NCBI Conserved Domain Search

Conserved domains on [gi|1907161258|ref|XP_036020806|]

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tyrosine-protein phosphatase non-receptor type 12 isoform X3 [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

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

7.09e-149

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: 7.09e-149

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14604   199 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1907161258 161 KEQYELVHRAIAQLFEKQL 179
Cdd:cd14604   279 KEQYELVHRAIAQLFEKQL 297

Name

Accession

Description

Interval

E-value

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

1-179

7.09e-149

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: 7.09e-149

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14604   199 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1907161258 161 KEQYELVHRAIAQLFEKQL 179
Cdd:cd14604   279 KEQYELVHRAIAQLFEKQL 297

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1-173

2.80e-73

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 236.79 E-value: 2.80e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258    1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNW 78
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 158
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMV 244

                          170
                   ....*....|....*
gi 1907161258  159 QTKEQYELVHRAIAQ 173
Cdd:smart00194 245 QTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1-173

4.48e-71

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 229.82 E-value: 4.48e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQART-DYFIRTLLLEF--QNESRRLYQFHYVN 77
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHS 156
Cdd:pfam00102 141 WPDHGVPESPNSLLDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPG 217

                         170
                  ....*....|....*..
gi 1907161258 157 AVQTKEQYELVHRAIAQ 173
Cdd:pfam00102 218 MVQTLEQYIFLYDAILE 234

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1-173

3.30e-24

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 102.86 E-value: 3.30e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVM--ACREFEMGRKKCERYWPLYGEdpitFAPFKISCE---NEQARTDYFIRTLLLEFQN---ESRRLYQ 72
Cdd:COG5599    96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  73 FHYVNWPDHDVPSSfDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQE 149
Cdd:COG5599   172 LHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVID 249

                         170       180
                  ....*....|....*....|....*.
gi 1907161258 150 MRTQR-HSAVQTKEQY-ELVHRAIAQ 173
Cdd:COG5599   250 MRTSRnGGMVQTSEQLdVLVKLAEQQ 275

PHA02738

hypothetical protein; Provisional

1-171

3.77e-21

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 94.99 E-value: 3.77e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNES-RRLYQFHYVNWP 79
Cdd:PHA02738  109 MLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  80 DHDVPSSFDSILDMISLMRKYQE--HEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNL 146
Cdd:PHA02738  189 DHDVPKNTSEFLNFVLEVRQCQKelAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT---VSIPSI 265

                         170       180
                  ....*....|....*....|....*
gi 1907161258 147 IQEMRTQRHSAVQTKEQYELVHRAI 171
Cdd:PHA02738  266 VSSIRNQRYYSLFIPFQYFFCYRAV 290

Name

Accession

Description

Interval

E-value

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

1-179

7.09e-149

Pssm-ID: 350452 [Multi-domain] Cd Length: 297 Bit Score: 433.20 E-value: 7.09e-149

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14604   199 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1907161258 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

5.98e-119

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: 352.88 E-value: 5.98e-119

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQART-DYFIRTLLLEFQNESRRLYQFHYVNWP 79
Cdd:cd14542    33 MIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKEKRVGpDFLIRTLKVTFQKESRTVYQFHYTAWP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  80 DHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQ 159
Cdd:cd14542   113 DHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQ 192

                         170
                  ....*....|
gi 1907161258 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

1.87e-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: 316.78 E-value: 1.87e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14602    60 MIWEYSVLIIVMACMEFEMGKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14602   140 HDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQT 219

                         170
                  ....*....|....*
gi 1907161258 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

2.28e-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: 263.22 E-value: 2.28e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYgEDPITFAPFKIS-CENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWP 79
Cdd:cd14603    92 MIWQYGVKVILMACREIEMGKKKCERYWAQE-QEPLQTGPFTITlVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  80 DHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQ 159
Cdd:cd14603   171 DHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQ 250

                         170
                  ....*....|....*.
gi 1907161258 160 TKEQYELVHRAIAQLF 175
Cdd:cd14603   251 TEEQYEFLYHTVAQMF 266

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1-173

2.80e-73

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 236.79 E-value: 2.80e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258    1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNW 78
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 158
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMV 244

                          170
                   ....*....|....*
gi 1907161258  159 QTKEQYELVHRAIAQ 173
Cdd:smart00194 245 QTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1-173

4.48e-71

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 229.82 E-value: 4.48e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQART-DYFIRTLLLEF--QNESRRLYQFHYVN 77
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHS 156
Cdd:pfam00102 141 WPDHGVPESPNSLLDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPG 217

                         170
                  ....*....|....*..
gi 1907161258 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

6.73e-65

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: 212.53 E-value: 6.73e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNW 78
Cdd:cd00047    33 MVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSEEELSDYTIRTLELSPKGcsESREVTHLHYTGW 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 158
Cdd:cd00047   113 PDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEG---EVDVFEIVKALRKQRPGMV 189

                         170
                  ....*....|.
gi 1907161258 159 QTKEQYELVHR 169
Cdd:cd00047   190 QTLEQYEFIYE 200

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

1-168

1.70e-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: 168.97 E-value: 1.70e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlYGEDPITFAPFKISC--ENEQARTDYFIRTLLLEF-QNESRRLYQFHYVN 77
Cdd:cd18533    34 MIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVELvsEEENDDGGFIVREFELSKeDGKVKKVYHIQYKS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRK--YQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFN------VFNLIQE 149
Cdd:cd18533   113 WPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQ 192

                         170
                  ....*....|....*....
gi 1907161258 150 MRTQRHSAVQTKEQYELVH 168
Cdd:cd18533   193 LRKQRMSMVQTLRQYIFLY 211

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

1-173

1.48e-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: 155.22 E-value: 1.48e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITF-APFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVN 77
Cdd:cd14538    35 MVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVSLEKYQSLQDFVIRRISLRDKetGEVHHITHLNFTT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSA 157
Cdd:cd14538   115 WPDHGTPQSADPLLRFIRYMRRI--HNSGPIVVHCSAGIGRTGVLITIDVALGLIERDL---PFDIQDIVKDLREQRQGM 189

                         170
                  ....*....|....*.
gi 1907161258 158 VQTKEQYELVHRAIAQ 173
Cdd:cd14538   190 IQTKDQYIFCYKACLE 205

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

1-168

3.10e-43

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

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 154.82 E-value: 3.10e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14548    58 MVWEQNSHTIVMLTQCMEKGRVKCDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 160
Cdd:cd14548   137 HGVPEAPDSLLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDR---LLQQIESEDYVDIFGIVYDLRKHRPLMVQT 213


                  ....*...
gi 1907161258 161 KEQYELVH 168
Cdd:cd14548   214 EAQYIFLH 221

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

1-168

1.41e-42

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: 152.51 E-value: 1.41e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL--------EFQNESRRLYQ 72
Cdd:cd14549    33 MVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE--TYGNIQVTLLSTEVLATYTVRTFSLknlklkkvKGRSSERVVYQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  73 FHYVNWPDHDVPssfDSILDMISLMRK---YQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQE 149
Cdd:cd14549   111 YHYTQWPDHGVP---DYTLPVLSFVRKssaANPPGAGPIVVHCSAGVGRTGTYIVID---SMLQQIQDKGTVNVFGFLKH 184

                         170
                  ....*....|....*....
gi 1907161258 150 MRTQRHSAVQTKEQYELVH 168
Cdd:cd14549   185 IRTQRNYLVQTEEQYIFIH 203

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

1-168

4.23e-42

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: 153.67 E-value: 4.23e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNW 78
Cdd:cd14543    91 MVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSW 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQ-------------EHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVF 144
Cdd:cd14543   171 PDFGVPSSAAALLDFLGEVRQQQalavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLeDVGTL----NVM 246

                         170       180
                  ....*....|....*....|....
gi 1907161258 145 NLIQEMRTQRHSAVQTKEQYELVH 168
Cdd:cd14543   247 QTVRRMRTQRAFSIQTPDQYYFCY 270

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

1-176

1.59e-40

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: 148.38 E-value: 1.59e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPiTFAPFKISCENEQARTDYFIRTLLL---EFQNESRRLYQFHYVN 77
Cdd:cd14544    71 MVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVsklDQGDPIREIWHYQYLS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRH 155
Cdd:cd14544   150 WPDHGVPSDPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRS 229

                         170       180
                  ....*....|....*....|.
gi 1907161258 156 SAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14544   230 GMVQTEAQYKFIYVAVAQYIE 250

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

1-171

2.81e-38

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: 140.65 E-value: 2.81e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLeFQNES---RRLYQFHYVN 77
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKL-VEKETgenRLIKHLQFTT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSA 157
Cdd:cd14596   114 WPDHGTPQSSDQLVKFICYMRKV--HNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGM 188

                         170
                  ....*....|....
gi 1907161258 158 VQTKEQYELVHRAI 171
Cdd:cd14596   189 IQTKDQYLFCYKVV 202

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

70-173

1.31e-36

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 132.48 E-value: 1.31e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   70 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLI 147
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1907161258  148 QEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

70-173

1.31e-36

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

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 132.48 E-value: 1.31e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   70 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLI 147
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1907161258  148 QEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

1-171

4.52e-36

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: 134.32 E-value: 4.52e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEdpITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNW 78
Cdd:cd14552    33 MIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS--VSSGDITVELKDQTDYEDYTLRDFLVTKgkGGSTRTVRQFHFHGW 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 157
Cdd:cd14552   111 PEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHM 187

                         170
                  ....*....|....
gi 1907161258 158 VQTKEQYELVHRAI 171
Cdd:cd14552   188 VQTLEQYEFCYKVV 201

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

1-173

6.00e-36

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

Pssm-ID: 350394 [Multi-domain] Cd Length: 208 Bit Score: 134.49 E-value: 6.00e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWP-----LYGEDPITFAPFKISCEneqartDYFIRTLLLE--FQNESRRLYQF 73
Cdd:cd14546    34 MIWEQGCVVIVMLTRLQENGVKQCARYWPeegseVYHIYEVHLVSEHIWCD------DYLVRSFYLKnlQTSETRTVTQF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQ 153
Cdd:cd14546   108 HFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQ 185

                         170       180
                  ....*....|....*....|
gi 1907161258 154 RHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14546   186 RPGMVKTKDQFEFVLTAVAE 205

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

1-169

7.99e-36

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: 134.45 E-value: 7.99e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMgRKKCERYWPLygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14547    60 MVWQEKTPIIVMITNLTEA-KEKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDM---ISLMRKYQEHEDvPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHS 156
Cdd:cd14547   137 HKTPEAAQPLLSLvqeVEEARQTEPHRG-PIVVHCSAGIGRTGCFIATSIGCQQLREeGVV----DVLGIVCQLRLDRGG 211

                         170
                  ....*....|...
gi 1907161258 157 AVQTKEQYELVHR 169
Cdd:cd14547   212 MVQTAEQYEFVHR 224

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

1-171

1.55e-35

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

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 133.12 E-value: 1.55e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNW 78
Cdd:cd14555    33 MVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVETEPLAEYVVRTFALERRgyHEIREVRQFHFTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14555   110 PDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMV 186

                         170
                  ....*....|...
gi 1907161258 159 QTKEQYELVHRAI 171
Cdd:cd14555   187 QTEEQYIFIHDAI 199

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

1-177

1.86e-35

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: 133.15 E-value: 1.86e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNW 78
Cdd:cd14601    38 MTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQVTCHSEEGNPAYVFREMTLTNLekNESRPLTQIQYIAW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14601   117 PDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVLITMETAMCLIECN---QPVYPLDIVRTMRDQRAMMI 193

                         170
                  ....*....|....*....
gi 1907161258 159 QTKEQYELVHRAIAQLFEK 177
Cdd:cd14601   194 QTPSQYRFVCEAILKVYEE 212

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1-177

2.18e-35

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: 132.84 E-value: 2.18e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpITFAPFKISCENEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNW 78
Cdd:cd14541    38 MVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGET-MQFGNLQITCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14541   117 PDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVLITMETAMCLIEAN---EPVYPLDIVRTMRDQRAMLI 193

                         170
                  ....*....|....*....
gi 1907161258 159 QTKEQYELVHRAIAQLFEK 177
Cdd:cd14541   194 QTPSQYRFVCEAILRVYEE 212

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

1-171

1.82e-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: 131.11 E-value: 1.82e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWP-LYGEDPITFAPFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYVN 77
Cdd:cd14597    62 MVWEQKSTVIAMMTQEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSA 157
Cdd:cd14597   142 WPDHDTPSQPEQLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGM 216

                         170
                  ....*....|....
gi 1907161258 158 VQTKEQYELVHRAI 171
Cdd:cd14597   217 VQTEDQYIFCYQVI 230

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

1-176

3.03e-34

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: 131.54 E-value: 3.03e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPiTFAPFKISCENEQARTDYFIRTLLLEFQNES---RRLYQFHYVN 77
Cdd:cd14606    86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLS 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRH 155
Cdd:cd14606   165 WPDHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRS 244

                         170       180
                  ....*....|....*....|.
gi 1907161258 156 SAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14606   245 GMVQTEAQYKFIYVAIAQFIE 265

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

1-163

8.20e-34

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: 129.05 E-value: 8.20e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITF--APFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYV 76
Cdd:cd14545    58 MVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYT 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDHDVPSSFDSILDMISLMRkyqEH----EDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKiPEEFNVFNLIQEMR 151
Cdd:cd14545   138 TWPDFGVPESPAAFLNFLQKVR---ESgslsSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGN-PSSVDVKKVLLEMR 213

                         170
                  ....*....|..
gi 1907161258 152 TQRHSAVQTKEQ 163
Cdd:cd14545   214 KYRMGLIQTPDQ 225

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

1-171

2.02e-33

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: 128.08 E-value: 2.02e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLyGEDPITFAPFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYVNW 78
Cdd:cd14619    59 MIWEQQSSTIVMLTNCMEAGRVKCEHYWPL-DYTPCTYGHLRVTVVSEEVMENWTVREFLLKqvEEQKTLSVRHFHFTAW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHS 156
Cdd:cd14619   138 PDHGVPSSTDTLLAFRRLLRQWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPL 214

                         170
                  ....*....|....*
gi 1907161258 157 AVQTKEQYELVHRAI 171
Cdd:cd14619   215 MVQTESQYVFLHQCI 229

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1-164

2.21e-33

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: 127.63 E-value: 2.21e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNW 78
Cdd:cd14615    58 MVWEKNVYAIVMLTKCVEQGRTKCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHS 156
Cdd:cd14615   136 PDHGVPETTDLLINFRHLVREYmkQNPPNSPILVHCSAGVGRTGTFIAID---RLIYQIENENVVDVYGIVYDLRMHRPL 212


                  ....*...
gi 1907161258 157 AVQTKEQY 164
Cdd:cd14615   213 MVQTEDQY 220

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

1-173

3.14e-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: 127.83 E-value: 3.14e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNW 78
Cdd:cd14630    65 MIWQENSASVVMVTNLVEVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSW 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMV 218

                         170
                  ....*....|....*
gi 1907161258 159 QTKEQYELVHRAIAQ 173
Cdd:cd14630   219 QTEEQYVFVHDAILE 233

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1-173

3.17e-33

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: 127.19 E-value: 3.17e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYG--EDPITFAPFKISCENEQARTDYFIRTLLLEFQNE--SRRLYQFHYV 76
Cdd:cd14540    35 MVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgeHDALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDHDVPSSFDSILDMISLMRKYQEH--EDV-------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLI 147
Cdd:cd14540   115 DWPDHGCPEDVSGFLDFLEEINSVRRHtnQDVaghnrnpPTLVHCSAGVGRTGVVILADLMLYCLDHN---EELDIPRVL 191

                         170       180
                  ....*....|....*....|....*.
gi 1907161258 148 QEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14540   192 ALLRHQRMLLVQTLAQYKFVYNVLIQ 217

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

1-171

3.65e-33

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: 127.51 E-value: 3.65e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNW 78
Cdd:cd14553    65 MVWEQRSATIVMMTKLEERSRVKCDQYWPTRGTE--TYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAW 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14553   143 PDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKT---VDIYGHVTCLRAQRNYMV 219

                         170
                  ....*....|...
gi 1907161258 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

6.71e-33

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: 125.86 E-value: 6.71e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL----------EFQNESRRL 70
Cdd:cd17668    33 MIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  71 YQFHYVNWPDHDVPssfDSILDMISLMRKY---QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLI 147
Cdd:cd17668   111 TQYHYTQWPDMGVP---EYTLPVLTFVRKAsyaKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFL 184

                         170       180
                  ....*....|....*....|....
gi 1907161258 148 QEMRTQRHSAVQTKEQYELVHRAI 171
Cdd:cd17668   185 KHIRSQRNYLVQTEEQYVFIHDAL 208

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

1-171

1.18e-32

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: 126.16 E-value: 1.18e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14614    74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWP-FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPS--SFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14614   153 HGVPTanAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRSYRMSMV 229

                         170
                  ....*....|...
gi 1907161258 159 QTKEQYELVHRAI 171
Cdd:cd14614   230 QTEEQYIFIHQCV 242

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

1-173

7.79e-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: 123.23 E-value: 7.79e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEdpITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNW 78
Cdd:cd14623    58 MIWEWKSCSIVMLTELEERGQEKCAQYWPSDGS--VSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 157
Cdd:cd14623   136 PEVGIPSDGKGMINIIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHM 212

                         170
                  ....*....|....*.
gi 1907161258 158 VQTKEQYELVHRAIAQ 173
Cdd:cd14623   213 VQTLEQYEFCYKVVQE 228

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1-170

8.30e-32

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: 123.79 E-value: 8.30e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPL--------YGEDPITfapfkiscenEQARTDYFIRtlllEFQ------NE 66
Cdd:cd14554    68 MLWEHNSTIIVMLTKLREMGREKCHQYWPAersaryqyFVVDPMA----------EYNMPQYILR----EFKvtdardGQ 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  67 SRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVF 144
Cdd:cd14554   134 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVF 210

                         170       180
                  ....*....|....*....|....*.
gi 1907161258 145 NLIQEMRTQRHSAVQTKEQYELVHRA 170
Cdd:cd14554   211 QTVKLLRTQRPAMVQTEDQYQFCYRA 236

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

1-173

1.70e-31

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: 122.05 E-value: 1.70e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNW 78
Cdd:cd14631    47 MIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGW 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14631   124 PDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMV 200

                         170
                  ....*....|....*
gi 1907161258 159 QTKEQYELVHRAIAQ 173
Cdd:cd14631   201 QTEEQYIFIHDAILE 215

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

1-173

2.20e-31

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: 121.31 E-value: 2.20e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRR--LYQFHYVNW 78
Cdd:cd14632    33 MVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSARheVKQFHFTSW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14632   110 PEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMI 186

                         170
                  ....*....|....*
gi 1907161258 159 QTKEQYELVHRAIAQ 173
Cdd:cd14632   187 QTEEQYIFIHDAILE 201

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

1-176

1.29e-30

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: 120.89 E-value: 1.29e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygeDPIT---FAPFKISCENEQARTDYFIRTLLLEF---QNESRRLYQFH 74
Cdd:cd14605    73 MVFQENSRVIVMTTKEVERGKSKCVKYWP----DEYAlkeYGVMRVRNVKESAAHDYILRELKLSKvgqGNTERTVWQYH 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  75 YVNWPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRT 152
Cdd:cd14605   149 FRTWPDHGVPSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRS 228

                         170       180
                  ....*....|....*....|....
gi 1907161258 153 QRHSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14605   229 QRSGMVQTEAQYRFIYMAVQHYIE 252

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

1-173

5.23e-30

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: 119.78 E-value: 5.23e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGED-----PITFAPFKISCEneqartDYFIRTLLLEF--QNESRRLYQF 73
Cdd:cd14610   107 MVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNlyhiyEVNLVSEHIWCE------DFLVRSFYLKNlqTNETRTVTQF 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNllKAGKIPEEFNVFNLIQEMRTQ 153
Cdd:cd14610   181 HFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLN--KMAKGAKEIDIAATLEHLRDQ 258

                         170       180
                  ....*....|....*....|
gi 1907161258 154 RHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14610   259 RPGMVQTKEQFEFALTAVAE 278

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

1-171

8.05e-30

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: 117.03 E-value: 8.05e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNE--SRRLYQFHYVNW 78
Cdd:cd14622    34 MVWEWKCHTIVMLTELQEREQEKCVQYWP--SEGSVTHGEITIEIKNDTLLETISIRDFLVTYNQEkqTRLVRQFHFHGW 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSA 157
Cdd:cd14622   112 PEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIALS---NILERVKAEGLLDVFQTVKSLRLQRPHM 188

                         170
                  ....*....|....
gi 1907161258 158 VQTKEQYELVHRAI 171
Cdd:cd14622   189 VQTLEQYEFCYRVV 202

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

1-169

2.16e-29

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

Pssm-ID: 350464 [Multi-domain] Cd Length: 224 Bit Score: 116.16 E-value: 2.16e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygED--PIT-FAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVN 77
Cdd:cd14616    59 MVWETRAKTIVMLTQCFEKGRIRCHQYWP---EDnkPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSA 157
Cdd:cd14616   136 WPEHGVPESSAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHINDHDFVDIYGLVAELRSERMCM 212

                         170
                  ....*....|..
gi 1907161258 158 VQTKEQYELVHR 169
Cdd:cd14616   213 VQNLAQYIFLHQ 224

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

1-165

3.83e-29

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: 114.80 E-value: 3.83e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWplyGEDPITFAPFKISCENEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNW 78
Cdd:cd14558    33 MIFQKKVKVIVMLTELKEGDQEQCAQYW---GDEKKTYGDIEVELKDTEKSPTYTVRVFEITHLKrkDSRTVYQYQYHKW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQE------HEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRT 152
Cdd:cd14558   110 KGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRK 186

                         170
                  ....*....|...
gi 1907161258 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

4.43e-29

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: 114.62 E-value: 4.43e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLLEFQNES------RRLYQFH 74
Cdd:cd14551    33 MIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDTVVLVDYTTRKFCIQKVNRGigekrvRLVTQFH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  75 YVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQ 153
Cdd:cd14551   111 FTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAeGKV----DVFGFVSRIRQQ 186

                         170
                  ....*....|....*.
gi 1907161258 154 RHSAVQTKEQYELVHR 169
Cdd:cd14551   187 RSQMVQTDMQYVFIYQ 202

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

1-173

8.09e-29

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: 116.28 E-value: 8.09e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITF--APFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYV 76
Cdd:cd14608    83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDHDVPSSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQR 154
Cdd:cd14608   163 TWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFR 242

                         170
                  ....*....|....*....
gi 1907161258 155 HSAVQTKEQYELVHRAIAQ 173
Cdd:cd14608   243 MGLIQTADQLRFSYLAVIE 261

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1-170

8.52e-29

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: 116.75 E-value: 8.52e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRtlllEFQ------NESRRLYQFH 74
Cdd:cd14629   115 MLWEHNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTIRQFQ 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  75 YVNWPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14629   189 FTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRT 265

                         170
                  ....*....|....*...
gi 1907161258 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14629   266 QRPAMVQTEDQYQLCYRA 283

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1-170

9.73e-29

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: 116.37 E-value: 9.73e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRtlllEFQ------NESRRLYQFH 74
Cdd:cd14628   114 MLWEHNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQ 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  75 YVNWPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14628   188 FTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRT 264

                         170
                  ....*....|....*...
gi 1907161258 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14628   265 QRPAMVQTEDQYQFCYRA 282

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

1-173

1.99e-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: 115.14 E-value: 1.99e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNW 78
Cdd:cd14633   102 MVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGW 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 158
Cdd:cd14633   179 PDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMV 255

                         170
                  ....*....|....*
gi 1907161258 159 QTKEQYELVHRAIAQ 173
Cdd:cd14633   256 QTEEQYVFIHDAILE 270

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

1-173

6.83e-28

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: 113.59 E-value: 6.83e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWP-----LYGEDPITFAPFKISCEneqartDYFIRTLLLEF--QNESRRLYQF 73
Cdd:cd14609   105 MVWENGCTVIVMLTPLVEDGVKQCDRYWPdegssLYHIYEVNLVSEHIWCE------DFLVRSFYLKNvqTQETRTLTQF 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQ 153
Cdd:cd14609   179 HFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQ 256

                         170       180
                  ....*....|....*....|
gi 1907161258 154 RHSAVQTKEQYELVHRAIAQ 173
Cdd:cd14609   257 RPGMVRTKDQFEFALTAVAE 276

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

1-177

1.00e-27

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: 113.02 E-value: 1.00e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlygeDP---ITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHY 75
Cdd:cd14600   101 VVWEQKLSLIVMLTTLTERGRTKCHQYWP----DPpdvMEYGGFRVQCHSEDCTIAYVFREMLLTNtqTGEERTVTHLQY 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  76 VNWPDHDVPSSFDSILDMISLMRKyQEHEDVPICIHCSAGCGRTGAICAIDYTWNLlkagkIPEEFNVFNL--IQEMRTQ 153
Cdd:cd14600   177 VAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCL-----TERNQPVYPLdiVRKMRDQ 250

                         170       180
                  ....*....|....*....|....
gi 1907161258 154 RHSAVQTKEQYELVHRAIAQLFEK 177
Cdd:cd14600   251 RAMMVQTSSQYKFVCEAILRVYEE 274

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

1-173

1.10e-27

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: 112.82 E-value: 1.10e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNW 78
Cdd:cd14626   103 MVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE--TYGMIQVTLLDTVELATYSVRTFALykNGSSEKREVRQFQFMAW 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14626   181 PDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMV 257

                         170
                  ....*....|....*
gi 1907161258 159 QTKEQYELVHRAIAQ 173
Cdd:cd14626   258 QTEDQYIFIHEALLE 272

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1-173

1.30e-27

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: 112.82 E-value: 1.30e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRTLLLE--------------FQNE 66
Cdd:cd17667    91 MIWEQNTGIIVMITNLVEKGRRKCDQYWP--TENSEEYGNIIVTLKSTKIHACYTVRRFSIRntkvkkgqkgnpkgRQNE 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  67 sRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNL 146
Cdd:cd17667   169 -RTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGF 244

                         170       180
                  ....*....|....*....|....*..
gi 1907161258 147 IQEMRTQRHSAVQTKEQYELVHRAIAQ 173
Cdd:cd17667   245 LKHIRTQRNYLVQTEEQYIFIHDALLE 271

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

1-173

1.62e-27

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: 111.47 E-value: 1.62e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEmGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14612    79 MVWQEECPIIVMITKLKE-KKEKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPD 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISlmrKYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRH 155
Cdd:cd14612   155 HQTPESAGPLLRLVA---EVEESRQTaaspgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRG 228

                         170
                  ....*....|....*...
gi 1907161258 156 SAVQTKEQYELVHRAIAQ 173
Cdd:cd14612   229 GMIQTSEQYQFLHHTLAL 246

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1-168

3.47e-27

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: 109.40 E-value: 3.47e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNW 78
Cdd:cd14539    34 MVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQSVRTTPTHVERIISIQHkdTRLSRSVVHLQFTTW 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGK-IPeefNVFNLIQEMRTQR 154
Cdd:cd14539   114 PELGLPDSPNPLLRFIEEVHSHYLQQRslqTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNgIP---DLPQLVRKMRQQR 190

                         170
                  ....*....|....
gi 1907161258 155 HSAVQTKEQYELVH 168
Cdd:cd14539   191 KYMLQEKEHLKFCY 204

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

1-171

3.92e-27

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: 110.03 E-value: 3.92e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLyGEDPITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNW 78
Cdd:cd14618    59 LVWEQQVCNIIMLTVGMENGRVLCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLwhEDLRKERRVKHLHYTAW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKY-QEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHS 156
Cdd:cd14618   138 PDHGIPESTSSLMAFRELVREHvQATKGKgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKV---VDVFNTVYILRMHRYL 214

                         170
                  ....*....|....*
gi 1907161258 157 AVQTKEQYELVHRAI 171
Cdd:cd14618   215 MIQTLSQYIFLHSCI 229

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

1-169

4.81e-27

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: 108.76 E-value: 4.81e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNE---SRRLYQFHYVN 77
Cdd:cd14557    33 MIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEEKICPDYIIRKLNINNKKEkgsGREVTHIQFTS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHS 156
Cdd:cd14557   113 WPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAeGRV----DVYGYVVKLRRQRCL 188

                         170
                  ....*....|...
gi 1907161258 157 AVQTKEQYELVHR 169
Cdd:cd14557   189 MVQVEAQYILIHQ 201

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1-170

5.28e-27

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: 111.36 E-value: 5.28e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRtlllEFQ------NESRRLYQFH 74
Cdd:cd14627   115 MLWENNSTIVVMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQ 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  75 YVNWPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14627   189 FTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRT 265

                         170
                  ....*....|....*...
gi 1907161258 153 QRHSAVQTKEQYELVHRA 170
Cdd:cd14627   266 QRPAMVQTEDEYQFCYQA 283

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

1-169

1.14e-26

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: 108.47 E-value: 1.14e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLyGEDPITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLY-QFHYVN 77
Cdd:cd14617    59 MVWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRLVrHFHYTV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRH 155
Cdd:cd14617   138 WPDHGVPETTQSLIQFVRTVRDYinRTPGSGPTVVHCSAGVGRTGTFIALD---RILQQLDSKDSVDIYGAVHDLRLHRV 214

                         170
                  ....*....|....
gi 1907161258 156 SAVQTKEQYELVHR 169
Cdd:cd14617   215 HMVQTECQYVYLHQ 228

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

1-176

1.80e-24

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: 101.98 E-value: 1.80e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYG--EDPITFAPFKISCENEQ-----ARTDYFIRTLLlefQNESRRLYQF 73
Cdd:cd14598    35 MVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKITTRFRTdsgcyATTGLKIKHLL---TGQERTVWHL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDHDVPSS---FDSILDMISLMRKYQ------EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVF 144
Cdd:cd14598   112 QYTDWPEHGCPEDlkgFLSYLEEIQSVRRHTnstidpKSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVL 191

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907161258 145 NLiqeMRTQRHSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14598   192 DM---LRQQRMMMVQTLSQYTFVYKVLIQFLK 220

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

1-171

2.05e-24

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: 103.12 E-value: 2.05e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAP--FKISCENEQARTDYFIRTLLLEFQN--ESRRLYQFHYV 76
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDHDVPSSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDyTWNLLKAGKIPEEFNVFNLIQEMRTQR 154
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGslSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYR 240

                         170
                  ....*....|....*..
gi 1907161258 155 HSAVQTKEQYELVHRAI 171
Cdd:cd14607   241 MGLIQTPDQLRFSYMAV 257

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

1-171

3.00e-24

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: 101.56 E-value: 3.00e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGedPITFAPFKISCENEQARTDYFIRTLLLEFQ-----NESRRLYQFHY 75
Cdd:cd14620    57 MVWEQKSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  76 VNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRH 155
Cdd:cd14620   135 TSWPDFGVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRP 211

                         170
                  ....*....|....*.
gi 1907161258 156 SAVQTKEQYELVHRAI 171
Cdd:cd14620   212 QMVQTDMQYSFIYQAL 227

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1-173

3.30e-24

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 102.86 E-value: 3.30e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVM--ACREFEMGRKKCERYWPLYGEdpitFAPFKISCE---NEQARTDYFIRTLLLEFQN---ESRRLYQ 72
Cdd:COG5599    96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  73 FHYVNWPDHDVPSSfDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQE 149
Cdd:COG5599   172 LHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVID 249

                         170       180
                  ....*....|....*....|....*.
gi 1907161258 150 MRTQR-HSAVQTKEQY-ELVHRAIAQ 173
Cdd:COG5599   250 MRTSRnGGMVQTSEQLdVLVKLAEQQ 275

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

1-173

1.27e-23

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: 101.32 E-value: 1.27e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNW 78
Cdd:cd14625   109 MVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE--TYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQFQFTAW 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 158
Cdd:cd14625   187 PDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRSQRNYMV 263

                         170
                  ....*....|....*
gi 1907161258 159 QTKEQYELVHRAIAQ 173
Cdd:cd14625   264 QTEDQYSFIHDALLE 278

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

1-168

2.41e-23

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: 98.25 E-value: 2.41e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMaCREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL----EFQNESRRLYQFHYV 76
Cdd:cd14556    33 LVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEGSG--TYGPIQVEFVSTTIDEDVISRIFRLqnttRPQEGYRMVQQFQFL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDH-DVPSSFDSILDMISLMRKYQEH-EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQR 154
Cdd:cd14556   110 GWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHR 186

                         170
                  ....*....|....
gi 1907161258 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

1.98e-22

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: 98.17 E-value: 1.98e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGedPITFAPFKISCENEQARTDYFIRTLLLE------FQNESRRLYQFH 74
Cdd:cd14621   114 MIWEQNTATIVMVTNLKERKECKCAQYWPDQG--CWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvtNKKPQRLITQFH 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  75 YVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQR 154
Cdd:cd14621   192 FTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQR 268

                         170
                  ....*....|....*....
gi 1907161258 155 HSAVQTKEQYELVHRAIAQ 173
Cdd:cd14621   269 CQMVQTDMQYVFIYQALLE 287

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

1-173

2.24e-22

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: 97.88 E-value: 2.24e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLLeFQN---ESRRLYQFHYVN 77
Cdd:cd14624   109 MIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE--TYGLIQVTLLDTVELATYCVRTFAL-YKNgssEKREVRQFQFTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSA 157
Cdd:cd14624   186 WPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRAQRNYM 262

                         170
                  ....*....|....*.
gi 1907161258 158 VQTKEQYELVHRAIAQ 173
Cdd:cd14624   263 VQTEDQYIFIHDALLE 278

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

1-172

5.08e-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: 96.08 E-value: 5.08e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGrKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPD 80
Cdd:cd14613    89 MVWQERSPIIVMITNIEEMN-EKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPD 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  81 HDVPSSFDSILDMISLM---RKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 157
Cdd:cd14613   165 QKTPDNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGM 241

                         170
                  ....*....|....*
gi 1907161258 158 VQTKEQYELVHRAIA 172
Cdd:cd14613   242 IQTCEQYQFVHHVLS 256

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

1-168

3.12e-21

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: 92.67 E-value: 3.12e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGrKKCERYWP----LYGEDPITFAPFKiSCENeqartdYFIRTLLLEFQNESRRLYQFHYV 76
Cdd:cd14611    63 MVWQEDSPVIVMITKLKEKN-EKCVLYWPekrgIYGKVEVLVNSVK-ECDN------YTIRNLTLKQGSQSRSVKHYWYT 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDHDVPSSFDSILdmiSLMRKYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMR 151
Cdd:cd14611   135 SWPDHKTPDSAQPLL---QLMLDVEEDRLAspgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGV---VDVLSIVCQLR 208

                         170
                  ....*....|....*..
gi 1907161258 152 TQRHSAVQTKEQYELVH 168
Cdd:cd14611   209 VDRGGMVQTSEQYEFVH 225

PHA02738

hypothetical protein; Provisional

1-171

3.77e-21

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 94.99 E-value: 3.77e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNES-RRLYQFHYVNWP 79
Cdd:PHA02738  109 MLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  80 DHDVPSSFDSILDMISLMRKYQE--HEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNL 146
Cdd:PHA02738  189 DHDVPKNTSEFLNFVLEVRQCQKelAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT---VSIPSI 265

                         170       180
                  ....*....|....*....|....*
gi 1907161258 147 IQEMRTQRHSAVQTKEQYELVHRAI 171
Cdd:PHA02738  266 VSSIRNQRYYSLFIPFQYFFCYRAV 290

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

1-176

5.17e-21

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: 93.91 E-value: 5.17e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYG--EDPITFAPFKISCENEQ-----ARTDYFIRTLLlefQNESRRLYQF 73
Cdd:cd14599   101 MVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskHSSATYGKFKVTTKFRTdsgcyATTGLKVKHLL---SGQERTVWHL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV----------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNV 143
Cdd:cd14599   178 QYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHN---EKVEV 254

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907161258 144 FNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 176
Cdd:cd14599   255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287

PHA02747

protein tyrosine phosphatase; Provisional

1-168

5.33e-21

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 94.30 E-value: 5.33e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMAC-REFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYfIRTLLL---EFQNESRRLYQFHYV 76
Cdd:PHA02747  112 AVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLIEitdKILKDSRKISHFQCS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDHDVPSS---FDSILDMISLMRK-----YQEHEDV--PICIHCSAGCGRTGAICAIDYTWN-LLKAGKIPEEFNVFN 145
Cdd:PHA02747  191 EWFEDETPSDhpdFIKFIKIIDINRKksgklFNPKDALlcPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAICLAKTAEK 270

                         170       180
                  ....*....|....*....|...
gi 1907161258 146 LiqemRTQRHSAVQTKEQYELVH 168
Cdd:PHA02747  271 I----REQRHAGIMNFDDYLFIQ 289

PHA02742

protein tyrosine phosphatase; Provisional

1-164

1.10e-20

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 93.14 E-value: 1.10e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRL--YQFHYVNW 78
Cdd:PHA02742  112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDW 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  79 PDHDVPSSFDSILDMISLMRKYQEHEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLI 147
Cdd:PHA02742  192 PHGGLPRDPNKFLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIV 268

                         170
                  ....*....|....*..
gi 1907161258 148 QEMRTQRHSAVQTKEQY 164
Cdd:PHA02742  269 RDLRKQRHNCLSLPQQY 285

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

1-164

3.00e-20

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: 89.45 E-value: 3.00e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRK-KCERYWPLYGEDPITFApfKISCENEQARTDYFIRTL-LLEFQ-NES----RRLYQF 73
Cdd:cd17658    35 MVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFG--RISVTNKKLKHSQHSITLrVLEVQyIESeeppLSVLHI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDHDVPSSFDSILDMISlmRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRT 152
Cdd:cd17658   113 QYPEWPDHGVPKDTRSVRELLK--RLYGIPPSAgPIVVHCSAGIGRTGAYCTIHNTIRRILEGDM-SAVDLSKTVRKFRS 189

                         170
                  ....*....|..
gi 1907161258 153 QRHSAVQTKEQY 164
Cdd:cd17658   190 QRIGMVQTQDQY 201

PHA02746

protein tyrosine phosphatase; Provisional

1-171

6.13e-18

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 85.47 E-value: 6.13e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVmACREFEMGRKKCERYWPLYGEDPITFAPF--KISCENEQARtdyFIRTLLL---EFQNESRRLYQFHY 75
Cdd:PHA02746  132 LISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFvaKILDIIEELS---FTKTRLMitdKISDTSREIHHFWF 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  76 VNWPDHDVPSSFDSILDMISL-------MRKYQEHEDV---PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFN 145
Cdd:PHA02746  208 PDWPDNGIPTGMAEFLELINKvneeqaeLIKQADNDPQtlgPIVVHCSAGIGRAGTFCAID---NALEQLEKEKEVCLGE 284

                         170       180
                  ....*....|....*....|....*.
gi 1907161258 146 LIQEMRTQRHSAVQTKEQYELVHRAI 171
Cdd:PHA02746  285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

1-168

1.10e-14

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: 73.13 E-value: 1.10e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACrefEMGRKK-CERYWP-----LYGEDPITFapfkISCENEQARTDYFIRTLLLEFQNESRRLYQ-F 73
Cdd:cd14634    33 LVFDYNCSSVVMLN---EMDAAQlCMQYWPektscCYGPIQVEF----VSADIDEDIISRIFRICNMARPQDGYRIVQhL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWPDH-DVPSSFDSILDMISLMRKYQEHEDVP---ICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQE 149
Cdd:cd14634   106 QYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGRegrTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKT 182

                         170
                  ....*....|....*....
gi 1907161258 150 MRTQRHSAVQTKEQYELVH 168
Cdd:cd14634   183 LRNNKSNMVETLEQYKFVY 201

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

1-168

1.94e-14

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: 72.75 E-value: 1.94e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMaCREFEMGrKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRTL----LLEFQNESRRLYQFHYV 76
Cdd:cd14636    33 LVYDYGCTSIVM-LNEVDLA-QGCPQYWP--EEGMLRYGPIQVECMSCSMDCDVISRIFricnLTRPQEGYLMVQQFQYL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  77 NWPDH-DVPSSFDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRT 152
Cdd:cd14636   109 GWASHrEVPGSKRSFLKLILQVEKWQEECDEgegRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRN 185

                         170
                  ....*....|....*.
gi 1907161258 153 QRHSAVQTKEQYELVH 168
Cdd:cd14636   186 SKPNMVETPEQYRFCY 201

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

1-171

2.30e-10

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: 60.78 E-value: 2.30e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCErYWPlYGEDPITFAPFKISCENEQAR-----TDYFIRTLLLEFQNESRRLYQFHY 75
Cdd:cd17669    33 MIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLIAEEHKclsneEKLIIQDFILEATQDDYVLEVRHF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  76 V--NWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQ 153
Cdd:cd17669   111 QcpKWPNPDSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPG 188

                         170
                  ....*....|....*...
gi 1907161258 154 RHSAVqtkEQYELVHRAI 171
Cdd:cd17669   189 VFTDI---EQYQFLYKAI 203

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

72-169

6.90e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 57.67 E-value: 6.90e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  72 QFHYVNWPDHDVPS--SFDSILDMIslMRKYQEHEdvPICIHCSAGCGRTGAICAidyTWnLLKAGKIPEEfnvfnLIQE 149
Cdd:COG2453    49 EYLHLPIPDFGAPDdeQLQEAVDFI--DEALREGK--KVLVHCRGGIGRTGTVAA---AY-LVLLGLSAEE-----ALAR 115

                          90       100
                  ....*....|....*....|
gi 1907161258 150 MRTQRHSAVQTKEQYELVHR 169
Cdd:COG2453   116 VRAARPGAVETPAQRAFLER 135

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

24-164

2.91e-09

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: 57.61 E-value: 2.91e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  24 CERYWPLYGEDpiTFAPFKISCENEQARTDyfIRTLLLEFQNESRR------LYQFHYVNW-PDHDVPSSFDSILDMISL 96
Cdd:cd14637    57 CLQYWPEPGLQ--QYGPMEVEFVSGSADED--IVTRLFRVQNITRLqeghlmVRHFQFLRWsAYRDTPDSKKAFLHLLAS 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161258  97 MRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 164
Cdd:cd14637   133 VEKWQrESGEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQY 198

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

24-168

5.38e-09

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: 56.62 E-value: 5.38e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  24 CERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL----EFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLMR 98
Cdd:cd14635    54 CPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907161258  99 KYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 168
Cdd:cd14635   132 KWQEEYNGgegRTVVHCLNGGGRSGTFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

73-166

3.06e-08

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: 54.71 E-value: 3.06e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  73 FHYVNWPDHDVPSSFDSIL--DMISLMRK--------------YQEHEDVPIcIHCSAGCGRTGAICAIdytwnlLKAGK 136
Cdd:cd14559   121 VHVTNWPDHTAISSEGLKElaDLVNKSAEekrnfykskgssaiNDKNKLLPV-IHCRAGVGRTGQLAAA------MELNK 193

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907161258 137 IPEEFNVFNLIQEMRTQR-HSAVQTKEQYEL 166
Cdd:cd14559   194 SPNNLSVEDIVSDMRTSRnGKMVQKDEQLDT 224

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

63-168

3.11e-08

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: 54.28 E-value: 3.11e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  63 FQNESRRLYQFhyvNWPDHDVPSsFDSILDMISLMRKYQEhEDVPICIHCSAGCGRTG-AICAIdytwnLLKAGKIPEEf 141
Cdd:cd14506    72 FMRAGIYFYNF---GWKDYGVPS-LTTILDIVKVMAFALQ-EGGKVAVHCHAGLGRTGvLIACY-----LVYALRMSAD- 140

                          90       100
                  ....*....|....*....|....*..
gi 1907161258 142 nvfNLIQEMRTQRHSAVQTKEQYELVH 168
Cdd:cd14506   141 ---QAIRLVRSKRPNSIQTRGQVLCVR 164

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

88-169

1.65e-07

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 50.04 E-value: 1.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  88 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwnLLKAGKIPeefnVFNLIQEMRTQR-HSAVQTKEQYEL 166
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACY----LVLLGGMS----AEEAVRIVRLIRpGGIPQTIEQLDF 110


                  ...
gi 1907161258 167 VHR 169
Cdd:cd14494   111 LIK 113

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

1-171

2.98e-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: 51.60 E-value: 2.98e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEMGRKKCErYWPlYGEDPITFAPFKIS-------C-ENEQartDYFIRTLLLEFQNESRRLYQ 72
Cdd:cd17670    33 MIWDHNAQIIVMLPDNQGLAEDEFV-YWP-SREESMNCEAFTVTliskdrlClSNEE---QIIIHDFILEATQDDYVLEV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  73 FHYV--NWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEM 150
Cdd:cd17670   108 RHFQcpKWPNPDAPIS--STFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLM 185

                         170       180
                  ....*....|....*....|.
gi 1907161258 151 RTQRHSAVqtkEQYELVHRAI 171
Cdd:cd17670   186 RPGVFTDI---EQYQFLYKAM 203

PHA02740

protein tyrosine phosphatase; Provisional

1-172

4.50e-07

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 51.89 E-value: 4.50e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVMACREFEmgrKKC-ERYWPLYGEDPITFAPFKISCEnEQARTDYFIRTLLL--EFQNESRRLYQFHYVN 77
Cdd:PHA02740  110 ALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETL-EIIIKPHFNLTLLSltDKFGQAQKISHFQYTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  78 WP----DHDVPSSFD---SILDMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQE 149
Cdd:PHA02740  186 WPadgfSHDPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFDKTGM---LSIANALKK 262

                         170       180
                  ....*....|....*....|...
gi 1907161258 150 MRTQRHSAVQTKEQYELVHRAIA 172
Cdd:PHA02740  263 VRQKKYGCMNCLDDYVFCYHLIA 285

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

70-167

6.90e-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: 49.20 E-value: 6.90e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  70 LYQFHYVNW-----PDHDVPSsFDSILDMISLMrKYQEHEDVPICIHCSAGCGRTGAICAIdYtwnLLKAGKIPEEfnvf 144
Cdd:cd14504    44 SDTCPGLRYhhipiEDYTPPT-LEQIDEFLDIV-EEANAKNEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV---- 113

                          90       100
                  ....*....|....*....|...
gi 1907161258 145 NLIQEMRTQRHSAVQTKEQYELV 167
Cdd:cd14504   114 DAINEIRRIRPGSIETSEQEKFV 136

PTP_PTEN-like

cd14497

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...

72-124

3.27e-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: 47.57 E-value: 3.27e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907161258  72 QFHYVNWPDHDVPSsFDSILDMISLMRKY-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

3.39e-06

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: 48.09 E-value: 3.39e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258   1 MIWEYNVVIIVM--ACREFEmgrkKCERYWPLyGEDPITFAPFKISCENE-----QARTDYFIRTLLLE-----FQNESR 68
Cdd:cd14550    33 MIWDHNSQTIVMltDNELNE----DEPIYWPT-KEKPLECETFKVTLSGEdhsclSNEIRLIVRDFILEstqddYVLEVR 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161258  69 rlyQFHYVNWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAI 125
Cdd:cd14550   108 ---QFQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

PTP_VSP_TPTE

cd14510

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...

67-168

1.25e-04

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: 43.12 E-value: 1.25e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  67 SRRLYQ---FHY----VNWPDHDVPSsfdsILDMISLMRKYQEH----EDVPICIHCSAGCGRTG-AICAidytWnLLKA 134
Cdd:cd14510    63 SERGYDpkyFHNrverVPIDDHNVPT----LDEMLSFTAEVREWmaadPKNVVAIHCKGGKGRTGtMVCA----W-LIYS 133

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907161258 135 GKIPEEFNVFNLIQEMRT-----QRHSAVQTKEQYELVH 168
Cdd:cd14510   134 GQFESAKEALEYFGERRTdksvsSKFQGVETPSQSRYVG 172

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

54-169

1.99e-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: 1.99e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  54 YFIRTLLLEFQneSRRLYQFHYVnWPDHDVPSSFDSIL----DMISLMRKYQEhedvpICIHCSAGCGRTGAICAIdytw 129
Cdd:cd14505    59 LGVPDLLEQYQ--QAGITWHHLP-IPDGGVPSDIAQWQelleELLSALENGKK-----VLIHCKGGLGRTGLIAAC---- 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907161258 130 NLLKAG-KIPEEfnvfNLIQEMRTQRHSAVQTKEQYELVHR 169
Cdd:cd14505   127 LLLELGdTLDPE----QAIAAVRALRPGAIQTPKQENFLHQ 163

TpbA-like

cd14529

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...

53-125

1.93e-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: 39.28 E-value: 1.93e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  53 DYFIRTLL-LEFQNESRRLY-------QFHYVN------WPDHDVPSSFDSILDMISlmrkyqehEDVPICIHCSAGCGR 118
Cdd:cd14529    31 KLGIKTVIdLRGADERAASEeaaakidGVKYVNlplsatRPTESDVQSFLLIMDLKL--------APGPVLIHCKHGKDR 102


                  ....*..
gi 1907161258 119 TGAICAI 125
Cdd:cd14529   103 TGLVSAL 109

PTP-IVa1

cd18537

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...

74-162

2.39e-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: 39.29 E-value: 2.39e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161258  74 HYVNWP-DHDVPSSFDSILDMISLMR-KYQEHEDVPICIHCSAGCGRTGAICAIdytwNLLKAGKIPEEfnvfnLIQEMR 151
Cdd:cd18537    64 QVLDWPfDDGAPPSNQIVDDWLNLLKvKFREEPGCCIAVHCVAGLGRAPVLVAL----ALIECGMKYED-----AVQFIR 134

                          90
                  ....*....|.
gi 1907161258 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