Cd Length: 145  Bit Score: 38.12  E-value: 3.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503774431 423 EERGLKHYWFTSWPDQKTPDRAPplLHLVREVEEAAQQEGPHcaPIIVHCSAGIGRTGCFIA 484
Cdd:cd18538   52 RENGIQHFHIAMLGNKDPKVSIP--DHTMNRILRIILDKENH--PILVHCNKGKHRTGCVIA 109
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 441-489 5.20e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.94  E-value: 5.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503774431 441 PDRAPP----LLHLVREVEEAAQQEGPHCApiIVHCSAGIGRTGcfiaTSICC 489
Cdd:cd14497   69 PDHHPPplglLLEIVDDIDSWLSEDPNNVA--VVHCKAGKGRTG----TVICA 115
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
450-484 8.14e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 36.88  E-value: 8.14e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 503774431   450 LVREVEEAAQQEGPhcapIIVHCSAGIGRTGCFIA 484
Cdd:smart00195  67 AVEFIEDAESKGGK----VLVHCQAGVSRSATLII 97
 
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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