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Conserved domains on  [gi|20139861|sp|Q9Y2R2|]
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RecName: Full=Tyrosine-protein phosphatase non-receptor type 22; AltName: Full=Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP; AltName: Full=Lymphoid phosphatase; Short=LyP; AltName: Full=PEST-domain phosphatase; Short=PEP

Protein Classification

PTPc-N22 domain-containing protein( domain architecture ID 12998656)

PTPc-N22 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 7.85e-180

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: 514.77  E-value: 7.85e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 137 KKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 216
Cdd:cd14602  81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20139861 217 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELF 290
Cdd:cd14602 161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 7.85e-180

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: 514.77  E-value: 7.85e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 137 KKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 216
Cdd:cd14602  81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20139861 217 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELF 290
Cdd:cd14602 161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 1.60e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.12  E-value: 1.60e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861     24 FANEFLKLKRQstkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITsDEDSSYINANFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    104 GPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF--NSE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    182 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 20139861    262 IREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 5.70e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 329.97  E-value: 5.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    54 NIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   134 MGKKKCERYWAEPGEMQLEFGPFSVSCEAEKR-KSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20139861   211 DVR-CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:pfam00102 159 KVRkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVD---IFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-280 1.37e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 1.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  13 EAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNikknRYKDILPYDYSRVElslitsdEDSSYINANFIKg 92
Cdd:COG5599   5 NPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  93 VYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--KKCERYWAEPGEMqlefgpFSVSCEAEKRKSDYI 170
Cdd:COG5599  73 VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGEY------GKYEVSSELTESIQL 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 171 -----IRTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDSV---PICIHCSAGCGRTGVICA 239
Cdd:COG5599 147 rdgieARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIA 225

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 20139861 240 IDYTWMLLKDGIIPEnFSVFSLIREMRTQR-PSLVQTQEQYE 280
Cdd:COG5599 226 CLALSKSINALVQIT-LSVEEIVIDMRTSRnGGMVQTSEQLD 266
PHA02738 PHA02738
hypothetical protein; Provisional
 33-286 3.40e-41

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.54  E-value: 3.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   33 RQSTKYKADKTYPTTVAEKpKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  113 FWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE-TRTIYQFHYK 191
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  192 NWPDHDVPSSIDPILELIWDVRCYQED-------------DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSV 258
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                        250       260
                 ....*....|....*....|....*...
gi 20139861  259 FSLIREMRTQRPSLVQTQEQYELVYNAV 286
Cdd:PHA02738 263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 7.85e-180

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: 514.77  E-value: 7.85e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 137 KKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 216
Cdd:cd14602  81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20139861 217 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELF 290
Cdd:cd14602 161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-294 2.87e-167

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: 485.21  E-value: 2.87e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   2 DQREILQKFLDEAQSKKIT----KEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLIT 77
Cdd:cd14604   1 EQVEILKKFIERVQAMKSTdhngEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  78 SDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFS 157
Cdd:cd14604  81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 158 VSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14604 161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20139861 238 CAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFKRQM 294
Cdd:cd14604 241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 84-284 6.96e-144

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: 421.45  E-value: 6.96e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAE 163
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKS-DYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDY 242
Cdd:cd14542  81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20139861 243 TWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYN 284
Cdd:cd14542 161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 25-290 5.26e-127

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: 380.71  E-value: 5.26e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14603   1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEmQLEFGPFSVSCEAEKR-KSDYIIRTLKVKFNSETR 183
Cdd:cd14603  81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQE-PLQTGPFTITLVKEKRlNEEVILRTLKVTFQKESR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 184 TIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIR 263
Cdd:cd14603 160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVL 239

                       250       260
                ....*....|....*....|....*..
gi 20139861 264 EMRTQRPSLVQTQEQYELVYNAVLELF 290
Cdd:cd14603 240 EMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 1.60e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.12  E-value: 1.60e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861     24 FANEFLKLKRQstkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITsDEDSSYINANFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    104 GPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF--NSE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    182 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 20139861    262 IREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 5.70e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 329.97  E-value: 5.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    54 NIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   134 MGKKKCERYWAEPGEMQLEFGPFSVSCEAEKR-KSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20139861   211 DVR-CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:pfam00102 159 KVRkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVD---IFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 84-283 1.93e-94

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: 293.42  E-value: 1.93e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAE 163
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd00047  81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20139861 242 YTWMLLKDGiipENFSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd00047 161 ILLERLEAE---GEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 51-283 6.51e-74

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: 241.88  E-value: 6.51e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  51 KPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 130
Cdd:cd14543  26 APANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 131 EYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVkFNSET---RTIYQFHYKNWPDHDVPSSIDPILE 207
Cdd:cd14543 106 VVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEI-HNTETdesRQVTHFQFTSWPDFGVPSSAAALLD 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 208 LIWDVRCYQEdDSV--------------PICIHCSAGCGRTGVICAIDYTWMLLKD-GIIpenfSVFSLIREMRTQRPSL 272
Cdd:cd14543 185 FLGEVRQQQA-LAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDvGTL----NVMQTVRRMRTQRAFS 259

                       250
                ....*....|.
gi 20139861 273 VQTQEQYELVY 283
Cdd:cd14543 260 IQTPDQYYFCY 270
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 59-279 2.19e-72

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: 236.10  E-value: 2.19e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  59 RYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKK 138
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 139 CERYWAEpGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQED 218
Cdd:cd14548  81 CDHYWPF-DQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20139861 219 DSVPICIHCSAGCGRTGVICAIDYtwmlLKDGIIPENF-SVFSLIREMRTQRPSLVQTQEQY 279
Cdd:cd14548 160 EKGPTIVHCSAGVGRTGTFIALDR----LLQQIESEDYvDIFGIVYDLRKHRPLMVQTEAQY 217
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-286 5.00e-68

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: 225.42  E-value: 5.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  54 NIKKNRYKDILPYDYSRVELSLITSDED-SSYINANFIK------GVYGP-KAYIATQGPLSTTLLDFWRMIWEYSVLII 125
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegpTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 126 VMACMEYEMGKKKCERYWAEPGeMQLEFGPFSVSCEAEKRKSDYIIRTL---KVKFNSETRTIYQFHYKNWPDHDVPSSI 202
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEG-MQKQYGPYRVQNVSEHDTTDYTLRELqvsKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 203 DPILELIWDVRCYQE--DDSVPICIHCSAGCGRTGVICAIDytwMLL----KDGIIPEnFSVFSLIREMRTQRPSLVQTQ 276
Cdd:cd14544 160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVID---MLLdqikRKGLDCD-IDIQKTIQMVRSQRSGMVQTE 235

                       250
                ....*....|
gi 20139861 277 EQYELVYNAV 286
Cdd:cd14544 236 AQYKFIYVAV 245
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 58-283 6.48e-66

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: 218.81  E-value: 6.48e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMgK 136
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 137 KKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCY 215
Cdd:cd14547  80 EKCAQYW--PEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVeEAR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 216 QEDDSV-PICIHCSAGCGRTGVICAIDYTWMLLKdgiiPENF-SVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14547 158 QTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLR----EEGVvDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 84-283 2.12e-64

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: 214.03  E-value: 2.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIK-GVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEpGEMQLEFGPFSVSC-- 160
Cdd:cd18533   1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELvs 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 161 EAEKRKSDYIIRTLKVKF-NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd18533  80 EEENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGTF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20139861 238 CAIDyTWM-LLKDGII---PENFS---VFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd18533 160 IALD-SLLdELKRGLSdsqDLEDSedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 54-288 3.92e-64

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: 214.57  E-value: 3.92e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  54 NIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 134 MGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWD 211
Cdd:cd14553  83 RSRVKCDQYW--PTRGTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20139861 212 VRCYQEDDSVPICIHCSAGCGRTGVICAIDYtwMLlkDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14553 161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDS--ML--ERIKHEKtVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-288 9.77e-63

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: 210.65  E-value: 9.77e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  53 KNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEY 132
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 133 EMGKKKCERYWAEPGEMqleFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 210
Cdd:cd14630  82 EVGRVKCVRYWPDDTEV---YGDIKVTLIETEPLAEYVIRTFTVqkKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20139861 211 DVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14630 159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLdMAENEGVV----DIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 49-287 1.32e-62

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: 210.46  E-value: 1.32e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14554   1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14554  81 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 207 ELIWDV-RCY-QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14554 159 DFIGQVhKTKeQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                ....
gi 20139861 284 NAVL 287
Cdd:cd14554 235 RAAL 238
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 58-289 4.40e-61

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: 205.89  E-value: 4.40e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA--CMeyEMG 135
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLtnCM--EAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 136 KKKCERYWaePGEMQ-LEFGPFSVSCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 212
Cdd:cd14619  79 RVKCEHYW--PLDYTpCTYGHLRVTVVSEEVMENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLL 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20139861 213 RCY--QEDDSVPICIHCSAGCGRTGVICAIDYtwmLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLEL 289
Cdd:cd14619 157 RQWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 84-279 6.50e-61

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: 204.51  E-value: 6.50e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW--PKEGTETYGNIQVTLLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTL--------KVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTG 235
Cdd:cd14549  79 EVLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20139861 236 VICAIDYTWMLLKD-GIIpenfSVFSLIREMRTQRPSLVQTQEQY 279
Cdd:cd14549 159 TYIVIDSMLQQIQDkGTV----NVFGFLKHIRTQRNYLVQTEEQY 199
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 24-288 1.81e-59

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 203.34  E-value: 1.81e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  24 FANEFLKLKRQStkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDED--SSYINANFIKGVYGPKAYIA 101
Cdd:cd17667   1 FSEDFEEVQRCT----ADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 102 TQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV----- 176
Cdd:cd17667  77 TQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYW--PTENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkv 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 177 --------KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK 248
Cdd:cd17667 155 kkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 20139861 249 DgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd17667 235 D---KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 45-287 5.35e-59

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: 200.89  E-value: 5.35e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  45 PTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLI 124
Cdd:cd14614   3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 125 IVMACMEYEMGKKKCERYW---AEPgemqLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPS- 200
Cdd:cd14614  83 IVMLTQCNEKRRVKCDHYWpftEEP----VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTa 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 201 -SIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIREMRTQRPSLVQTQEQY 279
Cdd:cd14614 159 nAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQY 235


                ....*...
gi 20139861 280 ELVYNAVL 287
Cdd:cd14614 236 IFIHQCVQ 243
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 58-279 2.35e-58

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: 198.50  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDILPYDYSRVELSLITSDEDSsYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTDD-YINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 138 KCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 215
Cdd:cd14615  80 KCEEYW--PSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 216 --QEDDSVPICIHCSAGCGRTGVICAIDYtwmLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQY 279
Cdd:cd14615 158 mkQNPPNSPILVHCSAGVGRTGTFIAIDR---LIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 47-291 7.06e-58

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: 198.92  E-value: 7.06e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  47 TVAEKPKNIKKNRYKDILPYDYSRVELslitsDEDSSYINANFIK----GVYGPKAYIATQGPLSTTLLDFWRMIWEYSV 122
Cdd:cd14600  33 TCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 123 LIIVMACMEYEMGKKKCERYWAEPGEMqLEFGPFSVSCEAEKRKSDYIIRTLKVKfNSET---RTIYQFHYKNWPDHDVP 199
Cdd:cd14600 108 SLIVMLTTLTERGRTKCHQYWPDPPDV-MEYGGFRVQCHSEDCTIAYVFREMLLT-NTQTgeeRTVTHLQYVAWPDHGVP 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 200 SSIDPILELIWDVRCYQEdDSVPICIHCSAGCGRTGVICAIDyTWMLLkdgiIPENFSVFSL--IREMRTQRPSLVQTQE 277
Cdd:cd14600 186 DDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTME-TAMCL----TERNQPVYPLdiVRKMRDQRAMMVQTSS 259

                       250
                ....*....|....
gi 20139861 278 QYELVYNAVLELFK 291
Cdd:cd14600 260 QYKFVCEAILRVYE 273
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 53-286 1.06e-57

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 197.55  E-value: 1.06e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  53 KNIKKNRYKDILPYDYSRVELSLITSDED-SSYINANFIKGVYG--------PKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 124 IIVMACMEYEMGKKKCERYWaePGEMQL-EFGPFSVSCEAEKRKSDYIIRTLKV----KFNSEtRTIYQFHYKNWPDHDV 198
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYW--PDEYALkEYGVMRVRNVKESAAHDYILRELKLskvgQGNTE-RTVWQYHFRTWPDHGV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 199 PSSIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQ 276
Cdd:cd14605 158 PSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTE 237

                       250
                ....*....|
gi 20139861 277 EQYELVYNAV 286
Cdd:cd14605 238 AQYRFIYMAV 247
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 50-288 4.20e-57

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 196.25  E-value: 4.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  50 EKPKNIKKNRYKDILPYDYSRVELSLITSD-EDSSYINANFIKG-VYG----PKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14606  14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENSR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 124 IIVMACMEYEMGKKKCERYWAEPGeMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF---NSETRTIYQFHYKNWPDHDVPS 200
Cdd:cd14606  94 VIVMTTREVEKGRNKCVPYWPEVG-MQRAYGPYSVTNCGEHDTTEYKLRTLQVSPldnGELIREIWHYQYLSWPDHGVPS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 201 SIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQ 278
Cdd:cd14606 173 EPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQ 252

                       250
                ....*....|
gi 20139861 279 YELVYNAVLE 288
Cdd:cd14606 253 YKFIYVAIAQ 262
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 31-288 6.32e-56

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 193.34  E-value: 6.32e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  31 LKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTL 110
Cdd:cd14633  17 FKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 111 LDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMqleFGPFSVSCEAEKRKSDYIIRTLKVKFNS--ETRTIYQF 188
Cdd:cd14633  97 YDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQF 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 189 HYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIREMRT 267
Cdd:cd14633 174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLdMAEREGVV----DIYNCVRELRS 249

                       250       260
                ....*....|....*....|.
gi 20139861 268 QRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14633 250 RRVNMVQTEEQYVFIHDAILE 270
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 14-288 1.60e-55

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: 193.02  E-value: 1.60e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  14 AQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTV--AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIK 91
Cdd:cd14628  10 AYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFisANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFID 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  92 GVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYII 171
Cdd:cd14628  90 GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYIL 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 172 RTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLL 247
Cdd:cd14628 168 REFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERM 247

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 20139861 248 K-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14628 248 RyEGVV----DIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-291 2.77e-55

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: 189.46  E-value: 2.77e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANF----IKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEmQLEFGPFSVS 159
Cdd:cd14541   2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 160 CEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14541  81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 238 CAIDyTWMLLkdgiIPENFSVFSL--IREMRTQRPSLVQTQEQYELVYNAVLELFK 291
Cdd:cd14541 161 ITME-TAMCL----IEANEPVYPLdiVRTMRDQRAMLIQTPSQYRFVCEAILRVYE 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-283 4.46e-55

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: 190.05  E-value: 4.46e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  52 PKNIKKNRYKDILPYDYSRVEL-SLITSDEDSSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC 129
Cdd:cd14612  13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 130 MEYEmGKKKCERYWAEPgemQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELI 209
Cdd:cd14612  93 KLKE-KKEKCVHYWPEK---EGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLV 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 210 WDVRCYQEDDSV--PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14612 169 AEVEESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 84-288 4.56e-55

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: 188.74  E-value: 4.56e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAE-PGEMQLEFGPFSVSC 160
Cdd:cd14538   1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDsLNKPLICGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 161 EAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQedDSVPICIHCSAGCGRTGVIC 238
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKetGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVLI 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20139861 239 AIDYTWMLLKDGIipeNFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14538 159 TIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 49-288 4.57e-55

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: 191.86  E-value: 4.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14629  48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14629 128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 207 ELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14629 206 DFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DMFQTVKTLRTQRPAMVQTEDQYQLCY 281


                ....*
gi 20139861 284 NAVLE 288
Cdd:cd14629 282 RAALE 286
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-287 5.46e-55

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: 189.27  E-value: 5.46e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  53 KNIKKNRYKDILPYDYSRVELSlitsdEDSSYINANFIKGVYGPK--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 130
Cdd:cd14597   2 ENRKKNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 131 EYEMGKKKCERYWAE-PGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILE 207
Cdd:cd14597  77 EVEGGKIKCQRYWPEiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 208 LIWDVRCYQEddSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSLIREMRTQRPSLVQTQEQYELVYNAVL 287
Cdd:cd14597 157 FISYMRHIHK--SGPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 57-283 9.99e-55

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: 188.75  E-value: 9.99e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  57 KNRYKDILPYDYSRVELSLitSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKL--KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 137 KKCERYW-AEPGEMQ-LEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 212
Cdd:cd14545  79 IKCAQYWpQGEGNAMiFEDTGLKVTLLSEEDKSYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139861 213 RCYQ--EDDSVPICIHCSAGCGRTGVICAIDyTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14545 159 RESGslSSDVGPPVVHCSAGIGRSGTFCLVD-TCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 49-288 2.44e-54

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 189.56  E-value: 2.44e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14627  48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14627 128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 207 ELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14627 206 DFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDEYQFCY 281


                ....*
gi 20139861 284 NAVLE 288
Cdd:cd14627 282 QAALE 286
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 38-288 6.43e-54

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: 188.32  E-value: 6.43e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  38 YKADktyPTT--VAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGvYGPK--AYIATQGPLSTTLLDF 113
Cdd:cd14609  27 YQAE---PNTcsTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADF 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 114 WRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEK-RKSDYIIRTLKVKF--NSETRTIYQFHY 190
Cdd:cd14609 103 WQMVWENGCTVIVMLTPLVEDGVKQCDRYW--PDEGSSLYHIYEVNLVSEHiWCEDFLVRSFYLKNvqTQETRTLTQFHF 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 191 KNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSLIREMRTQR 269
Cdd:cd14609 181 LSWPAEGIPSSTRPLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQR 257

                       250
                ....*....|....*....
gi 20139861 270 PSLVQTQEQYELVYNAVLE 288
Cdd:cd14609 258 PGMVRTKDQFEFALTAVAE 276
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 58-279 7.94e-53

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: 183.18  E-value: 7.94e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 138 KCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQE 217
Cdd:cd14616  81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139861 218 DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipENF-SVFSLIREMRTQRPSLVQTQEQY 279
Cdd:cd14616 161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHIND----HDFvDIYGLVAELRSERMCMVQNLAQY 219
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 44-288 2.37e-52

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: 183.69  E-value: 2.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSLitsdEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14608  15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 124 IIVMACMEYEMGKKKCERYWA--EPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVP 199
Cdd:cd14608  91 GVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 200 SSIDPILELIWDVRcyqEDDSV-----PICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQ 274
Cdd:cd14608 171 ESPASFLNFLFKVR---ESGSLspehgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQ 247

                       250
                ....*....|....
gi 20139861 275 TQEQYELVYNAVLE 288
Cdd:cd14608 248 TADQLRFSYLAVIE 261
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 25-288 6.60e-52

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: 182.54  E-value: 6.60e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14626  12 ANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SET 182
Cdd:cd14626  92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYW--PIRGTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEK 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 183 RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLI 262
Cdd:cd14626 170 REVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHV 246

                       250       260
                ....*....|....*....|....*.
gi 20139861 263 REMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14626 247 TCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 84-288 1.01e-51

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: 179.56  E-value: 1.01e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGvYGPK--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQleFGPFSVSCE 161
Cdd:cd14546   1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV--YHIYEVHLV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 162 AEKRKS-DYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14546  78 SEHIWCdDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYR-GRSCPIVVHCSDGAGRTGTY 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20139861 238 CAIDYTWMLLKDGIipENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14546 157 ILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 59-288 1.42e-51

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: 179.86  E-value: 1.42e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  59 RYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKK 138
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 139 CERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCY 215
Cdd:cd14623  81 CAQYW--PSDGSVSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20139861 216 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14623 159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKaEGIL----DVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 84-286 1.53e-51

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: 178.62  E-value: 1.53e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW--PEDGSVSSGDITVELKDQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14552  79 TDYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20139861 241 DYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAV 286
Cdd:cd14552 159 STVLERVKaEGVL----DVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 84-288 4.77e-51

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: 177.42  E-value: 4.77e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMqleFGPFSVSCEAE 163
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVET 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14555  78 EPLAEYVVRTFALerRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20139861 242 YTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14555 158 IMLdMAEREGVV----DIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 58-283 4.98e-51

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: 178.19  E-value: 4.98e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 138 KCERYWAEPGEmQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE---TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 214
Cdd:cd14617  81 KCDHYWPADQD-SLYYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139861 215 Y--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLL--KDGIipenfSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14617 160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 58-287 7.45e-51

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: 177.83  E-value: 7.45e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 138 KCERYWaePGEMQ-LEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 214
Cdd:cd14618  81 LCDHYW--PSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20139861 215 YQE--DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVL 287
Cdd:cd14618 159 HVQatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVD---VFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 84-287 9.33e-51

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: 176.71  E-value: 9.33e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW--PADGSEEYGNFLVTQKSV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKV----------KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGR 233
Cdd:cd17668  79 QVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20139861 234 TGVICAIDytwMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVL 287
Cdd:cd17668 159 TGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 38-288 2.96e-50

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: 177.94  E-value: 2.96e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  38 YKADKTyPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGvYGPK--AYIATQGPLSTTLLDFWR 115
Cdd:cd14610  29 YQAEPN-ATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQ 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 116 MIWEYSVLIIVMACMEYEMGKKKCERYWAEPGE-----MQLEFGPFSVSCEaekrksDYIIRTLKVKF--NSETRTIYQF 188
Cdd:cd14610 107 MVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSnlyhiYEVNLVSEHIWCE------DFLVRSFYLKNlqTNETRTVTQF 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 189 HYKNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiiPENFSVFSLIREMRT 267
Cdd:cd14610 181 HFLSWNDQGVPASTRSLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKG--AKEIDIAATLEHLRD 257

                       250       260
                ....*....|....*....|.
gi 20139861 268 QRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14610 258 QRPGMVQTKEQFEFALTAVAE 278
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 70-288 3.65e-50

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: 175.59  E-value: 3.65e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  70 RVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEM 149
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 150 qleFGPFSVSCEAEKRKSDYIIRTLKVK---FNsETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIH 226
Cdd:cd14631  81 ---YGDFKVTCVEMEPLAEYVVRTFTLErrgYN-EIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139861 227 CSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14631 157 CSAGAGRTGCYIVIDIMLdMAEREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 52-290 8.30e-50

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: 175.82  E-value: 8.30e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  52 PKNIKKNRYKDILPYDYSRVelSLITSDED---SSYINANFIKGvYG--PKAYIATQGPLSTTLLDFWRMIWEYSVLIIV 126
Cdd:cd14613  23 PGLVRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPIIV 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 127 MACMEYEMgKKKCERYWAEPgemQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14613 100 MITNIEEM-NEKCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 207 ELIWDV---RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipenfSVFSLIR---EMRTQRPSLVQTQEQYE 280
Cdd:cd14613 176 QLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNE------GVVDILRttcQLRLDRGGMIQTCEQYQ 249

                       250
                ....*....|
gi 20139861 281 LVYNaVLELF 290
Cdd:cd14613 250 FVHH-VLSLY 258
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-288 2.60e-49

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: 173.03  E-value: 2.60e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYW--AEPGEMQLEFGPFSVS 159
Cdd:cd14540   1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptLGGEHDALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 160 CEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-----RCYQEDD----SVPICIHCS 228
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPTLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 229 AGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELD---IPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 57-284 6.13e-49

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: 172.41  E-value: 6.13e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  57 KNRYKDILPYDYSRVELSLITSDED-SSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEM 134
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 135 gKKKCERYWAEPGEMqleFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVrc 214
Cdd:cd14611  82 -NEKCVLYWPEKRGI---YGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV-- 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 215 yQED-----DSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYN 284
Cdd:cd14611 156 -EEDrlaspGRGPVVVHCSAGIGRTGCFIATTIGCQQLKeEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 34-291 8.27e-49

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: 174.03  E-value: 8.27e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  34 QSTKYKADKTYptTVAEKPKNIKKNRYKDILPYDYSRVELsLITSDEDSSYINANFIKGVYGPKA--YIATQGPLSTTLL 111
Cdd:cd14599  20 QIPKKKADGVF--TTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCH 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 112 DFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQ--LEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQ 187
Cdd:cd14599  97 DFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHssATYGKFKVTTKFRTDSGCYATTGLKVKhlLSGQERTVWH 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 188 FHYKNWPDHDVPSSID---PILELIWDVRCY-------QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFS 257
Cdd:cd14599 177 LQYTDWPDHGCPEEVQgflSYLEEIQSVRRHtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHN---EKVE 253

                       250       260       270
                ....*....|....*....|....*....|....
gi 20139861 258 VFSLIREMRTQRPSLVQTQEQYELVYNAVLELFK 291
Cdd:cd14599 254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 25-288 8.98e-49

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: 173.74  E-value: 8.98e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14625  18 ANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SET 182
Cdd:cd14625  98 PLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYW--PSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEK 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 183 RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPE-NFSVFSL 261
Cdd:cd14625 176 REVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID----AMLERIKHEkTVDIYGH 251

                       250       260
                ....*....|....*....|....*..
gi 20139861 262 IREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14625 252 VTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 26-286 1.03e-47

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: 170.15  E-value: 1.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  26 NEFLKLKRQSTKYkadktyPTTVAEKPKNIKKNRYKDILPYDYSRVELSlitsDEDSSYINANFIKGVYGPKAYIATQGP 105
Cdd:cd14607   2 PLYLEIRNESHDY------PHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 106 LSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGP--FSVSCEAEKRKSDYIIRTLKVK-FNS-E 181
Cdd:cd14607  72 LPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLEnINSgE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 182 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRcyqEDDSV-----PICIHCSAGCGRTGVICAIDyTWMLLKDGIIPENF 256
Cdd:cd14607 152 TRTISHFHYTTWPDFGVPESPASFLNFLFKVR---ESGSLspehgPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSV 227

                       250       260       270
                ....*....|....*....|....*....|
gi 20139861 257 SVFSLIREMRTQRPSLVQTQEQYELVYNAV 286
Cdd:cd14607 228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 84-291 2.70e-47

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: 167.23  E-value: 2.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCE 161
Cdd:cd14596   1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 162 AEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIwdvrCYQED--DSVPICIHCSAGCGRTGVI 237
Cdd:cd14596  81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFI----CYMRKvhNTGPIVVHCSAGIGRAGVL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20139861 238 CAIDYTWMLLKDGIipeNFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFK 291
Cdd:cd14596 157 ICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 25-288 1.14e-46

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: 167.99  E-value: 1.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14624  18 ANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SET 182
Cdd:cd14624  98 ALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYW--PSRGTETYGLIQVTLLDTVELATYCVRTFALYKNgsSEK 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 183 RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLI 262
Cdd:cd14624 176 REVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHV 252

                       250       260
                ....*....|....*....|....*.
gi 20139861 263 REMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14624 253 TLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 84-283 9.25e-46

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: 162.56  E-value: 9.25e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEmqlEFGPFSVSCEAE 163
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK---TYGDIEVELKDT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDD------SVPICIHCSAGCGRTG 235
Cdd:cd14558  78 EKSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKnskhgrSVPIVVHCSDGSSRTG 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20139861 236 VICAIdytWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14558 158 IFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 84-283 2.43e-45

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: 161.40  E-value: 2.43e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGV--YGPKaYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCE 161
Cdd:cd14539   1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 162 AEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY---QEDDSVPICIHCSAGCGRTGV 236
Cdd:cd14539  80 SVRTTPTHVERIISIQHKdtRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTGA 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20139861 237 ICAIdYTWM--LLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14539 160 FCLL-YAAVqeIEAGNGIPD---LPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 60-288 2.92e-45

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: 162.03  E-value: 2.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  60 YKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKC 139
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 140 ERYWAEPGemQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE-----TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 214
Cdd:cd14620  81 YQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20139861 215 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14620 159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHA---EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-291 3.28e-45

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: 161.27  E-value: 3.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKA----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQlEFGPFSVS 159
Cdd:cd14601   2 YINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 160 CEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14601  81 CHSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 238 CAIDyTWMLLKDGiipeNFSVFSL--IREMRTQRPSLVQTQEQYELVYNAVLELFK 291
Cdd:cd14601 161 ITME-TAMCLIEC----NQPVYPLdiVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 84-283 1.19e-44

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: 159.61  E-value: 1.19e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAE 163
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14557  81 KICPDYIIRKLNINNKKEKgsgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 20139861 241 DytwmLLKDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14557 161 D----AMLEGLEAEGrVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 49-290 1.38e-44

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: 162.50  E-value: 1.38e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14621  47 ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMV 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTL------KVKFNSETRTIYQFHYKNWPDHDVPSSI 202
Cdd:cd14621 127 TNLKERKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTP 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 203 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELV 282
Cdd:cd14621 205 IGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHA---ERKVDVYGFVSRIRAQRCQMVQTDMQYVFI 281


                ....*...
gi 20139861 283 YNAVLELF 290
Cdd:cd14621 282 YQALLEHY 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-280 1.37e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 1.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  13 EAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNikknRYKDILPYDYSRVElslitsdEDSSYINANFIKg 92
Cdd:COG5599   5 NPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  93 VYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--KKCERYWAEPGEMqlefgpFSVSCEAEKRKSDYI 170
Cdd:COG5599  73 VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGEY------GKYEVSSELTESIQL 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 171 -----IRTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDSV---PICIHCSAGCGRTGVICA 239
Cdd:COG5599 147 rdgieARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIA 225

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 20139861 240 IDYTWMLLKDGIIPEnFSVFSLIREMRTQR-PSLVQTQEQYE 280
Cdd:COG5599 226 CLALSKSINALVQIT-LSVEEIVIDMRTSRnGGMVQTSEQLD 266
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-286 1.90e-43

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: 156.32  E-value: 1.90e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd14622   2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW--PSEGSVTHGEITIEIKND 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14622  80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20139861 241 DYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAV 286
Cdd:cd14622 160 SNILERVKaEGLL----DVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 84-288 1.74e-42

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: 153.67  E-value: 1.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMqleFGPFSVSCEAE 163
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT---YGDIKITLLKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14632  78 ETLAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20139861 242 YTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14632 158 VMLdMAECEGVV----DIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 84-283 8.18e-42

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: 151.41  E-value: 8.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEYEMGKKKCERYWAEPGemQLEFGPFSVSCEAE 163
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEG--SGTYGPIQVEFVST 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED-DSVPICIHCSAGCGRTGVI 237
Cdd:cd14556  78 TIDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVF 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20139861 238 CAIDYTWMLLKDgiipEN-FSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14556 158 CAISSVCERIKV----ENvVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02738 PHA02738
hypothetical protein; Provisional
 33-286 3.40e-41

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.54  E-value: 3.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   33 RQSTKYKADKTYPTTVAEKpKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  113 FWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE-TRTIYQFHYK 191
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  192 NWPDHDVPSSIDPILELIWDVRCYQED-------------DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSV 258
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                        250       260
                 ....*....|....*....|....*...
gi 20139861  259 FSLIREMRTQRPSLVQTQEQYELVYNAV 286
Cdd:PHA02738 263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 44-291 1.30e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 145.92  E-value: 1.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:PHA02742  42 FSCNESLELKNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  124 IIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKfNSETRT---IYQFHYKNWPDHDVPS 200
Cdd:PHA02742 120 VIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLT-DTNTGAsldIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  201 SIDPILELIWDVRCYQEDDSV-----------PICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIREMRTQR 269
Cdd:PHA02742 199 DPNKFLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQR 275

                        250       260
                 ....*....|....*....|..
gi 20139861  270 PSLVQTQEQYELVYNAVLELFK 291
Cdd:PHA02742 276 HNCLSLPQQYIFCYFIVLIFAK 297
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 84-283 3.87e-38

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: 141.20  E-value: 3.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQleFGPFSVSCEAE 163
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWT--YGNLRVRVEDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKV-KFNSET-----RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14551  79 VVLVDYTTRKFCIqKVNRGIgekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20139861 238 CAIDYTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVY 283
Cdd:cd14551 159 IVIDAMLdMMHAEGKV----DVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 84-291 6.30e-38

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: 141.27  E-value: 6.30e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQ--LEFGPFSVS 159
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 160 CEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSID---PILELIWDVRCYQEDDS------VPICIHCS 228
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCPEDLKgflSYLEEIQSVRRHTNSTIdpkspnPPVLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139861 229 AGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFK 291
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHN---EMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 50-303 9.83e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.60  E-value: 9.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   50 EKPKNIKKNRYKDILPYDYSRVELSlITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC 129
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  130 -MEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:PHA02747 126 pTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEItdKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  207 ELIWDV--------RCYQEDDSV--PICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQ 276
Cdd:PHA02747 206 KFIKIIdinrkksgKLFNPKDALlcPIVVHCSDGVGKTGIFCAVD---ICLNQLVKRKAICLAKTAEKIREQRHAGIMNF 282

                        250       260       270
                 ....*....|....*....|....*....|
gi 20139861  277 EQYELV---YNAVLELFKRQMDVIRDKHSG 303
Cdd:PHA02747 283 DDYLFIqpgYEVLHYFLSKIKAIDKIKFCG 312
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
184-288 4.43e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 4.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    184 TIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSL 261
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 20139861    262 IREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 184-288 4.43e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 4.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861    184 TIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSL 261
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 20139861    262 IREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 51-286 1.10e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 140.93  E-value: 1.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   51 KPKNIKKNRYKDILPYDYSRVELS------------------LITS-DEDSSYINANFIKGVYGPKAYIATQGPLSTTLL 111
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkiEVTSeDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  112 DFWRMIWEYSVLIIVmACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFH 189
Cdd:PHA02746 128 DFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMItdKISDTSREIHHFW 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  190 YKNWPDHDVPSSIDPILELIWDVRCYQ-------EDDSV---PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVF 259
Cdd:PHA02746 207 FPDWPDNGIPTGMAEFLELINKVNEEQaelikqaDNDPQtlgPIVVHCSAGIGRAGTFCAIDNALEQLEK---EKEVCLG 283

                        250       260
                 ....*....|....*....|....*..
gi 20139861  260 SLIREMRTQRPSLVQTQEQYELVYNAV 286
Cdd:PHA02746 284 EIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 84-284 1.36e-36

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: 136.83  E-value: 1.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKG---VYGPKaYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC-MEYEMGKKKCERYWAEPGEMQLEFGPFSVS 159
Cdd:cd17658   1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrLVDNYSTAKCADYFPAEENESREFGRISVT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 160 CEAEKRKSDYI-IRTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSIDPILELIwdVRCYQEDDSV-PICIHCSAGCGRT 234
Cdd:cd17658  80 NKKLKHSQHSItLRVLEVQYIEseePPLSVLHIQYPEWPDHGVPKDTRSVRELL--KRLYGIPPSAgPIVVHCSAGIGRT 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20139861 235 GVICAIDYTWMLLKDGIIpENFSVFSLIREMRTQRPSLVQTQEQYELVYN 284
Cdd:cd17658 158 GAYCTIHNTIRRILEGDM-SAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 84-288 1.01e-30

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: 120.13  E-value: 1.01e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEYEMgKKKCERYWAEPGemQLEFGPFSVSCEAE 163
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDL-AQGCPQYWPEEG--MLRYGPIQVECMSC 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVKFNSETRTIY----QFHYKNWPDH-DVPSSIDPILELIWDVRCYQED----DSVPIcIHCSAGCGRT 234
Cdd:cd14636  77 SMDCDVISRIFRICNLTRPQEGYlmvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdegEGRTI-IHCLNGGGRS 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20139861 235 GVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14636 156 GMFCAISIVCEMIKRQNVVD---VFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 84-288 5.72e-26

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: 106.26  E-value: 5.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAcmeYEMGKKK-CERYWaePGEMQLEFGPFSVSCEA 162
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDAAQlCMQYW--PEKTSCCYGPIQVEFVS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 163 EKRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED---DSVPICIHCSAGCGRT 234
Cdd:cd14634  76 ADIDEDIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGGGRS 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20139861 235 GVICAI-DYTWMLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14634 156 GTFCAIcSVCEMIQQQNII----DVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 84-288 1.03e-23

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 99.76  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacMEYEMGKKKCERYWAEPGEMQleFGPFSVSCEAE 163
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM--LNDVDPAQLCPQYWPENGVHR--HGPIQVEFVSA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKSDYIIRTLKVkFNSET-----RTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED---DSVPICIHCSAGCGRT 234
Cdd:cd14635  77 DLEEDIISRIFRI-YNAARpqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRS 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20139861 235 GVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14635 156 GTFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 84-288 1.06e-23

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: 99.60  E-value: 1.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC-MEYEMGKKKCERYWAEPGEMQleFGPFSVSCEA 162
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqLNQSNSAWPCLQYWPEPGLQQ--YGPMEVEFVS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 163 EKRKSDYIIRTLKVK----FNSETRTIYQFHYKNW-PDHDVPSSIDPILELIWDVRCYQEDDSV-PICIHCSAGCGRTGV 236
Cdd:cd14637  79 GSADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGRSGT 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20139861 237 ICAIDytwmLLKDGIIPENF-SVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 288
Cdd:cd14637 159 YCASA----MILEMIRCHNIvDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 84-284 8.72e-23

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: 97.01  E-value: 8.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEYEMGKKKCErYWAEPGEmQLEFGPFSVSCEAE 163
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVM-LTDNELNEDEPI-YWPTKEK-PLECETFKVTLSGE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 164 KRKS----------DYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCGR 233
Cdd:cd14550  78 DHSClsneirlivrDFILESTQDDYVLEVR---QFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQ 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 20139861 234 TGVICAidytWMLLKDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVYN 284
Cdd:cd14550 153 AATFCA----LTTLHQQLEHESsVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 84-287 1.79e-20

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: 90.44  E-value: 1.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCErYWAEPGE-MQLEfgPFSVSCEA 162
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpINCE--TFKVTLIA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 163 EKRK----------SDYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCG 232
Cdd:cd17669  78 EEHKclsneekliiQDFILEATQDDYVLEVR---HFQCPKWPNPDSP--ISKTFELISIIKEEAANRDGPMIVHDEHGGV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 233 RTGVICAIdYTWMllkDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVYNAVL 287
Cdd:cd17669 153 TAGTFCAL-TTLM---HQLEKENsVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 84-287 3.36e-19

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: 86.66  E-value: 3.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacMEYEMGKKKCER-YWAEPGE-MQLEfgPFSVSCE 161
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM--LPDNQGLAEDEFvYWPSREEsMNCE--AFTVTLI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 162 AEKRK----------SDYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGC 231
Cdd:cd17670  77 SKDRLclsneeqiiiHDFILEATQDDYVLEVR---HFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEFGA 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20139861 232 GRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMrtqRPSLVQTQEQYELVYNAVL 287
Cdd:cd17670 152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLM---RPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 58-281 1.26e-15

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: 76.67  E-value: 1.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  58 NRYKDIlpydYSRVELSlitsdeDSSYINANFIKgVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14559   1 NRFTNI----QTRVSTP------VGKNLNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 138 KCERYWAEPGEmqleFGpfSVSCEAEKRKSDYIIR-------TLKVKFNSETRTIYQFHYKNWPDHDVPSSID------- 203
Cdd:cd14559  70 GLPPYFRQSGT----YG--SVTVKSKKTGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDHTAISSEGlkeladl 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 204 ---------PILELIWDVRCYQEDDSVPIcIHCSAGCGRTGVICAIdytwMLLKDGiiPENFSVFSLIREMRTQRPS-LV 273
Cdd:cd14559 144 vnksaeekrNFYKSKGSSAINDKNKLLPV-IHCRAGVGRTGQLAAA----MELNKS--PNNLSVEDIVSDMRTSRNGkMV 216


                ....*...
gi 20139861 274 QTQEQYEL 281
Cdd:cd14559 217 QKDEQLDT 224
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 203-284 2.24e-09

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 55.82  E-value: 2.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 203 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGiipenFSVFSLIREMRTQRPS-LVQTQEQYEL 281
Cdd:cd14494  39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVAC---YLVLLGG-----MSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                ...
gi 20139861 282 VYN 284
Cdd:cd14494 111 LIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 49-298 4.84e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 55.36  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861   49 AEKPKNIKKNRYKD------ILPYDYSRVELSlitsdEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSV 122
Cdd:PHA02740  42 ANKACAQAENKAKDenlalhITRLLHRRIKLF-----NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  123 LIIVMACMEYEmgKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSEtRTIYQFHYKNWP----DH 196
Cdd:PHA02740 117 QIIVLISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLtdKFGQA-QKISHFQYTAWPadgfSH 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861  197 DVPSSID---PILELIWDVRCYQEDDSV-PICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIREMRTQRPS 271
Cdd:PHA02740 194 DPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFdKTGML----SIANALKKVRQKKYG 269

                        250       260
                 ....*....|....*....|....*..
gi 20139861  272 LVQTQEQYELVYNAVLELFKRQMDVIR 298
Cdd:PHA02740 270 CMNCLDDYVFCYHLIAAYLKEKFDILK 296
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
193-283 1.28e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.51  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 193 WPDHDVPS--SIDPILELIWdvRCYQEDDSVpiCIHCSAGCGRTGVICAidytWMLLKDGIIPENfsvfsLIREMRTQRP 270
Cdd:COG2453  55 IPDFGAPDdeQLQEAVDFID--EALREGKKV--LVHCRGGIGRTGTVAA----AYLVLLGLSAEE-----ALARVRAARP 121

                        90
                ....*....|...
gi 20139861 271 SLVQTQEQYELVY 283
Cdd:COG2453 122 GAVETPAQRAFLE 134
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 194-283 2.88e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 48.03  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 194 PDHDVPSSIDPILELIWDVR-CYQEDDSVpiCIHCSAGCGRTGVICAidYTWMLLKDGIIPEnfsvfSLIREMRTQRPSL 272
Cdd:cd14505  81 PDGGVPSDIAQWQELLEELLsALENGKKV--LIHCKGGLGRTGLIAA--CLLLELGDTLDPE-----QAIAAVRALRPGA 151

                        90
                ....*....|.
gi 20139861 273 VQTQEQYELVY 283
Cdd:cd14505 152 IQTPKQENFLH 162
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 185-282 6.17e-05

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: 45.03  E-value: 6.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 185 IYQFHYkNWPDHDVPSsidpiLELIWD---VRCYQEDDSVPICIHCSAGCGRTGVICAidyTWMLLKDGIIPENfsvfsL 261
Cdd:cd14506  77 IYFYNF-GWKDYGVPS-----LTTILDivkVMAFALQEGGKVAVHCHAGLGRTGVLIA---CYLVYALRMSADQ-----A 142

                        90       100
                ....*....|....*....|.
gi 20139861 262 IREMRTQRPSLVQTQEQYELV 282
Cdd:cd14506 143 IRLVRSKRPNSIQTRGQVLCV 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 187-239 8.92e-05

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: 43.72  E-value: 8.92e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20139861 187 QFHYKNWPDHDVPSsidpiLELIWDVrCY------QEDDSVPICIHCSAGCGRTGVICA 239
Cdd:cd14497  62 RVLHYGFPDHHPPP-----LGLLLEI-VDdidswlSEDPNNVAVVHCKAGKGRTGTVIC 114
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 222-282 1.16e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.03  E-value: 1.16e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139861 222 PICIHCSAGCGRTGVI--CAIDYTWMLlkDGIipenfsvfSLIREMRTQRPSLVQTQEQYELV 282
Cdd:cd14504  84 AVLVHCLAGKGRTGTMlaCYLVKTGKI--SAV--------DAINEIRRIRPGSIETSEQEKFV 136
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 194-282 6.28e-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: 41.58  E-value: 6.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139861 194 PDHDVPSsIDPILELIWDVRCY-QEDDSVPICIHCSAGCGRTG-VICAidytWmLLKDGIIPENFSVFSLIREMRTqRPS 271
Cdd:cd14510  82 DDHNVPT-LDEMLSFTAEVREWmAADPKNVVAIHCKGGKGRTGtMVCA----W-LIYSGQFESAKEALEYFGERRT-DKS 154

                        90
                ....*....|....*..
gi 20139861 272 L------VQTQEQYELV 282
Cdd:cd14510 155 VsskfqgVETPSQSRYV 171
PFA-DSP_Oca2 cd17661
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; ...
 179-240 5.08e-03

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; Oxidant-induced cell-cycle arrest protein 2 (Oca2) is an atypical dual specificity phosphatase of unknown function. It has been identified as a putative negative regulator acting on cell wall integrity and mating MAPK pathways in yeast. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca2 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350499 [Multi-domain]  Cd Length: 146  Bit Score: 38.15  E-value: 5.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20139861 179 NSETRTIYQFHYKNWPDHDVP---SSIDPILELIWDVRCYqeddsvPICIHCSAGCGRTGVICAI 240
Cdd:cd17661  53 QSQGIELYYFDFSSSSEPFTEedqERMEQALKLLLDKRNY------PILVHSNKGKHRVGVLVGI 111
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 188-239 7.59e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.95  E-value: 7.59e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20139861 188 FHYK--NWP--DHDVPSsIDPILELIWDVRCY-QEDDSVPICIHCSAGCGRTGV-ICA 239
Cdd:cd14509  58 FNGRvaEYPfdDHNPPP-LELIKPFCEDVDEWlKEDEKNVAAVHCKAGKGRTGVmICC 114
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
189-240 9.68e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 38.79  E-value: 9.68e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 20139861 189 HYKNWPDHDVPSSIDPILELIwdvrcyQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:COG2365 108 LYRAFVDPDAADAYRAAFRAL------ADAENGPVLFHCTAGKDRTGVAAAL 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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