NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958801476|ref|XP_038939141|]
View 

tyrosine-protein phosphatase non-receptor type 18 isoform X10 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 17-170 5.20e-97

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


The actual alignment was detected with superfamily member cd14603:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 266  Bit Score: 287.88  E-value: 5.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ 96
Cdd:cd14603   113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  97 GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 170
Cdd:cd14603   193 GSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 17-170 5.20e-97

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: 287.88  E-value: 5.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ 96
Cdd:cd14603   113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  97 GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 170
Cdd:cd14603   193 GSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
17-168 1.08e-57

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 186.29  E-value: 1.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQERE-PLQAGPFCITLTKETALTADITLRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:pfam00102  82 EKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  94 CLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:pfam00102 162 KSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
17-168 2.19e-55

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 180.93  E-value: 2.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476   17 RKCERYWAQE-REPLQAGPFCITLTKETAlTADITLRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:smart00194 109 EKCAQYWPDEeGEPLTYGDITVTLKSVEK-VDDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVR 187

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476   94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:smart00194 188 KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
12-162 1.18e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 98.24  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  12 GMPDTRKCERYWAQEReplQAGPFCI--TLTKETALTADITLRTLQVTFQ---KESRPVHQLQYMSWPDHGVPSSS---D 83
Cdd:COG5599   114 ISKPKVKMPVYFRQDG---EYGKYEVssELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEalkN 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  84 HILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFEVVLEMRKQR-PAAVQTEEQYRFL 162
Cdd:COG5599   191 LADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 15-178 2.07e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 87.39  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  15 DTRKCERYWAQERE-PLQAGPFCIT---LTKETALTADITLRTLQVTfqKESRPVHQLQYMSWPDHGVPSSSDHILTMV- 89
Cdd:PHA02746  150 DDEKCFELWTKEEDsELAFGRFVAKildIIEELSFTKTRLMITDKIS--DTSREIHHFWFPDWPDNGIPTGMAEFLELIn 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  90 ----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQY 159
Cdd:PHA02746  228 kvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEIVLKIRKQRHSSVFLPEQY 303

                         170
                  ....*....|....*....
gi 1958801476 160 RFLYHTVAQLFSRTLQNNS 178
Cdd:PHA02746  304 AFCYKALKYAIIEEAKKKF 322
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 17-170 5.20e-97

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: 287.88  E-value: 5.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ 96
Cdd:cd14603   113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  97 GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 170
Cdd:cd14603   193 GSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 18-164 2.13e-84

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: 253.50  E-value: 2.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREP-LQAGPFCITLTKETALTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ 96
Cdd:cd14542    55 KCERYWPEEGEEqLQFGPFKISLEKEKRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQ 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801476  97 GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYH 164
Cdd:cd14542   135 GSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 17-170 6.21e-66

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: 207.39  E-value: 6.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQE-REPLQAGPFCITLTKETALTaDITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14602    81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKS-DYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 170
Cdd:cd14602   160 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
17-168 1.08e-57

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 186.29  E-value: 1.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQERE-PLQAGPFCITLTKETALTADITLRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:pfam00102  82 EKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  94 CLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:pfam00102 162 KSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 15-164 4.74e-56

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: 180.94  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  15 DTRKCERYWAQERE-PLQAGPFCITLTKETALtADITLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 91
Cdd:cd00047    52 GREKCERYWPEEGGkPLEYGDITVTLVSEEEL-SDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRR 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  92 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPpnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 164
Cdd:cd00047   131 VRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 17-174 1.72e-55

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: 182.82  E-value: 1.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQE-REPLQAGPFCITLTKETALTaDITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14604   140 KKCERYWPLYgEEPMTFGPFRISCEAEQART-DYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY 218

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLFSRTL 174
Cdd:cd14604   219 QEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
17-168 2.19e-55

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 180.93  E-value: 2.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476   17 RKCERYWAQE-REPLQAGPFCITLTKETAlTADITLRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:smart00194 109 EKCAQYWPDEeGEPLTYGDITVTLKSVEK-VDDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVR 187

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476   94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:smart00194 188 KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 17-164 3.14e-45

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: 153.17  E-value: 3.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQAGPFCITLTKETALT-ADITLRTLQVTF-QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:cd18533    55 EKCDQYWPSGEYEGEYGDLTVELVSEEENDdGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801476  95 LQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLL---LTQTIPPNFSL---FEVVLEMRKQRPAAVQTEEQYRFLYH 164
Cdd:cd18533   135 LNDSASldPPIIVHCSAGVGRTGTFIALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
64-168 1.77e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.49  E-value: 1.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476   64 PVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFEV 141
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1958801476  142 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 64-168 1.77e-40

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: 137.49  E-value: 1.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476   64 PVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFEV 141
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1958801476  142 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 18-163 6.17e-36

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: 129.40  E-value: 6.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALTaDITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQG 97
Cdd:cd14548    80 KCDHYWPFDQDPVYYGDITVTMLSESVLP-DWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801476  98 LGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14548   159 QEKGPTIVHCSAGVGRTGTFIALDRlLQQIESEDYVDI----FGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 18-168 3.06e-35

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: 128.35  E-value: 3.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTFQKES---RPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:cd14544    93 KCVRYWPDEGMQKQYGPYRVQNVSEHD-TTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQ 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  95 LQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14544   172 RQEslPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQ 247
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 18-168 9.71e-35

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: 125.95  E-value: 9.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWA-QEREPL-QAGPFCITLTKETALtADITLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:cd14538    57 KCHRYWPdSLNKPLiCGGRLEVSLEKYQSL-QDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  94 CLQglGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPpnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14538   136 RIH--NSGPIVVHCSAGIGRTGVLITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 18-161 1.78e-31

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: 117.43  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALTA----DITLRTLQvtfQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:cd14541    60 KCHQYWPDLGETMQFGNLQITCVSEEVTPSfafrEFILTNTN---TGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801476  94 -CLQGLGPgPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRF 161
Cdd:cd14541   137 qNRVGMVE-PTVVHCSAGIGRTGVLITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 18-168 5.83e-31

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: 117.67  E-value: 5.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTFQKES---RPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:cd14606   108 KCVPYWPEVGMQRAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGeliREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQ 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  95 LQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14606   187 RQESLPhaGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 17-163 7.80e-31

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: 115.53  E-value: 7.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPlQAGPFCITLTKETALtADITLRTLQVTFQKESRP--------VHQLQYMSWPDHGVPSSSDHILTM 88
Cdd:cd14549    54 RKCDQYWPKEGTE-TYGNIQVTLLSTEVL-ATYTVRTFSLKNLKLKKVkgrsservVYQYHYTQWPDHGVPDYTLPVLSF 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  89 VEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14549   132 VRKSSAANPPGAGPIVVHCSAGVGRTGTYIVIDsMLQQIQDKGTV----NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 17-163 3.00e-30

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: 115.92  E-value: 3.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQV--TFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE--- 91
Cdd:cd14543   112 VKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEvrq 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  92 --ARCLQGLGPG--------PLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYR 160
Cdd:cd14543   192 qqALAVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLDIcLSQLEDVGTL----NVMQTVRRMRTQRAFSIQTPDQYY 267


                  ...
gi 1958801476 161 FLY 163
Cdd:cd14543   268 FCY 270
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 18-166 2.53e-29

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: 111.38  E-value: 2.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWA-QEREPLQAGPFCITLTKETALtADITLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:cd14596    57 KCHRYWPeTLQEPMELENYQLRLENYQAL-QYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801476  95 LQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14596   136 VHNT--GPIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 18-164 2.65e-29

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: 112.10  E-value: 2.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQErEPLQAGPFCITLTKeTALTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTM---VEEARc 94
Cdd:cd14547    81 KCAQYWPEE-ENETYGDFEVTVQS-VKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvqeVEEAR- 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801476  95 LQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 164
Cdd:cd14547   158 QTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 18-166 2.04e-28

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: 108.90  E-value: 2.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREpLQAGPFCITLTKETaLTADITLRTLQVTFQKE--SRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RC 94
Cdd:cd14552    55 KCAQYWPEDGS-VSSGDITVELKDQT-DYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQ 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801476  95 LQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14552   133 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 18-166 4.76e-28

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: 109.21  E-value: 4.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALTaDITLRTLQVTFQKESRPVHQLQYMSWPDHGVPS--SSDHILTMVEEARCL 95
Cdd:cd14614    96 KCDHYWPFTEEPVAYGDITVEMLSEEEQP-DWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESILQFVQMVRQQ 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14614   175 AVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 16-168 6.63e-28

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: 108.31  E-value: 6.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  16 TRKCERYWAQ---EREPLQAGPFCITLTKETAlTADITLRTLQV--TFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVE 90
Cdd:cd14540    55 REKCFRYWPTlggEHDALTFGEYKVSTKFSVS-SGCYTTTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  91 EA-----RCLQGLG----PGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNfsLFEVVLEMRKQRPAAVQTEEQYRF 161
Cdd:cd14540   134 EInsvrrHTNQDVAghnrNPPTLVHCSAGVGRTGVVILADLM-LYCLDHNEELD--IPRVLALLRHQRMLLVQTLAQYKF 210


                  ....*..
gi 1958801476 162 LYHTVAQ 168
Cdd:cd14540   211 VYNVLIQ 217
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 18-166 6.67e-28

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: 108.44  E-value: 6.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALtADITLR--TLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR-- 93
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVM-ENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRqw 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 18-170 7.33e-28

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: 107.72  E-value: 7.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALTA----DITLRTLQvtfQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:cd14601    60 KCHQYWPEPSGSSSYGGFQVTCHSEEGNPAyvfrEMTLTNLE---KNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801476  94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 170
Cdd:cd14601   137 NKRAGKDEPVVVHCSAGIGRTGVLITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 18-162 1.22e-26

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: 104.90  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQErEPLQAGPFCITLTKETALTaDITLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR-- 93
Cdd:cd14615    80 KCEEYWPSK-QKKDYGDITVTMTSEIVLP-EWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRey 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFL 162
Cdd:cd14615   158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 16-163 1.31e-26

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: 105.17  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  16 TRKCERYWAQErePLQAGPFCITLTKETALTADI----TLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSD---HIL 86
Cdd:cd14545    78 QIKCAQYWPQG--EGNAMIFEDTGLKVTLLSEEDksyyTVRTLELENLKtqETREVLHFHYTTWPDFGVPESPAaflNFL 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801476  87 TMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14545   156 QKVRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 16-163 2.15e-26

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: 103.70  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  16 TRKCERYW-AQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKESRP---VHQLQYMSWPDHGVPSSSDHILTMVee 91
Cdd:cd17658    56 TAKCADYFpAEENESREFGRISVTNKKLKHSQHSITLRVLEVQYIESEEPplsVLHIQYPEWPDHGVPKDTRSVRELL-- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  92 aRCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd17658   134 -KRLYGIPPsaGPIVVHCSAGIGRTGAYCTIHNTIRRILEGDMSA-VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 18-163 3.24e-26

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: 104.02  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQeREPLQAGPFCITLTKETALtADITLRTLQV--TFQKESRPVHQLQYMSWPDHGVPsssDHILTMVEEARCL 95
Cdd:cd14553    87 KCDQYWPT-RGTETYGLIQVTLLDTVEL-ATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP---EHPTPFLAFLRRV 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801476  96 QGLGP---GPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14553   162 KACNPpdaGPIVVHCSAGVGRTGCFIVIDsMLERIKHEKTV----DIYGHVTCLRAQRNYMVQTEDQYIFIH 229
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 18-166 5.11e-26

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: 103.94  E-value: 5.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRTL---QVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:cd14605    95 KCVKYWPDEYALKEYGVMRVRNVKESA-AHDYILRELklsKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHH 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  95 LQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14605   174 KQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 18-168 1.65e-25

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: 103.18  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREplQAGPFCITLTKETALTADI----TLRTLQVT--FQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 91
Cdd:cd14608   105 KCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNFLFK 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801476  92 ARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14608   183 VRESGSLSPehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 18-162 2.88e-25

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: 102.62  E-value: 2.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALTADITlRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14600   123 KCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVF-REMLLTNTQtgEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSK 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801476  96 QgLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRFL 162
Cdd:cd14600   202 R-VENEPVLVHCSAGIGRTGVLVTMETA--MCLTERNQPVYPL-DIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 18-168 3.21e-25

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: 101.84  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLqaGPFCITLtKETALTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSD---HILTMVEEARC 94
Cdd:cd14612   100 KCVHYWPEKEGTY--GRFEIRV-QDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGpllRLVAEVEESRQ 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  95 LQGlGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14612   177 TAA-SPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTGKV----DILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 12-163 5.10e-25

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: 100.79  E-value: 5.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  12 GMPDTRK-CERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQV---TFQKESRpVHQLQYMSWPDHGVPSSSDHILT 87
Cdd:cd14618    74 GMENGRVlCDHYWPSESTPVSYGHITVHLLAQSS-EDEWTRREFKLwheDLRKERR-VKHLHYTAWPDHGIPESTSSLMA 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801476  88 MVEEAR--CLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14618   152 FRELVRehVQATKGKGPTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIFLH 226
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 14-163 5.51e-25

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: 99.79  E-value: 5.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  14 PDTRKCERYWAQErEPLQAGPFCITLTKETaLTADITLRTLQVT----FQKESRPVHQLQYMSWPDHG-VPSSSDHILTM 88
Cdd:cd14556    50 PKDQSCPQYWPDE-GSGTYGPIQVEFVSTT-IDEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  89 VEEA-RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14556   128 LSEVeKWQEQSGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 18-168 6.35e-25

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: 100.49  E-value: 6.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLqaGPFCITLTkETALTADITLRTLqvTFQK----ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:cd14630    87 KCVRYWPDDTEVY--GDIKVTLI-ETEPLAEYVIRTF--TVQKkgyhEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVK 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14630   162 FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 18-165 6.50e-25

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: 100.68  E-value: 6.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREpLQAGPFCITLTKETALTADItLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHIL---TMVEEA 92
Cdd:cd14554    90 KCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIdfiGQVHKT 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  93 RCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 165
Cdd:cd14554   168 KEQFG-QEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 18-163 1.60e-24

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: 98.75  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYW-AQEREPLQAGPFCITLTKETaLTADITLRTLQVTFQKE---SRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR 93
Cdd:cd14557    55 KCAQYWpSMEEGSRAFGDVVVKINEEK-ICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  94 CLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14557   134 AFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEG---RVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 18-166 3.52e-24

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: 98.36  E-value: 3.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQE-------REPLQagpfcITLTKETALTA----DITLRTLQVtfqKESRPVHQLQYMSWPDHGVPSSSDHIL 86
Cdd:cd14597    84 KCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQLKNfvirVLELEDIQT---REVRHITHLNFTAWPDHDTPSQPEQLL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  87 TMVEEARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14597   156 TFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 18-166 7.44e-24

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: 96.91  E-value: 7.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLqaGPFCITLTkETALTADITLRTLQVTFQ--KESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14555    55 KCSRYWPDDTEVY--GDIKVTLV-ETEPLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKAS 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14555   132 NPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
12-162 1.18e-23

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 98.24  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  12 GMPDTRKCERYWAQEReplQAGPFCI--TLTKETALTADITLRTLQVTFQ---KESRPVHQLQYMSWPDHGVPSSS---D 83
Cdd:COG5599   114 ISKPKVKMPVYFRQDG---EYGKYEVssELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEalkN 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  84 HILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFEVVLEMRKQR-PAAVQTEEQYRFL 162
Cdd:COG5599   191 LADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 18-163 1.47e-23

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: 96.91  E-value: 1.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETALtADITLRTLQVTFQKE---SRPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801476  95 L--QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14617   160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 17-163 3.95e-23

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: 94.76  E-value: 3.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQER-EPLQAGPFCITLTKETALTADITlRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA- 92
Cdd:cd14539    55 QKVHRYWPTERgQALVYGAITVSLQSVRTTPTHVE-RIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVh 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801476  93 ------RCLQglgpGPLCVHCSAGCGRTGVLCAV-DYVRQLLLTQTIPpnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14539   134 shylqqRSLQ----TPIVVHCSSGVGRTGAFCLLyAAVQEIEAGNGIP---DLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 18-168 5.74e-23

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: 95.11  E-value: 5.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREpLQAGPFCITLTKETAlTADITLRTLQVTFQKE--SRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RC 94
Cdd:cd14623    80 KCAQYWPSDGS-VSYGDITIELKKEEE-CESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQ 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  95 LQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14623   158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 17-166 8.38e-23

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: 94.27  E-value: 8.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPlQAGPFCITLtKETALTADITLRTLQVTFQK----------ESRPVHQLQYMSWPDHGVPSSSDHIL 86
Cdd:cd17668    54 RKCDQYWPADGSE-EYGNFLVTQ-KSVQVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  87 TMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 165
Cdd:cd17668   132 TFVRKASYAKRHAVGPVVVHCSAGVGRTGTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDA 207


                  .
gi 1958801476 166 V 166
Cdd:cd17668   208 L 208
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 15-166 9.61e-23

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: 95.03  E-value: 9.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  15 DTRKCERYW-AQEREPL--QAGPFCITLTKETaLTADITLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTM- 88
Cdd:cd14607   101 DSVKCAQYWpTDEEEVLsfKETGFSVKLLSED-VKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPASFLNFl 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  89 --VEEARCLqGLGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14607   180 fkVRESGSL-SPEHGPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 19-163 9.83e-23

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: 94.00  E-value: 9.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  19 CERYWAQEREPLqaGPFCITLtKETALTADITLRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ 96
Cdd:cd14558    56 CAQYWGDEKKTY--GDIEVEL-KDTEKSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  97 GLGPG------PLCVHCSAGCGRTGVLCAVdyvRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14558   133 PYKNSkhgrsvPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 18-168 1.63e-22

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: 95.10  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQeREPLQAGPFCITLTKETALtADITLRTLQV--TFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14626   125 KCDQYWPI-RGTETYGMIQVTLLDTVEL-ATYSVRTFALykNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14626   203 NPPDAGPMVVHCSAGVGRTGCFIVIDaMLERMKHEKTV----DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 15-168 1.94e-22

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: 93.28  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  15 DTRKCERYWAQEREPLQaGPFCITLTKETALTADITLRT--LQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA 92
Cdd:cd14546    53 GVKQCARYWPEEGSEVY-HIYEVHLVSEHIWCDDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKV 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801476  93 -RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14546   132 nKSYRGRS-CPIVVHCSDGAGRTGTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 18-163 8.05e-22

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: 91.89  E-value: 8.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQA-GPFCIT-LTKETALtaDITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14616    81 RCHQYWPEDNKPVTVfGDIVITkLMEDVQI--DWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYvrqllLTQTIPPN--FSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14616   159 RAHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDHdfVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 18-166 1.03e-21

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: 91.22  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREpLQAGPFCITLTKETALTAdITLRTLQVTF--QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RC 94
Cdd:cd14622    56 KCVQYWPSEGS-VTHGEITIEIKNDTLLET-ISIRDFLVTYnqEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQ 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801476  95 LQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14622   134 QQQTGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 18-163 3.55e-21

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: 91.72  E-value: 3.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RC 94
Cdd:cd14628   136 KCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVhKT 213

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  95 LQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14628   214 KEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 17-168 3.98e-21

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: 91.25  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPlQAGPFCITLtKETALTADITLRTLQVTFQK-------------ESRPVHQLQYMSWPDHGVPSSSD 83
Cdd:cd17667   112 RKCDQYWPTENSE-EYGNIIVTL-KSTKIHACYTVRRFSIRNTKvkkgqkgnpkgrqNERTVIQYHYTQWPDMGVPEYAL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  84 HILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd17667   190 PVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266


                  ....*
gi 1958801476 164 HTVAQ 168
Cdd:cd17667   267 DALLE 271
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 17-163 5.58e-21

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: 89.20  E-value: 5.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREpLQAGPFCITLtKETALTADITLRTL------QVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVE 90
Cdd:cd14551    54 KKCSQYWPDQGC-WTYGNLRVRV-EDTVVLVDYTTRKFciqkvnRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLK 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  91 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14551   132 KVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 18-166 8.45e-21

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: 89.23  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWaqerePLQA----GPFCITLTKETALTaDITLRTLQVTFQ-----KESRPVHQLQYMSWPDHGVPSSSDHILTM 88
Cdd:cd14620    79 KCYQYW-----PDQGcwtyGNIRVAVEDCVVLV-DYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKF 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801476  89 VEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 18-168 9.13e-21

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: 90.56  E-value: 9.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RC 94
Cdd:cd14627   137 KCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVhKT 214

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  95 LQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14627   215 KEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 18-168 1.70e-20

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: 89.33  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQagPFCITLTkETALTADITLRTLQVTFQ--KESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14633   124 KCCKYWPDDTEIYK--DIKVTLI-ETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSK 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14633   201 SPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 18-168 2.92e-20

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: 87.38  E-value: 2.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLqaGPFCITLTkETALTADITLRTLQVTFQ--KESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14631    69 KCYKYWPDDTEVY--GDFKVTCV-EMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLS 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14631   146 NPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 18-168 3.13e-20

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: 87.03  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREplQAGPFCITLTKETALtADITLRTLQVTFQKES--RPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14632    55 KCSKYWPDDSD--TYGDIKITLLKTETL-AEYSVRTFALERRGYSarHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14632   132 TPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 18-163 1.37e-19

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: 87.09  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQK--ESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RC 94
Cdd:cd14629   137 KCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVhKT 214

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  95 LQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14629   215 KEQFGQdGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 15-178 2.07e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 87.39  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  15 DTRKCERYWAQERE-PLQAGPFCIT---LTKETALTADITLRTLQVTfqKESRPVHQLQYMSWPDHGVPSSSDHILTMV- 89
Cdd:PHA02746  150 DDEKCFELWTKEEDsELAFGRFVAKildIIEELSFTKTRLMITDKIS--DTSREIHHFWFPDWPDNGIPTGMAEFLELIn 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  90 ----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQY 159
Cdd:PHA02746  228 kvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEIVLKIRKQRHSSVFLPEQY 303

                         170
                  ....*....|....*....
gi 1958801476 160 RFLYHTVAQLFSRTLQNNS 178
Cdd:PHA02746  304 AFCYKALKYAIIEEAKKKF 322
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 18-164 3.44e-19

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: 84.58  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQEREPLQAGPFCITLTKETAltaDITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTM---VEEARc 94
Cdd:cd14611    84 KCVLYWPEKRGIYGKVEVLVNSVKECD---NYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLmldVEEDR- 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801476  95 LQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 164
Cdd:cd14611   160 LASPGRGPVVVHCSAGIGRTGCFIATTIgCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 18-168 8.63e-18

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: 82.06  E-value: 8.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQeREPLQAGPFCITLTkETALTADITLRT--LQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14625   131 KCDQYWPS-RGTETYGMIQVTLL-DTIELATFCVRTfsLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTC 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14625   209 NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 18-168 9.08e-18

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: 82.09  E-value: 9.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQeREPLQAGPFCITLTkETALTADITLRTLQV--TFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 95
Cdd:cd14624   131 KCDQYWPS-RGTETYGLIQVTLL-DTVELATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  96 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14624   209 NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 18-167 9.57e-18

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: 81.45  E-value: 9.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQERepLQAGPFCITLTKETAlTADITLRTLQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMV---EEARC 94
Cdd:cd14613   110 KCTEYWPEEQ--VTYEGIEITVKQVIH-ADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVqevEEARQ 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  95 LQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 167
Cdd:cd14613   187 QAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 17-168 8.16e-17

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: 79.31  E-value: 8.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQaGPFCITLTKETALTADITLRT--LQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-R 93
Cdd:cd14609   126 KQCDRYWPDEGSSLY-HIYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVnK 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  94 CLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14609   205 CYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-179 9.56e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 79.28  E-value: 9.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476   1 MLHPTiswqqPGMPDTRKCERYWA-QEREPLQAGPFCITlTKETALTADITLRTLQVTFQ--KESRPVHQLQYMSWPDHG 77
Cdd:PHA02747  123 MLTPT-----KGTNGEEKCYQYWClNEDGNIDMEDFRIE-TLKTSVRAKYILTLIEITDKilKDSRKISHFQCSEWFEDE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  78 VPSssDHI-----LTMVEEARCLQG--LGP-----GPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLE 144
Cdd:PHA02747  197 TPS--DHPdfikfIKIIDINRKKSGklFNPkdallCPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEK 270

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958801476 145 MRKQRPAAVQTEEQYRFL---YHTVAQLFSRTLQNNSP 179
Cdd:PHA02747  271 IREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKAIDKI 308
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 17-168 1.41e-16

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: 78.56  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQEREPLQAgPFCITLTKETALTADITLRT--LQVTFQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-R 93
Cdd:cd14610   128 KQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSfyLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVnK 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  94 CLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14610   207 CYRGRS-CPIIVHCSDGAGRSGTYILIDMVLNKMAKGA--KEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 18-168 1.35e-15

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: 75.83  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWaqerePLQAgpfCITL------TKETALTADITLRTL------QVTFQKESRPVHQLQYMSWPDHGVPSSSDHI 85
Cdd:cd14621   136 KCAQYW-----PDQG---CWTYgnirvsVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTPIGM 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  86 LTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 165
Cdd:cd14621   208 LKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQA 284


                  ...
gi 1958801476 166 VAQ 168
Cdd:cd14621   285 LLE 287
PHA02738 PHA02738
hypothetical protein; Provisional
 17-166 2.51e-15

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 75.35  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKCERYWAQ-EREPLQAGPFCITLTKETALTADITlRTLQVTFQKES-RPVHQLQYMSWPDHGVPSSSDHILTMVEEARC 94
Cdd:PHA02738  130 EKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVK-STLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQ 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  95 LQ-------------GLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYR 160
Cdd:PHA02738  209 CQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYF 284


                  ....*.
gi 1958801476 161 FLYHTV 166
Cdd:PHA02738  285 FCYRAV 290
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 16-163 6.32e-15

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 72.37  E-value: 6.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  16 TRKCERYWAQEREpLQAGPF---CITLTKETALTADItLRTLQVTFQKESR-PVHQLQYMSWPDH-GVPSSSDHILTMVE 90
Cdd:cd14636    51 AQGCPQYWPEEGM-LRYGPIqveCMSCSMDCDVISRI-FRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLIL 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801476  91 EARCLQ---GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14636   129 QVEKWQeecDEGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 83-164 7.16e-15

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: 69.69  E-value: 7.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  83 DHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLlltqtippNFSLFEVVLEMRKQRPA-AVQTEEQYRF 161
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                  ...
gi 1958801476 162 LYH 164
Cdd:cd14494   111 LIK 113
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 18-170 3.72e-14

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: 70.39  E-value: 3.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYW---AQEREPLQAGPFCIT--LTKETALTADITLRTLQVTFQKEsRPVHQLQYMSWPDHGVPSSSDHILTMVEEA 92
Cdd:cd14598    57 KSFRYWprlGSRHNTVTYGRFKITtrFRTDSGCYATTGLKIKHLLTGQE-RTVWHLQYTDWPEHGCPEDLKGFLSYLEEI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  93 RCL----------QGLGPgPLCVHCSAGCGRTGVLcavdyVRQLLLTQTIPPNFSL-FEVVLEM-RKQRPAAVQTEEQYR 160
Cdd:cd14598   136 QSVrrhtnstidpKSPNP-PVLVHCSAGVGRTGVV-----ILSEIMIACLEHNEMLdIPRVLDMlRQQRMMMVQTLSQYT 209

                         170
                  ....*....|
gi 1958801476 161 FLYHTVAQLF 170
Cdd:cd14598   210 FVYKVLIQFL 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 18-170 1.99e-13

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: 69.64  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  18 KCERYWAQ---EREPLQAGPFCITlTK---ETALTADITLRTLQVTFQKEsRPVHQLQYMSWPDHGVPSSSDHILTMVEE 91
Cdd:cd14599   123 KSHRYWPKlgsKHSSATYGKFKVT-TKfrtDSGCYATTGLKVKHLLSGQE-RTVWHLQYTDWPDHGCPEEVQGFLSYLEE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  92 ARCL-----------QGLGPgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYR 160
Cdd:cd14599   201 IQSVrrhtnsmldstKNCNP-PIVVHCSAGVGRTGVVILTELMIGCLEHNE---KVEVPVMLRHLREQRMFMIQTIAQYK 276

                         170
                  ....*....|
gi 1958801476 161 FLYHTVAQLF 170
Cdd:cd14599   277 FVYQVLIQFL 286
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 13-163 2.62e-13

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: 67.74  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  13 MPDTRKCERYWAqEREPLQAGPFCITLtketaLTADITLRTLQVTF--------QKESRPVHQLQYMSWPDH-GVPSSSD 83
Cdd:cd14634    48 MDAAQLCMQYWP-EKTSCCYGPIQVEF-----VSADIDEDIISRIFricnmarpQDGYRIVQHLQYIGWPAYrDTPPSKR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  84 HILTMVEEARCLQGL---GPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYR 160
Cdd:cd14634   122 SILKVVRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYK 198


                  ...
gi 1958801476 161 FLY 163
Cdd:cd14634   199 FVY 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 13-168 1.16e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 67.33  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  13 MPDTR-KCERYW-AQEREPLQAGPFCITlTKETALTADITLRTLQVTFQKE--SRPVHQLQYMSWPDHGVPSSSDHILTM 88
Cdd:PHA02742  128 MEDGKeACYPYWmPHERGKATHGEFKIK-TKKIKSFRNYAVTNLCLTDTNTgaSLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  89 VEEARCLQG-----------LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnfsLFEVVLEMRKQRPAAVQTEE 157
Cdd:PHA02742  207 VLAVREADLkadvdikgeniVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCLSLPQ 283

                         170
                  ....*....|.
gi 1958801476 158 QYRFLYHTVAQ 168
Cdd:PHA02742  284 QYIFCYFIVLI 294
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 19-166 3.32e-10

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: 58.77  E-value: 3.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  19 CERYWAqerEP--LQAGPFCITLTKETAlTADITLRTLQVT----FQKESRPVHQLQYMSW-PDHGVPSSSD---HILTM 88
Cdd:cd14637    57 CLQYWP---EPglQQYGPMEVEFVSGSA-DEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLLAS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  89 VE--EARClqglGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd14637   133 VEkwQRES----GEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 19-168 5.80e-10

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: 58.16  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  19 CERYWAqEREPLQAGPFCITLTkETALTADITLRTLQVTF----QKESRPVHQLQYMSWPDH-GVPSSSDHILTMVEEAR 93
Cdd:cd14635    54 CPQYWP-ENGVHRHGPIQVEFV-SADLEEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801476  94 CLQ---GLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 168
Cdd:cd14635   132 KWQeeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 72-162 8.36e-10

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: 57.74  E-value: 8.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  72 SWPDHGVPSSsDHILTMVE-EARCLQGlgPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPNfslfEVVLEMRKQRP 150
Cdd:cd14506    83 GWKDYGVPSL-TTILDIVKvMAFALQE--GGKVAVHCHAGLGRTGVLIAC----YLVYALRMSAD----QAIRLVRSKRP 151

                          90
                  ....*....|..
gi 1958801476 151 AAVQTEEQYRFL 162
Cdd:cd14506   152 NSIQTRGQVLCV 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
73-164 4.37e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.21  E-value: 4.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  73 WPDHGVPSSsDHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAvdyvrQLLLTQTIPPNfslfEVVLEMRKQRPAA 152
Cdd:COG2453    55 IPDFGAPDD-EQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA-----AYLVLLGLSAE----EALARVRAARPGA 123

                          90
                  ....*....|..
gi 1958801476 153 VQTEEQYRFLYH 164
Cdd:COG2453   124 VETPAQRAFLER 135
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 22-163 3.34e-08

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: 53.14  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  22 YWAQEREPLQAGPFCITL---------TKETALTADITLRTLQVTFQKESRpvhQLQYMSWPDHGVPSSSDHILTMV--E 90
Cdd:cd17670    58 YWPSREESMNCEAFTVTLiskdrlclsNEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTFELINVikE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801476  91 EARCLQGlgpgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd17670   135 EALTRDG----PTIVHDEFGAVSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 73-162 7.85e-08

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 52.40  E-value: 7.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  73 WPDHGVPSS------SDHI-------LTMVEEARCLQGLGPGPL--CVHCSAGCGRTGVLCAVDYVRQllltqtiPPN-F 136
Cdd:cd14559   126 WPDHTAISSeglkelADLVnksaeekRNFYKSKGSSAINDKNKLlpVIHCRAGVGRTGQLAAAMELNK-------SPNnL 198

                          90       100
                  ....*....|....*....|....*..
gi 1958801476 137 SLFEVVLEMRKQRPA-AVQTEEQYRFL 162
Cdd:cd14559   199 SVEDIVSDMRTSRNGkMVQKDEQLDTL 225
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 67-163 1.42e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 50.34  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  67 QLQYMSW-----PDHGVPSSSDHILTMVEEAR-CLQGlGPGPLcVHCSAGCGRTGVLCAvdyVRQLLLTQTIPPNfslfE 140
Cdd:cd14505    69 QQAGITWhhlpiPDGGVPSDIAQWQELLEELLsALEN-GKKVL-IHCKGGLGRTGLIAA---CLLLELGDTLDPE----Q 139

                          90       100
                  ....*....|....*....|...
gi 1958801476 141 VVLEMRKQRPAAVQTEEQYRFLY 163
Cdd:cd14505   140 AIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 56-162 1.81e-07

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 49.58  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  56 VTFQKESRPVHQLQY-------MSWPDHGVPSSS--DHILTMVEEARCLqglgPGPLCVHCSAGCGRTGVLCAVdYvrqL 126
Cdd:cd14504    33 VTLTEEPPPEHSDTCpglryhhIPIEDYTPPTLEqiDEFLDIVEEANAK----NEAVLVHCLAGKGRTGTMLAC-Y---L 104

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958801476 127 LLTQTIPPNfslfEVVLEMRKQRPAAVQTEEQYRFL 162
Cdd:cd14504   105 VKTGKISAV----DAINEIRRIRPGSIETSEQEKFV 136
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 22-166 8.39e-06

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: 46.14  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  22 YWAQEREPLQAGPFCITL---------TKETALTADITLRTLQVTFQKEsrpVHQLQYMSWPDHGVP-SSSDHILTMVEE 91
Cdd:cd17669    58 YWPNKDEPINCETFKVTLiaeehkclsNEEKLIIQDFILEATQDDYVLE---VRHFQCPKWPNPDSPiSKTFELISIIKE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  92 ARCLQGlgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 166
Cdd:cd17669   135 EAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 13-163 1.33e-03

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: 39.23  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  13 MPDTRKCER---YWAQEREPLQAGPFCITLTKET---------ALTADITLRTLQVTFQKESRpvhQLQYMSWPDHGVP- 79
Cdd:cd14550    45 LTDNELNEDepiYWPTKEKPLECETFKVTLSGEDhsclsneirLIVRDFILESTQDDYVLEVR---QFQCPSWPNPCSPi 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  80 SSSDHILTMVEEaRCLQglGPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPN-FSLFEVVLEMRKQRPAAVQTEEQ 158
Cdd:cd14550   122 HTVFELINTVQE-WAQQ--RDGPIVVHDRYGGVQAATFCAL----TTLHQQLEHESsVDVYQVAKLYHLMRPGVFTSKED 194


                  ....*
gi 1958801476 159 YRFLY 163
Cdd:cd14550   195 YQFLY 199
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 74-117 1.60e-03

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: 38.59  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801476  74 PDHGVPSssDHI----LTMVEEArclqglgPGPLCVHCSAGCGRTGVL 117
Cdd:cd14499    88 PDGSTPS--DDIvkkfLDICENE-------KGAIAVHCKAGLGRTGTL 126
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 17-174 2.58e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 39.18  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  17 RKC-ERYWA-QEREPLQAGPFCITlTKETALTADITLRTLQVTFQK-ESRPVHQLQYMSWPDHGVPSSSD-------HIL 86
Cdd:PHA02740  128 KKCfNQFWSlKEGCVITSDKFQIE-TLEIIIKPHFNLTLLSLTDKFgQAQKISHFQYTAWPADGFSHDPDafidffcNID 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801476  87 TMVEEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDyvrqLLLTQTIPPN-FSLFEVVLEMRKQRPAAVQTEEQYRFLYH 164
Cdd:PHA02740  207 DLCADLEKHKADGKiAPIIIDCIDGISSSAVFCVFD----ICATEFDKTGmLSIANALKKVRQKKYGCMNCLDDYVFCYH 282

                         170
                  ....*....|
gi 1958801476 165 TVAQLFSRTL 174
Cdd:PHA02740  283 LIAAYLKEKF 292
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 66-119 4.34e-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: 37.17  E-value: 4.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801476  66 HQLQYMSWPDHGVPSSsDHILTMVEEARCLQGLGPGPLCV-HCSAGCGRTGVLCA 119
Cdd:cd14497    61 GRVLHYGFPDHHPPPL-GLLLEIVDDIDSWLSEDPNNVAVvHCKAGKGRTGTVIC 114
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 99-129 8.31e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 37.22  E-value: 8.31e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958801476  99 GPGPLCVHCSAGCGRTGVLCAvdyvrqLLLT 129
Cdd:pfam13350 128 NDGPVLFHCTAGKDRTGVAAA------LLLS 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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