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Conserved domains on  [gi|564380626|ref|XP_006249882|]
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tyrosine-protein phosphatase non-receptor type 7 isoform X1 [Rattus norvegicus]

Protein Classification

PTPc-N7 domain-containing protein( domain architecture ID 12998695)

PTPc-N7 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 151-395 0e+00

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: 502.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 151 PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQ-EDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMV 229
Cdd:cd14612    1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 230 WQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPES 309
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 310 AGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14612  161 AGPLLRLVAEVeESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                 ....*..
gi 564380626 389 HHTLALY 395
Cdd:cd14612  241 HHTLALY 247
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 151-395 0e+00

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: 502.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 151 PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQ-EDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMV 229
Cdd:cd14612    1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 230 WQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPES 309
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 310 AGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14612  161 AGPLLRLVAEVeESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                 ....*..
gi 564380626 389 HHTLALY 395
Cdd:cd14612  241 HHTLALY 247
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
142-393 2.45e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 321.53  E-value: 2.45e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   142 QLEEEFLKIPSNFVNPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAHSqEDSDYINANYIRGYDGKeKVYIATQGPM 218
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   219 PNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRS 292
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   293 VKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLR 372
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRK-SQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|.
gi 564380626   373 LDRGGMIQTAEQYQFLHHTLA 393
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
165-393 1.71e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 313.41  E-value: 1.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626  165 HASKDRYKTILPNPQSRVCLGraHSQEDSDYINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLR 244
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626  245 E-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEH-PEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLV 317
Cdd:pfam00102  78 EkGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380626  318 AEVETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 393
Cdd:pfam00102 158 RKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 169-395 6.88e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.77  E-value: 6.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQedSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 247
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQEC-RSVKHILFSAWPDHQTPESAGPLLRLVAEVET- 322
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQc 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 323 -PETAANS----------GPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 391
Cdd:PHA02738 210 qKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 564380626 392 LALY 395
Cdd:PHA02738 290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
141-388 1.64e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 150.63  E-value: 1.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 141 KQLEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVclgrahsQEDSDYINANYIRGYDGKekVYIATQGPMPN 220
Cdd:COG5599   18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 221 TVADFWEMVWQEDVSLIVMLTQLREGKE---KCVHYWPTEEEaYGPFQIRI-----QGMKEHPEYTVRHLTIQHQ-QECR 291
Cdd:COG5599   89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSSeltesIQLRDGIEARTYVLTIKGTgQKKI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 292 SVKHILFSAWPDHQ--TPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDILGI 367
Cdd:COG5599  168 EIPVLHVKNWPDHGaiSAEALKNLADLIDKKEK-IKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEI 246

                        250       260
                 ....*....|....*....|..
gi 564380626 368 VCQLRLDRG-GMIQTAEQYQFL 388
Cdd:COG5599  247 VIDMRTSRNgGMVQTSEQLDVL 268
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 151-395 0e+00

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: 502.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 151 PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQ-EDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMV 229
Cdd:cd14612    1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 230 WQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPES 309
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 310 AGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14612  161 AGPLLRLVAEVeESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                 ....*..
gi 564380626 389 HHTLALY 395
Cdd:cd14612  241 HHTLALY 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 169-390 1.06e-153

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: 432.98  E-value: 1.06e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKE 248
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 249 KCVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVET-PETA 326
Cdd:cd14547   81 KCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEaRQTE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564380626 327 ANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 390
Cdd:cd14547  161 PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 143-395 2.57e-122

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: 354.55  E-value: 2.57e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 143 LEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLgRAHSQED--SDYINANYIRGYDGKEKVYIATQGPMPN 220
Cdd:cd14613    3 LQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCL-TSPDQDDplSSYINANYIRGYGGEEKVYIATQGPTVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 221 TVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSA 300
Cdd:cd14613   82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 301 WPDHQTPESAGPLLRLVAEVETPETAA--NSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGM 378
Cdd:cd14613  162 WPDQKTPDNAPPLLQLVQEVEEARQQAepNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                        250
                 ....*....|....*..
gi 564380626 379 IQTAEQYQFLHHTLALY 395
Cdd:cd14613  242 IQTCEQYQFVHHVLSLY 258
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 167-390 4.08e-117

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: 340.36  E-value: 4.08e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 167 SKDRYKTILPNPQSRVCLGRAHSQED-SDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE 245
Cdd:cd14611    1 TKNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 246 GKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPE 324
Cdd:cd14611   81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVeEDRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380626 325 TAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 390
Cdd:cd14611  161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
142-393 2.45e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 321.53  E-value: 2.45e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   142 QLEEEFLKIPSNFVNPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAHSqEDSDYINANYIRGYDGKeKVYIATQGPM 218
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   219 PNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRS 292
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   293 VKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLR 372
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRK-SQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|.
gi 564380626   373 LDRGGMIQTAEQYQFLHHTLA 393
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
165-393 1.71e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 313.41  E-value: 1.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626  165 HASKDRYKTILPNPQSRVCLGraHSQEDSDYINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLR 244
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626  245 E-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEH-PEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLV 317
Cdd:pfam00102  78 EkGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380626  318 AEVETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 393
Cdd:pfam00102 158 RKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 195-390 4.76e-93

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: 278.01  E-value: 4.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRIQG 270
Cdd:cd00047    1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkGREKCERYWPEEGGKpleYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 271 MKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIA 348
Cdd:cd00047   80 EEELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK-EARKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380626 349 TRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 390
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 170-389 2.14e-81

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: 249.19  E-value: 2.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 170 RYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKE 248
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 249 KCVHYWP--TEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETA 326
Cdd:cd14548   80 KCDHYWPfdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD-YIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380626 327 ANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14548  159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 168-392 1.26e-75

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: 234.98  E-value: 1.26e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 246
Cdd:cd14553    6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEErS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 KEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTI--QHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETp 323
Cdd:cd14553   85 RVKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA- 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 324 ETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14553  164 CNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 163-389 3.20e-73

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: 229.94  E-value: 3.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 163 PGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQ 242
Cdd:cd14543   27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 243 LRE-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRL 316
Cdd:cd14543  106 VVErGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLDF 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 317 VAEVETPETAA-------NSG-----PIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQ 384
Cdd:cd14543  186 LGEVRQQQALAvkamgdrWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQ 265


                 ....*
gi 564380626 385 YQFLH 389
Cdd:cd14543  266 YYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 195-389 6.98e-73

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: 226.46  E-value: 6.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMK 272
Cdd:cd14549    1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErGRRKCDQYWPKEgTETYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EHPEYTVRHLTIQHQQ--------ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetpeTAAN---SGPIVVHCSAGIG 341
Cdd:cd14549   80 VLATYTVRTFSLKNLKlkkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS----SAANppgAGPIVVHCSAGVG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380626 342 RTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14549  156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 166-395 3.66e-72

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: 226.58  E-value: 3.66e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 166 ASKDRYKTILPNPQSRVCL-GRAHSQEDSDYINANYIR------GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIV 238
Cdd:cd14544    2 KGKNRYKNILPFDHTRVILkDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 239 MLT-QLREGKEKCVHYWPTE--EEAYGPFqiRIQGMKEHP--EYTVRHLTIQ---HQQECRSVKHILFSAWPDHQTPESA 310
Cdd:cd14544   82 MTTkEVERGKNKCVRYWPDEgmQKQYGPY--RVQNVSEHDttDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 311 GPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQ 386
Cdd:cd14544  160 GGVLNFLEDVnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                 ....*....
gi 564380626 387 FLHHTLALY 395
Cdd:cd14544  240 FIYVAVAQY 248
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 161-394 4.31e-69

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: 218.22  E-value: 4.31e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 161 DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVML 240
Cdd:cd14614    8 DLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 241 TQLREGKE-KCVHYWPTEEE--AYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTP--ESAGPLLR 315
Cdd:cd14614   87 TQCNEKRRvKCDHYWPFTEEpvAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAESILQ 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 316 LVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLAL 394
Cdd:cd14614  167 FVQMVRQ-QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQL 244
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 195-390 1.79e-67

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: 212.88  E-value: 1.79e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA--YGPFQIRIQGM 271
Cdd:cd18533    1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEnGREKCDQYWPSGEYEgeYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 272 KEHPE--YTVRHLTIQH-QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFI 347
Cdd:cd18533   81 EENDDggFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKrELNDSASLDPPIIVHCSAGVGRTGTFI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564380626 348 A--------TRIGCQQLKARGEVD-ILGIVCQLRLDRGGMIQTAEQYQFLHH 390
Cdd:cd18533  161 AldslldelKRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 169-389 5.85e-65

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: 207.43  E-value: 5.85e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 247
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEaGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEEE--AYGPFQIRIQGMKEHPEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ET 322
Cdd:cd14619   80 VKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQveEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLrQW 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380626 323 PETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14619  160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 168-393 9.41e-65

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 207.76  E-value: 9.41e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGkEKVYIATQGPMPNTVADFWEMVWQEDVSLIVM-LTQLREG 246
Cdd:cd14603   33 KNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREIEMG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 KEKCVHYWPTEEE--AYGPFQI-RIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetP 323
Cdd:cd14603  112 KKKCERYWAQEQEplQTGPFTItLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELA--R 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380626 324 ETAANSG-PIVVHCSAGIGRTGCfIATRIGCQQL----KARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 393
Cdd:cd14603  190 RLQGSGPePLCVHCSAGCGRTGV-ICTVDYVRQLlltqRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 169-388 1.32e-64

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: 206.21  E-value: 1.32e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQEDsDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 247
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEqGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETP 323
Cdd:cd14615   79 TKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVrEYM 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380626 324 ETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14615  159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 169-389 3.39e-64

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: 205.15  E-value: 3.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 247
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEEEA--YGPFQIRIQGMKEHPEYTVRHLTI--QHQQEC-RSVKHILFSAWPDHQTPESAGPLLRLVAEVE- 321
Cdd:cd14617   80 VKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKIcsEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRd 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380626 322 ----TPetaaNSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14617  160 yinrTP----GSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 161-391 7.26e-64

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: 204.68  E-value: 7.26e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 161 DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVML 240
Cdd:cd14554    2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 241 TQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQ--HQQECRSVKHILFSAWPDHQTPESAGPLLRL 316
Cdd:cd14554   81 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380626 317 VAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 391
Cdd:cd14554  161 IGQVhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 195-387 1.66e-63

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 202.60  E-value: 1.66e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEK-VYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWP----TEEEAYGPFQIRI 268
Cdd:cd14538    1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEgGKVKCHRYWPdslnKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 269 QGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetpETAANSGPIVVHCSAGIGRTGCF 346
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYM---RRIHNSGPIVVHCSAGIGRTGVL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14538  158 ITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIF 198
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 163-392 6.39e-63

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: 203.34  E-value: 6.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 163 PGHASKDRYKTILPNPQSRVCLgRAHSQEDS---DYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVM 239
Cdd:cd17667   25 PDNKHKNRYINILAYDHSRVKL-RPLPGKDSkhsDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 240 LTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQH-------------QQECRSVKHILFSAWPDH 304
Cdd:cd17667  103 ITNLVEkGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkgRQNERTVIQYHYTQWPDM 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 305 QTPESAGPLLRLV---AEVETPETaansGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQT 381
Cdd:cd17667  183 GVPEYALPVLTFVrrsSAARTPEM----GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQT 258

                        250
                 ....*....|.
gi 564380626 382 AEQYQFLHHTL 392
Cdd:cd17667  259 EEQYIFIHDAL 269
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 158-392 1.69e-62

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: 202.57  E-value: 1.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 158 EDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLI 237
Cdd:cd14626   34 ENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 238 VMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPL 313
Cdd:cd14626  113 VMMTRLEEkSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQFQFMAWPDHGVPEYPTPI 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 314 LRLVAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14626  193 LAFLRRVKAC-NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 169-392 1.87e-61

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: 198.24  E-value: 1.87e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLT-QLREGK 247
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEEE--AYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ET 322
Cdd:cd14618   80 VLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEdlRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVrEH 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 323 PETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14618  160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 167-392 2.99e-61

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: 197.94  E-value: 2.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 167 SKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE- 245
Cdd:cd14630    5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEv 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 246 GKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-- 321
Cdd:cd14630   84 GRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKfl 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380626 322 TPETAansGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14630  164 NPPDA---GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 163-395 1.68e-60

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: 197.02  E-value: 1.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 163 PGHASKDRYKTILPNPQSRVCL-GRAHSQEDSDYINANYIR----GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLI 237
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILqGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 238 VMLT-QLREGKEKCVHYWPT--EEEAYGPFQIRIQGMKEHPEYTVRHL--TIQHQQEC-RSVKHILFSAWPDHQTPESAG 311
Cdd:cd14606   96 VMTTrEVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLqvSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 312 PLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14606  176 GVLSFLDQInQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKF 255


                 ....*...
gi 564380626 388 LHHTLALY 395
Cdd:cd14606  256 IYVAIAQF 263
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 195-389 3.35e-60

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: 193.98  E-value: 3.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEAYGPFQIRIQGMKE 273
Cdd:cd14555    1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvGRVKCSRYWPDDTEVYGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRI 351
Cdd:cd14555   80 LAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA-SNPPSAGPIVVHCSAGAGRTGCYIVIDI 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380626 352 GCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14555  159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 168-399 3.90e-60

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: 197.08  E-value: 3.90e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 246
Cdd:cd14604   60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEmG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 KEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVA---EV 320
Cdd:cd14604  139 RKKCERYWPLYGEEpmtFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISlmrKY 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 321 ETPETAansgPIVVHCSAGIGRTGCFIATRIGCQQLKA---RGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA-LYA 396
Cdd:cd14604  219 QEHEDV----PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqLFE 294


                 ...
gi 564380626 397 AQL 399
Cdd:cd14604  295 KQL 297
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 195-389 7.18e-60

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: 193.12  E-value: 7.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG-KEKCVHYWPTEEE---AYGPFQIRIQG 270
Cdd:cd14557    1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGnRNKCAQYWPSMEEgsrAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 271 MKEHPEYTVRHLTIQHQQECRS---VKHILFSAWPDHQTPESAGPLLRLVAEVETPETAAnSGPIVVHCSAGIGRTGCFI 347
Cdd:cd14557   80 EKICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF-SGPIVVHCSAGVGRTGTYI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380626 348 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 195-389 1.56e-59

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: 192.22  E-value: 1.56e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGkEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG-KEKCVHYWPTEEEAYGPFQIRIQGMKE 273
Cdd:cd14558    1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGdQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-----ETPETAANSGPIVVHCSAGIGRTGCF 346
Cdd:cd14558   80 SPTYTVRVFEITHLKrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpYKNSKHGRSVPIVVHCSDGSSRTGIF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14558  160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 194-387 3.50e-59

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: 191.77  E-value: 3.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 194 DYINANY----IRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA--YGPFQI 266
Cdd:cd14541    1 DYINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErGRVKCHQYWPDLGETmqFGNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 267 RIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSgPIVVHCSAGIGRTG 344
Cdd:cd14541   80 TCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 345 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14541  159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 143-387 4.22e-58

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: 191.48  E-value: 4.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 143 LEEEFLKIPSNFVNPEDL---DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMP 219
Cdd:cd14628   27 MELEFKRLASSKAHTSRFisaNLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 220 NTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKH 295
Cdd:cd14628  106 ETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 296 ILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 374
Cdd:cd14628  186 FQFTDWPEQGVPKSGEGFIDFIGQVhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 265

                        250
                 ....*....|...
gi 564380626 375 RGGMIQTAEQYQF 387
Cdd:cd14628  266 RPAMVQTEDQYQF 278
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 195-392 5.58e-58

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: 188.65  E-value: 5.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMK 272
Cdd:cd17668    1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEkGRRKCDQYWPADgSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EHPEYTVRHLTIQH----------QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANsGPIVVHCSAGIGR 342
Cdd:cd17668   80 VLAYYTVRNFTLRNtkikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAV-GPVVVHCSAGVGR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380626 343 TGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd17668  159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 168-389 2.00e-57

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: 187.74  E-value: 2.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 246
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 KEKCVHYW--PTEEE-AYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETP 323
Cdd:cd14602   80 KKKCERYWaePGEMQlEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 324 EtAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKAR---GEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14602  160 Q-EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 161-395 2.96e-57

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: 189.56  E-value: 2.96e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 161 DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVML 240
Cdd:cd14627   49 NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 241 TQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRL 316
Cdd:cd14627  128 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 317 VAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 395
Cdd:cd14627  208 IGQVhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 195-389 7.93e-57

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: 185.25  E-value: 7.93e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEAYGPFQIRIQGMKE 273
Cdd:cd14632    1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTIQHQQEC--RSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRI 351
Cdd:cd14632   80 LAEYSVRTFALERRGYSarHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA-STPPDAGPVVVHCSAGAGRTGCYIVLDV 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380626 352 GCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14632  159 MLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 167-395 8.46e-57

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: 186.76  E-value: 8.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 167 SKDRYKTILPNPQSRVCLGRAHSQED-SDYINANYI-------RGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIV 238
Cdd:cd14605    4 NKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 239 MLT-QLREGKEKCVHYWPTEE--EAYGpfQIRIQGMKEHP--EYTVRHLTI----QHQQEcRSVKHILFSAWPDHQTPES 309
Cdd:cd14605   84 MTTkEVERGKSKCVKYWPDEYalKEYG--VMRVRNVKESAahDYILRELKLskvgQGNTE-RTVWQYHFRTWPDHGVPSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 310 AGPLLRLVAEVE-TPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQY 385
Cdd:cd14605  161 PGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240

                        250
                 ....*....|
gi 564380626 386 QFLHHTLALY 395
Cdd:cd14605  241 RFIYMAVQHY 250
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 195-387 1.29e-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: 184.78  E-value: 1.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE-AYGPFQIRIQGMK 272
Cdd:cd14552    1 YINASFIDGYRQKDA-YIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErSQNKCAQYWPEDGSvSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EHPEYTVR--HLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIATR 350
Cdd:cd14552   80 DYEDYTLRdfLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380626 351 IGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14552  160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 181-392 1.32e-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: 185.22  E-value: 1.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 181 RVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE 259
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvGRVKCYKYWPDDTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 260 AYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCS 337
Cdd:cd14631   80 VYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKL-SNPPSAGPIVVHCS 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380626 338 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14631  159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 168-392 1.74e-56

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: 186.79  E-value: 1.74e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 246
Cdd:cd14633   43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 KEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpE 324
Cdd:cd14633  122 RVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-K 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380626 325 TAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14633  201 SPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 168-395 2.01e-56

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: 185.42  E-value: 2.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGrahsqEDSDYINANYIRGYDGKEK-VYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG 246
Cdd:cd14597    6 KNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 -KEKCVHYWPteeEAYGP-------FQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRL 316
Cdd:cd14597   81 gKIKCQRYWP---EILGKttmvdnrLQLTLVRMQQLKNFVIRVLELEDIQtrEVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 317 VAEVetpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLaLY 395
Cdd:cd14597  158 ISYM---RHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI-LY 232
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 142-392 2.67e-56

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: 186.45  E-value: 2.67e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 142 QLEEEFLKI-PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPN 220
Cdd:cd14625   23 KLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 221 TVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHI 296
Cdd:cd14625  102 TFGDFWRMVWEQRSATVVMMTKLEEkSRIKCDQYWPSRgTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 297 LFSAWPDHQTPESAGPLLRLVAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRG 376
Cdd:cd14625  182 QFTAWPDHGVPEYPTPFLAFLRRVKTC-NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRN 260

                        250
                 ....*....|....*.
gi 564380626 377 GMIQTAEQYQFLHHTL 392
Cdd:cd14625  261 YMVQTEDQYSFIHDAL 276
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 171-392 3.45e-56

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: 184.37  E-value: 3.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 171 YKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKE-K 249
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEeK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 250 CVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQHQ-----QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETP 323
Cdd:cd14620   80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 324 eTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14620  160 -NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 169-389 1.38e-55

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: 182.80  E-value: 1.38e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 247
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEEEAYGPF-QIRIQGMKE--HPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPE 324
Cdd:cd14616   80 IRCHQYWPEDNKPVTVFgDIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380626 325 TAANSgPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14616  160 AHDNT-PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 195-390 1.42e-55

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: 181.85  E-value: 1.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGkEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE---AYGPFQIRIQG 270
Cdd:cd14542    1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEmGKKKCERYWPEEGEeqlQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 271 MKE-HPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPEtAANSGPIVVHCSAGIGRTGCFIAT 349
Cdd:cd14542   80 EKRvGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGRTGTICAI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380626 350 RIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFLHH 390
Cdd:cd14542  159 DYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 168-392 1.78e-54

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: 181.85  E-value: 1.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 246
Cdd:cd14624   50 KNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEErS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 247 KEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETP 323
Cdd:cd14624  129 RVKCDQYWPSRgTETYGLIQVTLLDTVELATYCVRTFALYKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 324 eTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14624  209 -NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 168-387 2.63e-54

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: 179.51  E-value: 2.63e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 168 KDRYKTILPNPQSRVclgRAHS-QEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE- 245
Cdd:cd14545    1 LNRYRDRDPYDHDRS---RVKLkQGDNDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEk 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 246 GKEKCVHYWPTEEEA-----YGPFQIRIQGMKEHPEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLVA 318
Cdd:cd14545   77 GQIKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELENlkTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380626 319 EV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG--EVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14545  157 KVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 133-395 2.99e-54

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: 181.46  E-value: 2.99e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 133 LQHQPP--SPKQLEEEFLKIPSNFVNPEDL---DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgK 207
Cdd:cd14629   16 LTQVPPgeSVTAMELEFKLLANSKAHTSRFisaNLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYR-Q 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 208 EKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQ 285
Cdd:cd14629   95 QKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 286 HQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEV 362
Cdd:cd14629  175 DARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVV 254

                        250       260       270
                 ....*....|....*....|....*....|...
gi 564380626 363 DILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 395
Cdd:cd14629  255 DMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 195-396 1.03e-52

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: 174.95  E-value: 1.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIR-GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-----EEAYGPFQIR 267
Cdd:cd14540    1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLggehdALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 268 IQGMKEHPEYTVRHLTIQHQQEC--RSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSG--------PIVVHCS 337
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGqsRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDvaghnrnpPTLVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 338 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYA 396
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 152-387 4.26e-52

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: 175.63  E-value: 4.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 152 SNFVNPEDLDIPghasKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQ 231
Cdd:cd14610   35 ATNVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 232 EDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIqgMKEH---PEYTVRHLTIQHQQ--ECRSVKHILFSAWPDH 304
Cdd:cd14610  111 SGCVVIVMLTPLAEnGVKQCYHYWPDEgSNLYHIYEVNL--VSEHiwcEDFLVRSFYLKNLQtnETRTVTQFHFLSWNDQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 305 QTPESAGPLLRLVAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAE 383
Cdd:cd14610  189 GVPASTRSLLDFRRKVNKC-YRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKE 267


                 ....
gi 564380626 384 QYQF 387
Cdd:cd14610  268 QFEF 271
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 195-389 5.51e-52

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: 172.59  E-value: 5.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEA-YGPFQIRIQGMKE 273
Cdd:cd14556    1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGtYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTIQH----QQECRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIA 348
Cdd:cd14556   80 DEDVISRIFRLQNttrpQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFCA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564380626 349 TRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14556  160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 142-388 6.36e-52

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: 175.04  E-value: 6.36e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 142 QLEEEFLKIPSNFVN----PEDLDipghasKDRYKTILPNPQSRVCLgrahsQEDSDYINANY----IRGYDGKEKvYIA 213
Cdd:cd14600   19 QFEQLYRKKPGLAITcaklPQNMD------KNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNK-YIA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 214 TQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA--YGPFQIRIQGMKEHPEYTVRHLTIQHQQ-- 288
Cdd:cd14600   87 TQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTErGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQtg 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 289 ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAanSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIV 368
Cdd:cd14600  167 EERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVE--NEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIV 244

                        250       260
                 ....*....|....*....|
gi 564380626 369 CQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14600  245 RKMRDQRAMMVQTSSQYKFV 264
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 170-389 8.92e-52

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: 172.92  E-value: 8.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 170 RYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKE 248
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDS-YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErGQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 249 KCVHYWPTEEE-AYGPFQIRIQGMKEHPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPET 325
Cdd:cd14623   80 KCAQYWPSDGSvSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564380626 326 AANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14623  160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 195-389 1.10e-51

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: 172.02  E-value: 1.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMK 272
Cdd:cd14551    1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EHPEYTVRHLTIQHQ------QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAaNSGPIVVHCSAGIGRTGCF 346
Cdd:cd14551   80 VLVDYTTRKFCIQKVnrgigeKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPP-RAGPIVVHCSAGVGRTGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14551  159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 195-387 1.15e-51

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: 171.85  E-value: 1.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEK-VYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPteEEAYGP-----FQIR 267
Cdd:cd14596    1 YINASYITMPVGEEElFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErGKVKCHRYWP--ETLQEPmelenYQLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 268 IQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetpETAANSGPIVVHCSAGIGRTGC 345
Cdd:cd14596   79 LENYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYM---RKVHNTGPIVVHCSAGIGRAGV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380626 346 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14596  156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLF 197
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 141-392 1.35e-51

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: 174.83  E-value: 1.35e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 141 KQLEEEFLKIPSNFVNP--EDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPM 218
Cdd:cd14621   26 KLFREEFNALPACPIQAtcEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNK-FIAAQGPK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 219 PNTVADFWEMVWQEDVSLIVMLTQLREGKE-KCVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQH------QQEC 290
Cdd:cd14621  105 EETVNDFWRMIWEQNTATIVMVTNLKERKEcKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvtnKKPQ 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 291 RSVKHILFSAWPDHQTPESAGPLLRLVAEVET--PETAansGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIV 368
Cdd:cd14621  185 RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNcnPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261

                        250       260
                 ....*....|....*....|....
gi 564380626 369 CQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14621  262 SRIRAQRCQMVQTDMQYVFIYQAL 285
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 162-387 1.66e-51

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: 174.06  E-value: 1.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 162 IPGHASKDRYKTILPNPQSRVCLgrahSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLT 241
Cdd:cd14608   22 LPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 242 QLRE-GKEKCVHYWPTEEEAYGPFQ---IRIQGMKEHPE--YTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPL 313
Cdd:cd14608   97 RVMEkGSLKCAQYWPQKEEKEMIFEdtnLKLTLISEDIKsyYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASF 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380626 314 LRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIgC----QQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14608  177 LNFLFKVrESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 254
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 194-389 6.80e-50

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 167.49  E-value: 6.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 194 DYINANYIRGYDGKEkVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE-AYGPFQIRIQGM 271
Cdd:cd14622    1 DYINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQErEQEKCVQYWPSEGSvTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 272 KEHPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIAT 349
Cdd:cd14622   80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564380626 350 RIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14622  160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 194-388 5.02e-49

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: 165.50  E-value: 5.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 194 DYINANYIR---GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVML-TQLREGKEKCVHYWP--TEEEAYGPFQIR 267
Cdd:cd14601    1 DYINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPepSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 268 IQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGC 345
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEknESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN-KRAGKDEPVVVHCSAGIGRTGV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 346 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14601  160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 195-389 8.52e-49

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: 164.48  E-value: 8.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVML-TQLREGKEKCVHYWPTE---EEAYGPFQIRIQG 270
Cdd:cd14539    1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 271 MKEHPEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANS--GPIVVHCSAGIGRTGCF 346
Cdd:cd14539   81 VRTTPTHVERIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqTPIVVHCSSGVGRTGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380626 347 IATRIGCQQLKA-RGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14539  161 CLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 195-387 3.20e-48

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: 163.00  E-value: 3.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIqgMK 272
Cdd:cd14546    1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEnGVKQCARYWPEEgSEVYHIYEVHL--VS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EH---PEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETaANSGPIVVHCSAGIGRTGCFI 347
Cdd:cd14546   79 EHiwcDDYLVRSFYLKNLQtsETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYR-GRSCPIVVHCSDGAGRTGTYI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564380626 348 ATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14546  158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEF 198
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 141-392 1.22e-45

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: 159.01  E-value: 1.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 141 KQLEE-----EFLKIPSNFVNP--EDLDIPGHASKDRYKTILPNPQSRVCLgRAHSQEDSDYINANYIR-GYDGKEKVYI 212
Cdd:cd14599    7 RKLEEgmvftEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKvTVGGEEWHYI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 213 ATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPT-----EEEAYGPFQIRIQGMKEHPEYTVRHLTIQH 286
Cdd:cd14599   86 ATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEgGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 287 ---QQEcRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSG---------PIVVHCSAGIGRTGCFIATR--IG 352
Cdd:cd14599  166 llsGQE-RTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMldstkncnpPIVVHCSAGVGRTGVVILTElmIG 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 564380626 353 CqqLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14599  245 C--LEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 195-387 3.54e-45

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: 154.93  E-value: 3.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYD-GKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG--KEKCVHYWPTEE---EAYGPFQIRI 268
Cdd:cd17658    1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNysTAKCADYFPAEEnesREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 269 QGMKeHPEY--TVRHLTIQ---HQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVET-PETAansGPIVVHCSAGIGR 342
Cdd:cd17658   81 KKLK-HSQHsiTLRVLEVQyieSEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGiPPSA---GPIVVHCSAGIGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380626 343 TGCFIAT-----RIGCQQLKArgeVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd17658  157 TGAYCTIhntirRILEGDMSA---VDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 164-387 1.78e-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: 155.58  E-value: 1.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 164 GHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQL 243
Cdd:cd14609   41 ANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 244 RE-GKEKCVHYWPTEEEA-YGPFQIRIqgMKEH---PEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRL 316
Cdd:cd14609  121 VEdGVKQCDRYWPDEGSSlYHIYEVNL--VSEHiwcEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGIPSSTRPLLDF 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380626 317 VAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14609  199 RRKVNKC-YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 163-387 6.91e-44

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: 153.20  E-value: 6.91e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 163 PGHASKDRYKTILPNPQSRVCLGRAhsqeDSDYINANYIRgYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQ 242
Cdd:cd14607   22 PENRNRNRYRDVSPYDHSRVKLQNT----ENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 243 LRE-GKEKCVHYWPTEEEAYGPFQ---IRIQGMKEHPE--YTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLL 314
Cdd:cd14607   97 IVEkDSVKCAQYWPTDEEEVLSFKetgFSVKLLSEDVKsyYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPASFL 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380626 315 RLVAEV-ETPETAANSGPIVVHCSAGIGRTGCF--IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14607  177 NFLFKVrESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRF 252
PHA02738 PHA02738
hypothetical protein; Provisional
 169-395 6.88e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.77  E-value: 6.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 169 DRYKTILPNPQSRVCLGRAHSQedSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 247
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 248 EKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQEC-RSVKHILFSAWPDHQTPESAGPLLRLVAEVET- 322
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQc 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 323 -PETAANS----------GPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 391
Cdd:PHA02738 210 qKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 564380626 392 LALY 395
Cdd:PHA02738 290 VKRY 293
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 195-392 1.18e-42

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: 148.97  E-value: 1.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIR-GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWP-----TEEEAYGPFQIR 267
Cdd:cd14598    1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEgGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 268 IQGMKEHPEYTVRHLTIQH---QQEcRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSG--------PIVVHC 336
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHlltGQE-RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTidpkspnpPVLVHC 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380626 337 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd14598  160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
141-388 1.64e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 150.63  E-value: 1.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 141 KQLEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVclgrahsQEDSDYINANYIRGYDGKekVYIATQGPMPN 220
Cdd:COG5599   18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 221 TVADFWEMVWQEDVSLIVMLTQLREGKE---KCVHYWPTEEEaYGPFQIRI-----QGMKEHPEYTVRHLTIQHQ-QECR 291
Cdd:COG5599   89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSSeltesIQLRDGIEARTYVLTIKGTgQKKI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 292 SVKHILFSAWPDHQ--TPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDILGI 367
Cdd:COG5599  168 EIPVLHVKNWPDHGaiSAEALKNLADLIDKKEK-IKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEI 246

                        250       260
                 ....*....|....*....|..
gi 564380626 368 VCQLRLDRG-GMIQTAEQYQFL 388
Cdd:COG5599  247 VIDMRTSRNgGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 131-389 4.65e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 147.46  E-value: 4.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 131 WTLQHQPPSPKQLEEEFLKIPSNFVNP--EDLDIPGHASKDRYKTILPNPQSRVCLgRAHSQEDSDYINANYIRGYDgKE 208
Cdd:PHA02747  15 LKRRNQLNCFGIIRDEHHQIILKPFDGliANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFE-DD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 209 KVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLR--EGKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEY--TVRH 281
Cdd:PHA02747  93 KKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKgtNGEEKCYQYWCLNEDGnidMEDFRIETLKTSVRAKYilTLIE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 282 LTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVE----------TPETAANSgPIVVHCSAGIGRTGCFIATRI 351
Cdd:PHA02747 173 ITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDinrkksgklfNPKDALLC-PIVVHCSDGVGKTGIFCAVDI 251

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564380626 352 GCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:PHA02747 252 CLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 146-392 4.43e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 142.48  E-value: 4.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 146 EFLKIP-----SNFVNPEDLdipghaSKDRYKTILPNPQSRVCLGRAHS-----------------QEDSD--YINANYI 201
Cdd:PHA02746  33 EVMDIPirgttNHFLKKENL------KKNRFHDIPCWDHSRVVINAHESlkmfdvgdsdgkkievtSEDNAenYIHANFV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 202 RGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEE---AYGPFQIRIQGMKEHPEYT 278
Cdd:PHA02746 107 DGFKEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 279 VRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-----ETPETAANS----GPIVVHCSAGIGRTGCFI 347
Cdd:PHA02746 186 KTRLMITDKisDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVneeqaELIKQADNDpqtlGPIVVHCSAGIGRAGTFC 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564380626 348 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:PHA02746 266 AIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 193-396 9.20e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 138.60  E-value: 9.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 193 SDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRI 268
Cdd:PHA02742  78 DDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEdGKEACYPYWMPHERGkatHGEFKIKT 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 269 QGMKEHPEYTVRHLTIQHQQECRS--VKHILFSAWPDHQTPESAGPLLRLVAEVETPETAA---NSG-------PIVVHC 336
Cdd:PHA02742 157 KKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdIKGenivkepPILVHC 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 337 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYA 396
Cdd:PHA02742 237 SAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFA 296
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
292-393 4.00e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.86  E-value: 4.00e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   292 SVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 369
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVkKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 564380626   370 QLRLDRGGMIQTAEQYQFLHHTLA 393
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 292-393 4.00e-36

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: 127.86  E-value: 4.00e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626   292 SVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 369
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVkKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 564380626   370 QLRLDRGGMIQTAEQYQFLHHTLA 393
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 195-388 5.03e-34

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 125.51  E-value: 5.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEEEA--YGPFQIRIQGMK 272
Cdd:cd14550    1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPleCETFKVTLSGED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EHP-----EYTVRHLTIQHQQECR--SVKHILFSAWPDHQTP-ESAGPLLRLVAEvetpETAANSGPIVVH-----CSAG 339
Cdd:cd14550   79 HSClsneiRLIVRDFILESTQDDYvlEVRQFQCPSWPNPCSPiHTVFELINTVQE----WAQQRDGPIVVHdryggVQAA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380626 340 igrTGCFIATRigCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14550  155 ---TFCALTTL--HQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 195-389 9.99e-32

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: 119.74  E-value: 9.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEEE-AYGPFQIRIQGMKE 273
Cdd:cd14634    1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKTScCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTI----QHQQECRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVET--PETAANSGPIVVHCSAGIGRTGCF 346
Cdd:cd14634   79 DEDIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKwqEQYDGREGRTVVHCLNGGGRSGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14634  159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 195-387 2.48e-27

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: 107.69  E-value: 2.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEK--CVHYWPTE-EEAYGPFQIRIQGM 271
Cdd:cd14637    1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 272 KEHPEYTVRHLTIQH----QQECRSVKHILFSAW-PDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCF 346
Cdd:cd14637   80 SADEDIVTRLFRVQNitrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 387
Cdd:cd14637  160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRF 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 195-389 2.60e-26

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: 105.11  E-value: 2.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEEE-AYGPFQIRIQGMKE 273
Cdd:cd14636    1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMlRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTI----QHQQECRSVKHILFSAWPDH-QTPESAGPLLRLVAEVET--PETAANSGPIVVHCSAGIGRTGCF 346
Cdd:cd14636   79 DCDVISRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqEECDEGEGRTIIHCLNGGGRSGMF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14636  159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 195-392 1.23e-25

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: 103.15  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKE- 273
Cdd:cd17669    1 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 ------HPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTPESAG-PLLRLVAEvetpETAANSGPIVVHCSAGIGRTG 344
Cdd:cd17669   80 hkclsnEEKLIIQDFILEATQDdyVLEVRHFQCPKWPNPDSPISKTfELISIIKE----EAANRDGPMIVHDEHGGVTAG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380626 345 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd17669  156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 195-392 6.15e-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: 101.29  E-value: 6.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYG--PFQIRIQG-- 270
Cdd:cd17670    1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNceAFTVTLISkd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 271 ---MKEHPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTP-ESAGPLLRLVAEvetpETAANSGPIVVHCSAGIGRTG 344
Cdd:cd17670   80 rlcLSNEEQIIIHDFILEATQDdyVLEVRHFQCPKWPNPDAPiSSTFELINVIKE----EALTRDGPTIVHDEFGAVSAG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380626 345 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 392
Cdd:cd17670  156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 195-389 2.17e-24

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: 99.76  E-value: 2.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 195 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEE-EAYGPFQIRIQGMKE 273
Cdd:cd14635    1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 274 HPEYTVRHLTIQH----QQECRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVET--PETAANSGPIVVHCSAGIGRTGCF 346
Cdd:cd14635   79 EEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKwqEEYNGGEGRTVVHCLNGGGRSGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380626 347 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14635  159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 178-395 9.23e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.79  E-value: 9.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 178 PQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREgKEKCVHYWPTE 257
Cdd:PHA02740  61 HITRLLHRRIKLFNDEKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD-KKCFNQFWSLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 258 E---EAYGPFQIRIQGM--KEHPEYTVRHLTIQHQQEcRSVKHILFSAWPDHQTPESAGPLL-------RLVAEVETPET 325
Cdd:PHA02740 139 EgcvITSDKFQIETLEIiiKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDAFIdffcnidDLCADLEKHKA 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 326 AANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 395
Cdd:PHA02740 218 DGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 196-388 1.51e-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: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 196 INANYIRgyDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQI---RIQGMK 272
Cdd:cd14559   18 LNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGTYGSVTVkskKTGKDE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 273 EHPEYTVRH--LTIQHQQECRSVKHILFSAWPDHqTPESAGPLLRLVAEVE-------TPETAANSGPI--------VVH 335
Cdd:cd14559   96 LVDGLKADMynLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKELADLVNksaeekrNFYKSKGSSAIndknkllpVIH 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564380626 336 CSAGIGRTGCFIATRigcQQLKARGEVDILGIVCQLRLDRGG-MIQTAEQYQFL 388
Cdd:cd14559  175 CRAGVGRTGQLAAAM---ELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 314-390 8.36e-13

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: 64.29  E-value: 8.36e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380626 314 LRLVAEVETPEtaansGPIVVHCSAGIGRTGCFIATRIGCQQLKargevDILGIVCQLRLDRGGMI-QTAEQYQFLHH 390
Cdd:cd14494   46 LEVLDQAEKPG-----EPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
301-390 2.39e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.58  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 301 WPDHQTPESAgPLLRLVAEVEtpETAANSGPIVVHCSAGIGRTGCFIAtrigcQQLKARGeVDILGIVCQLRLDRGGMIQ 380
Cdd:COG2453   55 IPDFGAPDDE-QLQEAVDFID--EALREGKKVLVHCRGGIGRTGTVAA-----AYLVLLG-LSAEEALARVRAARPGAVE 125

                         90
                 ....*....|
gi 564380626 381 TAEQYQFLHH 390
Cdd:COG2453  126 TPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 332-389 3.71e-07

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: 49.57  E-value: 3.71e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564380626 332 IVVHCSAGIGRTGcFIATRIgCQQLKARGEVDilGIVCQLRLDRGGMIQTAEQYQFLH 389
Cdd:cd14505  109 VLIHCKGGLGRTG-LIAACL-LLELGDTLDPE--QAIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 286-388 1.07e-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: 44.96  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 286 HQQECRSVKHILFSAwPDHqTPESAGPLLRLVAEVEtpETAANSGPIVVHCSAGIGRTGCFIAtrigCQQLKARGEVDIL 365
Cdd:cd14504   43 HSDTCPGLRYHHIPI-EDY-TPPTLEQIDEFLDIVE--EANAKNEAVLVHCLAGKGRTGTMLA----CYLVKTGKISAVD 114

                         90       100
                 ....*....|....*....|...
gi 564380626 366 GIVcQLRLDRGGMIQTAEQYQFL 388
Cdd:cd14504  115 AIN-EIRRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 300-389 3.49e-04

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: 41.57  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 300 AWPDHQTPeSAGPLLRLVAEVETpeTAANSGPIVVHCSAGIGRTGCFIA------TRIGCQQLkargevdILGIvcqlRL 373
Cdd:cd14506   83 GWKDYGVP-SLTTILDIVKVMAF--ALQEGGKVAVHCHAGLGRTGVLIAcylvyaLRMSADQA-------IRLV----RS 148

                         90
                 ....*....|....*.
gi 564380626 374 DRGGMIQTAEQYQFLH 389
Cdd:cd14506  149 KRPNSIQTRGQVLCVR 164
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 330-348 5.95e-04

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: 40.51  E-value: 5.95e-04
                         10
                 ....*....|....*....
gi 564380626 330 GPIVVHCSAGIGRTGCFIA 348
Cdd:cd14499  110 GAIAVHCKAGLGRTGTLIA 128
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 301-348 8.87e-04

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: 39.49  E-value: 8.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380626 301 WPDHQTPesagPLLRLVAEVETPETAANSGP---IVVHCSAGIGRTGCFIA 348
Cdd:cd14497   68 FPDHHPP----PLGLLLEIVDDIDSWLSEDPnnvAVVHCKAGKGRTGTVIC 114
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 295-348 6.09e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 37.35  E-value: 6.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380626 295 HILFSAW-PDHQTPESAgplLRLVAevetpeTAANSGPIVVHCSAGIGRTGCFIA 348
Cdd:cd14529   63 NLPLSATrPTESDVQSF---LLIMD------LKLAPGPVLIHCKHGKDRTGLVSA 108
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 267-349 6.94e-03

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 37.23  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380626 267 RIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPesagPLLRLVAEVETPETAANSGP---IVVHCSAGIGRT 343
Cdd:cd14561   32 RMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAP----PLDKMCTICKAMESWLNSDPlhvVVIHCRGGKGRI 107


                 ....*.
gi 564380626 344 GCFIAT 349
Cdd:cd14561  108 GVVISS 113
 
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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