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Conserved domains on  [gi|1444494498|ref|XP_025923483|]
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tyrosine-protein phosphatase non-receptor type 12 isoform X2 [Apteryx rowi]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1-179 1.05e-148

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.


The actual alignment was detected with superfamily member cd14604:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 297  Bit Score: 433.20  E-value: 1.05e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14604   199 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1444494498 161 KEQYELVHRAIAQLFEKQL 179
Cdd:cd14604   279 KEQYELVHRAIAQLFEKQL 297
rad2 super family cl36701
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 330-584 2.37e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00600:

Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 41.42  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  330 EGNSLLNRGHAIKIK--PVSSCVTDKSFKPQEQISG----DSFVDASQNSCMECSVPQSNTALIPSPeslqsQQVPDtpp 403
Cdd:TIGR00600  438 DDLDYLDQGEGIPLMaaLQLSSVNSKPEAVASTKIArevtSSGHEAVPKAVQSLLLGATNDSPIPSE-----FTILD--- 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  404 RPDRLPLIEKGQAMWSLHGPENalrtsvSEDTSSDILRQGVKTVSLVSNN--------------TVELPSSDKVDHSTIA 469
Cdd:TIGR00600  510 RKSELSIERTVKPVSSEFGLPS------QREDKLAIPTEGTQNLQGISDHpeqfefqnelspleTKNNESNLSSDAETEG 583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  470 VRAPLCFTNPLHSDDSDTDDI-------NFDGAMTKSPSNISTASATVSAATNTENIsARKVLPMSIARQDLTAvtcseD 542
Cdd:TIGR00600  584 SPNPEMPSWSSVTVPSEALDNyettnpsNAKEVRNFAETGIQTTNVGESADLLLISN-PMEVEPMESEKEESES-----D 657

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1444494498  543 GKDAD------TSEDSSPPLPERTPESfvlatEQNSplPKPVTIAQSE 584
Cdd:TIGR00600  658 GSFIEvdsvssTLELQVPSKSQPTDES-----EENA--ENKVASIEGE 698
 
Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1-179 1.05e-148

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: 433.20  E-value: 1.05e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14604   199 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1444494498 161 KEQYELVHRAIAQLFEKQL 179
Cdd:cd14604   279 KEQYELVHRAIAQLFEKQL 297
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1-173 2.45e-74

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 239.87  E-value: 2.45e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498    1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEF--QNETRSVYQFHYVNW 78
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 158
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMV 244

                          170
                   ....*....|....*
gi 1444494498  159 QTKEQYELVHRAIAQ 173
Cdd:smart00194 245 QTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1-173 1.98e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 231.36  E-value: 1.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQART-DYFIRTLLLEF--QNETRSVYQFHYVN 77
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHS 156
Cdd:pfam00102 141 WPDHGVPESPNSLLDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPG 217

                         170
                  ....*....|....*..
gi 1444494498 157 AVQTKEQYELVHRAIAQ 173
Cdd:pfam00102 218 MVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1-173 2.66e-24

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 103.25  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVM--ACREFEMGRKKCERYWPLYGEsavtFGPFHVSCE---AEQARTDYFIRTLLLEFQN---ETRSVYQ 72
Cdd:COG5599    96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  73 FHYVNWPDHDVPSSfDSILDMISLMREYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQE 149
Cdd:COG5599   172 LHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVID 249

                         170       180
                  ....*....|....*....|....*.
gi 1444494498 150 MRTQR-HSAVQTKEQY-ELVHRAIAQ 173
Cdd:COG5599   250 MRTSRnGGMVQTSEQLdVLVKLAEQQ 275
PHA02738 PHA02738
hypothetical protein; Provisional
 1-171 2.20e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 98.46  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNE-TRSVYQFHYVNWP 79
Cdd:PHA02738  109 MLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFTAWP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  80 DHDVPSSFDSILDMISLMREYQE--HEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNL 146
Cdd:PHA02738  189 DHDVPKNTSEFLNFVLEVRQCQKelAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT---VSIPSI 265

                         170       180
                  ....*....|....*....|....*
gi 1444494498 147 IQEMRTQRHSAVQTKEQYELVHRAI 171
Cdd:PHA02738  266 VSSIRNQRYYSLFIPFQYFFCYRAV 290
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 330-584 2.37e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 41.42  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  330 EGNSLLNRGHAIKIK--PVSSCVTDKSFKPQEQISG----DSFVDASQNSCMECSVPQSNTALIPSPeslqsQQVPDtpp 403
Cdd:TIGR00600  438 DDLDYLDQGEGIPLMaaLQLSSVNSKPEAVASTKIArevtSSGHEAVPKAVQSLLLGATNDSPIPSE-----FTILD--- 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  404 RPDRLPLIEKGQAMWSLHGPENalrtsvSEDTSSDILRQGVKTVSLVSNN--------------TVELPSSDKVDHSTIA 469
Cdd:TIGR00600  510 RKSELSIERTVKPVSSEFGLPS------QREDKLAIPTEGTQNLQGISDHpeqfefqnelspleTKNNESNLSSDAETEG 583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  470 VRAPLCFTNPLHSDDSDTDDI-------NFDGAMTKSPSNISTASATVSAATNTENIsARKVLPMSIARQDLTAvtcseD 542
Cdd:TIGR00600  584 SPNPEMPSWSSVTVPSEALDNyettnpsNAKEVRNFAETGIQTTNVGESADLLLISN-PMEVEPMESEKEESES-----D 657

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1444494498  543 GKDAD------TSEDSSPPLPERTPESfvlatEQNSplPKPVTIAQSE 584
Cdd:TIGR00600  658 GSFIEvdsvssTLELQVPSKSQPTDES-----EENA--ENKVASIEGE 698
 
Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1-179 1.05e-148

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: 433.20  E-value: 1.05e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14604   199 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1444494498 161 KEQYELVHRAIAQLFEKQL 179
Cdd:cd14604   279 KEQYELVHRAIAQLFEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1-169 4.77e-116

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: 345.56  E-value: 4.77e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQART-DYFIRTLLLEFQNETRSVYQFHYVNWP 79
Cdd:cd14542    33 MIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKEKRVGpDFLIRTLKVTFQKESRTVYQFHYTAWP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  80 DHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQ 159
Cdd:cd14542   113 DHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQ 192

                         170
                  ....*....|
gi 1444494498 160 TKEQYELVHR 169
Cdd:cd14542   193 TKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1-175 1.65e-104

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: 317.17  E-value: 1.65e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14602    60 MIWEYSVLIIVMACMEFEMGKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14602   140 HDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQT 219

                         170
                  ....*....|....*
gi 1444494498 161 KEQYELVHRAIAQLF 175
Cdd:cd14602   220 KEQYELVYNAVIELF 234
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1-175 2.82e-83

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: 263.61  E-value: 2.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAvTFGPFHVS-CEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWP 79
Cdd:cd14603    92 MIWQYGVKVILMACREIEMGKKKCERYWAQEQEPL-QTGPFTITlVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  80 DHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQ 159
Cdd:cd14603   171 DHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQ 250

                         170
                  ....*....|....*.
gi 1444494498 160 TKEQYELVHRAIAQLF 175
Cdd:cd14603   251 TEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1-173 2.45e-74

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 239.87  E-value: 2.45e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498    1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEF--QNETRSVYQFHYVNW 78
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 158
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMV 244

                          170
                   ....*....|....*
gi 1444494498  159 QTKEQYELVHRAIAQ 173
Cdd:smart00194 245 QTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1-173 1.98e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 231.36  E-value: 1.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQART-DYFIRTLLLEF--QNETRSVYQFHYVN 77
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHS 156
Cdd:pfam00102 141 WPDHGVPESPNSLLDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPG 217

                         170
                  ....*....|....*..
gi 1444494498 157 AVQTKEQYELVHRAIAQ 173
Cdd:pfam00102 218 MVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1-169 5.15e-67

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: 218.31  E-value: 5.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQN--ETRSVYQFHYVNW 78
Cdd:cd00047    33 MVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSEEELSDYTIRTLELSPKGcsESREVTHLHYTGW 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 158
Cdd:cd00047   113 PDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEG---EVDVFEIVKALRKQRPGMV 189

                         170
                  ....*....|.
gi 1444494498 159 QTKEQYELVHR 169
Cdd:cd00047   190 QTLEQYEFIYE 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1-168 4.62e-48

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: 167.81  E-value: 4.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlYGESAVTFGPFHVSC--EAEQARTDYFIRTLLLEF-QNETRSVYQFHYVN 77
Cdd:cd18533    34 MIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVELvsEEENDDGGFIVREFELSKeDGKVKKVYHIQYKS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMRE--YQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFN------VFNLIQE 149
Cdd:cd18533   113 WPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQ 192

                         170
                  ....*....|....*....
gi 1444494498 150 MRTQRHSAVQTKEQYELVH 168
Cdd:cd18533   193 LRKQRMSMVQTLRQYIFLY 211
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1-168 9.75e-45

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: 160.99  E-value: 9.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLL--EFQNETRSVYQFHYVNW 78
Cdd:cd14543    91 MVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSW 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQ-------------EHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVF 144
Cdd:cd14543   171 PDFGVPSSAAALLDFLGEVRQQQalavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLeDVGTL----NVM 246

                         170       180
                  ....*....|....*....|....
gi 1444494498 145 NLIQEMRTQRHSAVQTKEQYELVH 168
Cdd:cd14543   247 QTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1-173 2.97e-43

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: 154.84  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWP-LYGESAVTFGPFHVSCEAEQARTDYFIRTLLLeFQNET---RSVYQFHYV 76
Cdd:cd14538    35 MVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLICGGRLEVSLEKYQSLQDFVIRRISL-RDKETgevHHITHLNFT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSSFDSILDMISLMREYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHS 156
Cdd:cd14538   114 TWPDHGTPQSADPLLRFIRYMRRI--HNSGPIVVHCSAGIGRTGVLITIDVALGLIERDL---PFDIQDIVKDLREQRQG 188

                         170
                  ....*....|....*..
gi 1444494498 157 AVQTKEQYELVHRAIAQ 173
Cdd:cd14538   189 MIQTKDQYIFCYKACLE 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1-168 3.63e-43

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: 154.43  E-value: 3.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESavTFGPFHVSCEAEQARTDYFIRTLLL--------EFQNETRSVYQ 72
Cdd:cd14549    33 MVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE--TYGNIQVTLLSTEVLATYTVRTFSLknlklkkvKGRSSERVVYQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  73 FHYVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRT 152
Cdd:cd14549   111 YHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTYIVID---SMLQQIQDKGTVNVFGFLKHIRT 187

                         170
                  ....*....|....*.
gi 1444494498 153 QRHSAVQTKEQYELVH 168
Cdd:cd14549   188 QRNYLVQTEEQYIFIH 203
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1-168 1.11e-42

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: 153.66  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14548    58 MVWEQNSHTIVMLTQCMEKGRVKCDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14548   137 HGVPEAPDSLLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDR---LLQQIESEDYVDIFGIVYDLRKHRPLMVQT 213


                  ....*...
gi 1444494498 161 KEQYELVH 168
Cdd:cd14548   214 EAQYIFLH 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1-176 1.63e-42

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: 154.16  E-value: 1.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAvTFGPFHVSCEAEQARTDYFIRTLLL---EFQNETRSVYQFHYVN 77
Cdd:cd14544    71 MVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVsklDQGDPIREIWHYQYLS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRH 155
Cdd:cd14544   150 WPDHGVPSDPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRS 229

                         170       180
                  ....*....|....*....|.
gi 1444494498 156 SAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14544   230 GMVQTEAQYKFIYVAVAQYIE 250
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1-169 1.19e-37

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: 139.84  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMgRKKCERYWPLygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14547    60 MVWQEKTPIIVMITNLTEA-KEKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILdmiSLMREYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQR 154
Cdd:cd14547   137 HKTPEAAQPLL---SLVQEVEEARQTephrgPIVVHCSAGIGRTGCFIATSIGCQQLREeGVV----DVLGIVCQLRLDR 209

                         170
                  ....*....|....*
gi 1444494498 155 HSAVQTKEQYELVHR 169
Cdd:cd14547   210 GGMVQTAEQYEFVHR 224
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1-173 1.77e-37

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: 138.73  E-value: 1.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWP-----LYGESAVTFGPFHVSCEaeqartDYFIRTLLLE--FQNETRSVYQF 73
Cdd:cd14546    34 MIWEQGCVVIVMLTRLQENGVKQCARYWPeegseVYHIYEVHLVSEHIWCD------DYLVRSFYLKnlQTSETRTVTQF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQ 153
Cdd:cd14546   108 HFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQ 185

                         170       180
                  ....*....|....*....|
gi 1444494498 154 RHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14546   186 RPGMVKTKDQFEFVLTAVAE 205
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
69-173 3.13e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 3.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   69 SVYQFHYVNWPDHDVPSSFDSILDMISLMREYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNL 146
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1444494498  147 IQEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 69-173 3.13e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 3.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   69 SVYQFHYVNWPDHDVPSSFDSILDMISLMREYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNL 146
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1444494498  147 IQEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1-171 6.62e-37

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: 137.19  E-value: 6.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLeFQNET---RSVYQFHYVN 77
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKL-VEKETgenRLIKHLQFTT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSA 157
Cdd:cd14596   114 WPDHGTPQSSDQLVKFICYMRKV--HNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGM 188

                         170
                  ....*....|....
gi 1444494498 158 VQTKEQYELVHRAI 171
Cdd:cd14596   189 IQTKDQYLFCYKVV 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1-171 9.61e-37

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: 136.63  E-value: 9.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRTLLLEF--QNETRSVYQFHYVNW 78
Cdd:cd14552    33 MIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQTDYEDYTLRDFLVTKgkGGSTRTVRQFHFHGW 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHE-DVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 157
Cdd:cd14552   111 PEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHM 187

                         170
                  ....*....|....
gi 1444494498 158 VQTKEQYELVHRAI 171
Cdd:cd14552   188 VQTLEQYEFCYKVV 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1-177 1.28e-36

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: 136.31  E-value: 1.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESaVTFGPFHVSCEAEQARTDYFIRTLLLEFQN--ETRSVYQFHYVNW 78
Cdd:cd14541    38 MVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGET-MQFGNLQITCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14541   117 PDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVLITMETAMCLIEAN---EPVYPLDIVRTMRDQRAMLI 193

                         170
                  ....*....|....*....
gi 1444494498 159 QTKEQYELVHRAIAQLFEK 177
Cdd:cd14541   194 QTPSQYRFVCEAILRVYEE 212
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1-177 2.11e-36

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 135.84  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAvTFGPFHVSCEAEQARTDYFIRTLLLEFQ--NETRSVYQFHYVNW 78
Cdd:cd14601    38 MTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQVTCHSEEGNPAYVFREMTLTNLekNESRPLTQIQYIAW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14601   117 PDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVLITMETAMCLIECN---QPVYPLDIVRTMRDQRAMMI 193

                         170
                  ....*....|....*....
gi 1444494498 159 QTKEQYELVHRAIAQLFEK 177
Cdd:cd14601   194 QTPSQYRFVCEAILKVYEE 212
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1-173 5.00e-36

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: 134.89  E-value: 5.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYG--ESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNE--TRSVYQFHYV 76
Cdd:cd14540    35 MVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgeHDALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSSFDSILDMISLMREYQEH--EDV-------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLI 147
Cdd:cd14540   115 DWPDHGCPEDVSGFLDFLEEINSVRRHtnQDVaghnrnpPTLVHCSAGVGRTGVVILADLMLYCLDHN---EELDIPRVL 191

                         170       180
                  ....*....|....*....|....*.
gi 1444494498 148 QEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14540   192 ALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1-176 5.35e-36

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: 136.55  E-value: 5.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGeSAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNET---RSVYQFHYVN 77
Cdd:cd14606    86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVG-MQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLS 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSS---FDSILDMISLMREYQEHEDvPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQR 154
Cdd:cd14606   165 WPDHGVPSEpggVLSFLDQINQRQESLPHAG-PIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQR 243

                         170       180
                  ....*....|....*....|..
gi 1444494498 155 HSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14606   244 SGMVQTEAQYKFIYVAIAQFIE 265
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1-171 8.75e-36

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: 134.63  E-value: 8.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLyGESAVTFGPFHVSCEAEQARTDYFIRTLLLE--FQNETRSVYQFHYVNW 78
Cdd:cd14619    59 MIWEQQSSTIVMLTNCMEAGRVKCEHYWPL-DYTPCTYGHLRVTVVSEEVMENWTVREFLLKqvEEQKTLSVRHFHFTAW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREY--QEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHS 156
Cdd:cd14619   138 PDHGVPSSTDTLLAFRRLLRQWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPL 214

                         170
                  ....*....|....*
gi 1444494498 157 AVQTKEQYELVHRAI 171
Cdd:cd14619   215 MVQTESQYVFLHQCI 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1-171 9.49e-36

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: 133.89  E-value: 9.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQ--NETRSVYQFHYVNW 78
Cdd:cd14555    33 MVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVETEPLAEYVVRTFALERRgyHEIREVRQFHFTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14555   110 PDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMV 186

                         170
                  ....*....|...
gi 1444494498 159 QTKEQYELVHRAI 171
Cdd:cd14555   187 QTEEQYIFIHDAI 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1-171 1.01e-35

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: 134.83  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESavTFGPFHVSCEAEQARTDYFIRTLLL--EFQNETRSVYQFHYVNW 78
Cdd:cd14553    65 MVWEQRSATIVMMTKLEERSRVKCDQYWPTRGTE--TYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAW 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14553   143 PDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKT---VDIYGHVTCLRAQRNYMV 219

                         170
                  ....*....|...
gi 1444494498 159 QTKEQYELVHRAI 171
Cdd:cd14553   220 QTEDQYIFIHDAL 232
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1-171 5.36e-35

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: 131.64  E-value: 5.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLygESAVTFGPFHVSCEAEQARTDYFIRTLLL----------EFQNETRSV 70
Cdd:cd17668    33 MIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  71 YQFHYVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEM 150
Cdd:cd17668   111 TQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHI 187

                         170       180
                  ....*....|....*....|.
gi 1444494498 151 RTQRHSAVQTKEQYELVHRAI 171
Cdd:cd17668   188 RSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1-164 1.04e-34

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: 131.48  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRTLLLEF--QNETRSVYQFHYVNW 78
Cdd:cd14615    58 MVWEKNVYAIVMLTKCVEQGRTKCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHS 156
Cdd:cd14615   136 PDHGVPETTDLLINFRHLVREYmkQNPPNSPILVHCSAGVGRTGTFIAID---RLIYQIENENVVDVYGIVYDLRMHRPL 212


                  ....*...
gi 1444494498 157 AVQTKEQY 164
Cdd:cd14615   213 MVQTEDQY 220
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1-171 4.84e-34

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: 129.95  E-value: 4.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWP-LYGESAVTFGPFHVSCEAEQARTDYFIRTLLLE--FQNETRSVYQFHYVN 77
Cdd:cd14597    62 MVWEQKSTVIAMMTQEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSA 157
Cdd:cd14597   142 WPDHDTPSQPEQLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGM 216

                         170
                  ....*....|....
gi 1444494498 158 VQTKEQYELVHRAI 171
Cdd:cd14597   217 VQTEDQYIFCYQVI 230
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1-170 5.43e-34

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: 129.95  E-value: 5.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLygESAVTFGPFHVSCEAEQARTDYFIRtlllEFQ------NETRSVYQFH 74
Cdd:cd14554    68 MLWEHNSTIIVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14554   142 FTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRT 218

                         170
                  ....*....|....*...
gi 1444494498 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14554   219 QRPAMVQTEDQYQFCYRA 236
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1-163 1.05e-33

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: 128.66  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTF--GPFHVSCEAEQARTDYFIRTLLLE--FQNETRSVYQFHYV 76
Cdd:cd14545    58 MVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYT 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSSFDSILDMISLMREYQE-HEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKiPEEFNVFNLIQEMRTQR 154
Cdd:cd14545   138 TWPDFGVPESPAAFLNFLQKVRESGSlSSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGN-PSSVDVKKVLLEMRKYR 216


                  ....*....
gi 1444494498 155 HSAVQTKEQ 163
Cdd:cd14545   217 MGLIQTPDQ 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1-176 2.44e-33

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: 128.60  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVT-FGPFHVSCEAEQARTDYFIRTLLLEF---QNETRSVYQFHYV 76
Cdd:cd14605    73 MVFQENSRVIVMTTKEVERGKSKCVKYWP--DEYALKeYGVMRVRNVKESAAHDYILRELKLSKvgqGNTERTVWQYHFR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSSFDSILDMISLMREYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQR 154
Cdd:cd14605   151 TWPDHGVPSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQR 230

                         170       180
                  ....*....|....*....|..
gi 1444494498 155 HSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14605   231 SGMVQTEAQYRFIYMAVQHYIE 252
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1-173 3.71e-33

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: 127.45  E-value: 3.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQ--NETRSVYQFHYVNW 78
Cdd:cd14630    65 MIWQENSASVVMVTNLVEVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSW 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMV 218

                         170
                  ....*....|....*
gi 1444494498 159 QTKEQYELVHRAIAQ 173
Cdd:cd14630   219 QTEEQYVFVHDAILE 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1-171 6.51e-33

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: 126.93  E-value: 6.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14614    74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWP-FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPS--SFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14614   153 HGVPTanAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRSYRMSMV 229

                         170
                  ....*....|...
gi 1444494498 159 QTKEQYELVHRAI 171
Cdd:cd14614   230 QTEEQYIFIHQCV 242
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1-173 1.35e-32

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: 125.13  E-value: 1.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQ--NETRSVYQFHYVNW 78
Cdd:cd14631    47 MIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGW 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14631   124 PDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMV 200

                         170
                  ....*....|....*
gi 1444494498 159 QTKEQYELVHRAIAQ 173
Cdd:cd14631   201 QTEEQYIFIHDAILE 215
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1-173 2.81e-32

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: 124.77  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGesAVTFGPFHVSCEAEQARTDYFIRTLLL--EFQNETRSVYQFHYVNW 78
Cdd:cd14623    58 MIWEWKSCSIVMLTELEERGQEKCAQYWPSDG--SVSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMIS-LMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 157
Cdd:cd14623   136 PEVGIPSDGKGMINIIAaVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHM 212

                         170
                  ....*....|....*.
gi 1444494498 158 VQTKEQYELVHRAIAQ 173
Cdd:cd14623   213 VQTLEQYEFCYKVVQE 228
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1-169 2.54e-31

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: 121.94  E-value: 2.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14616    59 MVWETRAKTIVMLTQCFEKGRIRCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14616   139 HGVPESSAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHINDHDFVDIYGLVAELRSERMCMVQN 215


                  ....*....
gi 1444494498 161 KEQYELVHR 169
Cdd:cd14616   216 LAQYIFLHQ 224
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1-173 4.84e-31

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: 122.86  E-value: 4.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWP-----LYGESAVTFGPFHVSCEaeqartDYFIRTLLLEF--QNETRSVYQF 73
Cdd:cd14610   107 MVWESGCVVIVMLTPLAENGVKQCYHYWPdegsnLYHIYEVNLVSEHIWCE------DFLVRSFYLKNlqTNETRTVTQF 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNllKAGKIPEEFNVFNLIQEMRTQ 153
Cdd:cd14610   181 HFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLN--KMAKGAKEIDIAATLEHLRDQ 258

                         170       180
                  ....*....|....*....|
gi 1444494498 154 RHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14610   259 RPGMVQTKEQFEFALTAVAE 278
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1-168 6.28e-31

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 120.18  E-value: 6.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEF--QNETRSVYQFHYVNW 78
Cdd:cd14539    34 MVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQSVRTTPTHVERIISIQHkdTRLSRSVVHLQFTTW 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGK-IPeefNVFNLIQEMRTQR 154
Cdd:cd14539   114 PELGLPDSPNPLLRFIEEVHSHYLQQRslqTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNgIP---DLPQLVRKMRQQR 190

                         170
                  ....*....|....
gi 1444494498 155 HSAVQTKEQYELVH 168
Cdd:cd14539   191 KYMLQEKEHLKFCY 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1-171 8.30e-31

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: 119.72  E-value: 8.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNE--TRSVYQFHYVNW 78
Cdd:cd14622    34 MVWEWKCHTIVMLTELQEREQEKCVQYWP--SEGSVTHGEITIEIKNDTLLETISIRDFLVTYNQEkqTRLVRQFHFHGW 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHE-DVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSA 157
Cdd:cd14622   112 PEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIALS---NILERVKAEGLLDVFQTVKSLRLQRPHM 188

                         170
                  ....*....|....
gi 1444494498 158 VQTKEQYELVHRAI 171
Cdd:cd14622   189 VQTLEQYEFCYRVV 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1-173 1.13e-30

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: 119.39  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNET--RSVYQFHYVNW 78
Cdd:cd14632    33 MVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSarHEVKQFHFTSW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14632   110 PEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMI 186

                         170
                  ....*....|....*
gi 1444494498 159 QTKEQYELVHRAIAQ 173
Cdd:cd14632   187 QTEEQYIFIHDAILE 201
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1-173 1.80e-30

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: 120.91  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRTLLLE--------------FQNE 66
Cdd:cd17667    91 MIWEQNTGIIVMITNLVEKGRRKCDQYWP--TENSEEYGNIIVTLKSTKIHACYTVRRFSIRntkvkkgqkgnpkgRQNE 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  67 tRSVYQFHYVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNL 146
Cdd:cd17667   169 -RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGF 244

                         170       180
                  ....*....|....*....|....*..
gi 1444494498 147 IQEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:cd17667   245 LKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1-165 2.31e-30

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: 118.26  E-value: 2.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWplyGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQN--ETRSVYQFHYVNW 78
Cdd:cd14558    33 MIFQKKVKVIVMLTELKEGDQEQCAQYW---GDEKKTYGDIEVELKDTEKSPTYTVRVFEITHLKrkDSRTVYQYQYHKW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQE------HEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRT 152
Cdd:cd14558   110 KGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRK 186

                         170
                  ....*....|...
gi 1444494498 153 QRHSAVQTKEQYE 165
Cdd:cd14558   187 QRPGMVSTLEQYQ 199
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1-169 2.53e-30

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: 118.48  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESavTFGPFHVSCEAEQARTDYFIRTLLLEFQNE------TRSVYQFH 74
Cdd:cd14551    33 MIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDTVVLVDYTTRKFCIQKVNRgigekrVRLVTQFH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQ 153
Cdd:cd14551   111 FTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAeGKV----DVFGFVSRIRQQ 186

                         170
                  ....*....|....*.
gi 1444494498 154 RHSAVQTKEQYELVHR 169
Cdd:cd14551   187 RSQMVQTDMQYVFIYQ 202
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1-170 6.67e-30

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: 119.84  E-value: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRtlllEFQ------NETRSVYQFH 74
Cdd:cd14628   114 MLWEHNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQ 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14628   188 FTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRT 264

                         170
                  ....*....|....*...
gi 1444494498 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14628   265 QRPAMVQTEDQYQFCYRA 282
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1-177 6.78e-30

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: 119.18  E-value: 6.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEsAVTFGPFHVSCEAEQARTDYFIRTLLLEF--QNETRSVYQFHYVNW 78
Cdd:cd14600   101 VVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD-VMEYGGFRVQCHSEDCTIAYVFREMLLTNtqTGEERTVTHLQYVAW 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREyQEHEDVPICIHCSAGCGRTGAICAIDYTWNLlkagkIPEEFNVFNL--IQEMRTQRHS 156
Cdd:cd14600   180 PDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCL-----TERNQPVYPLdiVRKMRDQRAM 253

                         170       180
                  ....*....|....*....|.
gi 1444494498 157 AVQTKEQYELVHRAIAQLFEK 177
Cdd:cd14600   254 MVQTSSQYKFVCEAILRVYEE 274
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1-170 8.25e-30

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: 119.45  E-value: 8.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRtlllEFQ------NETRSVYQFH 74
Cdd:cd14629   115 MLWEHNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTIRQFQ 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14629   189 FTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRT 265

                         170
                  ....*....|....*...
gi 1444494498 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14629   266 QRPAMVQTEDQYQLCYRA 283
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1-173 1.87e-29

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: 117.24  E-value: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEmGRKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14612    79 MVWQEECPIIVMITKLKE-KKEKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPD 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISlmrEYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRH 155
Cdd:cd14612   155 HQTPESAGPLLRLVA---EVEESRQTaaspgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRG 228

                         170
                  ....*....|....*...
gi 1444494498 156 SAVQTKEQYELVHRAIAQ 173
Cdd:cd14612   229 GMIQTSEQYQFLHHTLAL 246
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1-169 5.67e-29

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 114.54  E-value: 5.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRS---VYQFHYVN 77
Cdd:cd14557    33 MIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEEKICPDYIIRKLNINNKKEKGSgreVTHIQFTS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHS 156
Cdd:cd14557   113 WPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAeGRV----DVYGYVVKLRRQRCL 188

                         170
                  ....*....|...
gi 1444494498 157 AVQTKEQYELVHR 169
Cdd:cd14557   189 MVQVEAQYILIHQ 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1-171 7.40e-29

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: 115.04  E-value: 7.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLyGESAVTFGPFHVSCEAEQARTDYFIRTLLL--EFQNETRSVYQFHYVNW 78
Cdd:cd14618    59 LVWEQQVCNIIMLTVGMENGRVLCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLwhEDLRKERRVKHLHYTAW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREY-QEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHS 156
Cdd:cd14618   138 PDHGIPESTSSLMAFRELVREHvQATKGKgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKV---VDVFNTVYILRMHRYL 214

                         170
                  ....*....|....*
gi 1444494498 157 AVQTKEQYELVHRAI 171
Cdd:cd14618   215 MIQTLSQYIFLHSCI 229
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1-173 8.47e-29

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: 116.29  E-value: 8.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWP-----LYGESAVTFGPFHVSCEaeqartDYFIRTLLLEF--QNETRSVYQF 73
Cdd:cd14609   105 MVWENGCTVIVMLTPLVEDGVKQCDRYWPdegssLYHIYEVNLVSEHIWCE------DFLVRSFYLKNvqTQETRTLTQF 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQ 153
Cdd:cd14609   179 HFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQ 256

                         170       180
                  ....*....|....*....|
gi 1444494498 154 RHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14609   257 RPGMVRTKDQFEFALTAVAE 276
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1-173 1.22e-28

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: 115.90  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESavTFGPFHVSCEAEQARTDYFIRTLLL--EFQNETRSVYQFHYVNW 78
Cdd:cd14626   103 MVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE--TYGMIQVTLLDTVELATYSVRTFALykNGSSEKREVRQFQFMAW 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14626   181 PDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMV 257

                         170
                  ....*....|....*
gi 1444494498 159 QTKEQYELVHRAIAQ 173
Cdd:cd14626   258 QTEDQYIFIHEALLE 272
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1-173 3.00e-28

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: 114.74  E-value: 3.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTF--GPFHVSCEAEQARTDYFIRTLLLE--FQNETRSVYQFHYV 76
Cdd:cd14608    83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSSFDSILDMISLMREYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQR 154
Cdd:cd14608   163 TWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFR 242

                         170
                  ....*....|....*....
gi 1444494498 155 HSAVQTKEQYELVHRAIAQ 173
Cdd:cd14608   243 MGLIQTADQLRFSYLAVIE 261
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1-170 3.25e-28

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: 114.83  E-value: 3.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRtlllEFQ------NETRSVYQFH 74
Cdd:cd14627   115 MLWENNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQ 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14627   189 FTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRT 265

                         170
                  ....*....|....*...
gi 1444494498 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14627   266 QRPAMVQTEDEYQFCYQA 283
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1-173 3.55e-28

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: 114.37  E-value: 3.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQ--NETRSVYQFHYVNW 78
Cdd:cd14633   102 MVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGW 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14633   179 PDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMV 255

                         170
                  ....*....|....*
gi 1444494498 159 QTKEQYELVHRAIAQ 173
Cdd:cd14633   256 QTEEQYVFIHDAILE 270
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1-169 9.08e-27

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: 108.85  E-value: 9.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESaVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRS---VYQFHYVN 77
Cdd:cd14617    59 MVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAprlVRHFHYTV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRH 155
Cdd:cd14617   138 WPDHGVPETTQSLIQFVRTVRDYinRTPGSGPTVVHCSAGVGRTGTFIALD---RILQQLDSKDSVDIYGAVHDLRLHRV 214

                         170
                  ....*....|....
gi 1444494498 156 SAVQTKEQYELVHR 169
Cdd:cd14617   215 HMVQTECQYVYLHQ 228
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1-171 7.97e-26

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: 106.18  E-value: 7.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGesAVTFGPFHVSCEAEQARTDYFIRTLLLEFQ-----NETRSVYQFHY 75
Cdd:cd14620    57 MVWEQKSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  76 VNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRH 155
Cdd:cd14620   135 TSWPDFGVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRP 211

                         170
                  ....*....|....*.
gi 1444494498 156 SAVQTKEQYELVHRAI 171
Cdd:cd14620   212 QMVQTDMQYSFIYQAL 227
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1-171 9.13e-26

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 106.97  E-value: 9.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGP--FHVSCEAEQARTDYFIRTLLLEFQN--ETRSVYQFHYV 76
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSSFDSILDMISLMREYQ--EHEDVPICIHCSAGCGRTGAICAIDyTWNLLKAGKIPEEFNVFNLIQEMRTQR 154
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGslSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYR 240

                         170
                  ....*....|....*..
gi 1444494498 155 HSAVQTKEQYELVHRAI 171
Cdd:cd14607   241 MGLIQTPDQLRFSYMAV 257
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1-176 1.53e-25

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: 105.06  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYG--ESAVTFGPFHVSCEAEQ-----ARTDYFIRTLLlefQNETRSVYQF 73
Cdd:cd14598    35 MVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKITTRFRTdsgcyATTGLKIKHLL---TGQERTVWHL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWPDHDVPSS---FDSILDMISLMREYQ------EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVF 144
Cdd:cd14598   112 QYTDWPEHGCPEDlkgFLSYLEEIQSVRRHTnstidpKSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVL 191

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1444494498 145 NLiqeMRTQRHSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14598   192 DM---LRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1-173 1.15e-24

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: 104.40  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQ--NETRSVYQFHYVNW 78
Cdd:cd14625   109 MVWEQRSATVVMMTKLEEKSRIKCDQYWP--SRGTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQFQFTAW 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14625   187 PDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRSQRNYMV 263

                         170
                  ....*....|....*
gi 1444494498 159 QTKEQYELVHRAIAQ 173
Cdd:cd14625   264 QTEDQYSFIHDALLE 278
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1-173 2.66e-24

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 103.25  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVM--ACREFEMGRKKCERYWPLYGEsavtFGPFHVSCE---AEQARTDYFIRTLLLEFQN---ETRSVYQ 72
Cdd:COG5599    96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  73 FHYVNWPDHDVPSSfDSILDMISLMREYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQE 149
Cdd:COG5599   172 LHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVID 249

                         170       180
                  ....*....|....*....|....*.
gi 1444494498 150 MRTQR-HSAVQTKEQY-ELVHRAIAQ 173
Cdd:COG5599   250 MRTSRnGGMVQTSEQLdVLVKLAEQQ 275
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1-168 6.25e-24

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: 99.79  E-value: 6.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMaCREFEMGRKKCERYWPLYGESavTFGPFHVSCEAEQARTDYFIRTLLL----EFQNETRSVYQFHYV 76
Cdd:cd14556    33 LVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEGSG--TYGPIQVEFVSTTIDEDVISRIFRLqnttRPQEGYRMVQQFQFL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDH-DVPSSFDSILDMISLMREYQEH-EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQR 154
Cdd:cd14556   110 GWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHR 186

                         170
                  ....*....|....
gi 1444494498 155 HSAVQTKEQYELVH 168
Cdd:cd14556   187 PNMVETEEQYKFCY 200
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1-173 1.15e-23

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: 101.64  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGesAVTFGPFHVSCEAEQARTDYFIRTLLLE------FQNETRSVYQFH 74
Cdd:cd14621   114 MIWEQNTATIVMVTNLKERKECKCAQYWPDQG--CWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvtNKKPQRLITQFH 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQR 154
Cdd:cd14621   192 FTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQR 268

                         170
                  ....*....|....*....
gi 1444494498 155 HSAVQTKEQYELVHRAIAQ 173
Cdd:cd14621   269 CQMVQTDMQYVFIYQALLE 287
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1-176 1.26e-23

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: 101.61  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYG--ESAVTFGPFHVSCEAEQ-----ARTDYFIRTLLlefQNETRSVYQF 73
Cdd:cd14599   101 MVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskHSSATYGKFKVTTKFRTdsgcyATTGLKVKHLL---SGQERTVWHL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWPDHDVPSSFDSILDMISLMREYQEHEDV----------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNV 143
Cdd:cd14599   178 QYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHN---EKVEV 254

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1444494498 144 FNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14599   255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1-173 1.32e-23

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: 101.35  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESavTFGPFHVSCEAEQARTDYFIRTLLLeFQN---ETRSVYQFHYVN 77
Cdd:cd14624   109 MIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE--TYGLIQVTLLDTVELATYCVRTFAL-YKNgssEKREVRQFQFTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WPDHDVPSSFDSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSA 157
Cdd:cd14624   186 WPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRAQRNYM 262

                         170
                  ....*....|....*.
gi 1444494498 158 VQTKEQYELVHRAIAQ 173
Cdd:cd14624   263 VQTEDQYIFIHDALLE 278
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1-168 3.15e-23

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: 98.84  E-value: 3.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGrKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14611    63 MVWQEDSPVIVMITKLKEKN-EKCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILdmiSLMREYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRH 155
Cdd:cd14611   139 HKTPDSAQPLL---QLMLDVEEDRLAspgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGV---VDVLSIVCQLRVDRG 212

                         170
                  ....*....|...
gi 1444494498 156 SAVQTKEQYELVH 168
Cdd:cd14611   213 GMVQTSEQYEFVH 225
PHA02738 PHA02738
hypothetical protein; Provisional
 1-171 2.20e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 98.46  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNE-TRSVYQFHYVNWP 79
Cdd:PHA02738  109 MLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFTAWP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  80 DHDVPSSFDSILDMISLMREYQE--HEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNL 146
Cdd:PHA02738  189 DHDVPKNTSEFLNFVLEVRQCQKelAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT---VSIPSI 265

                         170       180
                  ....*....|....*....|....*
gi 1444494498 147 IQEMRTQRHSAVQTKEQYELVHRAI 171
Cdd:PHA02738  266 VSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-164 3.55e-22

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 97.38  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRS--VYQFHYVNW 78
Cdd:PHA02742  112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDW 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  79 PDHDVPSSFDSILDMISLMREYQEHEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLI 147
Cdd:PHA02742  192 PHGGLPRDPNKFLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIV 268

                         170
                  ....*....|....*..
gi 1444494498 148 QEMRTQRHSAVQTKEQY 164
Cdd:PHA02742  269 RDLRKQRHNCLSLPQQY 285
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1-172 8.49e-22

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: 95.31  E-value: 8.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGrKKCERYWPlygESAVTFGPFHVSCEAEQARTDYFIRTLLLEFQNETRSVYQFHYVNWPD 80
Cdd:cd14613    89 MVWQERSPIIVMITNIEEMN-EKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPD 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  81 HDVPSSFDSILDMISLM---REYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 157
Cdd:cd14613   165 QKTPDNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGM 241

                         170
                  ....*....|....*
gi 1444494498 158 VQTKEQYELVHRAIA 172
Cdd:cd14613   242 IQTCEQYQFVHHVLS 256
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1-164 2.45e-21

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: 92.53  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRK-KCERYWPLYGESAVTFGPFHVSCEAEQArTDYFIRTLLLEFQ-NET----RSVYQFH 74
Cdd:cd17658    35 MVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTNKKLKH-SQHSITLRVLEVQyIESeeppLSVLHIQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISlmREYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRTQ 153
Cdd:cd17658   114 YPEWPDHGVPKDTRSVRELLK--RLYGIPPSAgPIVVHCSAGIGRTGAYCTIHNTIRRILEGDM-SAVDLSKTVRKFRSQ 190

                         170
                  ....*....|.
gi 1444494498 154 RHSAVQTKEQY 164
Cdd:cd17658   191 RIGMVQTQDQY 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1-181 1.20e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 90.47  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVmACREFEMGRKKCERYWPLYGESAVTFGPFHVSC-----EAEQARTdyfiRTLLLEFQNET-RSVYQFH 74
Cdd:PHA02746  132 LISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFVAKIldiieELSFTKT----RLMITDKISDTsREIHHFW 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDHDVPSSFDSILDMISLMREYQE----------HEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVF 144
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAID---NALEQLEKEKEVCLG 283

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1444494498 145 NLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQK 181
Cdd:PHA02746  284 EIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAKK 320
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-168 8.03e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 84.67  E-value: 8.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMAC-REFEMGRKKCERYWPLYGESAVTFGPFHVSCEAEQARTDYfIRTLLL---EFQNETRSVYQFHYV 76
Cdd:PHA02747  112 AVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLIEitdKILKDSRKISHFQCS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  77 NWPDHDVPSS---FDSILDMISLMRE-------YQEHEDVPICIHCSAGCGRTGAICAIDYTWN-LLKAGKIPEEFNVFN 145
Cdd:PHA02747  191 EWFEDETPSDhpdFIKFIKIIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAICLAKTAEK 270

                         170       180
                  ....*....|....*....|...
gi 1444494498 146 LiqemRTQRHSAVQTKEQYELVH 168
Cdd:PHA02747  271 I----REQRHAGIMNFDDYLFIQ 289
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1-168 1.55e-16

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: 78.91  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACrefEMGRKK-CERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRTL----LLEFQNETRSVYQFHY 75
Cdd:cd14634    33 LVFDYNCSSVVMLN---EMDAAQlCMQYWP--EKTSCCYGPIQVEFVSADIDEDIISRIFricnMARPQDGYRIVQHLQY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  76 VNWPDH-DVPSSFDSILDMISLMREYQEHEDVP---ICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMR 151
Cdd:cd14634   108 IGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGRegrTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLR 184

                         170
                  ....*....|....*..
gi 1444494498 152 TQRHSAVQTKEQYELVH 168
Cdd:cd14634   185 NNKSNMVETLEQYKFVY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1-168 1.08e-15

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: 76.22  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMaCREFEMGrKKCERYWPlyGESAVTFGPFHVSCEAEQARTDYFIRtlLLEFQNETRS------VYQFH 74
Cdd:cd14636    33 LVYDYGCTSIVM-LNEVDLA-QGCPQYWP--EEGMLRYGPIQVECMSCSMDCDVISR--IFRICNLTRPqegylmVQQFQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  75 YVNWPDH-DVPSSFDSILDMISLMREYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEM 150
Cdd:cd14636   107 YLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgegRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTL 183

                         170
                  ....*....|....*...
gi 1444494498 151 RTQRHSAVQTKEQYELVH 168
Cdd:cd14636   184 RNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 24-164 1.04e-10

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: 61.85  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  24 CERYWPLYGESavTFGPFHVSCEAEQARTDyfIRTLLLEFQNETRS------VYQFHYVNW-PDHDVPSSFDSILDMISL 96
Cdd:cd14637    57 CLQYWPEPGLQ--QYGPMEVEFVSGSADED--IVTRLFRVQNITRLqeghlmVRHFQFLRWsAYRDTPDSKKAFLHLLAS 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444494498  97 MREYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 164
Cdd:cd14637   133 VEKWQrESGEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQY 198
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
72-169 3.91e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 58.44  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  72 QFHYVNWPDHDVPS--SFDSILDMIslmrEYQEHEDVPICIHCSAGCGRTGAICAidyTWnLLKAGKIPEEfnvfnLIQE 149
Cdd:COG2453    49 EYLHLPIPDFGAPDdeQLQEAVDFI----DEALREGKKVLVHCRGGIGRTGTVAA---AY-LVLLGLSAEE-----ALAR 115

                          90       100
                  ....*....|....*....|
gi 1444494498 150 MRTQRHSAVQTKEQYELVHR 169
Cdd:COG2453   116 VRAARPGAVETPAQRAFLER 135
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 24-168 7.34e-10

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: 59.32  E-value: 7.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  24 CERYWPLYGesAVTFGPFHVSCEAEQARTDYFIRTLLL----EFQNETRSVYQFHYVNWPDH-DVPSSFDSILDMISLMR 98
Cdd:cd14635    54 CPQYWPENG--VHRHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444494498  99 EYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 168
Cdd:cd14635   132 KWQEEYNGgegRTVVHCLNGGGRSGTFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1-171 1.61e-09

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: 58.08  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCErYWPLYGESAVTFGpFHVSCEAEQAR-----TDYFIRTLLLEFQNE--TRSVYQF 73
Cdd:cd17669    33 MIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCET-FKVTLIAEEHKclsneEKLIIQDFILEATQDdyVLEVRHF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWPDHDVPSSfdSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQ 153
Cdd:cd17669   111 QCPKWPNPDSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPG 188

                         170
                  ....*....|....*...
gi 1444494498 154 RHSAVqtkEQYELVHRAI 171
Cdd:cd17669   189 VFTDI---EQYQFLYKAI 203
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 63-168 6.09e-09

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: 56.59  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  63 FQNETRSVYQFhyvNWPDHDVPSsFDSILDMISLMREYQEhEDVPICIHCSAGCGRTG-AICAIdytwnLLKAGKIPEEf 141
Cdd:cd14506    72 FMRAGIYFYNF---GWKDYGVPS-LTTILDIVKVMAFALQ-EGGKVAVHCHAGLGRTGvLIACY-----LVYALRMSAD- 140

                          90       100
                  ....*....|....*....|....*..
gi 1444494498 142 nvfNLIQEMRTQRHSAVQTKEQYELVH 168
Cdd:cd14506   141 ---QAIRLVRSKRPNSIQTRGQVLCVR 164
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1-166 9.00e-09

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: 56.25  E-value: 9.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKceryWPLYGESAVTFGPFHVSCEAEQA-----RTDYFIRTLLLEFQNETRSVYQFHY 75
Cdd:cd14559    48 MLADNRTPCLVVLASNKDIQRKG----LPPYFRQSGTYGSVTVKSKKTGKdelvdGLKADMYNLKITDGNKTITIPVVHV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  76 VNWPDHDVPSSFDSIL--DMISLMRE--------------YQEHEDVPIcIHCSAGCGRTGAICAIdytwnlLKAGKIPE 139
Cdd:cd14559   124 TNWPDHTAISSEGLKElaDLVNKSAEekrnfykskgssaiNDKNKLLPV-IHCRAGVGRTGQLAAA------MELNKSPN 196

                         170       180
                  ....*....|....*....|....*...
gi 1444494498 140 EFNVFNLIQEMRTQR-HSAVQTKEQYEL 166
Cdd:cd14559   197 NLSVEDIVSDMRTSRnGKMVQKDEQLDT 224
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 88-169 1.12e-07

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 50.43  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  88 DSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDytwnLLKAGKIPeefnVFNLIQEMRTQR-HSAVQTKEQYEL 166
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACY----LVLLGGMS----AEEAVRIVRLIRpGGIPQTIEQLDF 110


                  ...
gi 1444494498 167 VHR 169
Cdd:cd14494   111 LIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 69-167 1.18e-07

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: 51.12  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  69 SVYQFHYVNW-----PDHDVPSsFDSILDMISLMrEYQEHEDVPICIHCSAGCGRTGAICAIdYtwnLLKAGKIPEEfnv 143
Cdd:cd14504    43 HSDTCPGLRYhhipiEDYTPPT-LEQIDEFLDIV-EEANAKNEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV--- 113

                          90       100
                  ....*....|....*....|....
gi 1444494498 144 fNLIQEMRTQRHSAVQTKEQYELV 167
Cdd:cd14504   114 -DAINEIRRIRPGSIETSEQEKFV 136
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1-171 1.86e-07

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: 51.99  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEMGRKKCErYWPLYGES------AVTFGPFHVSCEAEQART---DYFIRTLLLEFQNETRsvy 71
Cdd:cd17670    33 MIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREESmnceafTVTLISKDRLCLSNEEQIiihDFILEATQDDYVLEVR--- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  72 QFHYVNWPDHDVPSSfdSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMR 151
Cdd:cd17670   109 HFQCPKWPNPDAPIS--STFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMR 186

                         170       180
                  ....*....|....*....|
gi 1444494498 152 TQRHSAVqtkEQYELVHRAI 171
Cdd:cd17670   187 PGVFTDI---EQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-172 2.47e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 49.97  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVMACREFEmgrKKC-ERYWPLYGESAVTFGPFHVScEAEQARTDYFIRTLLL--EFQNETRSVYQFHYVN 77
Cdd:PHA02740  110 ALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIE-TLEIIIKPHFNLTLLSltDKFGQAQKISHFQYTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  78 WP----DHDVPSSFDSILDMISLMREYQEHEDV----PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQE 149
Cdd:PHA02740  186 WPadgfSHDPDAFIDFFCNIDDLCADLEKHKADgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGM---LSIANALKK 262

                         170       180
                  ....*....|....*....|...
gi 1444494498 150 MRTQRHSAVQTKEQYELVHRAIA 172
Cdd:PHA02740  263 VRQKKYGCMNCLDDYVFCYHLIA 285
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 72-124 2.57e-06

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: 47.96  E-value: 2.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1444494498  72 QFHYVNWPDHDVPSsFDSILDMISLMREY-QEHEDVPICIHCSAGCGRTGAICA 124
Cdd:cd14497    62 RVLHYGFPDHHPPP-LGLLLEIVDDIDSWlSEDPNNVAVVHCKAGKGRTGTVIC 114
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1-125 1.38e-05

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: 46.55  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498   1 MIWEYNVAIIVM--ACREFEmgrkKCERYWPLYGES--AVTFGPFHVSCEAEQARTD--YFIRTLLLEFQNETR--SVYQ 72
Cdd:cd14550    33 MIWDHNSQTIVMltDNELNE----DEPIYWPTKEKPleCETFKVTLSGEDHSCLSNEirLIVRDFILESTQDDYvlEVRQ 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1444494498  73 FHYVNWPDHDVPSSfdSILDMISLMREYQEHEDVPICIHCSAGCGRTGAICAI 125
Cdd:cd14550   109 FQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 73-168 2.97e-05

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 45.05  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  73 FHY----VNWPDHDVPSsFDSILDMISLMREY--QEHEDVpICIHCSAGCGRTG-AICAidytWnLLKAGKIPEEFNVFN 145
Cdd:cd14510    72 FHNrverVPIDDHNVPT-LDEMLSFTAEVREWmaADPKNV-VAIHCKGGKGRTGtMVCA----W-LIYSGQFESAKEALE 144

                          90       100
                  ....*....|....*....|....*...
gi 1444494498 146 LIQEMRT-----QRHSAVQTKEQYELVH 168
Cdd:cd14510   145 YFGERRTdksvsSKFQGVETPSQSRYVG 172
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 110-169 2.56e-04

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 42.25  E-value: 2.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444494498 110 IHCSAGCGRTGAICAIdytwNLLKAG-KIPEEfnvfNLIQEMRTQRHSAVQTKEQYELVHR 169
Cdd:cd14505   111 IHCKGGLGRTGLIAAC----LLLELGdTLDPE----QAIAAVRALRPGAIQTPKQENFLHQ 163
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 330-584 2.37e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 41.42  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  330 EGNSLLNRGHAIKIK--PVSSCVTDKSFKPQEQISG----DSFVDASQNSCMECSVPQSNTALIPSPeslqsQQVPDtpp 403
Cdd:TIGR00600  438 DDLDYLDQGEGIPLMaaLQLSSVNSKPEAVASTKIArevtSSGHEAVPKAVQSLLLGATNDSPIPSE-----FTILD--- 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  404 RPDRLPLIEKGQAMWSLHGPENalrtsvSEDTSSDILRQGVKTVSLVSNN--------------TVELPSSDKVDHSTIA 469
Cdd:TIGR00600  510 RKSELSIERTVKPVSSEFGLPS------QREDKLAIPTEGTQNLQGISDHpeqfefqnelspleTKNNESNLSSDAETEG 583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  470 VRAPLCFTNPLHSDDSDTDDI-------NFDGAMTKSPSNISTASATVSAATNTENIsARKVLPMSIARQDLTAvtcseD 542
Cdd:TIGR00600  584 SPNPEMPSWSSVTVPSEALDNyettnpsNAKEVRNFAETGIQTTNVGESADLLLISN-PMEVEPMESEKEESES-----D 657

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1444494498  543 GKDAD------TSEDSSPPLPERTPESfvlatEQNSplPKPVTIAQSE 584
Cdd:TIGR00600  658 GSFIEvdsvssTLELQVPSKSQPTDES-----EENA--ENKVASIEGE 698
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 72-125 3.16e-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: 38.89  E-value: 3.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  72 QFHYVN------WPDHDVPSSFDSILDMISlmreyqehEDVPICIHCSAGCGRTGAICAI 125
Cdd:cd14529    58 GVKYVNlplsatRPTESDVQSFLLIMDLKL--------APGPVLIHCKHGKDRTGLVSAL 109
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 74-162 6.47e-03

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 38.13  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444494498  74 HYVNWP-DHDVPSSFDSILDMISLMR-EYQEHEDVPICIHCSAGCGRTGAICAIdytwNLLKAGKIPEEfnvfnLIQEMR 151
Cdd:cd18537    64 QVLDWPfDDGAPPSNQIVDDWLNLLKvKFREEPGCCIAVHCVAGLGRAPVLVAL----ALIECGMKYED-----AVQFIR 134

                          90
                  ....*....|.
gi 1444494498 152 TQRHSAVQTKE 162
Cdd:cd18537   135 QKRRGAFNSKQ 145
 
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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