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Conserved domains on  [gi|1178878191|ref|NP_001337271|]
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Tyrosine-protein phosphatase domain-containing protein [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

cys-based protein tyrosine phosphatase (PTP) family protein, such as tyrosine-protein phosphatase that catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004721|GO:0006470
PubMed:  27514797|17057753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
212-469 9.27e-65

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 210.59  E-value: 9.27e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  212 KIREEFGFLDSL---VCNKTTEDFEANKVRNREGCPKIYDENRVQLNRPGHEDVNYINASVITLKDFEHKLIVAQLPQme 288
Cdd:smart00194   1 GLEEEFEKLDRLkpdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  289 nESFVEDFWYMIYQEQINLVYLMV-PDDKLKNTTTSLFNDENGGYQYTGKMFINNRRADVSGDPKEYTIEVLPEGNSDSV 367
Cdd:smart00194  79 -PSTVEDFWRMVWEQKVTVIVMLTeLVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  368 ICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIK 447
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 1178878191  448 QQRPGGVESFAQCASIYAIVFD 469
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
212-469 9.27e-65

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 210.59  E-value: 9.27e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  212 KIREEFGFLDSL---VCNKTTEDFEANKVRNREGCPKIYDENRVQLNRPGHEDVNYINASVITLKDFEHKLIVAQLPQme 288
Cdd:smart00194   1 GLEEEFEKLDRLkpdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  289 nESFVEDFWYMIYQEQINLVYLMV-PDDKLKNTTTSLFNDENGGYQYTGKMFINNRRADVSGDPKEYTIEVLPEGNSDSV 367
Cdd:smart00194  79 -PSTVEDFWRMVWEQKVTVIVMLTeLVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  368 ICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIK 447
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 1178878191  448 QQRPGGVESFAQCASIYAIVFD 469
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
235-469 2.70e-53

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 179.75  E-value: 2.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 235 NKVRNREGCPKIYDENRVQL-NRPGHEDvnYINASVITLKDFEHKLIVAQLPQmenESFVEDFWYMIYQEQINLVYLMV- 312
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLtGDPGPSD--YINASYIDGYKKPKKYIATQGPL---PNTVEDFWRMVWEEKVTIIVMLTe 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 313 PDDKLKNTTTSLFNDENGGYQYTGKMFINNRraDVSGDPKEYTIEVL--PEGNSDSVIC-QVHHHAPWKHLQQPPKTLPI 389
Cdd:pfam00102  76 LEEKGREKCAQYWPEEEGESLEYGDFTVTLK--KEKEDEKDYTVRTLevSNGGSEETRTvKHFHYTGWPDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 390 IKMIHQFLSEKQ-VQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIYAIVF 468
Cdd:pfam00102 154 LDLLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233


                  .
gi 1178878191 469 D 469
Cdd:pfam00102 234 E 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 264-464 8.27e-49

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: 166.69  E-value: 8.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVyLMV--PDDKLKNTTTSLFNDENGGYQYTGKMFIN 341
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNT---VEDFWRMVWEQKVSVI-VMLtnLVEKGREKCERYWPEEGGKPLEYGDITVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 342 NRRADVSGDPKEYTIEVLPEGNSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVSLFGCGRACSF 421
Cdd:cd00047    77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1178878191 422 IGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIY 464
Cdd:cd00047   157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 199-459 1.12e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 62.71  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 199 SALNFCNKNNDI---QKIREEFGFLDSLVCNKTTEDFEA--NKVRNREGCPKIYDENRVQLNRPGHEDVNYINASVITLK 273
Cdd:PHA02747   10 RAIDFLKRRNQLncfGIIRDEHHQIILKPFDGLIANFEKpeNQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 274 DFEHKLIVAQLPqMENESfvEDFWYMIYQEQINLVYLMVPddklknttTSLFNDENGGYQY-----TGKMFINNRR---A 345
Cdd:PHA02747   90 EDDKKFIATQGP-FAETC--ADFWKAVWQEHCSIIVMLTP--------TKGTNGEEKCYQYwclneDGNIDMEDFRietL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 346 DVSGDPK--EYTIEVLPEGNSDSVICQVHHHAPWKHLQQP---PKTLPIIKMI----HQFLSEKQVQNAGVCVVSLF--- 413
Cdd:PHA02747  159 KTSVRAKyiLTLIEITDKILKDSRKISHFQCSEWFEDETPsdhPDFIKFIKIIdinrKKSGKLFNPKDALLCPIVVHcsd 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1178878191 414 GCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:PHA02747  239 GVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDD 284
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
212-469 9.27e-65

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 210.59  E-value: 9.27e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  212 KIREEFGFLDSL---VCNKTTEDFEANKVRNREGCPKIYDENRVQLNRPGHEDVNYINASVITLKDFEHKLIVAQLPQme 288
Cdd:smart00194   1 GLEEEFEKLDRLkpdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  289 nESFVEDFWYMIYQEQINLVYLMV-PDDKLKNTTTSLFNDENGGYQYTGKMFINNRRADVSGDPKEYTIEVLPEGNSDSV 367
Cdd:smart00194  79 -PSTVEDFWRMVWEQKVTVIVMLTeLVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  368 ICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIK 447
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 1178878191  448 QQRPGGVESFAQCASIYAIVFD 469
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
235-469 2.70e-53

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 179.75  E-value: 2.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 235 NKVRNREGCPKIYDENRVQL-NRPGHEDvnYINASVITLKDFEHKLIVAQLPQmenESFVEDFWYMIYQEQINLVYLMV- 312
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLtGDPGPSD--YINASYIDGYKKPKKYIATQGPL---PNTVEDFWRMVWEEKVTIIVMLTe 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 313 PDDKLKNTTTSLFNDENGGYQYTGKMFINNRraDVSGDPKEYTIEVL--PEGNSDSVIC-QVHHHAPWKHLQQPPKTLPI 389
Cdd:pfam00102  76 LEEKGREKCAQYWPEEEGESLEYGDFTVTLK--KEKEDEKDYTVRTLevSNGGSEETRTvKHFHYTGWPDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 390 IKMIHQFLSEKQ-VQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIYAIVF 468
Cdd:pfam00102 154 LDLLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233


                  .
gi 1178878191 469 D 469
Cdd:pfam00102 234 E 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 264-464 8.27e-49

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: 166.69  E-value: 8.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVyLMV--PDDKLKNTTTSLFNDENGGYQYTGKMFIN 341
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNT---VEDFWRMVWEQKVSVI-VMLtnLVEKGREKCERYWPEEGGKPLEYGDITVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 342 NRRADVSGDPKEYTIEVLPEGNSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVSLFGCGRACSF 421
Cdd:cd00047    77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1178878191 422 IGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIY 464
Cdd:cd00047   157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
368-467 1.35e-19

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 83.95  E-value: 1.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  368 ICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQ--VQNAGVCVVSLFGCGRACSFIGALYAINQLNNG-IEPNICEIMK 444
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|...
gi 1178878191  445 NIKQQRPGGVESFAQCASIYAIV 467
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 368-467 1.35e-19

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: 83.95  E-value: 1.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191  368 ICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQ--VQNAGVCVVSLFGCGRACSFIGALYAINQLNNG-IEPNICEIMK 444
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|...
gi 1178878191  445 NIKQQRPGGVESFAQCASIYAIV 467
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 235-471 3.06e-11

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: 63.88  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 235 NKVRNREGCPKIYDENRVQLNR--PGHEDVNYINASVItLKDFEHKLIVAQLPQ--------MENEsfVEDFWYMIYQEQ 304
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPVSDYINANII-MPEFETKCNNSKPKKsyiatqgcLQNT--VNDFWRMVFQEN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 305 INLVYLMVPD-DKLKNTTTSLFNDENGGYQYtGKMFINNRRADVSGD--PKEYTIEVLPEGNSDSVICQVH------HHA 375
Cdd:cd14605    79 SRVIVMTTKEvERGKSKCVKYWPDEYALKEY-GVMRVRNVKESAAHDyiLRELKLSKVGQGNTERTVWQYHfrtwpdHGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 376 PwkhlQQPPKTLPIIKMIHqfLSEKQVQNAGVCVVSL-FGCGRACSFIGALYAINQL-NNGIEpniCEI-----MKNIKQ 448
Cdd:cd14605   158 P----SDPGGVLDFLEEVH--HKQESIMDAGPVVVHCsAGIGRTGTFIVIDILIDIIrEKGVD---CDIdvpktIQMVRS 228

                         250       260
                  ....*....|....*....|...
gi 1178878191 449 QRPGGVESFAQCASIYAIVFDYI 471
Cdd:cd14605   229 QRSGMVQTEAQYRFIYMAVQHYI 251
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 199-459 1.12e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 62.71  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 199 SALNFCNKNNDI---QKIREEFGFLDSLVCNKTTEDFEA--NKVRNREGCPKIYDENRVQLNRPGHEDVNYINASVITLK 273
Cdd:PHA02747   10 RAIDFLKRRNQLncfGIIRDEHHQIILKPFDGLIANFEKpeNQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 274 DFEHKLIVAQLPqMENESfvEDFWYMIYQEQINLVYLMVPddklknttTSLFNDENGGYQY-----TGKMFINNRR---A 345
Cdd:PHA02747   90 EDDKKFIATQGP-FAETC--ADFWKAVWQEHCSIIVMLTP--------TKGTNGEEKCYQYwclneDGNIDMEDFRietL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 346 DVSGDPK--EYTIEVLPEGNSDSVICQVHHHAPWKHLQQP---PKTLPIIKMI----HQFLSEKQVQNAGVCVVSLF--- 413
Cdd:PHA02747  159 KTSVRAKyiLTLIEITDKILKDSRKISHFQCSEWFEDETPsdhPDFIKFIKIIdinrKKSGKLFNPKDALLCPIVVHcsd 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1178878191 414 GCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:PHA02747  239 GVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDD 284
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 264-459 1.37e-08

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: 55.09  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVyLMVPDdkLKNtttslfNDENGGYQYTGKMFINNR 343
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDT---IADFWQMIFQKKVKVI-VMLTE--LKE------GDQEQCAQYWGDEKKTYG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 344 RADV----SGDPKEYTIEVL----PEGNSDSVICQVHHHApWKHLQQPPKTLPIIKMIhQFLSEKQVQNAGVCVVSL--- 412
Cdd:cd14558    69 DIEVelkdTEKSPTYTVRVFeithLKRKDSRTVYQYQYHK-WKGEELPEKPKDLVDMI-KSIKQKLPYKNSKHGRSVpiv 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1178878191 413 FGCGRACSFIGALYAI-NQLNNG-IEP--NICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14558   147 VHCSDGSSRTGIFCALwNLLESAeTEKvvDVFQVVKALRKQRPGMVSTLEQ 197
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 249-459 1.45e-08

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: 55.61  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 249 ENRVQLNRPGH--EDVNYINASVITLKDFEHKLIVAQLPQMENEsfVEDFWYMIYQEQINLVyLMVPDDKLKNTTTSLF- 325
Cdd:cd14612    29 QSRVCLRRAGSqeEEGSYINANYIRGYDGKEKAYIATQGPMLNT--VSDFWEMVWQEECPII-VMITKLKEKKEKCVHYw 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 326 NDENGGYqytGKMFInnRRADVSGDPkEYTIEVLP---EGNSDSVicqVHH-HAPWKHLQQPPKTLPIIKMIHQFLSEKQ 401
Cdd:cd14612   106 PEKEGTY---GRFEI--RVQDMKECD-GYTIRDLTiqlEEESRSV---KHYwFSSWPDHQTPESAGPLLRLVAEVEESRQ 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 402 VQ-NAGVCVV-SLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14612   177 TAaSPGPIVVhCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQ 236
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 247-467 1.70e-08

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: 55.23  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 247 YDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQmenESFVEDFWYMIYQEQINLVYLMVPDDKLKNTTTSLF 325
Cdd:cd14602    10 YDHSRVELSLiTSDEDSDYINANFIKGVYGPRAYIATQGPL---STTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 326 NDENGGYQYTGKMFinNRRADVSGDPKEYTIEVLPEG-NSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQN 404
Cdd:cd14602    87 WAEPGEMQLEFGPF--SVTCEAEKRKSDYIIRTLKVKfNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDS 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178878191 405 AGVCVVSLFGCGRACSFIGALYAINQLNNGIEP---NICEIMKNIKQQRPGGVESFAQCASIYAIV 467
Cdd:cd14602   165 VPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 235-471 1.73e-08

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: 55.55  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 235 NKVRNREGCPKIYDENRVQL-----NRPGHEdvnYINASVI------TLKDFEHKLIVAQLPQMENEsfVEDFWYMIYQE 303
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILkdrdpNVPGSD---YINANYIrnenegPTTDENAKTYIATQGCLENT--VSDFWSMVWQE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 304 QINLVYLMVPD-DKLKNTTTSLFNDENGGYQYtGKMFINNRRADVSGDPKEYTIEVLPEGNSDSVICQVHHH-APWKHLQ 381
Cdd:cd14544    76 NSRVIVMTTKEvERGKNKCVRYWPDEGMQKQY-GPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQyLSWPDHG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 382 QPPKTLPIIKMIHQFLSEKQVQNAG--VCVVSLFGCGRACSFIGALYAINQLN-NGIEpniCEI-----MKNIKQQRPGG 453
Cdd:cd14544   155 VPSDPGGVLNFLEDVNQRQESLPHAgpIVVHCSAGIGRTGTFIVIDMLLDQIKrKGLD---CDIdiqktIQMVRSQRSGM 231

                         250
                  ....*....|....*...
gi 1178878191 454 VESFAQCASIYAIVFDYI 471
Cdd:cd14544   232 VQTEAQYKFIYVAVAQYI 249
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 264-464 2.73e-08

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: 54.18  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEH-KLIVAQLPQMENesfVEDFWYMIYQEQINLVyLMVpddklknttTSLFndENGG---YQYtgkmF 339
Cdd:cd18533     1 YINASYITLPGTSSkRYIATQGPLPAT---IGDFWKMIWQNNVGVI-VML---------TPLV--ENGRekcDQY----W 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 340 INNRradVSGDPKEYTIEVLPEGNSDSVICQV------HHHAPWKHLQQ-----------PPKTLPIIKMIhQFLSEK-- 400
Cdd:cd18533    62 PSGE---YEGEYGDLTVELVSEEENDDGGFIVrefelsKEDGKVKKVYHiqykswpdfgvPDSPEDLLTLI-KLKRELnd 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178878191 401 QVQNAGVCVV--SLfGCGRACSFIgalyAINQLNNGIEPN-------------ICEIMKNIKQQRPGGVESFAQCASIY 464
Cdd:cd18533   138 SASLDPPIIVhcSA-GVGRTGTFI----ALDSLLDELKRGlsdsqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 247-464 4.08e-08

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: 54.18  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 247 YDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVYLMVPDDKLKNTTTSLF 325
Cdd:cd14620     7 YDHSRVILSQlDGIPCSDYINASYIDGYKEKNKFIAAQGPKQET---VNDFWRMVWEQKSATIVMLTNLKERKEEKCYQY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 326 NDENGGYQYtGKMFINNRRADVSGDpkeYTIE------VLPEGNSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSE 399
Cdd:cd14620    84 WPDQGCWTY-GNIRVAVEDCVVLVD---YTIRkfciqpQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178878191 400 KQVQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIY 464
Cdd:cd14620   160 NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIY 224
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 208-470 3.69e-07

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: 51.95  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 208 NDIQKIREEFGFLDSLVCNKTTE--DFEANKVRNREGCPKIYDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQL 284
Cdd:cd14621    23 DDNKLFREEFNALPACPIQATCEaaSKEENKEKNRYVNILPYDHSRVHLTPvEGVPDSDYINASFINGYQEKNKFIAAQG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 285 PQMENesfVEDFWYMIYQEQINLVYLMVPDDKLKNTTTSLFNDENGGYQYTG-KMFINNRRADVSGDPKEYTIEVLPE-- 361
Cdd:cd14621   103 PKEET---VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNiRVSVEDVTVLVDYTVRKFCIQQVGDvt 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 362 GNSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQfLSEKQVQNAGVCVVSL-FGCGRACSFIGALYAINQLNNGIEPNIC 440
Cdd:cd14621   180 NKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKK-VKNCNPQYAGAIVVHCsAGVGRTGTFIVIDAMLDMMHAERKVDVY 258

                         250       260       270
                  ....*....|....*....|....*....|
gi 1178878191 441 EIMKNIKQQRPGGVESFAQCASIYAIVFDY 470
Cdd:cd14621   259 GFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 251-459 1.22e-06

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: 49.32  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 251 RVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQMENEsfVEDFWYMIYQEQINLVyLMVPDDKLKNTTTSLFNDEN 329
Cdd:cd14547    13 RVCLPSvDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNT--VADFWRMVWQEKTPII-VMITNLTEAKEKCAQYWPEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 330 GGYQYtGKMFINNRRADVSgdpKEYTI-EVLPEGNSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQ--FLSEKQVQNAG 406
Cdd:cd14547    90 ENETY-GDFEVTVQSVKET---DGYTVrKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEveEARQTEPHRGP 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1178878191 407 VCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14547   166 IVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQ 218
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 247-459 1.94e-06

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: 48.89  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 247 YDENRVQLN-RPGHEDVNYINASVITLKDFEHKLIVAQ--LPQMenesfVEDFWYMIYQEQIN-LVYLMVPDDKLK---- 318
Cdd:cd14548     8 YDHSRVKLIpINEEEGSDYINANYIPGYNSPREFIATQgpLPGT-----KDDFWRMVWEQNSHtIVMLTQCMEKGRvkcd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 319 ----NTTTSLfndenggyqYTGKMFINNRRADVSgdpKEYTI-EVLPEGNSDSVICQVHHHAPWKHLQQPPKTLPIIKMI 393
Cdd:cd14548    83 hywpFDQDPV---------YYGDITVTMLSESVL---PDWTIrEFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFV 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178878191 394 hQFLSEKQVQNAGVCVV-SLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14548   151 -RLVRDYIKQEKGPTIVhCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQ 216
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 264-467 3.48e-06

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: 48.03  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVYLMVPDDKLKNTTTSLFNDENGGYQYtGKMFINNR 343
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHT---VEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSS-GDITVELK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 344 RADvsgDPKEYTIE----VLPEGNSDSVICQVHHHApWKHLQQPPKTLPIIKMIHQFlsEKQVQNAG---VCVVSLFGCG 416
Cdd:cd14552    77 DQT---DYEDYTLRdflvTKGKGGSTRTVRQFHFHG-WPEVGIPDNGKGMIDLIAAV--QKQQQQSGnhpITVHCSAGAG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1178878191 417 RACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIYAIV 467
Cdd:cd14552   151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 247-467 4.61e-06

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: 47.73  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 247 YDENRVQLN-RPGHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVYLMVPDDKLKNTTTSLF 325
Cdd:cd14623     8 YEFNRVIIPvKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHT---IEDFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 326 NDENGGYQYtGKMFINNRRADvsgDPKEYTIEVL----PEGNSDSVICQVHHHApWKHLQQPPKTLPIIKMIHQFlsEKQ 401
Cdd:cd14623    85 WPSDGSVSY-GDITIELKKEE---ECESYTVRDLlvtnTRENKSRQIRQFHFHG-WPEVGIPSDGKGMINIIAAV--QKQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178878191 402 VQNAG---VCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIYAIV 467
Cdd:cd14623   158 QQQSGnhpITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 264-465 8.27e-06

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: 46.69  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFE--HKLIVAQLPQMENesfVEDFWYMIYQEQINLVYLMVP--DDKLKNTTTSLFNDENGGYQYTGKMF 339
Cdd:cd17658     1 YINASLVETPASEslPKFIATQGPLPHT---FEDFWEMVIQQRCPVIIMLTRlvDNYSTAKCADYFPAEENESREFGRIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 340 INNRRADVSGDPKEY-TIEVLPEGNSDSVICQVHHHAP-WKHLQQPPKTLPIIKMIHQFLSEKqvQNAGVCVVSL-FGCG 416
Cdd:cd17658    78 VTNKKLKHSQHSITLrVLEVQYIESEEPPLSVLHIQYPeWPDHGVPKDTRSVRELLKRLYGIP--PSAGPIVVHCsAGIG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1178878191 417 RACSFIGALYAINQLNNG--IEPNICEIMKNIKQQRPGGVESFAQCASIYA 465
Cdd:cd17658   156 RTGAYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 235-471 1.25e-05

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: 46.80  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 235 NKVRNREGCPKIYDENRVQL-----NRPGHEdvnYINASVItlkdfEHKLIVAQLPQMEN-------ESFVEDFWYMIYQ 302
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILqgrdsNIPGSD---YINANYV-----KNQLLGPDENAKTYiasqgclEATVNDFWQMAWQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 303 EQINLVYLMVPDDKLKNTTTSLFNDENGGYQYTGKMFINNRRADVSGDPKEYTIEVLPEGNSDSVIcQVHHHA--PWKHL 380
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIR-EIWHYQylSWPDH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 381 ---QQPPKTLPIIKMIHQflSEKQVQNAGVCVVSlfgCGRACSFIGALYAINQL-----NNGIEPNIcEIMKNI---KQQ 449
Cdd:cd14606   169 gvpSEPGGVLSFLDQINQ--RQESLPHAGPIIVH---CSAGIGRTGTIIVIDMLmenisTKGLDCDI-DIQKTIqmvRAQ 242

                         250       260
                  ....*....|....*....|..
gi 1178878191 450 RPGGVESFAQCASIYAIVFDYI 471
Cdd:cd14606   243 RSGMVQTEAQYKFIYVAIAQFI 264
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 234-308 1.81e-05

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: 46.59  E-value: 1.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178878191 234 ANKVRNREGCPKIYDENRVQLNRP-GHEDVNYINASVITLKDFEHKLIVAQLPqMENESfvEDFWYMIYQEQINLV 308
Cdd:cd14543    28 ANQEKNRYGDVLCLDQSRVKLPKRnGDERTDYINANFMDGYKQKNAYIATQGP-LPKTY--SDFWRMVWEQKVLVI 100
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 229-472 2.14e-05

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: 46.26  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 229 TEDFEANKVRNREGCPKIYDENRVQLnRP--GHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQIN 306
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCL-QPirGVEGSDYINASFIDGYRQQKAYIATQGPLAET---TEDFWRMLWEHNST 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 307 LVYLMVPDDKLKNTTTSLF--NDENGGYQYtgkmFINNRRADVSGDP---KEYTIEVLPEGNSDSVicQVHHHAPWKHLQ 381
Cdd:cd14628   122 IVVMLTKLREMGREKCHQYwpAERSARYQY----FVVDPMAEYNMPQyilREFKVTDARDGQSRTV--RQFQFTDWPEQG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 382 QPPKTLPIIKMIHQFLSEKQV--QNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14628   196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275

                         250
                  ....*....|...
gi 1178878191 460 CASIYAIVFDYIA 472
Cdd:cd14628   276 YQFCYRAALEYLG 288
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 264-471 3.43e-05

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: 45.14  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLK--DFEHKLIVAQLPQmenESFVEDFWYMIYQEQINLVyLMVPDDKLKNTTTSL--FNDENGGYQ--YTGK 337
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPL---QNTVGDFWQMVWEQGVYLV-VMVTAEEEGGREKCFryWPTLGGEHDalTFGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 338 MFINNRRADVSGdpkEYTIEVL-----PEGNSDSVicqvhhhapWkHLQQ---PPKTLPiiKMIHQFLS--EK------- 400
Cdd:cd14540    77 YKVSTKFSVSSG---CYTTTGLrvkhtLSGQSRTV---------W-HLQYtdwPDHGCP--EDVSGFLDflEEinsvrrh 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178878191 401 -------QVQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIYAIVFDYI 471
Cdd:cd14540   142 tnqdvagHNRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 229-472 4.00e-05

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: 45.49  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 229 TEDFEANKVRNREGCPKIYDENRVQLnRP--GHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQIN 306
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCL-QPirGVEGSDYINASFIDGYRQQKAYIATQGPLAET---TEDFWRMLWENNST 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 307 LVYLMVPDDKLKNTTTSLF--NDENGGYQYtgkmFINNRRADVSGDP---KEYTIEVLPEGNSDSVicQVHHHAPWKHLQ 381
Cdd:cd14627   123 IVVMLTKLREMGREKCHQYwpAERSARYQY----FVVDPMAEYNMPQyilREFKVTDARDGQSRTV--RQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 382 QPPKTLPIIKMIHQFLSEKQV--QNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14627   197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276

                         250
                  ....*....|...
gi 1178878191 460 CASIYAIVFDYIA 472
Cdd:cd14627   277 YQFCYQAALEYLG 289
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 264-459 4.10e-05

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: 44.72  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQ--LPQMenesfVEDFWYMIYQEQInLVYLMVPDDKL--KNTTTSLFNDENGGYQYTGKMF 339
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQgpLPNT-----VLDFWRMIWEYNV-QVIVMACREFEmgKKKCERYWPEEGEEQLQFGPFK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 340 INNRRADVSGDpkEYTIEVLPE--GNSDSVICQVHHHApWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVSLFGCGR 417
Cdd:cd14542    75 ISLEKEKRVGP--DFLIRTLKVtfQKESRTVYQFHYTA-WPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1178878191 418 ACSFIGALYAINQLNNGIEP---NICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKIPeefSLFDLVREMRKQRPAMVQTKEQ 196
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 247-467 5.15e-05

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: 45.20  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 247 YDENRVQLN---RPGHEDvnYINASVITLKDFEHKLIVAQLPQmenESFVEDFWYMIYQEQINlVYLM----VPDDKLKN 319
Cdd:cd14603    42 YDQTRVILSllqEEGHSD--YINANFIKGVDGSRAYIATQGPL---SHTVLDFWRMIWQYGVK-VILMacreIEMGKKKC 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 320 TTTSLFNDENGGYqytGKMFINNRRADVSGDPKEYTIEVLPEGNSDSVICQVHHHApWKHLQQPPKTLPIIKMIHQFLSE 399
Cdd:cd14603   116 ERYWAQEQEPLQT---GPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMA-WPDHGIPDSPDCMLAMIELARRL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178878191 400 KQVQNAGVCVVSLFGCGRAcSFIGALYAINQL--NNGIEP--NICEIMKNIKQQRPGGVESFAQCASIYAIV 467
Cdd:cd14603   192 QGSGPEPLCVHCSAGCGRT-GVICTVDYVRQLllTQRIPPdfSIFDVVLEMRKQRPAAVQTEEQYEFLYHTV 262
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 225-470 5.46e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 44.99  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 225 CNKTTEDfeANKVRNREGCPKIYDENRVQLN-RPGHEDvnYINASVITLKDFEHKLIVAQLPQMENESfveDFWYMIYQE 303
Cdd:PHA02742   44 CNESLEL--KNMKKCRYPDAPCFDRNRVILKiEDGGDD--FINASYVDGHNAKGRFICTQAPLEETAL---DFWQAIFQD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 304 QINLVYLMVPD-DKLKNTTTSLFNDENGGYQYTGKMFINNRRADVSGDPKEYTIEVLPEGNSDSVICQVHHHAPWKH--- 379
Cdd:PHA02742  117 QVRVIVMITKImEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHggl 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 380 LQQPPKTLPIIKMIHQFLSEKQVQNAG--------VCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRP 451
Cdd:PHA02742  197 PRDPNKFLDFVLAVREADLKADVDIKGenivkeppILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRH 276

                         250
                  ....*....|....*....
gi 1178878191 452 GGVESFAQCASIYAIVFDY 470
Cdd:PHA02742  277 NCLSLPQQYIFCYFIVLIF 295
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 235-312 6.22e-05

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: 44.44  E-value: 6.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178878191 235 NKVRNREGCPKIYDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQINLVYLMV 312
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPiRGVEGSDYINASFIDGYRQRGAYIATQGPLAET---TEDFWRMLWEHNSTIIVMLT 81
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 238-308 6.46e-05

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: 44.30  E-value: 6.46e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178878191 238 RNREGCPKIYDENRVQLNRpghEDVNYINASVITLKDFEHKLIVAQLPQmenESFVEDFWYMIYQEQINLV 308
Cdd:cd14545     3 RYRDRDPYDHDRSRVKLKQ---GDNDYINASLVEVEEAKRSYILTQGPL---PNTSGHFWQMVWEQNSKAV 67
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 229-472 6.48e-05

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: 44.72  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 229 TEDFEANKVRNREGCPKIYDENRVQLnRP--GHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQIN 306
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCL-QPirGVEGSDYINASFIDGYRQQKAYIATQGPLAET---TEDFWRMLWEHNST 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 307 LVYLMVPDDKLKNTTTSLF--NDENGGYQYtgkmFINNRRADVSGDP---KEYTIEVLPEGNSDSVicQVHHHAPWKHlQ 381
Cdd:cd14629   123 IVVMLTKLREMGREKCHQYwpAERSARYQY----FVVDPMAEYNMPQyilREFKVTDARDGQSRTI--RQFQFTDWPE-Q 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 382 QPPKT----LPIIKMIHQfLSEKQVQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESF 457
Cdd:cd14629   196 GVPKTgegfIDFIGQVHK-TKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTE 274

                         250
                  ....*....|....*
gi 1178878191 458 AQCASIYAIVFDYIA 472
Cdd:cd14629   275 DQYQLCYRAALEYLG 289
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 228-316 1.22e-04

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: 43.83  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 228 TTEDFEANKVRNR--EGCPkiYDENRVQLNRPGHEDVNYINASVI--TLKDFEHKLIVAQLPQMENesfVEDFWYMIYQE 303
Cdd:cd14599    31 TTATLPENAERNRirEVVP--YEENRVELVPTKENNTGYINASHIkvTVGGEEWHYIATQGPLPHT---CHDFWQMVWEQ 105

                          90
                  ....*....|...
gi 1178878191 304 QINLVYLMVPDDK 316
Cdd:cd14599   106 GVNVIAMVTAEEE 118
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 247-311 1.57e-04

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: 43.27  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178878191 247 YDENRVQLNRPGHEDVNYINASVI----TLKDFehklIVAQLPQmenESFVEDFWYMIYQEQINLVYLM 311
Cdd:cd14615     9 YDISRVKLSVQSHSTDDYINANYMpgynSKKEF----IAAQGPL---PNTVKDFWRMVWEKNVYAIVML 70
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 264-450 1.73e-04

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: 42.76  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVIT-LKDFEHKLIVAQLPQmenESFVEDFWYMIYQEQINLVYLMVPDDKL-KNTTTSLFNDENGGYQYTGKMFIN 341
Cdd:cd14539     1 YINASLIEdLTPYCPRFIATQAPL---PGTAADFWLMVYEQQVSVIVMLVSEQENeKQKVHRYWPTERGQALVYGAITVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 342 --NRRADVSGDPKEYTIEVLPEGNSDSVIcqvH-HHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQN---AGVCVVSLFGC 415
Cdd:cd14539    78 lqSVRTTPTHVERIISIQHKDTRLSRSVV---HlQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRslqTPIVVHCSSGV 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1178878191 416 GRACSFIGALYAINQLN--NGIePNICEIMKNIKQQR 450
Cdd:cd14539   155 GRTGAFCLLYAAVQEIEagNGI-PDLPQLVRKMRQQR 190
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 235-304 1.96e-04

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: 43.48  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 235 NKVRNREGCPKIYDENRVQLNRpghEDVNYINASVITLKDFEHKLIVAQLPqMENEsfVEDFWYMIYQEQ 304
Cdd:cd14608    25 NKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQRSYILTQGP-LPNT--CGHFWEMVWEQK 88
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 250-459 2.50e-04

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: 42.93  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 250 NRVQLNRPGHED--VNYINASVITLKDFEHKLIVAQlpQMENESFVEDFWYMIYQEQINLVYLMVPDDKLKNTTTSLFND 327
Cdd:cd14613    40 SRVCLTSPDQDDplSSYINANYIRGYGGEEKVYIAT--QGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 328 ENGGY---QYTGKMFINNrradvsgdpKEYTIEVLPEGNSDSVICQVHH-HAPWKHLQQPPKTLPIIKMIHQFLSEKQ-- 401
Cdd:cd14613   118 EQVTYegiEITVKQVIHA---------DDYRLRLITLKSGGEERGLKHYwYTSWPDQKTPDNAPPLLQLVQEVEEARQqa 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178878191 402 -VQNAGVCVVSLFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14613   189 ePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQ 247
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 232-311 3.73e-04

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: 42.26  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 232 FEANKVRNREGCPKIYDENRVQLNrpgHEDVNYINASVITLKDFEHKLIVAQLPqMENESFveDFWYMIYQEQINLVYLM 311
Cdd:cd14607    21 YPENRNRNRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGP-LPNTCC--HFWLMVWQQKTKAVVML 94
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 247-312 5.86e-04

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: 41.47  E-value: 5.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178878191 247 YDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQEQI-NLVYLMV 312
Cdd:cd14618     9 YDHSRVRLSQlGGEPHSDYINANFIPGYTSPQEFIATQGPLKKT---IEDFWRLVWEQQVcNIIMLTV 73
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 264-464 9.30e-04

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: 40.67  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYqEQINLVYLMVPDdkLKNtttslfNDENGGYQY---TGKMFI 340
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDET---VNDFWRMIW-EQGSATIVMVTN--LKE------RKEKKCSQYwpdQGCWTY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 341 NNRRADVSGDPK--EYTI------EVLPEGNSDSVICQVH-HHAPWKHLQQPPKTLPIIKMIHQFLSEKQVQNAGVCVVS 411
Cdd:cd14551    69 GNLRVRVEDTVVlvDYTTrkfciqKVNRGIGEKRVRLVTQfHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHC 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1178878191 412 LFGCGRACSFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQCASIY 464
Cdd:cd14551   149 SAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 233-303 1.38e-03

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: 40.39  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178878191 233 EANKVRNREGCPKIYDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQE 303
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLlDGDPHSDYINANYIDGYHRPRHYIATQGPMQET---VKDFWRMIWQE 69
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 264-459 2.05e-03

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: 39.90  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 264 YINASVITLKDFEHKLIVAQLPQMENEsfVEDFWYMIYQEQINLVyLMVPDDKLKNTTTSLFNDENGGYQYTGKMFINNR 343
Cdd:cd14611    30 YINANYIRGYGGKEKAFIATQGPMINT--VNDFWQMVWQEDSPVI-VMITKLKEKNEKCVLYWPEKRGIYGKVEVLVNSV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178878191 344 RadvsgDPKEYTIE--VLPEGnSDSVICQVHHHAPWKHLQQPPKTLPIIKMIHQFLSEKQ-VQNAGVCVVSL-FGCGRAC 419
Cdd:cd14611   107 K-----ECDNYTIRnlTLKQG-SQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLaSPGRGPVVVHCsAGIGRTG 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1178878191 420 SFIGALYAINQLNNGIEPNICEIMKNIKQQRPGGVESFAQ 459
Cdd:cd14611   181 CFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQ 220
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 233-303 2.18e-03

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: 40.03  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178878191 233 EANKVRNREGCPKIYDENRVQLNR-PGHEDVNYINASVITLKDFEHKLIVAQLPQMENesfVEDFWYMIYQE 303
Cdd:cd14633    38 DENRMKNRYGNIIAYDHSRVRLQPiEGETSSDYINGNYIDGYHRPNHYIATQGPMQET---IYDFWRMVWHE 106
 
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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