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Conserved domains on  [gi|83753798]
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Chain A, Tyrosine-protein phosphatase, non-receptor type 7

Protein Classification

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

PTPc-N7 domain-containing protein

Graphical summary

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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 ...
 54-299 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: 521.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  54 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 132
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 133 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 212
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 213 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 83753798 293 HHTLALY 299
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 ...
 54-299 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: 521.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  54 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 132
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 133 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 212
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 213 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 83753798 293 HHTLALY 299
Cdd:cd14612 241 HHTLALY 247
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
45-297 4.04e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 319.99  E-value: 4.04e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798     45 QLEEEFLKIPSNFVSPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAQSqEDGDYINANYIRGYDGKeKVYIATQGPM 121
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    122 PNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEE---ETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRS 195
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    196 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 275
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST--GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|..
gi 83753798    276 RLDRGGMIQTAEQYQFLHHTLA 297
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
68-297 5.04e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 308.40  E-value: 5.04e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    68 HASKDRYKTILPNPQSRVCLGRaqSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 147
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   148 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKE-CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLV 220
Cdd:pfam00102  78 EkGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83753798   221 AEVEESPETAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 297
Cdd:pfam00102 158 RKVRKSSLDGRS-GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 72-299 5.59e-45

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 155.47  E-value: 5.59e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   72 DRYKTILPNPQSRVCLGRAQSQedGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 150
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  151 EKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTI-QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 226
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLtDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQC 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  227 PETAA-----------HPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 295
Cdd:PHA02738 210 QKELAqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 83753798  296 LALY 299
Cdd:PHA02738 290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
44-292 7.38e-45

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.71  E-value: 7.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  44 KQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVclgraqsQEDGDYINANYIRGYDGKekVYIATQGPMPN 123
Cdd:COG5599  18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 124 TVSDFWEMVWQEEVSLIVMLTQLREGKE---KCVHYWPTEEEtYGPFQIR--------IQDMKECPEYTVRQLtiQYQEE 192
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSseltesiqLRDGIEARTYVLTIK--GTGQK 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 193 RRSVKHILFSAWPDHQTPeSAGPLLRLVAEVEESPETAAHP-GPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDIL 269
Cdd:COG5599 166 KIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVE 244

                       250       260
                ....*....|....*....|....
gi 83753798 270 GIVCQLRLDRG-GMIQTAEQYQFL 292
Cdd:COG5599 245 EIVIDMRTSRNgGMVQTSEQLDVL 268
 
Name Accession Description Interval E-value
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 54-299 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: 521.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  54 PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQ-EDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMV 132
Cdd:cd14612   1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 133 WQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPES 212
Cdd:cd14612  81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 213 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14612 161 AGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                ....*..
gi 83753798 293 HHTLALY 299
Cdd:cd14612 241 HHTLALY 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 72-294 1.35e-161

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: 448.77  E-value: 1.35e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  72 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE 151
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 152 KCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETA 230
Cdd:cd14547  81 KCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQTE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83753798 231 AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 294
Cdd:cd14547 161 PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 46-299 1.50e-124

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: 356.48  E-value: 1.50e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  46 LEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLgRAQSQED--GDYINANYIRGYDGKEKVYIATQGPMPN 123
Cdd:cd14613   3 LQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCL-TSPDQDDplSSYINANYIRGYGGEEKVYIATQGPTVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 124 TVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSA 203
Cdd:cd14613  82 TVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 204 WPDHQTPESAGPLLRLVAEVEESPETA-AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGM 282
Cdd:cd14613 162 WPDQKTPDNAPPLLQLVQEVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                       250
                ....*....|....*..
gi 83753798 283 IQTAEQYQFLHHTLALY 299
Cdd:cd14613 242 IQTCEQYQFVHHVLSLY 258
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 70-294 2.44e-119

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: 342.28  E-value: 2.44e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  70 SKDRYKTILPNPQSRVCLGRAQSQED-GDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE 148
Cdd:cd14611   1 TKNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 149 GKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPE 228
Cdd:cd14611  81 KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83753798 229 TAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 294
Cdd:cd14611 161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
45-297 4.04e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 319.99  E-value: 4.04e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798     45 QLEEEFLKIPSNFVSPEDLDI---PGHASKDRYKTILPNPQSRVCLGRAQSqEDGDYINANYIRGYDGKeKVYIATQGPM 121
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGP-KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    122 PNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEE---ETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRS 195
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEkGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    196 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 275
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST--GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|..
gi 83753798    276 RLDRGGMIQTAEQYQFLHHTLA 297
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
68-297 5.04e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 308.40  E-value: 5.04e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    68 HASKDRYKTILPNPQSRVCLGRaqSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 147
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   148 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKE-CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLV 220
Cdd:pfam00102  78 EkGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83753798   221 AEVEESPETAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 297
Cdd:pfam00102 158 RKVRKSSLDGRS-GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 98-294 6.30e-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: 274.16  E-value: 6.30e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQD 173
Cdd:cd00047   1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkGREKCERYWPEEGGkplEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 174 MKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPEtaAHPGPIVVHCSAGIGRTGCFI 251
Cdd:cd00047  80 EEELSDYTIRTLELSPKgcSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR--KPNGPIVVHCSAGVGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83753798 252 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHH 294
Cdd:cd00047 158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 71-296 4.50e-79

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: 240.38  E-value: 4.50e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 149
Cdd:cd14553   6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEErS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 150 KEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEes 226
Cdd:cd14553  85 RVKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK-- 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83753798 227 petAAHP---GPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14553 163 ---ACNPpdaGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 73-293 1.41e-78

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: 238.41  E-value: 1.41e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  73 RYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKE 151
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkGRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 152 KCVHYWP--TEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEspET 229
Cdd:cd14548  80 KCDHYWPfdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD--YI 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83753798 230 AAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14548 158 KQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 66-293 7.48e-75

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: 230.71  E-value: 7.48e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  66 PGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQ 145
Cdd:cd14543  27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQK-NAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 146 LRE-GKEKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRL 219
Cdd:cd14543 106 VVErGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLDF 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 220 VAEVEE---------SPETAAHPG--PIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQ 288
Cdd:cd14543 186 LGEVRQqqalavkamGDRWKGHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQ 265


                ....*
gi 83753798 289 YQFLH 293
Cdd:cd14543 266 YYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 98-293 2.56e-74

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: 226.85  E-value: 2.56e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 175
Cdd:cd14549   1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVErGRRKCDQYWPKEgTETYGNIQVTLLSTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 176 ECPEYTVRQLTIQY--------QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVeespeTAAHP---GPIVVHCSAGI 244
Cdd:cd14549  80 VLATYTVRTFSLKNlklkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS-----SAANPpgaGPIVVHCSAGV 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 83753798 245 GRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14549 155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 69-299 5.97e-73

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: 225.03  E-value: 5.97e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  69 ASKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYIR------GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIV 141
Cdd:cd14544   2 KGKNRYKNILPFDHTRVILKDRDPNVPGsDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 142 MLT-QLREGKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQEER---RSVKHILFSAWPDHQTPESAGP 215
Cdd:cd14544  82 MTTkEVERGKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPGG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 216 LLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14544 162 VLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKFI 241


                ....*..
gi 83753798 293 HHTLALY 299
Cdd:cd14544 242 YVAVAQY 248
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 58-298 6.17e-69

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: 214.75  E-value: 6.17e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  58 VSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEV 137
Cdd:cd14614   2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 138 SLIVMLTQLREGKE-KCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTP--ES 212
Cdd:cd14614  81 QIIVMLTQCNEKRRvKCDHYWPFTEEpvAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 213 AGPLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14614 161 AESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238


                ....*.
gi 83753798 293 HHTLAL 298
Cdd:cd14614 239 HQCVQL 244
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 71-297 3.91e-68

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: 213.53  E-value: 3.91e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVM-LTQLREG 149
Cdd:cd14603  33 KNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDG-SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREIEMG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 150 KEKCVHYWPTEEET--YGPFQI-RIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEs 226
Cdd:cd14603 112 KKKCERYWAQEQEPlqTGPFTItLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARR- 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83753798 227 pETAAHPGPIVVHCSAGIGRTGCfIATRIGCQQL----KARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA 297
Cdd:cd14603 191 -LQGSGPEPLCVHCSAGCGRTGV-ICTVDYVRQLlltqRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 98-294 9.87e-68

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: 210.18  E-value: 9.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQIRIQDM 174
Cdd:cd18533   1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEnGREKCDQYWPSGEYEgeYGDLTVELVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 175 KECPE--YTVRQLTIQY-QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFI 251
Cdd:cd18533  81 EENDDggFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 83753798 252 A--------TRIGCQQLKARGEVD-ILGIVCQLRLDRGGMIQTAEQYQFLHH 294
Cdd:cd18533 161 AldslldelKRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 72-292 2.00e-67

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: 210.06  E-value: 2.00e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  72 DRYKTILPNPQSRVCLGRAQSQEDgDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 150
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEqGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 151 EKCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESP 227
Cdd:cd14615  79 TKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83753798 228 ETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14615 159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 72-293 1.62e-66

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: 207.85  E-value: 1.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  72 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 150
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEkGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 151 EKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQEE---RRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE 225
Cdd:cd14617  80 VKCDHYWPADQDSlyYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83753798 226 SPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14617 160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 45-296 1.82e-66

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: 209.51  E-value: 1.82e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  45 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 123
Cdd:cd14626  17 KFSQEYESIdPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR-KQNAYIATQGPLPE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 124 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHI 199
Cdd:cd14626  96 TLSDFWRMVWEQRTATIVMMTRLEEkSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQF 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 200 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 278
Cdd:cd14626 176 QFMAWPDHGVPEYPTPILAFLRRVKAcNPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQ 252

                       250
                ....*....|....*...
gi 83753798 279 RGGMIQTAEQYQFLHHTL 296
Cdd:cd14626 253 RNYMVQTEDQYIFIHEAL 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 72-293 5.05e-65

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: 204.35  E-value: 5.05e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  72 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 150
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEaGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 151 EKCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 226
Cdd:cd14619  80 VKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQveEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83753798 227 PETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14619 160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 98-291 3.03e-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: 201.45  E-value: 3.03e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET----YGPFQIRI 171
Cdd:cd14538   1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEgGKVKCHRYWPDSLNKplicGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 172 QDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpetaAHPGPIVVHCSAGIGRTGC 249
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI----HNSGPIVVHCSAGIGRTGV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83753798 250 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14538 157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIF 198
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 72-296 3.14e-64

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: 202.10  E-value: 3.14e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  72 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLT-QLREGK 150
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 151 EKCVHYWPTEEE--TYGPFQIRIQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 226
Cdd:cd14618  80 VLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRkeRRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 227 PETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14618 160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 98-293 4.10e-63

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: 198.22  E-value: 4.10e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEETYGPFQIRIQDMKE 176
Cdd:cd14555   1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvGRVKCSRYWPDDTEVYGDIKVTLVETEP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 CPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIGRTGCFIATR 254
Cdd:cd14555  80 LAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA--GPIVVHCSAGAGRTGCYIVID 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83753798 255 IGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14555 158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 64-295 1.01e-62

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 198.52  E-value: 1.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  64 DIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML 143
Cdd:cd14554   2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 144 TQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRL 219
Cdd:cd14554  81 TKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGqsRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83753798 220 VAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 295
Cdd:cd14554 161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 70-296 4.05e-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: 197.17  E-value: 4.05e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  70 SKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE- 148
Cdd:cd14630   5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEv 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 149 GKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-- 224
Cdd:cd14630  84 GRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKfl 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83753798 225 ESPETaahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14630 164 NPPDA----GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 58-296 2.19e-61

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: 196.41  E-value: 2.19e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  58 VSPEDLDIPGHASKDRYKTILPNPQSRVCLgRAQSQEDG---DYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 134
Cdd:cd17667  17 ITAEHSNHPDNKHKNRYINILAYDHSRVKL-RPLPGKDSkhsDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 135 EEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQY-------------QEERRSVKHI 199
Cdd:cd17667  95 QNTGIIVMITNLVEkGRRKCDQYWPTEnSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkgRQNERTVIQY 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 200 LFSAWPDHQTPESAGPLLRLVAEveESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDR 279
Cdd:cd17667 175 HYTQWPDMGVPEYALPVLTFVRR--SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                       250
                ....*....|....*..
gi 83753798 280 GGMIQTAEQYQFLHHTL 296
Cdd:cd17667 253 NYLVQTEEQYIFIHDAL 269
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 98-293 2.78e-61

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: 193.50  E-value: 2.78e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG-KEKCVHYWPTEEE---TYGPFQIRIQD 173
Cdd:cd14557   1 YINASYIDGFKEPRK-YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGnRNKCAQYWPSMEEgsrAFGDVVVKINE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 174 MKECPEYTVRQLTIQYQEERRS---VKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCF 250
Cdd:cd14557  80 EKICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGTY 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83753798 251 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14557 158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 97-291 3.95e-60

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: 191.00  E-value: 3.95e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  97 DYINANY----IRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQI 169
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErGRVKCHQYWPDLGETmqFGNLQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 170 RIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHpgPIVVHCSAGIGRT 247
Cdd:cd14541  80 TCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIGRT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 83753798 248 GCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14541 158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 71-303 6.37e-60

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: 193.23  E-value: 6.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 149
Cdd:cd14604  60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEmG 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 150 KEKCVHYWPTEEE---TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 226
Cdd:cd14604 139 RKKCERYWPLYGEepmTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 227 PEtaAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKA---RGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLA-LYAGQ 302
Cdd:cd14604 219 QE--HEDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqLFEKQ 296


                .
gi 83753798 303 L 303
Cdd:cd14604 297 L 297
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 74-296 7.92e-60

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: 190.92  E-value: 7.92e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  74 YKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE-K 152
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEeK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 153 CVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQYQ-----EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 226
Cdd:cd14620  80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 227 peTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14620 160 --NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 98-294 8.80e-60

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: 189.56  E-value: 8.80e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE---TYGPFQIRIQD 173
Cdd:cd14542   1 YINANFIKGVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEmGKKKCERYWPEEGEeqlQFGPFKISLEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 174 MKE-CPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIA 252
Cdd:cd14542  80 EKRvGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGTICA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 83753798 253 TRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQFLHH 294
Cdd:cd14542 158 IDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 98-293 9.01e-60

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: 189.88  E-value: 9.01e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEETYGPFQIRIQDMKE 176
Cdd:cd14632   1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 CPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATR 254
Cdd:cd14632  80 LAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYIVLD 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 83753798 255 IGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14632 158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 70-299 1.21e-59

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: 191.00  E-value: 1.21e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  70 SKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYI-------RGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIV 141
Cdd:cd14605   4 NKNRYKNILPFDHTRVVLHDGDPNEPVsDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 142 MLT-QLREGKEKCVHYWPTEE--ETYGpfQIRIQDMKECP--EYTVRQLTI----QYQEERrSVKHILFSAWPDHQTPES 212
Cdd:cd14605  84 MTTkEVERGKSKCVKYWPDEYalKEYG--VMRVRNVKESAahDYILRELKLskvgQGNTER-TVWQYHFRTWPDHGVPSD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 213 AGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQY 289
Cdd:cd14605 161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240

                       250
                ....*....|
gi 83753798 290 QFLHHTLALY 299
Cdd:cd14605 241 RFIYMAVQHY 250
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 66-299 1.46e-59

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: 191.25  E-value: 1.46e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  66 PGHASKDRYKTILPNPQSRVCLGRAQSQEDG-DYINANYIR----GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLI 140
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVKnqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 141 VMLT-QLREGKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQL---TIQYQEERRSVKHILFSAWPDHQTPESAG 214
Cdd:cd14606  96 VMTTrEVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELIREIWHYQYLSWPDHGVPSEPG 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 215 PLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG---EVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14606 176 GVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKF 255


                ....*...
gi 83753798 292 LHHTLALY 299
Cdd:cd14606 256 IYVAIAQF 263
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 98-293 1.90e-59

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: 188.76  E-value: 1.90e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGkEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG-KEKCVHYWPTEEETYGPFQIRIQDMKE 176
Cdd:cd14558   1 YINASFIDGYWG-PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGdQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 CPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES-PETAAHPG---PIVVHCSAGIGRTGCF 250
Cdd:cd14558  80 SPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKlPYKNSKHGrsvPIVVHCSDGSSRTGIF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83753798 251 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14558 160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 45-296 2.52e-59

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: 191.46  E-value: 2.52e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  45 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 123
Cdd:cd14625  23 KLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 124 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHI 199
Cdd:cd14625 102 TFGDFWRMVWEQRSATVVMMTKLEEkSRIKCDQYWPSRgTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 200 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 278
Cdd:cd14625 182 QFTAWPDHGVPEYPTPFLAFLRRVKTcNPPDA---GPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQ 258

                       250
                ....*....|....*...
gi 83753798 279 RGGMIQTAEQYQFLHHTL 296
Cdd:cd14625 259 RNYMVQTEDQYSFIHDAL 276
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 46-303 5.09e-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: 190.71  E-value: 5.09e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  46 LEEEFLKIPSN------FVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQG 119
Cdd:cd14628  27 MELEFKRLASSkahtsrFISA---NLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 120 PMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRS 195
Cdd:cd14628 103 PLAETTEDFWRMLWEHNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRT 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 196 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQL 275
Cdd:cd14628 183 VRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKML 262

                       250       260
                ....*....|....*....|....*...
gi 83753798 276 RLDRGGMIQTAEQYQFLHHTLALYAGQL 303
Cdd:cd14628 263 RTQRPAMVQTEDQYQFCYRAALEYLGSF 290
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 84-296 7.63e-59

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: 187.92  E-value: 7.63e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  84 RVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE 162
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvGRVKCYKYWPDDTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 163 TYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHC 240
Cdd:cd14631  80 VYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA--GPIVVHC 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 83753798 241 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14631 158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 55-301 2.31e-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: 189.17  E-value: 2.31e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  55 SNFVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 134
Cdd:cd14627  43 SRFISA---NLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 135 EEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTP 210
Cdd:cd14627 119 NNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVP 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 211 ESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 290
Cdd:cd14627 199 KSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQ 278

                       250
                ....*....|.
gi 83753798 291 FLHHTLALYAG 301
Cdd:cd14627 279 FCYQAALEYLG 289
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 98-291 1.29e-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: 1.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE-TYGPFQIRIQDMK 175
Cdd:cd14552   1 YINASFIDGYRQKDA-YIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErSQNKCAQYWPEDGSvSSGDITVELKDQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 176 ECPEYTVRQ--LTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGCFIAT 253
Cdd:cd14552  80 DYEDYTLRDflVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGN-HPITVHCSAGAGRTGTFCAL 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 83753798 254 RIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14552 159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEF 196
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 45-296 1.59e-57

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: 186.86  E-value: 1.59e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  45 QLEEEFLKI-PSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPN 123
Cdd:cd14624  23 KFSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYR-KQNAYIATQGALPE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 124 TVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHI 199
Cdd:cd14624 102 TFGDFWRMIWEQRSATVVMMTKLEErSRVKCDQYWPSRgTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKREVRQF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 200 LFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLD 278
Cdd:cd14624 182 QFTAWPDHGVPEHPTPFLAFLRRVKTcNPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQ 258

                       250
                ....*....|....*...
gi 83753798 279 RGGMIQTAEQYQFLHHTL 296
Cdd:cd14624 259 RNYMVQTEDQYIFIHDAL 276
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 98-296 1.57e-56

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: 181.72  E-value: 1.57e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 175
Cdd:cd17668   1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEkGRRKCDQYWPADgSEEYGNFLVTQKSVQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 176 ECPEYTVRQLTIQ-------YQEER---RSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpGPIVVHCSAGIG 245
Cdd:cd17668  80 VLAYYTVRNFTLRntkikkgSQKGRpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAV--GPVVVHCSAGVG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 83753798 246 RTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd17668 158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 71-299 2.95e-56

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: 181.95  E-value: 2.95e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVCLGraqsqEDGDYINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG 149
Cdd:cd14597   6 KNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEEfVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 150 -KEKCVHYWPteeETYGP-------FQIRIQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAGPLLRL 219
Cdd:cd14597  81 gKIKCQRYWP---EILGKttmvdnrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 220 VAEVEESPETaahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLaLY 299
Cdd:cd14597 158 ISYMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI-LY 232
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 71-293 3.19e-56

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: 181.58  E-value: 3.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 149
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 150 KEKCVHYW--PTEEE-TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEV--- 223
Cdd:cd14602  80 KKKCERYWaePGEMQlEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVrcy 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83753798 224 --EESPetaahpgPIVVHCSAGIGRTGCFIATRIGCQQLKAR---GEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14602 160 qeDDSV-------PICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 71-296 8.75e-56

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 181.78  E-value: 8.75e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-G 149
Cdd:cd14633  43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvG 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 150 KEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ--EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEsp 227
Cdd:cd14633 122 RVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 199

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83753798 228 ETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14633 200 KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 55-303 1.36e-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: 181.85  E-value: 1.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  55 SNFVSPedlDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQ 134
Cdd:cd14629  43 SRFISA---NLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 135 EEVSLIVMLTQLRE-GKEKCVHYWPTEEET-YGPFQIRIQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTP 210
Cdd:cd14629 119 HNSTIVVMLTKLREmGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTIRQFQFTDWPEQGVP 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 211 ESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 290
Cdd:cd14629 199 KTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQ 278

                       250
                ....*....|...
gi 83753798 291 FLHHTLALYAGQL 303
Cdd:cd14629 279 LCYRAALEYLGSF 291
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 37-296 9.28e-55

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: 179.83  E-value: 9.28e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  37 QRQPPSPKQLEEEFLKIPSNFV--SPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvY 114
Cdd:cd14621  19 RRMADDNKLFREEFNALPACPIqaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNK-F 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 115 IATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKE-KCVHYWPTEE-ETYGPFQIRIQDMKECPEYTVRQLTIQY--- 189
Cdd:cd14621  98 IAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKEcKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgd 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 190 ---QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-SPETAahpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGE 265
Cdd:cd14621 178 vtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNcNPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERK 254

                       250       260       270
                ....*....|....*....|....*....|.
gi 83753798 266 VDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14621 255 VDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 65-291 1.24e-54

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: 179.07  E-value: 1.24e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  65 IPGHASKDRYKTILPNPQSRVCLgraqSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLT 144
Cdd:cd14608  22 LPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 145 QLRE-GKEKCVHYWPTEEETYGPFQ---IRI----QDMKEcpEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAG 214
Cdd:cd14608  97 RVMEkGSLKCAQYWPQKEEKEMIFEdtnLKLtlisEDIKS--YYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPA 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 215 PLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIgC----QQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQ 290
Cdd:cd14608 175 SFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-ClllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLR 253


                .
gi 83753798 291 F 291
Cdd:cd14608 254 F 254
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 98-293 1.70e-54

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: 176.26  E-value: 1.70e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIRIQDMK 175
Cdd:cd14551   1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 176 ECPEYTVRQLTIQYQ------EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGC 249
Cdd:cd14551  80 VLVDYTTRKFCIQKVnrgigeKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA--NPPRAGPIVVHCSAGVGRTGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 83753798 250 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14551 158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 71-291 4.65e-54

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: 176.04  E-value: 4.65e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  71 KDRYKTILPNPQSRVclgRAQS-QEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE- 148
Cdd:cd14545   1 LNRYRDRDPYDHDRS---RVKLkQGDNDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEk 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 149 GKEKCVHYWPTEEET-----YGPFQIRIQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQTPESAGPLLRLVA 221
Cdd:cd14545  77 GQIKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83753798 222 EVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARG--EVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14545 157 KVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 98-291 1.57e-53

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: 173.78  E-value: 1.57e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEK-VYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWP-TEEETY--GPFQIRIQ 172
Cdd:cd14596   1 YINASYITMPVGEEElFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErGKVKCHRYWPeTLQEPMelENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 173 DMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETaahpGPIVVHCSAGIGRTGCF 250
Cdd:cd14596  81 NYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGVL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 83753798 251 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14596 157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLF 197
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 72-293 1.66e-53

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 174.32  E-value: 1.66e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  72 DRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 150
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEkGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 151 EKCVHYWPTEEETYGPF-QIRIQDMKE--CPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESp 227
Cdd:cd14616  80 IRCHQYWPEDNKPVTVFgDIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS- 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83753798 228 eTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14616 159 -RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 98-300 1.06e-52

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: 172.26  E-value: 1.06e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-----EETYGPFQIR 170
Cdd:cd14540   1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLggehdALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 171 IQDMKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEV--------EESPETAAHPgPIVVHC 240
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGqsRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrhtnQDVAGHNRNP-PTLVHC 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 241 SAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYA 300
Cdd:cd14540 160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 97-293 1.54e-52

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: 171.34  E-value: 1.54e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  97 DYINANYIRGYDGKEkVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEE-TYGPFQIRIQDM 174
Cdd:cd14622   1 DYINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQErEQEKCVQYWPSEGSvTHGEITIEIKND 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 175 KECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVE-ESPETAAHPgpIVVHCSAGIGRTGCFI 251
Cdd:cd14622  80 TLLETISIRDFLVTYNQEKqtRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQkQQQQTGNHP--IVVHCSAGAGRTGTFI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83753798 252 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14622 158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 73-293 1.60e-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: 172.15  E-value: 1.60e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  73 RYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKE 151
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDS-YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErGQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 152 KCVHYWPTEEE-TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRS--VKHILFSAWPDHQTPESAGPLLRLVAEVEESPE 228
Cdd:cd14623  80 KCAQYWPSDGSvSYGDITIELKKEEECESYTVRDLLVTNTRENKSrqIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83753798 229 TAAHpGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14623 160 QSGN-HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 45-292 2.93e-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: 172.73  E-value: 2.93e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  45 QLEEEFLKIPSNFVS----PEDLDipghasKDRYKTILPNPQSRVCLgraqsQEDGDYINANY----IRGYDGKEKvYIA 116
Cdd:cd14600  19 QFEQLYRKKPGLAITcaklPQNMD------KNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNK-YIA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 117 TQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTEEET--YGPFQIRIQDMKECPEYTVRQLTIQYQE-- 191
Cdd:cd14600  87 TQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTErGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQtg 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 192 ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhpgPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGI 271
Cdd:cd14600 167 EERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE---PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDI 243

                       250       260
                ....*....|....*....|.
gi 83753798 272 VCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14600 244 VRKMRDQRAMMVQTSSQYKFV 264
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 97-292 4.85e-52

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: 170.13  E-value: 4.85e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  97 DYINANYIR---GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML-TQLREGKEKCVHYWP--TEEETYGPFQIR 170
Cdd:cd14601   1 DYINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPepSGSSSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 171 IQDMKECPEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTG 248
Cdd:cd14601  81 CHSEEGNPAYVFREMTLTNLEknESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 83753798 249 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14601 159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 98-293 2.81e-51

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: 167.97  E-value: 2.81e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKeKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEE-TYGPFQIRIQDMKE 176
Cdd:cd14556   1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 CPEYTVRQLTIQ----YQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGCFI 251
Cdd:cd14556  80 DEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGE-GPIVVHCLNGVGRSGVFC 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83753798 252 ATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14556 159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 55-291 3.81e-51

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: 170.24  E-value: 3.81e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  55 SNFVSPEDLDIPghasKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQ 134
Cdd:cd14610  35 ATNVAQREENVQ----KNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWE 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 135 EEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIR-IQDMKECPEYTVRQLTIQ--YQEERRSVKHILFSAWPDHQT 209
Cdd:cd14610 111 SGCVVIVMLTPLAEnGVKQCYHYWPDEgSNLYHIYEVNlVSEHIWCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGV 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 210 PESAGPLLRLVAEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQ 288
Cdd:cd14610 191 PASTRSLLDFRRKVNKC--YRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQ 268


                ...
gi 83753798 289 YQF 291
Cdd:cd14610 269 FEF 271
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 98-293 1.29e-50

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: 166.41  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML-TQLREGKEKCVHYWPTE---EETYGPFQIRIQD 173
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 174 MKECPEYTVRQLTIQYQEER--RSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-----SPETAahpgPIVVHCSAGIGR 246
Cdd:cd14539  81 VRTTPTHVERIISIQHKDTRlsRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylqqRSLQT----PIVVHCSSGVGR 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 83753798 247 TGCFIATRIGCQQLKA-RGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14539 157 TGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 98-291 5.23e-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: 162.23  E-value: 5.23e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWPTE-EETYGPFQIR-IQDM 174
Cdd:cd14546   1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEnGVKQCARYWPEEgSEVYHIYEVHlVSEH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 175 KECPEYTVRQL---TIQYQEErRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPEtaAHPGPIVVHCSAGIGRTGCFI 251
Cdd:cd14546  81 IWCDDYLVRSFylkNLQTSET-RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYR--GRSCPIVVHCSDGAGRTGTYI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 83753798 252 ATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14546 158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEF 198
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 98-291 6.27e-47

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: 156.86  E-value: 6.27e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYD-GKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREG--KEKCVHYWPTEE---ETYGPFQIRI 171
Cdd:cd17658   1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNysTAKCADYFPAEEnesREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 172 QDMKeCPEY--TVRQLTIQY---QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAahpGPIVVHCSAGIGR 246
Cdd:cd17658  81 KKLK-HSQHsiTLRVLEVQYiesEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA---GPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 83753798 247 TGCFIAT-----RIGCQQLKArgeVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd17658 157 TGAYCTIhntirRILEGDMSA---VDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 66-291 1.57e-46

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: 157.44  E-value: 1.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  66 PGHASKDRYKTILPNPQSRVCLGRAqsqeDGDYINANYIRgYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQ 145
Cdd:cd14607  22 PENRNRNRYRDVSPYDHSRVKLQNT----ENDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 146 LRE-GKEKCVHYWPTEEETYGPFQ-----IRI--QDMKEcpEYTVRQLTIQYQE--ERRSVKHILFSAWPDHQTPESAGP 215
Cdd:cd14607  97 IVEkDSVKCAQYWPTDEEEVLSFKetgfsVKLlsEDVKS--YYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPAS 174

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83753798 216 LLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCF--IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14607 175 FLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRF 252
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 65-296 2.99e-45

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: 155.16  E-value: 2.99e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  65 IPGHASKDRYKTILPNPQSRVCLGRAQSQEDGdYINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVML 143
Cdd:cd14599  35 LPENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKvTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 144 TQLRE-GKEKCVHYWPT-----EEETYGPFQIRIQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGP 215
Cdd:cd14599 114 TAEEEgGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEEVQG 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 216 LLRLVAEVEE---------SPETAAHPgPIVVHCSAGIGRTGCFIATR--IGCqqLKARGEVDILGIVCQLRLDRGGMIQ 284
Cdd:cd14599 194 FLSYLEEIQSvrrhtnsmlDSTKNCNP-PIVVHCSAGVGRTGVVILTElmIGC--LEHNEKVEVPVMLRHLREQRMFMIQ 270

                       250
                ....*....|..
gi 83753798 285 TAEQYQFLHHTL 296
Cdd:cd14599 271 TIAQYKFVYQVL 282
PHA02738 PHA02738
hypothetical protein; Provisional
 72-299 5.59e-45

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 155.47  E-value: 5.59e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   72 DRYKTILPNPQSRVCLGRAQSQedGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GK 150
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnGR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  151 EKCVHYWPTEEET---YGPFQIRIQDMKECPEYTVRQLTI-QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEES 226
Cdd:PHA02738 130 EKCFPYWSDVEQGsirFGKFKITTTQVETHPHYVKSTLLLtDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQC 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  227 PETAA-----------HPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHT 295
Cdd:PHA02738 210 QKELAqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....
gi 83753798  296 LALY 299
Cdd:PHA02738 290 VKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
44-292 7.38e-45

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 153.71  E-value: 7.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  44 KQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVclgraqsQEDGDYINANYIRGYDGKekVYIATQGPMPN 123
Cdd:COG5599  18 SRLSTLTNELAPSHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNH--RYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 124 TVSDFWEMVWQEEVSLIVMLTQLREGKE---KCVHYWPTEEEtYGPFQIR--------IQDMKECPEYTVRQLtiQYQEE 192
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEISKpkvKMPVYFRQDGE-YGKYEVSseltesiqLRDGIEARTYVLTIK--GTGQK 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 193 RRSVKHILFSAWPDHQTPeSAGPLLRLVAEVEESPETAAHP-GPIVVHCSAGIGRTGCFIATRIGCQQLKARGE--VDIL 269
Cdd:COG5599 166 KIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVE 244

                       250       260
                ....*....|....*....|....
gi 83753798 270 GIVCQLRLDRG-GMIQTAEQYQFL 292
Cdd:COG5599 245 EIVIDMRTSRNgGMVQTSEQLDVL 268
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 67-291 1.37e-44

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: 153.27  E-value: 1.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  67 GHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQL 146
Cdd:cd14609  41 ANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 147 RE-GKEKCVHYWPTEEET-YGPFQIR-IQDMKECPEYTVRQL---TIQYQEErRSVKHILFSAWPDHQTPESAGPLLRLV 220
Cdd:cd14609 121 VEdGVKQCDRYWPDEGSSlYHIYEVNlVSEHIWCEDFLVRSFylkNVQTQET-RTLTQFHFLSWPAEGIPSSTRPLLDFR 199

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83753798 221 AEVEESpeTAAHPGPIVVHCSAGIGRTGCFIATRIGCQQL-KARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14609 200 RKVNKC--YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 98-296 2.18e-42

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: 145.50  E-value: 2.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIR-GYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLRE-GKEKCVHYWP-----TEEETYGPFQIR 170
Cdd:cd14598   1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEgGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 171 IQDMKECPEYTVRQLTIQY--QEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVE-------ESPETAAHPGPIVVHCS 241
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnSTIDPKSPNPPVLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 83753798 242 AGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 23-296 4.83e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 145.17  E-value: 4.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   23 FLRTAGHPlTRWALQRQPPSpkqleeEFLKIP-----SNFVSPEDLdipghaSKDRYKTILPNPQSRVCLGRAQS----- 92
Cdd:PHA02746  14 FFDKTNHA-KFCEFVLLEHA------EVMDIPirgttNHFLKKENL------KKNRFHDIPCWDHSRVVINAHESlkmfd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   93 ------------QEDGD--YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWP 158
Cdd:PHA02746  81 vgdsdgkkievtSEDNAenYIHANFVDGFKEANK-FICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  159 TEEE---TYGPFQIRIQDMKECPEYTVRQLTI--QYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEE-------- 225
Cdd:PHA02746 160 KEEDselAFGRFVAKILDIIEELSFTKTRLMItdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikq 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83753798  226 SPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:PHA02746 240 ADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 70-300 5.00e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 144.37  E-value: 5.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   70 SKDRYKTILPNPQSRVCLgraqSQEDG--DYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLR 147
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVIL----KIEDGgdDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  148 E-GKEKCVHYWPTEEE---TYGPFQIRIQDMKECPEYTVRQLTIQYQEERRS--VKHILFSAWPDHQTPESAGPLLRLV- 220
Cdd:PHA02742 129 EdGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVl 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  221 --------AEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:PHA02742 209 avreadlkADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFC 288


                 ....*...
gi 83753798  293 HHTLALYA 300
Cdd:PHA02742 289 YFIVLIFA 296
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 50-293 1.35e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.60  E-value: 1.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   50 FLKIPSNFVSPEDldipghASKDRYKTILPNPQSRVCLgRAQSQEDGDYINANYIRGYDgKEKVYIATQGPMPNTVSDFW 129
Cdd:PHA02747  39 FDGLIANFEKPEN------QPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFE-DDKKFIATQGPFAETCADFW 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  130 EMVWQEEVSLIVMLTQLR--EGKEKCVHYW-PTEEETYGPFQIRIQDMKEC--PEY--TVRQLTIQYQEERRSVKHILFS 202
Cdd:PHA02747 111 KAVWQEHCSIIVMLTPTKgtNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSvrAKYilTLIEITDKILKDSRKISHFQCS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  203 AWPDHQTPESAGPLLRLVAEVEESPETA--------AHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQ 274
Cdd:PHA02747 191 EWFEDETPSDHPDFIKFIKIIDINRKKSgklfnpkdALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                        250
                 ....*....|....*....
gi 83753798  275 LRLDRGGMIQTAEQYQFLH 293
Cdd:PHA02747 271 IREQRHAGIMNFDDYLFIQ 289
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
195-297 1.77e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 131.71  E-value: 1.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    195 SVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 273
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 83753798    274 QLRLDRGGMIQTAEQYQFLHHTLA 297
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 195-297 1.77e-38

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: 131.71  E-value: 1.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798    195 SVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKAR-GEVDILGIVC 273
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 83753798    274 QLRLDRGGMIQTAEQYQFLHHTLA 297
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 98-293 3.32e-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: 118.59  E-value: 3.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEE-TYGPFQIRI--QDM 174
Cdd:cd14634   1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQLCMQYWPEKTScCYGPIQVEFvsADI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 175 KEcpEYTVRQLTI----QYQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEESPETA-AHPGPIVVHCSAGIGRTG 248
Cdd:cd14634  79 DE--DIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYdGREGRTVVHCLNGGGRSG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 83753798 249 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14634 157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 98-292 2.71e-31

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: 115.88  E-value: 2.71e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEET--YGPFQIRIQDMK 175
Cdd:cd14550   1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPleCETFKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 176 ECP-----EYTVRQLTIQYQEERR--SVKHILFSAWPDHQTP-ESAGPLLRLVAEveespETAAHPGPIVVH-----CSA 242
Cdd:cd14550  79 HSClsneiRLIVRDFILESTQDDYvlEVRQFQCPSWPNPCSPiHTVFELINTVQE-----WAQQRDGPIVVHdryggVQA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 83753798 243 GigrTGCFIATRigCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFL 292
Cdd:cd14550 154 A---TFCALTTL--HQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 98-291 6.23e-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: 107.30  E-value: 6.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEK--CVHYWPTE-EETYGPFQIRIQDM 174
Cdd:cd14637   1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPgLQQYGPMEVEFVSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 175 KECPEYTVRQLTIQ----YQEERRSVKHILFSAW-PDHQTPESAGPLLRLVAEVEESPETAAHpGPIVVHCSAGIGRTGC 249
Cdd:cd14637  80 SADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGE-GRTVVHCLNGGGRSGT 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 83753798 250 FIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQF 291
Cdd:cd14637 159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRF 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 98-293 4.44e-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: 105.11  E-value: 4.44e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEEE-TYGPFQIRIQDMKE 176
Cdd:cd14636   1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMlRYGPIQVECMSCSM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 CPEYTVRQLTI----QYQEERRSVKHILFSAWPDH-QTPESAGPLLRLVAEVEE-SPETAAHPGPIVVHCSAGIGRTGCF 250
Cdd:cd14636  79 DCDVISRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGRSGMF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83753798 251 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14636 159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 98-296 5.03e-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: 99.75  E-value: 5.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYdGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYG--PFQIR-IQDM 174
Cdd:cd17670   1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNceAFTVTlISKD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 175 KEC----PEYTVRQLTIQYQEERR--SVKHILFSAWPDHQTPESAgpLLRLVAEVEEspETAAHPGPIVVHCSAGIGRTG 248
Cdd:cd17670  80 RLClsneEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPISS--TFELINVIKE--EALTRDGPTIVHDEFGAVSAG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 83753798 249 CFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd17670 156 TLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 98-296 5.10e-25

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: 99.68  E-value: 5.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKE- 176
Cdd:cd17669   1 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEe 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 --CPEyTVRQLTIQ------YQEER-RSVKHILFSAWPDHQTPESAgpLLRLVAEVEEspETAAHPGPIVVHCSAGIGRT 247
Cdd:cd17669  80 hkCLS-NEEKLIIQdfileaTQDDYvLEVRHFQCPKWPNPDSPISK--TFELISIIKE--EAANRDGPMIVHDEHGGVTA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 83753798 248 GCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTL 296
Cdd:cd17669 155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 98-293 5.11e-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: 99.76  E-value: 5.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  98 YINANYIRGYDgKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLrEGKEKCVHYWPTEE-ETYGPFQIRIQDMKE 176
Cdd:cd14635   1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 177 CPEYTVRQLTI----QYQEERRSVKHILFSAWPDHQ-TPESAGPLLRLVAEVEE-SPETAAHPGPIVVHCSAGIGRTGCF 250
Cdd:cd14635  79 EEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKwQEEYNGGEGRTVVHCLNGGGRSGTF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 83753798 251 IATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14635 159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 81-299 2.48e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 86.17  E-value: 2.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   81 PQSRVCLGRAQSQEDGDYINANYIRGYDGKEKvYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREgKEKCVHYWPTE 160
Cdd:PHA02740  61 HITRLLHRRIKLFNDEKVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD-KKCFNQFWSLK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  161 E---ETYGPFQIRIQDMKECPEY--TVRQLTIQYQEERRsVKHILFSAWPDHQTPESAGPLLRLVAEVE------ESPET 229
Cdd:PHA02740 139 EgcvITSDKFQIETLEIIIKPHFnlTLLSLTDKFGQAQK-ISHFQYTAWPADGFSHDPDAFIDFFCNIDdlcadlEKHKA 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  230 AAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALY 299
Cdd:PHA02740 218 DGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 77-292 8.08e-18

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: 80.52  E-value: 8.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  77 ILPNPQSRVclgraqSQEDGDYINANYIRgyDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHY 156
Cdd:cd14559   2 RFTNIQTRV------STPVGKNLNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 157 WPTEEETYGpfQIRIQDMKECPEYTVR-------QLTIQYQEERRSVKHILFSAWPDHqTPESAGPLLRLVAEVEESPET 229
Cdd:cd14559  74 YFRQSGTYG--SVTVKSKKTGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKELADLVNKSAEE 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83753798 230 ------AAHPGPI--------VVHCSAGIGRTGCFIATRigcQQLKARGEVDILGIVCQLRLDRGG-MIQTAEQYQFL 292
Cdd:cd14559 151 krnfykSKGSSAIndknkllpVIHCRAGVGRTGQLAAAM---ELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 101-294 1.79e-14

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: 68.53  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 101 ANYIRGydgkeKVYIATQGPMPNtVSDFWEMVWQEEVSLIVMLTqlregkekcvhywpteeetygpfqiriqdmkecpey 180
Cdd:cd14494   1 FNWIDP-----LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLT------------------------------------ 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 181 tvrqltiqyqeerrsvkhilfsawpdhqtpesaGPLLRLVAEVEESPETaaHPGPIVVHCSAGIGRTGCFIATRIGCQQL 260
Cdd:cd14494  39 ---------------------------------LAMVDRFLEVLDQAEK--PGEPVLVHCKAGVGRTGTLVACYLVLLGG 83

                       170       180       190
                ....*....|....*....|....*....|....*
gi 83753798 261 KargevDILGIVCQLRLDRGGMI-QTAEQYQFLHH 294
Cdd:cd14494  84 M-----SAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 179-293 4.24e-09

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: 54.58  E-value: 4.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 179 EYTVRQLTIQYQEERRSVKHILFsawPDHQTPESAGPLLRLVAEVEESPETAAHpgpIVVHCSAGIGRTGcFIATRIgCQ 258
Cdd:cd14505  58 ELGVPDLLEQYQQAGITWHHLPI---PDGGVPSDIAQWQELLEELLSALENGKK---VLIHCKGGLGRTG-LIAACL-LL 129

                        90       100       110
                ....*....|....*....|....*....|....*
gi 83753798 259 QLKARGEVDilGIVCQLRLDRGGMIQTAEQYQFLH 293
Cdd:cd14505 130 ELGDTLDPE--QAIAAVRALRPGAIQTPKQENFLH 162
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
204-294 1.61e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.58  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 204 WPDHQTPESAgPLLRLVAEVEESpetAAHPGPIVVHCSAGIGRTGCFIAtrigcQQLKARGeVDILGIVCQLRLDRGGMI 283
Cdd:COG2453  55 IPDFGAPDDE-QLQEAVDFIDEA---LREGKKVLVHCRGGIGRTGTVAA-----AYLVLLG-LSAEEALARVRAARPGAV 124

                        90
                ....*....|.
gi 83753798 284 QTAEQYQFLHH 294
Cdd:COG2453 125 ETPAQRAFLER 135
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 209-292 4.11e-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: 45.73  E-value: 4.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 209 TPESAGPLLRLVAEVEESPetaAHPGPIVVHCSAGIGRTGCFIAtrigCQQLKARGEVDILGIVcQLRLDRGGMIQTAEQ 288
Cdd:cd14504  61 TPPTLEQIDEFLDIVEEAN---AKNEAVLVHCLAGKGRTGTMLA----CYLVKTGKISAVDAIN-EIRRIRPGSIETSEQ 132


                ....
gi 83753798 289 YQFL 292
Cdd:cd14504 133 EKFV 136
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
44-289 4.26e-06

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 47.87  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   44 KQLEEEFLKIPSNFVSPEDLDIPGHA-SKDRYKTILPNPQSRVCLgraqsqEDGDYINANYIRgYDGKEkvyIATQGPMP 122
Cdd:PRK15375 273 KNVTAELEKIEAGAPMPQTMSGPTLGlARFAVSSIPINQQTQVKL------SDGMPVPVNTLT-FDGKP---VALAGSYP 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  123 NTVSDFWE----MVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEY-TVRQLTIQYQ--EERRS 195
Cdd:PRK15375 343 KNTPDALEahmkMLLEKECSCLVVLTSEDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLScgEKRYT 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798  196 VKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAhPG--------PIvVHCSAGIGRTGCFIATRIgcqqLKARGEVD 267
Cdd:PRK15375 423 IPVLHVKNWPDHQPLPSTDQLEYLADRVKNSNQNGA-PGrsssdkhlPM-IHCLGGVGRTGTMAAALV----LKDNPHSN 496

                        250       260
                 ....*....|....*....|...
gi 83753798  268 ILGIVCQLRLDRGG-MIQTAEQY 289
Cdd:PRK15375 497 LEQVRADFRNSRNNrMLEDASQF 519
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 193-293 5.53e-05

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 43.49  E-value: 5.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798 193 RRSVKHILFsAWPDHQTPeSAGPLLRLVAEVEESPEtaaHPGPIVVHCSAGIGRTGCFIA------TRIGCQQLkargev 266
Cdd:cd14506  74 RAGIYFYNF-GWKDYGVP-SLTTILDIVKVMAFALQ---EGGKVAVHCHAGLGRTGVLIAcylvyaLRMSADQA------ 142

                        90       100
                ....*....|....*....|....*..
gi 83753798 267 dILGIvcqlRLDRGGMIQTAEQYQFLH 293
Cdd:cd14506 143 -IRLV----RSKRPNSIQTRGQVLCVR 164
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 231-252 1.17e-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: 42.05  E-value: 1.17e-04
                        10        20
                ....*....|....*....|..
gi 83753798 231 AHPGPIVVHCSAGIGRTGCFIA 252
Cdd:cd14499 107 NEKGAIAVHCKAGLGRTGTLIA 128
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 204-252 1.15e-03

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: 38.72  E-value: 1.15e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 83753798 204 WPDHQTPeSAGPLLRLVAEVE----ESPETAAhpgpiVVHCSAGIGRTGCFIA 252
Cdd:cd14497  68 FPDHHPP-PLGLLLEIVDDIDswlsEDPNNVA-----VVHCKAGKGRTGTVIC 114
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 198-252 6.31e-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: 36.58  E-value: 6.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 83753798 198 HILFSAW-PDHQTPESAgplLRLVAeveespeTAAHPGPIVVHCSAGIGRTGCFIA 252
Cdd:cd14529  63 NLPLSATrPTESDVQSF---LLIMD-------LKLAPGPVLIHCKHGKDRTGLVSA 108
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 146-247 6.64e-03

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 36.52  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83753798   146 LREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAwPDHQTPEsAGPLLRLVAEVEE 225
Cdd:pfam14566  51 LAEAKKNGGRVLVHDETEDGIGVLTVVDVWESDVQTPEEVYERLKAEGPGVDYRRIPI-TDEKAPL-EEDFDALISIVKD 128

                          90       100
                  ....*....|....*....|..
gi 83753798   226 SPETAAhpgpIVVHCSAGIGRT 247
Cdd:pfam14566 129 APEDTA----LVFNCQMGRGRT 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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