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Conserved domains on  [gi|1370473690|ref|XP_024306996|]
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tyrosine-protein phosphatase non-receptor type 2 isoform X6 [Homo sapiens]

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

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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 ...
 19-227 5.02e-157

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 cd14607:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 257  Bit Score: 440.17  E-value: 5.02e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607     1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  99 LMVWQQKTKAVVMLNRIVEKES----------------------------------------------SGETRTISHFHY 132
Cdd:cd14607    81 LMVWQQKTKAVVMLNRIVEKDSvkcaqywptdeeevlsfketgfsvkllsedvksyytvhllqleninSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 133 TTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GDDINIKQVLLNMRKYR 210
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYR 240

                         250
                  ....*....|....*..
gi 1370473690 211 MGLIQTPDQLRFSYMAI 227
Cdd:cd14607   241 MGLIQTPDQLRFSYMAV 257
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 19-227 5.02e-157

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: 440.17  E-value: 5.02e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607     1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  99 LMVWQQKTKAVVMLNRIVEKES----------------------------------------------SGETRTISHFHY 132
Cdd:cd14607    81 LMVWQQKTKAVVMLNRIVEKDSvkcaqywptdeeevlsfketgfsvkllsedvksyytvhllqleninSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 133 TTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GDDINIKQVLLNMRKYR 210
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYR 240

                         250
                  ....*....|....*..
gi 1370473690 211 MGLIQTPDQLRFSYMAI 227
Cdd:cd14607   241 MGLIQTPDQLRFSYMAV 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
42-229 2.02e-90

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 270.27  E-value: 2.02e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  42 NRNRNRYRDVSPYDHSRVKLQNAE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE 119
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 S---------------------------------------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 154
Cdd:pfam00102  81 RekcaqywpeeegesleygdftvtlkkekedekdytvrtlevsnggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370473690 155 RESgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:pfam00102 161 RKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-229 1.23e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 264.14  E-value: 1.23e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690    5 IEREFEELDtqrrwqplyleiRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQR 81
Cdd:smart00194   2 LEEEFEKLD------------RLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690   82 SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES----------------------------------------- 120
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGRekcaqywpdeegepltygditvtlksvekvddytirtlevt 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  121 ---SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNpdHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDI 197
Cdd:smart00194 150 ntgCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1370473690  198 NIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 41-234 2.56e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 133.20  E-value: 2.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  41 ENRNRNRYRDVSPYDHSRV--KLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVilKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 --------------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 154
Cdd:PHA02742  131 gkeacypywmphergkathgefkiktkkiksfrnyavtnlcltdTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAV 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 155 RE---------SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM 225
Cdd:PHA02742  211 REadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYF 290


                  ....*....
gi 1370473690 226 AIIEGAKCI 234
Cdd:PHA02742  291 IVLIFAKLM 299
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
40-220 1.71e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 117.11  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVklqNAENDYINASLVDIEEAQRsYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN------ 113
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAsddeis 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 114 ----------------------------------------RIVEKESSGETRTISHFHYTTWPDFGVPESPAsFLNFLFK 153
Cdd:COG5599   116 kpkvkmpvyfrqdgeygkyevsseltesiqlrdgieartyVLTIKGTGQKKIEIPVLHVKNWPDHGAISAEA-LKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370473690 154 VRES-GSLNPDHGPAVIHCSAGIGRSGTFSLvdtCLVLMEKGD-----DINIKQVLLNMRKYR-MGLIQTPDQL 220
Cdd:COG5599   195 IDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSKSINalvqiTLSVEEIVIDMRTSRnGGMVQTSEQL 265
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 19-227 5.02e-157

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: 440.17  E-value: 5.02e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607     1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  99 LMVWQQKTKAVVMLNRIVEKES----------------------------------------------SGETRTISHFHY 132
Cdd:cd14607    81 LMVWQQKTKAVVMLNRIVEKDSvkcaqywptdeeevlsfketgfsvkllsedvksyytvhllqleninSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 133 TTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GDDINIKQVLLNMRKYR 210
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYR 240

                         250
                  ....*....|....*..
gi 1370473690 211 MGLIQTPDQLRFSYMAI 227
Cdd:cd14607   241 MGLIQTPDQLRFSYMAV 257
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 18-245 3.86e-142

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: 403.25  E-value: 3.86e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  18 WQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHF 97
Cdd:cd14608     1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  98 WLMVWQQKTKAVVMLNRIVEKES----------------------------------------------SGETRTISHFH 131
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSlkcaqywpqkeekemifedtnlkltlisediksyytvrqlelenltTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 132 YTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD---INIKQVLLNMRK 208
Cdd:cd14608   161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRK 240

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370473690 209 YRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWK 245
Cdd:cd14608   241 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 43-225 7.77e-129

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: 367.87  E-value: 7.77e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  43 RNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES-- 120
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQik 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 121 --------------------------------------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE 156
Cdd:cd14545    81 caqywpqgegnamifedtglkvtllseedksyytvrtlelenlkTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370473690 157 SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGD--DINIKQVLLNMRKYRMGLIQTPDQLRFSYM 225
Cdd:cd14545   161 SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
42-229 2.02e-90

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 270.27  E-value: 2.02e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  42 NRNRNRYRDVSPYDHSRVKLQNAE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE 119
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 S---------------------------------------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 154
Cdd:pfam00102  81 RekcaqywpeeegesleygdftvtlkkekedekdytvrtlevsnggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370473690 155 RESgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:pfam00102 161 RKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-229 1.23e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 264.14  E-value: 1.23e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690    5 IEREFEELDtqrrwqplyleiRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQR 81
Cdd:smart00194   2 LEEEFEKLD------------RLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690   82 SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES----------------------------------------- 120
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGRekcaqywpdeegepltygditvtlksvekvddytirtlevt 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  121 ---SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNpdHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDI 197
Cdd:smart00194 150 ntgCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1370473690  198 NIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 68-225 8.13e-65

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: 203.67  E-value: 8.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE---------------------------- 119
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrekcerywpeeggkpleygditvtlvse 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 ----------------SSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgsLNPDHGPAVIHCSAGIGRSGTFSL 183
Cdd:cd00047    81 eelsdytirtlelspkGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370473690 184 VDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM 225
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 22-225 4.20e-64

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: 204.14  E-value: 4.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  22 YLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHF 97
Cdd:cd14543     9 YEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpkrnGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  98 WLMVWQQKTKAVVMLNRIVEK--------------------------------------------ESSGETRTISHFHYT 133
Cdd:cd14543    89 WRMVWEQKVLVIVMTTRVVERgrvkcgqywpleegsslrygdltvtnlsvenkehykkttleihnTETDESRQVTHFQFT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 134 TWPDFGVPESPASFLNFLFKVRESGSLN-----------PDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQV 202
Cdd:cd14543   169 SWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQT 248

                         250       260
                  ....*....|....*....|...
gi 1370473690 203 LLNMRKYRMGLIQTPDQLRFSYM 225
Cdd:cd14543   249 VRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 42-233 3.70e-61

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: 195.69  E-value: 3.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  42 NRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE 117
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgvpgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 ------------------------------------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR 155
Cdd:cd14553    83 rsrvkcdqywptrgtetygliqvtlldtvelatytvrtfalhKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473690 156 ESGslNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 233
Cdd:cd14553   163 ACN--PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 47-222 7.79e-56

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: 181.40  E-value: 7.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  47 RYRDVSPYDHSRVKL--QNAE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK---- 118
Cdd:cd14548     1 RYTNILPYDHSRVKLipINEEegSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgrvk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 -----------------------ESS--------------GETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgsLN 161
Cdd:cd14548    81 cdhywpfdqdpvyygditvtmlsESVlpdwtirefklergDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY--IK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370473690 162 PDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14548   159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 42-227 3.14e-54

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: 178.43  E-value: 3.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  42 NRNRNRYRDVSPYDHSRVKLQNAEN-----DYINASLVDIEEAQR-------SYILTQGPLPNTCCHFWLMVWQQKTKAV 109
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPnvpgsDYINANYIRNENEGPttdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 110 VMLNRIVE---------------------------KESSGE-----------------TRTISHFHYTTWPDFGVPESPA 145
Cdd:cd14544    81 VMTTKEVErgknkcvrywpdegmqkqygpyrvqnvSEHDTTdytlrelqvskldqgdpIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 146 SFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGDD--INIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLdQIKRKGLDcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  ....*
gi 1370473690 223 SYMAI 227
Cdd:cd14544   241 IYVAV 245
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 37-228 1.86e-52

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 174.27  E-value: 1.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  37 AKFPENRNRNRYRDVSPYDHSRVKLQNAEnDYINASLVDIEEAQRS----YILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVLQGNE-DYINASYVNMEIPSANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 113 NRIVEK-------------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLN 149
Cdd:cd14600   114 TTLTERgrtkchqywpdppdvmeyggfrvqchsedctiayvfremlltnTQTGEERTVTHLQYVAWPDHGVPDDSSDFLE 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 150 FLFKVResgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd14600   194 FVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 68-229 1.54e-50

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: 167.17  E-value: 1.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLV--DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE-------------------------- 119
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGkvkchrywpdslnkplicggrlevsl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 -------------------SSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGslnpDHGPAVIHCSAGIGRSGT 180
Cdd:cd14538    81 ekyqslqdfvirrislrdkETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH----NSGPIVVHCSAGIGRTGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1370473690 181 FSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 46-222 1.41e-49

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: 165.37  E-value: 1.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE----- 117
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVqshSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEqgrtk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 -------------------------------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSL 160
Cdd:cd14615    81 ceeywpskqkkdygditvtmtseivlpewtirdftvkNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473690 161 NPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14615   161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 40-229 1.13e-48

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: 164.23  E-value: 1.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 115
Cdd:cd14603    28 KENVKKNRYKDILPYDQTRVILsllqEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 116 VE---------------------------KES---------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFK 153
Cdd:cd14603   108 IEmgkkkcerywaqeqeplqtgpftitlvKEKrlneevilrtlkvtfQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 154 VRESGSLNPDhgPAVIHCSAGIGRSGTFSLVDTC--LVLMEK-GDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14603   188 ARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVrqLLLTQRiPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 41-227 1.54e-48

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: 163.65  E-value: 1.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  41 ENRNRNRYRDVSPYDHSRVKLQNAE-----NDYINASLVDIE--------EAQRSYILTQGPLPNTCCHFWLMVWQQKTK 107
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDpnepvSDYINANIIMPEfetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 108 AVVMLNRIVEKESS-------------------------------------------GET-RTISHFHYTTWPDFGVPES 143
Cdd:cd14605    81 VIVMTTKEVERGKSkcvkywpdeyalkeygvmrvrnvkesaahdyilrelklskvgqGNTeRTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 144 PASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGD--DINIKQVLLNMRKYRMGLIQTPDQL 220
Cdd:cd14605   161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIdIIREKGVdcDIDVPKTIQMVRSQRSGMVQTEAQY 240


                  ....*..
gi 1370473690 221 RFSYMAI 227
Cdd:cd14605   241 RFIYMAV 247
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 7-233 2.12e-48

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: 164.05  E-value: 2.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690   7 REFEELD--TQRRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQ 80
Cdd:cd14626    20 QEYESIDpgQQFTWENSNLEV----------------NKPKNRYANVIAYDHSRVILTSVDgvpgSDYINANYIDGYRKQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  81 RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE----------------------------------------- 119
Cdd:cd14626    84 NAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSrvkcdqywpirgtetygmiqvtlldtvelatysvrtfalyk 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 -SSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDIN 198
Cdd:cd14626   164 nGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNP--PDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVD 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370473690 199 IKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 233
Cdd:cd14626   242 IYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 46-222 6.03e-48

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: 161.03  E-value: 6.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSPYDHSRVKLQNAEND----YINASLV---DIEEaqRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIrgyDGEE--KAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 ---------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGS 159
Cdd:cd14547    79 kekcaqywpeeenetygdfevtvqsvketdgytvrkltlKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473690 160 LNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14547   159 TEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 46-225 7.96e-48

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: 160.85  E-value: 7.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSPYDHSRVKLQNAEN----DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK--- 118
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgrv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 ------------------------ES------------SGET-----RTISHFHYTTWPDFGVPESPASFLNFLFKVRES 157
Cdd:cd14617    81 kcdhywpadqdslyygdlivqmlsESvlpewtirefkiCSEEqldapRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473690 158 GSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQlrFSYM 225
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQ--YVYL 226
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 41-228 1.34e-46

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: 158.07  E-value: 1.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  41 ENRNRNRYRDVSPYDHSRVKLQNaENDYINASLVDIEEAQRS--YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGD-EGGYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 E---------------------------------------------SSGETRTISHFHYTTWPDFGVPESPASFLNFLFK 153
Cdd:cd14597    81 GkikcqrywpeilgkttmvdnrlqltlvrmqqlknfvirvlelediQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370473690 154 VRESGSLnpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd14597   161 MRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 68-222 1.67e-46

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: 156.74  E-value: 1.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK----------------------------- 118
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgrrkcdqywpkegtetygniqvtllstev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 -------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFlfkVRESGSLNPDH-GPAVIHCSAGIGRS 178
Cdd:cd14549    81 latytvrtfslknlklkkvKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGaGPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370473690 179 GTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 40-229 2.39e-46

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: 158.50  E-value: 2.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVKLQNAEN-----DYINAS-----LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 109
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSnipgsDYINANyvknqLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 110 VMLNRIVEK--------------------------------------------ESSGETRTISHFHYTTWPDFGVPESPA 145
Cdd:cd14606    96 VMTTREVEKgrnkcvpywpevgmqraygpysvtncgehdtteyklrtlqvsplDNGELIREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 146 SFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLME-KG--DDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14606   176 GVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStKGldCDIDIQKTIQMVRAQRSGMVQTEAQYKF 255


                  ....*..
gi 1370473690 223 SYMAIIE 229
Cdd:cd14606   256 IYVAIAQ 262
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 5-233 2.98e-46

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: 158.72  E-value: 2.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690   5 IEREFEELD--TQRRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEE 78
Cdd:cd14625    24 LSQEYESIDpgQQFTWEHSNLEV----------------NKPKNRYANVIAYDHSRVILQPIEgimgSDYINANYIDGYR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  79 AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE--------------------------------------- 119
Cdd:cd14625    88 KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSrikcdqywpsrgtetygmiqvtlldtielatfcvrtfsl 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 ---SSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD 196
Cdd:cd14625   168 hknGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNP--PDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKT 245

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370473690 197 INIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 233
Cdd:cd14625   246 VDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 67-228 9.46e-46

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: 155.18  E-value: 9.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  67 DYINASLVDIE----EAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE------------------------- 117
Cdd:cd14541     1 DYINANYVNMEipgsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVErgrvkchqywpdlgetmqfgnlqit 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 --KES----------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR--ESGSLNPdhgpAVIHCSAGIGR 177
Cdd:cd14541    81 cvSEEvtpsfafrefiltntnTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRqnRVGMVEP----TVVHCSAGIGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370473690 178 SGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd14541   157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 31-222 8.60e-45

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: 153.51  E-value: 8.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  31 DYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAEN----DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 106
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEeegsDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 107 KAVVMLNRIVEKES-----------------------------------------SGETRTISHFHYTTWPDFGVPESPA 145
Cdd:cd14614    81 QIIVMLTQCNEKRRvkcdhywpfteepvaygditvemlseeeqpdwairefrvsyADEVQDVMHFNYTAWPDHGVPTANA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 146 --SFLNFLFKVRESGSLNPdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14614   161 aeSILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 41-233 1.26e-44

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: 152.87  E-value: 1.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  41 ENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIV 116
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 117 E-----------------------------------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFlfkVR 155
Cdd:cd14630    82 EvgrvkcvrywpddtevygdikvtlieteplaeyvirtftvqKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF---VR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 156 ESGSLNP-DHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 233
Cdd:cd14630   159 QVKFLNPpDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 40-229 2.75e-44

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: 153.27  E-value: 2.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVKLQ------NAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 113
Cdd:cd17667    25 PDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 114 RIVEK-----------ESSGE------------------------------------------TRTISHFHYTTWPDFGV 140
Cdd:cd17667   105 NLVEKgrrkcdqywptENSEEygniivtlkstkihacytvrrfsirntkvkkgqkgnpkgrqnERTVIQYHYTQWPDMGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 141 PESPASFLNFLfkVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQL 220
Cdd:cd17667   185 PEYALPVLTFV--RRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 262


                  ....*....
gi 1370473690 221 RFSYMAIIE 229
Cdd:cd17667   263 IFIHDALLE 271
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 48-229 4.61e-44

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: 151.25  E-value: 4.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  48 YRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK----- 118
Cdd:cd14620     1 YPNILPYDHSRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERkeekc 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 ----------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVResg 158
Cdd:cd14620    81 yqywpdqgcwtygnirvavedcvvlvdytirkfciqpqlpDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK--- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473690 159 SLNPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14620   158 SVNPVHaGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 7-233 1.43e-43

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: 151.81  E-value: 1.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690   7 REFEELD--TQRRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQ 80
Cdd:cd14624    26 QEYESIDpgQQFTWEHSNLEV----------------NKPKNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYRKQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  81 RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE------------------------------------------K 118
Cdd:cd14624    90 NAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEErsrvkcdqywpsrgtetygliqvtlldtvelatycvrtfalyK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDIN 198
Cdd:cd14624   170 NGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNP--PDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD 247

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370473690 199 IKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 233
Cdd:cd14624   248 IYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTC 282
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 36-234 1.66e-43

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: 151.36  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  36 VAKFPENRNRNRYRDVSPYDHSRV--KLQNAEN--DYINAS-LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 110
Cdd:cd14610    38 VAQREENVQKNRSLAVLPYDHSRIilKAENSHShsDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 111 MLNRIVEK-----------ESS--------------------------------GETRTISHFHYTTWPDFGVPESPASF 147
Cdd:cd14610   118 MLTPLAENgvkqcyhywpdEGSnlyhiyevnlvsehiwcedflvrsfylknlqtNETRTVTQFHFLSWNDQGVPASTRSL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 148 LNFLFKVREsgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-DDINIKQVLLNMRKYRMGLIQTPDQLRFSYMA 226
Cdd:cd14610   198 LDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTA 275


                  ....*...
gi 1370473690 227 IIEGAKCI 234
Cdd:cd14610   276 VAEEVNAI 283
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 68-224 3.95e-43

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: 148.17  E-value: 3.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEA-QRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE----------------------------- 117
Cdd:cd18533     1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEngrekcdqywpsgeyegeygdltvelvse 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 ---------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFS 182
Cdd:cd18533    81 eenddggfivrefelSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTFI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370473690 183 LVDTCLVLMEKGDDIN---------IKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd18533   161 ALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 22-229 9.61e-43

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: 149.38  E-value: 9.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  22 YLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKL-QNAEND--YINAS--LVDIEEAQRSYILTQGPLPNTCCH 96
Cdd:cd14599    18 YEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvPTKENNtgYINAShiKVTVGGEEWHYIATQGPLPHTCHD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  97 FWLMVWQQKTKAVVMLN---------------RIVEKESS-------------------------------GETRTISHF 130
Cdd:cd14599    98 FWQMVWEQGVNVIAMVTaeeeggrskshrywpKLGSKHSSatygkfkvttkfrtdsgcyattglkvkhllsGQERTVWHL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 131 HYTTWPDFGVPESPASFLNFLFKVRE-----------SGSLNPdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINI 199
Cdd:cd14599   178 QYTDWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmldsTKNCNP---PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEV 254

                         250       260       270
                  ....*....|....*....|....*....|
gi 1370473690 200 KQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14599   255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 68-229 1.84e-42

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: 146.43  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIE--EAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK--------------------------- 118
Cdd:cd14596     1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERgkvkchrywpetlqepmelenyqlrle 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 -----------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLnpdhGPAVIHCSAGIGRSGTF 181
Cdd:cd14596    81 nyqalqyfiiriiklveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370473690 182 SLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 36-234 5.28e-42

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: 147.49  E-value: 5.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  36 VAKFPENRNRNRYRDVSPYDHSRVKLQNAEN----DYINAS-LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 110
Cdd:cd14609    36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrsDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 111 MLNRIVE-------------------------------------------KESSGETRTISHFHYTTWPDFGVPESPASF 147
Cdd:cd14609   116 MLTPLVEdgvkqcdrywpdegsslyhiyevnlvsehiwcedflvrsfylkNVQTQETRTLTQFHFLSWPAEGIPSSTRPL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 148 LNFLFKVREsgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-DDINIKQVLLNMRKYRMGLIQTPDQLRFSYMA 226
Cdd:cd14609   196 LDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGMVRTKDQFEFALTA 273


                  ....*...
gi 1370473690 227 IIEGAKCI 234
Cdd:cd14609   274 VAEEVNAI 281
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 46-229 1.27e-41

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: 145.03  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE---- 117
Cdd:cd14619     1 NRFRNVLPYDWSRVPLkpihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEagrv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 ---------------------------------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESG 158
Cdd:cd14619    81 kcehywpldytpctyghlrvtvvseevmenwtvrefllkQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370473690 159 SLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14619   161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 46-228 1.93e-41

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: 144.32  E-value: 1.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE---- 117
Cdd:cd14618     1 NRYPHVLPYDHSRVRLsqlgGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMEngrv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 ------------------------KESSGE---------------TRTISHFHYTTWPDFGVPESPASFLNFLFKVRESG 158
Cdd:cd14618    81 lcdhywpsestpvsyghitvhllaQSSEDEwtrrefklwhedlrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 159 SLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 37-226 1.97e-41

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: 144.59  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  37 AKFPENRNRNRYRDVSPYDHSRVKLQ---NAE-NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQpirGVEgSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 113 NRIVEKE------------------------------------------SSGETRTISHFHYTTWPDFGVPESPASFLNF 150
Cdd:cd14554    81 TKLREMGrekchqywpaersaryqyfvvdpmaeynmpqyilrefkvtdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370473690 151 LFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMA 226
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 68-229 7.37e-41

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: 142.60  E-value: 7.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEE--AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN-----------------------------RIV 116
Cdd:cd14540     1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTaeeeggrekcfrywptlggehdaltfgeyKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 117 EKES-----------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR--------ESGSLNPdHGPAVIHC 171
Cdd:cd14540    81 TKFSvssgcytttglrvkhtlSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvrrhtnqDVAGHNR-NPPTLVHC 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473690 172 SAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 68-229 9.58e-41

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: 141.81  E-value: 9.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES-------------------------- 120
Cdd:cd14546     1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVkqcarywpeegsevyhiyevhlvseh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 121 -----------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsgSLNPDHGPAVIHCSAGIGRSGTFSL 183
Cdd:cd14546    81 iwcddylvrsfylknlqTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK--SYRGRSCPIVVHCSDGAGRTGTYIL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370473690 184 VDTCLVLMEKG-DDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14546   159 IDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 28-230 4.35e-40

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: 142.10  E-value: 4.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  28 ESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQ 103
Cdd:cd14633    26 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgetsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 104 QKTKAVVMLNRIVE-----------------------------------------KESSGETRTISHFHYTTWPDFGVPE 142
Cdd:cd14633   106 ENTASIIMVTNLVEvgrvkcckywpddteiykdikvtlietellaeyvirtfaveKRGVHEIREIRQFHFTGWPDHGVPY 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 143 SPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14633   186 HATGLLGFVRQVKSKSP--PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVF 263


                  ....*...
gi 1370473690 223 SYMAIIEG 230
Cdd:cd14633   264 IHDAILEA 271
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 40-224 4.88e-40

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: 141.13  E-value: 4.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVKLQNA-----ENDYINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 113
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLRRAgsqeeEGSYINANYIrGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 114 RIVE-----------KESS---------------------------GETRTISHFHYTTWPDFGVPESPASFLNFLFKVR 155
Cdd:cd14612    93 KLKEkkekcvhywpeKEGTygrfeirvqdmkecdgytirdltiqleEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 156 ESGSLNPDHGPAVIHCSAGIGRSGTFSLVDT-CLVLMEKGdDINIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd14612   173 ESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTG-KVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
126-229 6.30e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.33  E-value: 6.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  126 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD-INIKQVLL 204
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1370473690  205 NMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 126-229 6.30e-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: 136.33  E-value: 6.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  126 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD-INIKQVLL 204
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1370473690  205 NMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 32-227 8.85e-40

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: 141.99  E-value: 8.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  32 YPHRVAKFPENRNRNRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 107
Cdd:cd14604    47 YPTATGEKEENVKKNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 108 AVVMLNRIVEK------------------------------------------ESSGETRTISHFHYTTWPDFGVPESPA 145
Cdd:cd14604   127 IIVMACREFEMgrkkcerywplygeepmtfgpfrisceaeqartdyfirtlllEFQNETRRLYQFHYVNWPDHDVPSSFD 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 146 SFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG---DDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14604   207 SILDMISLMRKYQE--HEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYEL 284


                  ....*
gi 1370473690 223 SYMAI 227
Cdd:cd14604   285 VHRAI 289
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 41-229 7.39e-39

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: 139.77  E-value: 7.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  41 ENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIV 116
Cdd:cd14621    51 ENKEKNRYVNILPYDHSRVHLTPVEgvpdSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 117 EKE----------------------------------------------SSGETRTISHFHYTTWPDFGVPESPASFLNF 150
Cdd:cd14621   131 ERKeckcaqywpdqgcwtygnirvsvedvtvlvdytvrkfciqqvgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKF 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 151 LFKVResgSLNPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14621   211 LKKVK---NCNPQYaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 67-229 2.27e-38

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: 135.84  E-value: 2.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  67 DYINASLVDIEEAQRS----YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE----------------------- 119
Cdd:cd14601     1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGrvkchqywpepsgsssyggfqvt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 120 --------------------SSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDhgPAVIHCSAGIGRSG 179
Cdd:cd14601    81 chseegnpayvfremtltnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370473690 180 TFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 3-229 6.77e-38

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: 137.17  E-value: 6.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690   3 TTIEREFEELDTQRrwqplyleirneSHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEE 78
Cdd:cd14628    25 TGMELEFKRLASSK------------AHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRgvegSDYINASFIDGYR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  79 AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI------------------------------------------V 116
Cdd:cd14628    93 QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLremgrekchqywpaersaryqyfvvdpmaeynmpqyilrefkV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 117 EKESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD 196
Cdd:cd14628   173 TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV 252

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370473690 197 INIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14628   253 VDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 68-224 9.92e-38

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: 134.05  E-value: 9.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML-----------------NR--------------- 114
Cdd:cd14539     1 YINASLIeDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLvseqenekqkvhrywptERgqalvygaitvslqs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 115 -------------IVEKESSgETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSL-NPDHGPAVIHCSAGIGRSGT 180
Cdd:cd14539    81 vrttpthveriisIQHKDTR-LSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQqRSLQTPIVVHCSSGVGRTGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370473690 181 FSLVDTCLVLMEKGDDI-NIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd14539   160 FCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 45-229 1.83e-37

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: 134.20  E-value: 1.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  45 RNRYRDVSPYDHSRVKLQ----NAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVM--------- 111
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitsDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacmefemgk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 112 ---------------------------------LNRIVEKESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVResg 158
Cdd:cd14602    81 kkcerywaepgemqlefgpfsvtceaekrksdyIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR--- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370473690 159 SLNPDHG-PAVIHCSAGIGRSGTFSLVDTCLVLMEKG---DDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14602   158 CYQEDDSvPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 37-229 9.86e-37

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: 133.70  E-value: 9.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  37 AKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 113 NRI------------------------------------------VEKESSGETRTISHFHYTTWPDFGVPESPASFLNF 150
Cdd:cd14627   128 TKLremgrekchqywpaersaryqyfvvdpmaeynmpqyilrefkVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 151 LFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14627   208 IGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 45-222 1.21e-36

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: 132.68  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  45 RNRYRDVSPYDHSRVKLQNAEND-----YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDdplssYINANYIrGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 --------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES-GS 159
Cdd:cd14613   108 nekcteywpeeqvtyegieitvkqvihaddyrlrlitlKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEArQQ 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473690 160 LNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14613   188 AEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 41-234 2.56e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 133.20  E-value: 2.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  41 ENRNRNRYRDVSPYDHSRV--KLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVilKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 --------------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 154
Cdd:PHA02742  131 gkeacypywmphergkathgefkiktkkiksfrnyavtnlcltdTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAV 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 155 RE---------SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM 225
Cdd:PHA02742  211 REadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYF 290


                  ....*....
gi 1370473690 226 AIIEGAKCI 234
Cdd:PHA02742  291 IVLIFAKLM 299
PHA02738 PHA02738
hypothetical protein; Provisional
 42-227 9.73e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 131.97  E-value: 9.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  42 NRNRNRYRDVSPYDHSRVKLQNAEN--DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR----- 114
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKkkeng 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 115 --------------------------------------IVEKESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE 156
Cdd:PHA02738  129 rekcfpywsdveqgsirfgkfkitttqvethphyvkstLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQ 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 157 ------SGSLNPDHG-----PAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM 225
Cdd:PHA02738  209 cqkelaQESLQIGHNrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYR 288


                  ..
gi 1370473690 226 AI 227
Cdd:PHA02738  289 AV 290
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 46-222 3.30e-35

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: 128.10  E-value: 3.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSPYDHSRVKLQN----AENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK--- 118
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIAdagvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKgri 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 ---------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGS 159
Cdd:cd14616    81 rchqywpednkpvtvfgdivitklmedvqidwtirdlkiERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473690 160 lnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14616   161 --HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 40-222 3.55e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 130.12  E-value: 3.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN--- 113
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 114 -------------------------------------------RIVEKeSSGETRTISHFHYTTWPDFGVPESPASFLNF 150
Cdd:PHA02747  129 gtngeekcyqywclnedgnidmedfrietlktsvrakyiltliEITDK-ILKDSRKISHFQCSEWFEDETPSDHPDFIKF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 151 LFKV----RESGSL-NPDHG---PAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:PHA02747  208 IKIIdinrKKSGKLfNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 37-229 5.23e-35

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: 129.46  E-value: 5.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  37 AKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 113 NRI------------------------------------------VEKESSGETRTISHFHYTTWPDFGVPESPASFLNF 150
Cdd:cd14629   128 TKLremgrekchqywpaersaryqyfvvdpmaeynmpqyilrefkVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDF 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 151 LFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14629   208 IGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 68-224 2.06e-34

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: 125.02  E-value: 2.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES---------SGE--------------- 123
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEkkcsqywpdQGCwtygnlrvrvedtvv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 124 ----------------------TRTISHFHYTTWPDFGVPESPASFLNFLFKVResgSLNPDH-GPAVIHCSAGIGRSGT 180
Cdd:cd14551    81 lvdyttrkfciqkvnrgigekrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK---SANPPRaGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370473690 181 FSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 40-232 3.27e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 127.84  E-value: 3.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVKL-----------------------QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCH 96
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkievtsEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  97 FWLMVWQQKTKAVVMLNRI-------------------------------------------VEKESSGETRTISHFHYT 133
Cdd:PHA02746  129 FFKLISEHESQVIVSLTDIddddekcfelwtkeedselafgrfvakildiieelsftktrlmITDKISDTSREIHHFWFP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 134 TWPDFGVPESPASFLNFLFKVRE--------SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLN 205
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370473690 206 MRKYRMGLIQTPDQLRFSYM----AIIEGAK 232
Cdd:PHA02746  289 IRKQRHSSVFLPEQYAFCYKalkyAIIEEAK 319
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 68-229 6.98e-34

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: 123.87  E-value: 6.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE------------------------------ 117
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvgrvkcsrywpddtevygdikvtlvetepl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 -----------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDT 186
Cdd:cd14555    81 aeyvvrtfaleRRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP--PSAGPIVVHCSAGAGRTGCYIVIDI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370473690 187 CLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14555   159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 45-222 3.78e-33

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: 122.72  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  45 RNRYRDVSPYDHSRVKLQ-----NAENDYINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKpknsnDSLSTYINANYIrGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 119 --------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSL 160
Cdd:cd14611    82 nekcvlywpekrgiygkvevlvnsvkecdnytirnltlKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473690 161 NPDHGPAVIHCSAGIGRSGTF-SLVDTCLVLMEKGdDINIKQVLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14611   162 SPGRGPVVVHCSAGIGRTGCFiATTIGCQQLKEEG-VVDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 68-224 5.41e-33

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: 121.35  E-value: 5.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI-------------VEKESSG------------ 122
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkegdqeqcaqywgDEKKTYGdievelkdteks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 123 ----------------ETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESG----SLNPDHGPAVIHCSAGIGRSGTFs 182
Cdd:cd14558    81 ptytvrvfeithlkrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSVPIVVHCSDGSSRTGIF- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370473690 183 lvdtC--LVLMEKGDD---INIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd14558   160 ----CalWNLLESAETekvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 68-228 1.63e-32

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: 120.47  E-value: 1.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK-----------ESSGE------------- 123
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrkcdqywpaDGSEEygnflvtqksvqv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 124 --------------------------TRTISHFHYTTWPDFGVPESPASFLNFLFKvrESGSLNPDHGPAVIHCSAGIGR 177
Cdd:cd17668    81 layytvrnftlrntkikkgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK--ASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370473690 178 SGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 58-230 1.74e-32

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: 120.51  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  58 RVKLQNAEND----YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE---------------- 117
Cdd:cd14631     1 RVILQPVEDDpssdYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvgrvkcykywpddtev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 -------------------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCS 172
Cdd:cd14631    81 ygdfkvtcvemeplaeyvvrtftleRRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNP--PSAGPIVVHCS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473690 173 AGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEG 230
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 68-224 4.56e-32

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: 119.11  E-value: 4.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLV--DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE---------------------------- 117
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnystakcadyfpaeenesrefgrisvtn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 -------------------KESSGETRTISHFHYTTWPDFGVPESPASFLNFLfkvRESGSLNPDHGPAVIHCSAGIGRS 178
Cdd:cd17658    81 kklkhsqhsitlrvlevqyIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELL---KRLYGIPPSAGPIVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370473690 179 GTFSLVDTCLVLMEKGD--DINIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd17658   158 GAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 68-233 9.61e-31

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: 115.53  E-value: 9.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE-------------KESSGETRT-------- 126
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvgrvkcskywpddSDTYGDIKItllktetl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 127 --------------------ISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDT 186
Cdd:cd14632    81 aeysvrtfalerrgysarheVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP--PDAGPVVVHCSAGAGRTGCYIVLDV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370473690 187 CLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 233
Cdd:cd14632   159 MLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 68-224 1.63e-30

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: 114.83  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRivEKES--------------------------- 120
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR--EFEMgkkkcerywpeegeeqlqfgpfkisle 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 121 ------------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR---ESGSLnpdhgPAVIHCSAGIGRSG 179
Cdd:cd14542    79 kekrvgpdflirtlkvtfQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRdyqGSEDV-----PICVHCSAGCGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370473690 180 TFSLVDTCLVLMEKG---DDINIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd14542   154 TICAIDYVWNLLKTGkipEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
40-220 1.71e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 117.11  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  40 PENRNRNRYRDVSPYDHSRVklqNAENDYINASLVDIEEAQRsYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN------ 113
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAsddeis 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 114 ----------------------------------------RIVEKESSGETRTISHFHYTTWPDFGVPESPAsFLNFLFK 153
Cdd:COG5599   116 kpkvkmpvyfrqdgeygkyevsseltesiqlrdgieartyVLTIKGTGQKKIEIPVLHVKNWPDHGAISAEA-LKNLADL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370473690 154 VRES-GSLNPDHGPAVIHCSAGIGRSGTFSLvdtCLVLMEKGD-----DINIKQVLLNMRKYR-MGLIQTPDQL 220
Cdd:COG5599   195 IDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSKSINalvqiTLSVEEIVIDMRTSRnGGMVQTSEQL 265
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 68-227 8.49e-30

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: 113.13  E-value: 8.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE--------------SSGE---------- 123
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqnkcaqywpedgsvSSGDitvelkdqtd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 124 ------------------TRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHgPAVIHCSAGIGRSGTFSLVD 185
Cdd:cd14552    81 yedytlrdflvtkgkggsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFCALS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370473690 186 TCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 227
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 68-229 2.35e-29

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: 112.38  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINAS--LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNriVEKES------------------------- 120
Cdd:cd14598     1 YINAShiKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT--AEEEGgreksfrywprlgsrhntvtygrfk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 121 -----------------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE-----SGSLNPD--HGPAVIH 170
Cdd:cd14598    79 ittrfrtdsgcyattglkikhllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtNSTIDPKspNPPVLVH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 171 CSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14598   159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 47-229 1.04e-26

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: 105.51  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  47 RYRDVSPYDHSRVKL---QNAEN-DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE----- 117
Cdd:cd14623     1 RVLQIIPYEFNRVIIpvkRGEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgqek 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 118 ---------------------KESSGET----------------RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSL 160
Cdd:cd14623    81 caqywpsdgsvsygditielkKEEECESytvrdllvtntrenksRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 161 NPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14623   161 SGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 67-227 1.66e-26

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: 104.32  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  67 DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE--------------SSGE--------- 123
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREqekcvqywpsegsvTHGEitieikndt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 124 -------------------TRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHgPAVIHCSAGIGRSGTFSLV 184
Cdd:cd14622    81 lletisirdflvtynqekqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH-PIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370473690 185 DTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 227
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 68-219 4.61e-26

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: 102.98  E-value: 4.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR--------------------------------- 114
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRceegnrnkcaqywpsmeegsrafgdvvvkinee 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 115 ------------IVEKESSGETRTISHFHYTTWPDFGVPESPasflNFLFKVRE--SGSLNPDHGPAVIHCSAGIGRSGT 180
Cdd:cd14557    81 kicpdyiirklnINNKKEKGSGREVTHIQFTSWPDHGVPEDP----HLLLKLRRrvNAFNNFFSGPIVVHCSAGVGRTGT 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370473690 181 FSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQ 219
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQ 195
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 68-224 6.80e-26

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: 102.49  E-value: 6.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI---------------------VEKESSGET-- 124
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLdpkdqscpqywpdegsgtygpIQVEFVSTTid 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 125 --------------------RTISHFHYTTWPDFG-VPESPASFLNFLFKV----RESGSlnpdhGPAVIHCSAGIGRSG 179
Cdd:cd14556    81 edvisrifrlqnttrpqegyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVekwqEQSGE-----GPIVVHCLNGVGRSG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370473690 180 TFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSY 224
Cdd:cd14556   156 VFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 42-227 1.48e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 87.33  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  42 NRNRNRYRD------VSPYDHSRVKLQNAENdYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 115
Cdd:PHA02740   47 AQAENKAKDenlalhITRLLHRRIKLFNDEK-VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 116 VEK-----------------------------------------ESSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 154
Cdd:PHA02740  126 ADKkcfnqfwslkegcvitsdkfqietleiiikphfnltllsltDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNI 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473690 155 R------ESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 227
Cdd:PHA02740  206 DdlcadlEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 68-229 4.34e-18

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: 81.22  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI----------VEKES-----------SGET-- 124
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMdaaqlcmqywPEKTSccygpiqvefvSADIde 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 125 -------------------RTISHFHYTTWPDF-GVPESPASFLNFLFKVRE-SGSLNPDHGPAVIHCSAGIGRSGTFSL 183
Cdd:cd14634    81 diisrifricnmarpqdgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKwQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370473690 184 VDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14634   161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 68-224 1.81e-17

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: 79.29  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---------------------------------NR 114
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLtdnelnedepiywptkekplecetfkvtlsgedHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 115 IVEKESSGETR-------------TISHFHYTTWPDfgvPESPAS-FLNFLFKVRESGSLNpdHGPAVIHCSAGIGRSGT 180
Cdd:cd14550    81 CLSNEIRLIVRdfilestqddyvlEVRQFQCPSWPN---PCSPIHtVFELINTVQEWAQQR--DGPIVVHDRYGGVQAAT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370473690 181 FSLVDTCLVLMEKGDDINIKQV--LLNMRkyRMGLIQTPDQLRFSY 224
Cdd:cd14550   156 FCALTTLHQQLEHESSVDVYQVakLYHLM--RPGVFTSKEDYQFLY 199
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 68-229 3.91e-16

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: 76.10  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES------------------------SGE 123
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSawpclqywpepglqqygpmevefvSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 124 ------TRT---------------ISHFHYTTWPDF-GVPESPASFLNFLFKV----RESGSlnpdhGPAVIHCSAGIGR 177
Cdd:cd14637    81 adedivTRLfrvqnitrlqeghlmVRHFQFLRWSAYrDTPDSKKAFLHLLASVekwqRESGE-----GRTVVHCLNGGGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370473690 178 SGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14637   156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 68-229 1.23e-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: 74.68  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI----------------------VEKES-SGET 124
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdlaqgcpqywpeegmlrygpiqVECMScSMDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 125 RTIS-------------------HFHYTTWPDF-GVPESPASFLNFLFKVRE-SGSLNPDHGPAVIHCSAGIGRSGTFSL 183
Cdd:cd14636    81 DVISrifricnltrpqegylmvqQFQYLGWASHrEVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370473690 184 VDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14636   161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 68-229 7.71e-14

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: 69.33  E-value: 7.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN---------------------------------- 113
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNdvdpaqlcpqywpengvhrhgpiqvefvsadlee 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 114 ----RIVEKESSGET----RTISHFHYTTWPDF-GVPESPASFLNFLFKV-RESGSLNPDHGPAVIHCSAGIGRSGTFSL 183
Cdd:cd14635    81 diisRIFRIYNAARPqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370473690 184 VDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 229
Cdd:cd14635   161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
107-222 4.48e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 62.68  E-value: 4.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 107 KAVVMLNRIVE-KESSGETRTISHFHYTtWPDFGVPEsPASFLNFLFKVREsgsLNPDHGPAVIHCSAGIGRSGTFslvd 185
Cdd:COG2453    27 DAVVSLTEEEElLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTGTV---- 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370473690 186 TCLVLMEKGDDIN--IKQVllnmRKYRMGLIQTPDQLRF 222
Cdd:COG2453    98 AAAYLVLLGLSAEeaLARV----RAARPGAVETPAQRAF 132
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 68-228 1.32e-11

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: 63.09  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML----------------------------------- 112
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLpdgqnmaedefvywpnkdepincetfkvtliaeeh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 113 ------------NRIVEKESSGETRTISHFHYTTWPDfgvPESPASFLNFLFKVRESGSLNPDhGPAVIHCSAGIGRSGT 180
Cdd:cd17669    81 kclsneekliiqDFILEATQDDYVLEVRHFQCPKWPN---PDSPISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370473690 181 FSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd17669   157 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 68-228 1.72e-11

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: 62.77  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRIVEKES------------------------ 120
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFvywpsreesmnceaftvtliskdr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 121 ---SGETRTI-----------------SHFHYTTWPDfgvPESPASFLNFLFKVRESGSLNPDhGPAVIHCSAGIGRSGT 180
Cdd:cd17670    81 lclSNEEQIIihdfileatqddyvlevRHFQCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEFGAVSAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370473690 181 FSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 228
Cdd:cd17670   157 LCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 136-222 1.01e-09

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 56.50  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 136 PDFGVPESPASFLNFLfkvRESGSLNPDHGPAVIHCSAGIGRSGtfsLVDTCLvLMEKGDDINIKQVLLNMRKYRMGLIQ 215
Cdd:cd14505    81 PDGGVPSDIAQWQELL---EELLSALENGKKVLIHCKGGLGRTG---LIAACL-LLELGDTLDPEQAIAAVRALRPGAIQ 153


                  ....*..
gi 1370473690 216 TPDQLRF 222
Cdd:cd14505   154 TPKQENF 160
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 46-220 5.17e-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: 52.79  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  46 NRYRDVSpydhSRVKLQNAENdyINASLVDIEEaQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR----------- 114
Cdd:cd14559     1 NRFTNIQ----TRVSTPVGKN--LNANRVQIGN-KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASnkdiqrkglpp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 115 -------------IVEKESSGE-------------------TRTISHFHYTTWPDFG-------------VPESPASFLN 149
Cdd:cd14559    74 yfrqsgtygsvtvKSKKTGKDElvdglkadmynlkitdgnkTITIPVVHVTNWPDHTaisseglkeladlVNKSAEEKRN 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473690 150 FLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSlvdTCLVLMEKGDDINIKQVLLNMRKYRMG-LIQTPDQL 220
Cdd:cd14559   154 FYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQL 222
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 83-222 8.21e-07

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: 46.96  E-value: 8.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690  83 YILTQGPLPNTCcHFWLMVWQQKTKAVVMLNrivekessgetrtishfhyttwpdfgvpesPASFLNFLFKVRESGSLNP 162
Cdd:cd14494     9 LIAGALPLSPLE-ADSRFLKQLGVTTIVDLT------------------------------LAMVDRFLEVLDQAEKPGE 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 163 dhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDInIKQVllnMRKYRMGLIQTPDQLRF 222
Cdd:cd14494    58 ---PVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA-VRIV---RLIRPGGIPQTIEQLDF 110
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 127-222 2.43e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 41.57  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 127 ISHFHYTtWPDFGVPeSPASFLN----FLFKVRESGSLnpdhgpaVIHCSAGIGRSGtfsLVDTC-LVLMEKgddINIKQ 201
Cdd:cd14506    77 IYFYNFG-WKDYGVP-SLTTILDivkvMAFALQEGGKV-------AVHCHAGLGRTG---VLIACyLVYALR---MSADQ 141

                          90       100
                  ....*....|....*....|.
gi 1370473690 202 VLLNMRKYRMGLIQTPDQLRF 222
Cdd:cd14506   142 AIRLVRSKRPNSIQTRGQVLC 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 136-222 2.85e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 40.34  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 136 PDFGVP--ESPASFLNFLFKVRESGslnpdhGPAVIHCSAGIGRSGTFSlvdTC-LVLMEK--GDDInIKQVllnmRKYR 210
Cdd:cd14504    58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTML---ACyLVKTGKisAVDA-INEI----RRIR 123

                          90
                  ....*....|..
gi 1370473690 211 MGLIQTPDQLRF 222
Cdd:cd14504   124 PGSIETSEQEKF 135
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 135-224 1.36e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 38.72  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 135 WPDfgvpESPASFlNFLFKVRESG----SLNPDHgPAVIHCSAGIGRSGTFslvdTCLVLMEKGDDINIKQVL--LNMRK 208
Cdd:cd14497    68 FPD----HHPPPL-GLLLEIVDDIdswlSEDPNN-VAVVHCKAGKGRTGTV----ICAYLLYYGQYSTADEALeyFAKKR 137

                          90
                  ....*....|....*...
gi 1370473690 209 YRMGL--IQTPDQLRFSY 224
Cdd:cd14497   138 FKEGLpgVTIPSQLRYLQ 155
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 128-222 7.06e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 36.96  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473690 128 SHFHYTT----WPDFGVPESPaSFLNFLFKVRESGSLNPDHGPAvIHCSAGIGRSGTFslvdTCLVLMEKGDDINIKQVL 203
Cdd:cd14510    70 KYFHNRVervpIDDHNVPTLD-EMLSFTAEVREWMAADPKNVVA-IHCKGGKGRTGTM----VCAWLIYSGQFESAKEAL 143

                          90       100
                  ....*....|....*....|....*..
gi 1370473690 204 --LNMRKYRMGL------IQTPDQLRF 222
Cdd:cd14510   144 eyFGERRTDKSVsskfqgVETPSQSRY 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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