NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21728414|ref|NP_663716|]
View 

tyrosine-protein phosphatase non-receptor type 7 [Rattus norvegicus]

Protein Classification

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

PTPc-N7 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 105-349 0e+00

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


:

Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 505.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 105 PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQ-EDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMV 183
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 184 WQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPES 263
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 264 AGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14612 161 AGPLLRLVAEVeESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 21728414 343 HHTLALY 349
Cdd:cd14612 241 HHTLALY 247
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 105-349 0e+00

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 505.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 105 PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQ-EDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMV 183
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 184 WQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPES 263
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 264 AGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14612 161 AGPLLRLVAEVeESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 21728414 343 HHTLALY 349
Cdd:cd14612 241 HHTLALY 247
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
96-347 2.94e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 319.60  E-value: 2.94e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414     96 QLEEEFLKIPSNFVNPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAHSqEDSDYINANYIRGYDGKeKVYIATQGPM 172
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414    173 PNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRS 246
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414    247 VKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLR 326
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRK-SQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|.
gi 21728414    327 LDRGGMIQTAEQYQFLHHTLA 347
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
119-347 1.30e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 311.87  E-value: 1.30e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414   119 HASKDRYKTILPNPQSRVCLGraHSQEDSDYINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLR 198
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414   199 E-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEH-PEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:pfam00102  78 EkGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21728414   272 AEVETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 347
Cdd:pfam00102 158 RKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 123-349 3.66e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 3.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  123 DRYKTILPNPQSRVCLGRAHSQedSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 201
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  202 EKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQEC-RSVKHILFSAWPDHQTPESAGPLLRLVAEVET- 276
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQc 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  277 -PETAANS----------GPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 345
Cdd:PHA02738 210 qKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 21728414  346 LALY 349
Cdd:PHA02738 290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
95-342 5.62e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 150.63  E-value: 5.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  95 KQLEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVclgrahsQEDSDYINANYIRGYDGKekVYIATQGPMPN 174
Cdd:COG5599  18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 175 TVADFWEMVWQEDVSLIVMLTQLREGKE---KCVHYWPTEEEaYGPFQIRI-----QGMKEHPEYTVRHLTIQHQ-QECR 245
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSSeltesIQLRDGIEARTYVLTIKGTgQKKI 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 246 SVKHILFSAWPDHQ--TPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDILGI 321
Cdd:COG5599 168 EIPVLHVKNWPDHGaiSAEALKNLADLIDKKEK-IKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEI 246

                       250       260
                ....*....|....*....|..
gi 21728414 322 VCQLRLDRG-GMIQTAEQYQFL 342
Cdd:COG5599 247 VIDMRTSRNgGMVQTSEQLDVL 268
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 105-349 0e+00

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 505.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 105 PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQ-EDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMV 183
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 184 WQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPES 263
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 264 AGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14612 161 AGPLLRLVAEVeESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 21728414 343 HHTLALY 349
Cdd:cd14612 241 HHTLALY 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 123-344 6.98e-155

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: 434.13  E-value: 6.98e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 123 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKE 202
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 203 KCVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVET-PETA 280
Cdd:cd14547  81 KCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEaRQTE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21728414 281 ANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 344
Cdd:cd14547 161 PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 97-349 1.27e-123

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: 356.09  E-value: 1.27e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  97 LEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLgRAHSQED--SDYINANYIRGYDGKEKVYIATQGPMPN 174
Cdd:cd14613   3 LQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCL-TSPDQDDplSSYINANYIRGYGGEEKVYIATQGPTVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 175 TVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSA 254
Cdd:cd14613  82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 255 WPDHQTPESAGPLLRLVAEVETPETAA--NSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGM 332
Cdd:cd14613 162 WPDQKTPDNAPPLLQLVQEVEEARQQAepNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                       250
                ....*....|....*..
gi 21728414 333 IQTAEQYQFLHHTLALY 349
Cdd:cd14613 242 IQTCEQYQFVHHVLSLY 258
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 121-344 5.15e-118

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 340.74  E-value: 5.15e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 121 SKDRYKTILPNPQSRVCLGRAHSQED-SDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE 199
Cdd:cd14611   1 TKNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 200 GKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPE 278
Cdd:cd14611  81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVeEDRL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21728414 279 TAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 344
Cdd:cd14611 161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
96-347 2.94e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 319.60  E-value: 2.94e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414     96 QLEEEFLKIPSNFVNPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAHSqEDSDYINANYIRGYDGKeKVYIATQGPM 172
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414    173 PNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRS 246
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414    247 VKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLR 326
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRK-SQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|.
gi 21728414    327 LDRGGMIQTAEQYQFLHHTLA 347
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
119-347 1.30e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 311.87  E-value: 1.30e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414   119 HASKDRYKTILPNPQSRVCLGraHSQEDSDYINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLR 198
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414   199 E-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEH-PEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLV 271
Cdd:pfam00102  78 EkGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21728414   272 AEVETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 347
Cdd:pfam00102 158 RKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 149-344 3.60e-93

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 276.47  E-value: 3.60e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRIQG 224
Cdd:cd00047   1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkGREKCERYWPEEGGKpleYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 225 MKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIA 302
Cdd:cd00047  80 EEELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK-EARKPNGPIVVHCSAGVGRTGTFIA 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21728414 303 TRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 344
Cdd:cd00047 159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 124-343 3.47e-82

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


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 249.58  E-value: 3.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 124 RYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKE 202
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkGRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 203 KCVHYWP--TEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETA 280
Cdd:cd14548  80 KCDHYWPfdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD-YIK 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21728414 281 ANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14548 159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 122-346 2.81e-76

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 234.98  E-value: 2.81e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 200
Cdd:cd14553   6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEErS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 KEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTI--QHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETp 277
Cdd:cd14553  85 RVKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA- 163

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 278 ETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14553 164 CNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 117-343 6.85e-74

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 229.94  E-value: 6.85e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 117 PGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQ 196
Cdd:cd14543  27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 197 LRE-GKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14543 106 VVErGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLDF 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 271 VAEVETPETAA-------NSG-----PIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQ 338
Cdd:cd14543 186 LGEVRQQQALAvkamgdrWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQ 265


                ....*
gi 21728414 339 YQFLH 343
Cdd:cd14543 266 YYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 149-343 2.77e-73

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 226.08  E-value: 2.77e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMK 226
Cdd:cd14549   1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErGRRKCDQYWPKEgTETYGNIQVTLLSTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EHPEYTVRHLTIQHQQ--------ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetpeTAAN---SGPIVVHCSAGIG 295
Cdd:cd14549  80 VLATYTVRTFSLKNLKlkkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS----SAANppgAGPIVVHCSAGVG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21728414 296 RTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14549 156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 120-349 1.39e-72

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 225.80  E-value: 1.39e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 120 ASKDRYKTILPNPQSRVCL-GRAHSQEDSDYINANYIR------GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIV 192
Cdd:cd14544   2 KGKNRYKNILPFDHTRVILkDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 193 MLT-QLREGKEKCVHYWPTE--EEAYGPFqiRIQGMKEHP--EYTVRHLTIQ---HQQECRSVKHILFSAWPDHQTPESA 264
Cdd:cd14544  82 MTTkEVERGKNKCVRYWPDEgmQKQYGPY--RVQNVSEHDttDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 265 GPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQ 340
Cdd:cd14544 160 GGVLNFLEDVnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                ....*....
gi 21728414 341 FLHHTLALY 349
Cdd:cd14544 240 FIYVAVAQY 248
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 115-348 8.96e-70

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 218.60  E-value: 8.96e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 115 DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVML 194
Cdd:cd14614   8 DLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 195 TQLREGKE-KCVHYWPTEEE--AYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTP--ESAGPLLR 269
Cdd:cd14614  87 TQCNEKRRvKCDHYWPFTEEpvAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAESILQ 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 270 LVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLAL 348
Cdd:cd14614 167 FVQMVRQ-QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQL 244
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 149-344 1.23e-67

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 211.72  E-value: 1.23e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA--YGPFQIRIQGM 225
Cdd:cd18533   1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEnGREKCDQYWPSGEYEgeYGDLTVELVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 226 KEHPE--YTVRHLTIQH-QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFI 301
Cdd:cd18533  81 EENDDggFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKrELNDSASLDPPIIVHCSAGVGRTGTFI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21728414 302 A--------TRIGCQQLKARGEVD-ILGIVCQLRLDRGGMIQTAEQYQFLHH 344
Cdd:cd18533 161 AldslldelKRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 123-343 3.89e-66

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 208.97  E-value: 3.89e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 123 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 201
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEaGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 202 EKCVHYWPTEEE--AYGPFQIRIQGMKEHPEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ET 276
Cdd:cd14619  80 VKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQveEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLrQW 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21728414 277 PETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14619 160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 122-347 1.72e-65

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 208.14  E-value: 1.72e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGkEKVYIATQGPMPNTVADFWEMVWQEDVSLIVM-LTQLREG 200
Cdd:cd14603  33 KNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREIEMG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 KEKCVHYWPTEEE--AYGPFQI-RIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetP 277
Cdd:cd14603 112 KKKCERYWAQEQEplQTGPFTItLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELA--R 189

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21728414 278 ETAANSG-PIVVHCSAGIGRTGCfIATRIGCQQL----KARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 347
Cdd:cd14603 190 RLQGSGPePLCVHCSAGCGRTGV-ICTVDYVRQLlltqRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 123-342 3.48e-65

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 206.21  E-value: 3.48e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 123 DRYKTILPNPQSRVCLGRAHSQEDsDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 201
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEqGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 202 EKCVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETP 277
Cdd:cd14615  79 TKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVrEYM 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21728414 278 ETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14615 159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 123-343 8.05e-65

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 205.15  E-value: 8.05e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 123 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 201
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 202 EKCVHYWPTEEEA--YGPFQIRIQGMKEHPEYTVRHLTI--QHQQEC-RSVKHILFSAWPDHQTPESAGPLLRLVAEVE- 275
Cdd:cd14617  80 VKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKIcsEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRd 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21728414 276 ----TPetaaNSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14617 160 yinrTP----GSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 115-345 1.16e-64

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 205.07  E-value: 1.16e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 115 DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVML 194
Cdd:cd14554   2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 195 TQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQ--HQQECRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14554  81 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21728414 271 VAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 345
Cdd:cd14554 161 IGQVhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 149-341 9.01e-64

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 201.83  E-value: 9.01e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEK-VYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWP----TEEEAYGPFQIRI 222
Cdd:cd14538   1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEgGKVKCHRYWPdslnKPLICGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 223 QGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetpETAANSGPIVVHCSAGIGRTGCF 300
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYM---RRIHNSGPIVVHCSAGIGRTGVL 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14538 158 ITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIF 198
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 117-346 1.70e-63

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 203.34  E-value: 1.70e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 117 PGHASKDRYKTILPNPQSRVCLgRAHSQEDS---DYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVM 193
Cdd:cd17667  25 PDNKHKNRYINILAYDHSRVKL-RPLPGKDSkhsDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 194 LTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQH-------------QQECRSVKHILFSAWPDH 258
Cdd:cd17667 103 ITNLVEkGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkgRQNERTVIQYHYTQWPDM 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 259 QTPESAGPLLRLV---AEVETPETaansGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQT 335
Cdd:cd17667 183 GVPEYALPVLTFVrrsSAARTPEM----GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQT 258

                       250
                ....*....|.
gi 21728414 336 AEQYQFLHHTL 346
Cdd:cd17667 259 EEQYIFIHDAL 269
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 112-346 2.10e-63

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 203.34  E-value: 2.10e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 112 EDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLI 191
Cdd:cd14626  34 ENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATI 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 192 VMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPL 267
Cdd:cd14626 113 VMMTRLEEkSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQFQFMAWPDHGVPEYPTPI 192

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 268 LRLVAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14626 193 LAFLRRVKAC-NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 123-346 1.94e-62

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: 199.40  E-value: 1.94e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 123 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLT-QLREGK 201
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 202 EKCVHYWPTEEE--AYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ET 276
Cdd:cd14618  80 VLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEdlRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVrEH 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 277 PETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14618 160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 121-346 7.53e-62

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 197.94  E-value: 7.53e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 121 SKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE- 199
Cdd:cd14630   5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEv 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 200 GKEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-- 275
Cdd:cd14630  84 GRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKfl 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21728414 276 TPETAansGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14630 164 NPPDA---GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 117-349 2.42e-61

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 197.80  E-value: 2.42e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 117 PGHASKDRYKTILPNPQSRVCL-GRAHSQEDSDYINANYIR----GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLI 191
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILqGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 192 VMLT-QLREGKEKCVHYWPT--EEEAYGPFQIRIQGMKEHPEYTVRHL--TIQHQQEC-RSVKHILFSAWPDHQTPESAG 265
Cdd:cd14606  96 VMTTrEVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLqvSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 266 PLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14606 176 GVLSFLDQInQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKF 255


                ....*...
gi 21728414 342 LHHTLALY 349
Cdd:cd14606 256 IYVAIAQF 263
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 122-353 8.11e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 197.46  E-value: 8.11e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 200
Cdd:cd14604  60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEmG 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 KEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVA---EV 274
Cdd:cd14604 139 RKKCERYWPLYGEEpmtFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISlmrKY 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 275 ETPETAansgPIVVHCSAGIGRTGCFIATRIGCQQLKA---RGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA-LYA 350
Cdd:cd14604 219 QEHEDV----PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqLFE 294


                ...
gi 21728414 351 AQL 353
Cdd:cd14604 295 KQL 297
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 149-343 9.13e-61

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 193.98  E-value: 9.13e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEAYGPFQIRIQGMKE 227
Cdd:cd14555   1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvGRVKCSRYWPDDTEVYGDIKVTLVETEP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRI 305
Cdd:cd14555  80 LAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA-SNPPSAGPIVVHCSAGAGRTGCYIVIDI 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21728414 306 GCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14555 159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 149-343 1.96e-60

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 193.12  E-value: 1.96e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG-KEKCVHYWPTEEE---AYGPFQIRIQG 224
Cdd:cd14557   1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGnRNKCAQYWPSMEEgsrAFGDVVVKINE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 225 MKEHPEYTVRHLTIQHQQECRS---VKHILFSAWPDHQTPESAGPLLRLVAEVETPETAAnSGPIVVHCSAGIGRTGCFI 301
Cdd:cd14557  80 EKICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF-SGPIVVHCSAGVGRTGTYI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21728414 302 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14557 159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 149-343 8.15e-60

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: 191.45  E-value: 8.15e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGkEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG-KEKCVHYWPTEEEAYGPFQIRIQGMKE 227
Cdd:cd14558   1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGdQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-----ETPETAANSGPIVVHCSAGIGRTGCF 300
Cdd:cd14558  80 SPTYTVRVFEITHLKrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpYKNSKHGRSVPIVVHCSDGSSRTGIF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14558 160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 148-341 1.31e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 191.39  E-value: 1.31e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 148 DYINANY----IRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA--YGPFQI 220
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErGRVKCHQYWPDLGETmqFGNLQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 221 RIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSgPIVVHCSAGIGRTG 298
Cdd:cd14541  80 TCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 299 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14541 159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 97-341 5.85e-59

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: 192.25  E-value: 5.85e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  97 LEEEFLKIPSNFVNPEDL---DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMP 173
Cdd:cd14628  27 MELEFKRLASSKAHTSRFisaNLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLA 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 174 NTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKH 249
Cdd:cd14628 106 ETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQ 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 250 ILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 328
Cdd:cd14628 186 FQFTDWPEQGVPKSGEGFIDFIGQVhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 265

                       250
                ....*....|...
gi 21728414 329 RGGMIQTAEQYQF 341
Cdd:cd14628 266 RPAMVQTEDQYQF 278
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 149-346 2.10e-58

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 188.26  E-value: 2.10e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMK 226
Cdd:cd17668   1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEkGRRKCDQYWPADgSEEYGNFLVTQKSVQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EHPEYTVRHLTIQH----------QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANsGPIVVHCSAGIGR 296
Cdd:cd17668  80 VLAYYTVRNFTLRNtkikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAV-GPVVVHCSAGVGR 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21728414 297 TGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd17668 159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 115-349 2.56e-58

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: 190.71  E-value: 2.56e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 115 DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVML 194
Cdd:cd14627  49 NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 195 TQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14627 128 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 271 VAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 349
Cdd:cd14627 208 IGQVhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 122-343 4.04e-58

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: 188.13  E-value: 4.04e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 200
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 KEKCVHYW--PTEEE-AYGPFQIRIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETP 277
Cdd:cd14602  80 KKKCERYWaePGEMQlEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 278 EtAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKAR---GEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14602 160 Q-EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 149-343 2.27e-57

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 185.25  E-value: 2.27e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEAYGPFQIRIQGMKE 227
Cdd:cd14632   1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTIQHQQEC--RSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRI 305
Cdd:cd14632  80 LAEYSVRTFALERRGYSarHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA-STPPDAGPVVVHCSAGAGRTGCYIVLDV 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21728414 306 GCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14632 159 MLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 96-346 2.36e-57

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 187.99  E-value: 2.36e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  96 QLEEEFLKI-PSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPN 174
Cdd:cd14625  23 KLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 175 TVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHI 250
Cdd:cd14625 102 TFGDFWRMVWEQRSATVVMMTKLEEkSRIKCDQYWPSRgTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 251 LFSAWPDHQTPESAGPLLRLVAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRG 330
Cdd:cd14625 182 QFTAWPDHGVPEYPTPFLAFLRRVKTC-NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRN 260

                       250
                ....*....|....*.
gi 21728414 331 GMIQTAEQYQFLHHTL 346
Cdd:cd14625 261 YMVQTEDQYSFIHDAL 276
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 121-349 2.40e-57

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 186.76  E-value: 2.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 121 SKDRYKTILPNPQSRVCLGRAHSQED-SDYINANYI-------RGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIV 192
Cdd:cd14605   4 NKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 193 MLT-QLREGKEKCVHYWPTEE--EAYGpfQIRIQGMKEHP--EYTVRHLTI----QHQQEcRSVKHILFSAWPDHQTPES 263
Cdd:cd14605  84 MTTkEVERGKSKCVKYWPDEYalKEYG--VMRVRNVKESAahDYILRELKLskvgQGNTE-RTVWQYHFRTWPDHGVPSD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 264 AGPLLRLVAEVE-TPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQY 339
Cdd:cd14605 161 PGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240

                       250
                ....*....|
gi 21728414 340 QFLHHTLALY 349
Cdd:cd14605 241 RFIYMAVQHY 250
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 135-346 2.82e-57

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 185.61  E-value: 2.82e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 135 RVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE 213
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvGRVKCYKYWPDDTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 214 AYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCS 291
Cdd:cd14631  80 VYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKL-SNPPSAGPIVVHCS 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21728414 292 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14631 159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 149-341 4.82e-57

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 184.39  E-value: 4.82e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE-AYGPFQIRIQGMK 226
Cdd:cd14552   1 YINASFIDGYRQKDA-YIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErSQNKCAQYWPEDGSvSSGDITVELKDQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EHPEYTVR--HLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIATR 304
Cdd:cd14552  80 DYEDYTLRdfLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21728414 305 IGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14552 160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 122-346 4.94e-57

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 186.79  E-value: 4.94e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 200
Cdd:cd14633  43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvG 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 KEKCVHYWPTEEEAYGPFQIRIQGMKEHPEYTVRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpE 278
Cdd:cd14633 122 RVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-K 200

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21728414 279 TAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14633 201 SPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 125-346 5.65e-57

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: 185.14  E-value: 5.65e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 125 YKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKE-K 203
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEeK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 204 CVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQHQ-----QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETP 277
Cdd:cd14620  80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 278 eTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14620 160 -NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 122-349 7.49e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 185.03  E-value: 7.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGrahsqEDSDYINANYIRGYDGKEK-VYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG 200
Cdd:cd14597   6 KNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 -KEKCVHYWPteeEAYGP-------FQIRIQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14597  81 gKIKCQRYWP---EILGKttmvdnrLQLTLVRMQQLKNFVIRVLELEDIQtrEVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 271 VAEVetpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLaLY 349
Cdd:cd14597 158 ISYM---RHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI-LY 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 149-344 2.53e-56

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: 182.62  E-value: 2.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGkEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE---AYGPFQIRIQG 224
Cdd:cd14542   1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEmGKKKCERYWPEEGEeqlQFGPFKISLEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 225 MKE-HPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPEtAANSGPIVVHCSAGIGRTGCFIAT 303
Cdd:cd14542  80 EKRvGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGRTGTICAI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21728414 304 RIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFLHH 344
Cdd:cd14542 159 DYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 123-343 3.37e-56

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 182.80  E-value: 3.37e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 123 DRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 201
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 202 EKCVHYWPTEEEAYGPF-QIRIQGMKE--HPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPE 278
Cdd:cd14616  80 IRCHQYWPEDNKPVTVFgDIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASR 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21728414 279 TAANSgPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14616 160 AHDNT-PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 122-346 2.03e-55

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 183.01  E-value: 2.03e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-G 200
Cdd:cd14624  50 KNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEErS 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 201 KEKCVHYWPTE-EEAYGPFQIRIQGMKEHPEYTVRHLTI--QHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETP 277
Cdd:cd14624 129 RVKCDQYWPSRgTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC 208

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 278 eTAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14624 209 -NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 87-349 2.95e-55

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 182.62  E-value: 2.95e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  87 LQHQPP--SPKQLEEEFLKIPSNFVNPEDL---DIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDgK 161
Cdd:cd14629  16 LTQVPPgeSVTAMELEFKLLANSKAHTSRFisaNLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYR-Q 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 162 EKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA-YGPFQIRIQGMKEHPEYTVRHLTIQ 239
Cdd:cd14629  95 QKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVT 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 240 HQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEV 316
Cdd:cd14629 175 DARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVV 254

                       250       260       270
                ....*....|....*....|....*....|...
gi 21728414 317 DILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 349
Cdd:cd14629 255 DMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 122-341 6.54e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 179.90  E-value: 6.54e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 122 KDRYKTILPNPQSRVclgRAHS-QEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE- 199
Cdd:cd14545   1 LNRYRDRDPYDHDRS---RVKLkQGDNDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEk 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 200 GKEKCVHYWPTEEEA-----YGPFQIRIQGMKEHPEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLVA 272
Cdd:cd14545  77 GQIKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELENlkTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21728414 273 EV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARG--EVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14545 157 KVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 149-350 3.09e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 174.95  E-value: 3.09e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIR-GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-----EEAYGPFQIR 221
Cdd:cd14540   1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLggehdALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 222 IQGMKEHPEYTVRHLTIQHQQEC--RSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSG--------PIVVHCS 291
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGqsRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDvaghnrnpPTLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 292 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYA 350
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 106-341 1.27e-52

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 175.63  E-value: 1.27e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 106 SNFVNPEDLDIPghasKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQ 185
Cdd:cd14610  35 ATNVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWE 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 186 EDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIqgMKEH---PEYTVRHLTIQHQQ--ECRSVKHILFSAWPDH 258
Cdd:cd14610 111 SGCVVIVMLTPLAEnGVKQCYHYWPDEgSNLYHIYEVNL--VSEHiwcEDFLVRSFYLKNLQtnETRTVTQFHFLSWNDQ 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 259 QTPESAGPLLRLVAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAE 337
Cdd:cd14610 189 GVPASTRSLLDFRRKVNKC-YRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKE 267


                ....
gi 21728414 338 QYQF 341
Cdd:cd14610 268 QFEF 271
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 96-342 1.62e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 175.04  E-value: 1.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  96 QLEEEFLKIPSNFVN----PEDLDipghasKDRYKTILPNPQSRVCLgrahsQEDSDYINANY----IRGYDGKEKvYIA 167
Cdd:cd14600  19 QFEQLYRKKPGLAITcaklPQNMD------KNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNK-YIA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 168 TQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA--YGPFQIRIQGMKEHPEYTVRHLTIQHQQ-- 242
Cdd:cd14600  87 TQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTErGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQtg 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 243 ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAanSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIV 322
Cdd:cd14600 167 EERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVE--NEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIV 244

                       250       260
                ....*....|....*....|
gi 21728414 323 CQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14600 245 RKMRDQRAMMVQTSSQYKFV 264
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 124-343 1.87e-52

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 173.31  E-value: 1.87e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 124 RYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKE 202
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDS-YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErGQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 203 KCVHYWPTEEE-AYGPFQIRIQGMKEHPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPET 279
Cdd:cd14623  80 KCAQYWPSDGSvSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21728414 280 AANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14623 160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 149-343 2.07e-52

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 172.21  E-value: 2.07e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKeKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEA-YGPFQIRIQGMKE 227
Cdd:cd14556   1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGtYGPIQVEFVSTTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTIQH----QQECRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIA 302
Cdd:cd14556  80 DEDVISRIFRLQNttrpQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFCA 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21728414 303 TRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14556 160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 95-346 3.08e-52

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: 175.21  E-value: 3.08e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  95 KQLEEEFLKIPSNFVNP--EDLDIPGHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPM 172
Cdd:cd14621  26 KLFREEFNALPACPIQAtcEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNK-FIAAQGPK 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 173 PNTVADFWEMVWQEDVSLIVMLTQLREGKE-KCVHYWPTEE-EAYGPFQIRIQGMKEHPEYTVRHLTIQH------QQEC 244
Cdd:cd14621 105 EETVNDFWRMIWEQNTATIVMVTNLKERKEcKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvtnKKPQ 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 245 RSVKHILFSAWPDHQTPESAGPLLRLVAEVET--PETAansGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIV 322
Cdd:cd14621 185 RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNcnPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261

                       250       260
                ....*....|....*....|....
gi 21728414 323 CQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14621 262 SRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 149-343 4.68e-52

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: 171.63  E-value: 4.68e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIQGMK 226
Cdd:cd14551   1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EHPEYTVRHLTIQHQ------QECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAaNSGPIVVHCSAGIGRTGCF 300
Cdd:cd14551  80 VLVDYTTRKFCIQKVnrgigeKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPP-RAGPIVVHCSAGVGRTGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14551 159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 116-341 5.00e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 174.06  E-value: 5.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 116 IPGHASKDRYKTILPNPQSRVCLgrahSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLT 195
Cdd:cd14608  22 LPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 196 QLRE-GKEKCVHYWPTEEEAYGPFQ---IRIQGMKEHPE--YTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPL 267
Cdd:cd14608  97 RVMEkGSLKCAQYWPQKEEKEMIFEdtnLKLTLISEDIKsyYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASF 176

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21728414 268 LRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIgC----QQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14608 177 LNFLFKVrESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 254
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 149-341 6.95e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 171.08  E-value: 6.95e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEK-VYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPteEEAYGP-----FQIR 221
Cdd:cd14596   1 YINASYITMPVGEEElFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErGKVKCHRYWP--ETLQEPmelenYQLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 222 IQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVetpETAANSGPIVVHCSAGIGRTGC 299
Cdd:cd14596  79 LENYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYM---RKVHNTGPIVVHCSAGIGRAGV 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21728414 300 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14596 156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLF 197
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 148-343 2.74e-50

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 167.10  E-value: 2.74e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 148 DYINANYIRGYDGKEkVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEE-AYGPFQIRIQGM 225
Cdd:cd14622   1 DYINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQErEQEKCVQYWPSEGSvTHGEITIEIKND 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 226 KEHPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIAT 303
Cdd:cd14622  80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21728414 304 RIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14622 160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 148-342 6.15e-50

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 166.27  E-value: 6.15e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 148 DYINANYIR---GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVML-TQLREGKEKCVHYWP--TEEEAYGPFQIR 221
Cdd:cd14601   1 DYINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPepSGSSSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 222 IQGMKEHPEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGC 299
Cdd:cd14601  81 CHSEEGNPAYVFREMTLTNLEknESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN-KRAGKDEPVVVHCSAGIGRTGV 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 300 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14601 160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 149-343 2.22e-49

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 164.86  E-value: 2.22e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVML-TQLREGKEKCVHYWPTE---EEAYGPFQIRIQG 224
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 225 MKEHPEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANS--GPIVVHCSAGIGRTGCF 300
Cdd:cd14539  81 VRTTPTHVERIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlqTPIVVHCSSGVGRTGAF 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21728414 301 IATRIGCQQLKA-RGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14539 161 CLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 149-341 9.98e-49

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 163.00  E-value: 9.98e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTE-EEAYGPFQIRIqgMK 226
Cdd:cd14546   1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEnGVKQCARYWPEEgSEVYHIYEVHL--VS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EH---PEYTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETaANSGPIVVHCSAGIGRTGCFI 301
Cdd:cd14546  79 EHiwcDDYLVRSFYLKNLQtsETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYR-GRSCPIVVHCSDGAGRTGTYI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21728414 302 ATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14546 158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEF 198
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 95-346 2.50e-46

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 159.39  E-value: 2.50e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  95 KQLEE-----EFLKIPSNFVNP--EDLDIPGHASKDRYKTILPNPQSRVCLgRAHSQEDSDYINANYIR-GYDGKEKVYI 166
Cdd:cd14599   7 RKLEEgmvftEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKvTVGGEEWHYI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 167 ATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPT-----EEEAYGPFQIRIQGMKEHPEYTVRHLTIQH 240
Cdd:cd14599  86 ATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEgGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKH 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 241 ---QQEcRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSG---------PIVVHCSAGIGRTGCFIATR--IG 306
Cdd:cd14599 166 llsGQE-RTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMldstkncnpPIVVHCSAGVGRTGVVILTElmIG 244

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21728414 307 CqqLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14599 245 C--LEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 149-341 1.19e-45

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 154.93  E-value: 1.19e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYD-GKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREG--KEKCVHYWPTEE---EAYGPFQIRI 222
Cdd:cd17658   1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNysTAKCADYFPAEEnesREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 223 QGMKeHPEY--TVRHLTIQ---HQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVET-PETAansGPIVVHCSAGIGR 296
Cdd:cd17658  81 KKLK-HSQHsiTLRVLEVQyieSEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGiPPSA---GPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21728414 297 TGCFIAT-----RIGCQQLKArgeVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd17658 157 TGAYCTIhntirRILEGDMSA---VDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 118-341 2.85e-45

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 156.35  E-value: 2.85e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 118 GHASKDRYKTILPNPQSRVCLGRAHSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQL 197
Cdd:cd14609  41 ANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 198 RE-GKEKCVHYWPTEEEA-YGPFQIRIqgMKEH---PEYTVRHLTIQH--QQECRSVKHILFSAWPDHQTPESAGPLLRL 270
Cdd:cd14609 121 VEdGVKQCDRYWPDEGSSlYHIYEVNL--VSEHiwcEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGIPSSTRPLLDF 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21728414 271 VAEVETPeTAANSGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14609 199 RRKVNKC-YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 117-341 1.11e-44

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 154.35  E-value: 1.11e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 117 PGHASKDRYKTILPNPQSRVCLGRAhsqeDSDYINANYIRgYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQ 196
Cdd:cd14607  22 PENRNRNRYRDVSPYDHSRVKLQNT----ENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 197 LRE-GKEKCVHYWPTEEEAYGPFQ---IRIQGMKEHPE--YTVRHLTIQHQQ--ECRSVKHILFSAWPDHQTPESAGPLL 268
Cdd:cd14607  97 IVEkDSVKCAQYWPTDEEEVLSFKetgFSVKLLSEDVKsyYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPASFL 176

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21728414 269 RLVAEV-ETPETAANSGPIVVHCSAGIGRTGCF--IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14607 177 NFLFKVrESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRF 252
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 149-346 3.26e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 149.36  E-value: 3.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIR-GYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWP-----TEEEAYGPFQIR 221
Cdd:cd14598   1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEgGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 222 IQGMKEHPEYTVRHLTIQH---QQEcRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSG--------PIVVHC 290
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHlltGQE-RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTidpkspnpPVLVHC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21728414 291 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd14598 160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PHA02738 PHA02738
hypothetical protein; Provisional
 123-349 3.66e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 3.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  123 DRYKTILPNPQSRVCLGRAHSQedSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GK 201
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  202 EKCVHYWPTEEEA---YGPFQIRIQGMKEHPEYTVRHLTIQHQQEC-RSVKHILFSAWPDHQTPESAGPLLRLVAEVET- 276
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQc 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  277 -PETAANS----------GPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 345
Cdd:PHA02738 210 qKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 21728414  346 LALY 349
Cdd:PHA02738 290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
95-342 5.62e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 150.63  E-value: 5.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  95 KQLEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVclgrahsQEDSDYINANYIRGYDGKekVYIATQGPMPN 174
Cdd:COG5599  18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 175 TVADFWEMVWQEDVSLIVMLTQLREGKE---KCVHYWPTEEEaYGPFQIRI-----QGMKEHPEYTVRHLTIQHQ-QECR 245
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSSeltesIQLRDGIEARTYVLTIKGTgQKKI 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 246 SVKHILFSAWPDHQ--TPESAGPLLRLVAEVETpETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDILGI 321
Cdd:COG5599 168 EIPVLHVKNWPDHGaiSAEALKNLADLIDKKEK-IKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEI 246

                       250       260
                ....*....|....*....|..
gi 21728414 322 VCQLRLDRG-GMIQTAEQYQFL 342
Cdd:COG5599 247 VIDMRTSRNgGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 85-343 1.63e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 147.46  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414   85 WTLQHQPPSPKQLEEEFLKIPSNFVNP--EDLDIPGHASKDRYKTILPNPQSRVCLgRAHSQEDSDYINANYIRGYDgKE 162
Cdd:PHA02747  15 LKRRNQLNCFGIIRDEHHQIILKPFDGliANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFE-DD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  163 KVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLR--EGKEKCVHYWPTEEEA---YGPFQIRIQGMKEHPEY--TVRH 235
Cdd:PHA02747  93 KKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKgtNGEEKCYQYWCLNEDGnidMEDFRIETLKTSVRAKYilTLIE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  236 LTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVE----------TPETAANSgPIVVHCSAGIGRTGCFIATRI 305
Cdd:PHA02747 173 ITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDinrkksgklfNPKDALLC-PIVVHCSDGVGKTGIFCAVDI 251

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21728414  306 GCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:PHA02747 252 CLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 100-346 1.60e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 142.48  E-value: 1.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  100 EFLKIP-----SNFVNPEDLdipghaSKDRYKTILPNPQSRVCLGRAHS-----------------QEDSD--YINANYI 155
Cdd:PHA02746  33 EVMDIPirgttNHFLKKENL------KKNRFHDIPCWDHSRVVINAHESlkmfdvgdsdgkkievtSEDNAenYIHANFV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  156 RGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEE---AYGPFQIRIQGMKEHPEYT 232
Cdd:PHA02746 107 DGFKEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDselAFGRFVAKILDIIEELSFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  233 VRHLTIQHQ--QECRSVKHILFSAWPDHQTPESAGPLLRLVAEV-----ETPETAANS----GPIVVHCSAGIGRTGCFI 301
Cdd:PHA02746 186 KTRLMITDKisDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVneeqaELIKQADNDpqtlGPIVVHCSAGIGRAGTFC 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 21728414  302 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:PHA02746 266 AIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 147-350 3.43e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 138.60  E-value: 3.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  147 SDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLRE-GKEKCVHYWPTEEEA---YGPFQIRI 222
Cdd:PHA02742  78 DDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEdGKEACYPYWMPHERGkatHGEFKIKT 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  223 QGMKEHPEYTVRHLTIQHQQECRS--VKHILFSAWPDHQTPESAGPLLRLVAEVETPETAA---NSG-------PIVVHC 290
Cdd:PHA02742 157 KKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdIKGenivkepPILVHC 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  291 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYA 350
Cdd:PHA02742 237 SAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFA 296
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
246-347 4.36e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 126.70  E-value: 4.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414    246 SVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 323
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVkKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 21728414    324 QLRLDRGGMIQTAEQYQFLHHTLA 347
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 246-347 4.36e-36

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 126.70  E-value: 4.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414    246 SVKHILFSAWPDHQTPESAGPLLRLVAEV-ETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 323
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVkKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 21728414    324 QLRLDRGGMIQTAEQYQFLHHTLA 347
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 149-342 3.23e-34

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 124.74  E-value: 3.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEEEA--YGPFQIRIQGMK 226
Cdd:cd14550   1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPleCETFKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EHP-----EYTVRHLTIQHQQECR--SVKHILFSAWPDHQTP-ESAGPLLRLVAEvetpETAANSGPIVVH-----CSAG 293
Cdd:cd14550  79 HSClsneiRLIVRDFILESTQDDYvlEVRQFQCPSWPNPCSPiHTVFELINTVQE----WAQQRDGPIVVHdryggVQAA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21728414 294 igrTGCFIATRigCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14550 155 ---TFCALTTL--HQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 149-343 4.38e-32

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 119.74  E-value: 4.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEEE-AYGPFQIRIQGMKE 227
Cdd:cd14634   1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKTScCYGPIQVEFVSADI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTI----QHQQECRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVET--PETAANSGPIVVHCSAGIGRTGCF 300
Cdd:cd14634  79 DEDIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKwqEQYDGREGRTVVHCLNGGGRSGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14634 159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 149-341 7.94e-28

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 108.07  E-value: 7.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEK--CVHYWPTE-EEAYGPFQIRIQGM 225
Cdd:cd14637   1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVEFVSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 226 KEHPEYTVRHLTIQH----QQECRSVKHILFSAW-PDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCF 300
Cdd:cd14637  80 SADEDIVTRLFRVQNitrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTY 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 341
Cdd:cd14637 160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRF 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 149-343 8.00e-27

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 105.49  E-value: 8.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEEE-AYGPFQIRIQGMKE 227
Cdd:cd14636   1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMlRYGPIQVECMSCSM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTI----QHQQECRSVKHILFSAWPDH-QTPESAGPLLRLVAEVET--PETAANSGPIVVHCSAGIGRTGCF 300
Cdd:cd14636  79 DCDVISRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqEECDEGEGRTIIHCLNGGGRSGMF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14636 159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 149-346 6.43e-26

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 103.15  E-value: 6.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQGMKE- 227
Cdd:cd17669   1 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 ------HPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTPESAG-PLLRLVAEvetpETAANSGPIVVHCSAGIGRTG 298
Cdd:cd17669  80 hkclsnEEKLIIQDFILEATQDdyVLEVRHFQCPKWPNPDSPISKTfELISIIKE----EAANRDGPMIVHDEHGGVTAG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21728414 299 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd17669 156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 149-346 3.28e-25

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 101.29  E-value: 3.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYdGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYG--PFQIRIQG-- 224
Cdd:cd17670   1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNceAFTVTLISkd 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 225 ---MKEHPEYTVRHLTIQHQQE--CRSVKHILFSAWPDHQTP-ESAGPLLRLVAEvetpETAANSGPIVVHCSAGIGRTG 298
Cdd:cd17670  80 rlcLSNEEQIIIHDFILEATQDdyVLEVRHFQCPKWPNPDAPiSSTFELINVIKE----EALTRDGPTIVHDEFGAVSAG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21728414 299 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 346
Cdd:cd17670 156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 149-343 7.41e-25

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 100.15  E-value: 7.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 149 YINANYIRGYDgKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLrEGKEKCVHYWPTEE-EAYGPFQIRIQGMKE 227
Cdd:cd14635   1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 228 HPEYTVRHLTIQH----QQECRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVET--PETAANSGPIVVHCSAGIGRTGCF 300
Cdd:cd14635  79 EEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKwqEEYNGGEGRTVVHCLNGGGRSGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21728414 301 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14635 159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 132-349 5.81e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.79  E-value: 5.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  132 PQSRVCLGRAHSQEDSDYINANYIRGYDGKEKvYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREgKEKCVHYWPTE 211
Cdd:PHA02740  61 HITRLLHRRIKLFNDEKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD-KKCFNQFWSLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  212 E---EAYGPFQIRIQGM--KEHPEYTVRHLTIQHQQEcRSVKHILFSAWPDHQTPESAGPLL-------RLVAEVETPET 279
Cdd:PHA02740 139 EgcvITSDKFQIETLEIiiKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDAFIdffcnidDLCADLEKHKA 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414  280 AANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 349
Cdd:PHA02740 218 DGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 150-342 1.15e-13

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 69.35  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 150 INANYIRgyDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQI---RIQGMK 226
Cdd:cd14559  18 LNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGTYGSVTVkskKTGKDE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 227 EHPEYTVRH--LTIQHQQECRSVKHILFSAWPDHqTPESAGPLLRLVAEVE-------TPETAANSGPI--------VVH 289
Cdd:cd14559  96 LVDGLKADMynLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKELADLVNksaeekrNFYKSKGSSAIndknkllpVIH 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21728414 290 CSAGIGRTGCFIATRigcQQLKARGEVDILGIVCQLRLDRGG-MIQTAEQYQFL 342
Cdd:cd14559 175 CRAGVGRTGQLAAAM---ELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 268-344 9.40e-13

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 63.91  E-value: 9.40e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21728414 268 LRLVAEVETPEtaansGPIVVHCSAGIGRTGCFIATRIGCQQLKargevDILGIVCQLRLDRGGMI-QTAEQYQFLHH 344
Cdd:cd14494  46 LEVLDQAEKPG-----EPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
255-344 1.48e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.97  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 255 WPDHQTPESAgPLLRLVAEVEtpETAANSGPIVVHCSAGIGRTGCFIAtrigcQQLKARGeVDILGIVCQLRLDRGGMIQ 334
Cdd:COG2453  55 IPDFGAPDDE-QLQEAVDFID--EALREGKKVLVHCRGGIGRTGTVAA-----AYLVLLG-LSAEEALARVRAARPGAVE 125

                        90
                ....*....|
gi 21728414 335 TAEQYQFLHH 344
Cdd:COG2453 126 TPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 286-343 3.07e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 49.57  E-value: 3.07e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21728414 286 IVVHCSAGIGRTGcFIATRIgCQQLKARGEVDilGIVCQLRLDRGGMIQTAEQYQFLH 343
Cdd:cd14505 109 VLIHCKGGLGRTG-LIAACL-LLELGDTLDPE--QAIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 240-342 8.69e-06

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 44.96  E-value: 8.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 240 HQQECRSVKHILFSAwPDHqTPESAGPLLRLVAEVEtpETAANSGPIVVHCSAGIGRTGCFIAtrigCQQLKARGEVDIL 319
Cdd:cd14504  43 HSDTCPGLRYHHIPI-EDY-TPPTLEQIDEFLDIVE--EANAKNEAVLVHCLAGKGRTGTMLA----CYLVKTGKISAVD 114

                        90       100
                ....*....|....*....|...
gi 21728414 320 GIVcQLRLDRGGMIQTAEQYQFL 342
Cdd:cd14504 115 AIN-EIRRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 254-343 3.41e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 41.18  E-value: 3.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 254 AWPDHQTPeSAGPLLRLVAEVETpeTAANSGPIVVHCSAGIGRTGCFIA------TRIGCQQLkargevdILGIvcqlRL 327
Cdd:cd14506  83 GWKDYGVP-SLTTILDIVKVMAF--ALQEGGKVAVHCHAGLGRTGVLIAcylvyaLRMSADQA-------IRLV----RS 148

                        90
                ....*....|....*.
gi 21728414 328 DRGGMIQTAEQYQFLH 343
Cdd:cd14506 149 KRPNSIQTRGQVLCVR 164
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 284-302 5.27e-04

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 40.13  E-value: 5.27e-04
                        10
                ....*....|....*....
gi 21728414 284 GPIVVHCSAGIGRTGCFIA 302
Cdd:cd14499 110 GAIAVHCKAGLGRTGTLIA 128
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 255-302 8.04e-04

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 39.49  E-value: 8.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21728414 255 WPDHQTPesagPLLRLVAEVETPETAANSGP---IVVHCSAGIGRTGCFIA 302
Cdd:cd14497  68 FPDHHPP----PLGLLLEIVDDIDSWLSEDPnnvAVVHCKAGKGRTGTVIC 114
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 249-302 5.23e-03

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 37.35  E-value: 5.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21728414 249 HILFSAW-PDHQTPESAgplLRLVAevetpeTAANSGPIVVHCSAGIGRTGCFIA 302
Cdd:cd14529  63 NLPLSATrPTESDVQSF---LLIMD------LKLAPGPVLIHCKHGKDRTGLVSA 108
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 221-303 5.95e-03

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


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 37.23  E-value: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21728414 221 RIQGMKEHPEYTVRHLTIQHQQECRSVKHILFSAWPDHQTPesagPLLRLVAEVETPETAANSGP---IVVHCSAGIGRT 297
Cdd:cd14561  32 RMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAP----PLDKMCTICKAMESWLNSDPlhvVVIHCRGGKGRI 107


                ....*.
gi 21728414 298 GCFIAT 303
Cdd:cd14561 108 GVVISS 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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