NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907136856|ref|XP_036015580|]
View 

tyrosine-protein phosphatase non-receptor type 1 isoform X3 [Mus musculus]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1-217 2.24e-178

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 cd14608:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 277  Bit Score: 489.54  E-value: 2.24e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   1 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYY 80
Cdd:cd14608    59 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYY 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  81 TVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLL 160
Cdd:cd14608   139 TVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLL 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136856 161 LMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQHE 217
Cdd:cd14608   219 LMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQ 275
 
Name Accession Description Interval E-value
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1-217 2.24e-178

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: 489.54  E-value: 2.24e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   1 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYY 80
Cdd:cd14608    59 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYY 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  81 TVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLL 160
Cdd:cd14608   139 TVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLL 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136856 161 LMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQHE 217
Cdd:cd14608   219 LMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQ 275
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
5-203 2.33e-93

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.96  E-value: 2.33e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISE-DVKSYYTVR 83
Cdd:pfam00102  41 PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGD--FTVTLKKEkEDEKDYTVR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESgSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMD 163
Cdd:pfam00102 119 TLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLE 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 164 KRKDpssVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:pfam00102 198 AEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-203 6.49e-91

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 267.60  E-value: 6.49e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856    5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:smart00194  68 PKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGD--ITVTLKSVEKVDDYTIRT 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSleHGPIVVHCSAGIGRSGTFCLADTCLLLMDK 164
Cdd:smart00194 146 LEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEA 223

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907136856  165 RKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:smart00194 224 GK---EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 4-208 2.12e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 150.15  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   4 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDdtglKLTLISEDVKS--YYT 81
Cdd:PHA02742   91 AKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHG----EFKIKTKKIKSfrNYA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  82 VRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRE---------SGSLSLEHGPIVVHCSAGIGRSGTF 152
Cdd:PHA02742  167 VTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAF 246

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136856 153 CLADTCLLLMDKRkdpSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFI 208
Cdd:PHA02742  247 CAIDICISKYNER---AIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
6-194 2.68e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 118.27  E-value: 2.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRIMEKGSLKCAQYWPQQEEKEmvfddtglKLTLISEDVKSYYTVR 83
Cdd:COG5599    77 HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLasDDEISKPKVKMPVYFRQDGEYG--------KYEVSSELTESIQLRD 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENL------TTKETREILHFHYTTWPDFGVPESPAsFLNFLFKVRESGSLSLEH-GPIVVHCSAGIGRSGTFcLAD 156
Cdd:COG5599   149 GIEARTYvltikgTGQKKIEIPVLHVKNWPDHGAISAEA-LKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTL-IAC 226

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 157 TCLLLMDKRKDPSSVDIKKVLLEMRRFR-MGLIQTADQL 194
Cdd:COG5599   227 LALSKSINALVQITLSVEEIVIDMRTSRnGGMVQTSEQL 265
 
Name Accession Description Interval E-value
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1-217 2.24e-178

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: 489.54  E-value: 2.24e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   1 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYY 80
Cdd:cd14608    59 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYY 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  81 TVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLL 160
Cdd:cd14608   139 TVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLL 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136856 161 LMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQHE 217
Cdd:cd14608   219 LMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQ 275
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1-199 1.33e-145

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: 404.85  E-value: 1.33e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   1 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYY 80
Cdd:cd14545    34 VEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYY 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  81 TVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLL 160
Cdd:cd14545   114 TVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLV 193

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 161 LMDKRkDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYL 199
Cdd:cd14545   194 LIEKG-NPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1-201 1.67e-138

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: 388.17  E-value: 1.67e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   1 MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYY 80
Cdd:cd14607    58 IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYY 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  81 TVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLL 160
Cdd:cd14607   138 TVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLV 217

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 161 LMDKrKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:cd14607   218 LMEK-KDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
5-203 2.33e-93

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.96  E-value: 2.33e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISE-DVKSYYTVR 83
Cdd:pfam00102  41 PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGD--FTVTLKKEkEDEKDYTVR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESgSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMD 163
Cdd:pfam00102 119 TLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLE 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 164 KRKDpssVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:pfam00102 198 AEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-203 6.49e-91

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 267.60  E-value: 6.49e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856    5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:smart00194  68 PKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGD--ITVTLKSVEKVDDYTIRT 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSleHGPIVVHCSAGIGRSGTFCLADTCLLLMDK 164
Cdd:smart00194 146 LEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEA 223

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907136856  165 RKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:smart00194 224 GK---EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 5-198 2.11e-86

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: 253.75  E-value: 2.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd00047    13 PKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGD--ITVTLVSEEELSDYTIRT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDK 164
Cdd:cd00047    91 LELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK--EARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEA 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907136856 165 RKDpssVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd00047   169 EGE---VDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 8-199 5.98e-72

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: 219.93  E-value: 5.98e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14543    74 YIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGD--LTVTNLSVENKEHYKKTTLEI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSL---------EHG--PIVVHCSAGIGRSGTFCLAD 156
Cdd:cd14543   152 HNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVkamgdrwkgHPPgpPIVVHCSAGIGRTGTFCTLD 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907136856 157 TCLllmDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYL 199
Cdd:cd14543   232 ICL---SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 5-196 1.42e-66

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: 203.74  E-value: 1.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQqeEKEMVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14549    13 ARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK--EGTETYGN--IQVTLLSTEVLATYTVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTK------ETREILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSLEH-GPIVVHCSAGIGRSGTFCLADT 157
Cdd:cd14549    89 FSLKNLKLKkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGaGPIVVHCSAGVGRTGTYIVIDS 165

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 158 CLLLMdkrKDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14549   166 MLQQI---QDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 8-196 2.57e-65

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: 201.02  E-value: 2.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEkEMVFDdtGLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14541    21 YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFG--NLQITCVSEEVTPSFAFREFIL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEhgPIVVHCSAGIGRSGTFCLADTCLLLMDKRKD 167
Cdd:cd14541    98 TNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIGRTGVLITMETAMCLIEANEP 175

                         170       180
                  ....*....|....*....|....*....
gi 1907136856 168 PSSVDIKKvllEMRRFRMGLIQTADQLRF 196
Cdd:cd14541   176 VYPLDIVR---TMRDQRAMLIQTPSQYRF 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 2-203 1.58e-64

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 198.75  E-value: 1.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   2 EEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTgLKLTLISEDVKSYYT 81
Cdd:cd14538    12 GGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGR-LEVSLEKYQSLQDFV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  82 VRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVResgsLSLEHGPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd14538    91 IRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR----RIHNSGPIVVHCSAGIGRTGVLITIDVALGL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907136856 162 MDKRKDpssVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14538   167 IERDLP---FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 6-196 2.48e-63

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: 196.04  E-value: 2.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqQEEKEMVFDDtgLKLTLISEDVKSYYTVRQL 85
Cdd:cd14548    39 REFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWP-FDQDPVYYGD--ITVTMLSESVLPDWTIREF 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENltTKETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSLEHGPIVVHCSAGIGRSGTFCLADTcllLMDKR 165
Cdd:cd14548   116 KLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD--YIKQEKGPTIVHCSAGVGRTGTFIALDR---LLQQI 188

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907136856 166 KDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14548   189 ESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 5-205 1.12e-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: 192.61  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKemVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14553    45 QNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQYWPTRGTE--TYGL--IQVTLLDTVELATYTVRT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTCLllmDK 164
Cdd:cd14553   121 FALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACN--PPDAGPIVVHCSAGVGRTGCFIVIDSML---ER 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGA 205
Cdd:cd14553   196 IKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 5-198 6.91e-61

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: 189.38  E-value: 6.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDdtgLKLTLISEDV--KSYYTV 82
Cdd:cd18533    14 SKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGD---LTVELVSEEEndDGGFIV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELeNLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRE-SGSLSLEhGPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd18533    91 REFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElNDSASLD-PPIIVHCSAGVGRTGTFIALDSLLDE 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907136856 162 MDK----RKDPSSVD--IKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd18533   169 LKRglsdSQDLEDSEdpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 3-201 5.27e-58

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: 183.43  E-value: 5.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEmvfDDTGLKLTLISEDVKSYYTV 82
Cdd:cd14544    49 ENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQK---QYGPYRVQNVSEHDTTDYTL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENL-TTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd14544   126 RELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQ 205

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 162 MDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:cd14544   206 IKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 5-196 2.20e-56

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: 178.86  E-value: 2.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKemvfDDTGLKLTLISEDVKSYYTVRQ 84
Cdd:cd14615    38 KKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTcllLMDK 164
Cdd:cd14615   114 FTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDR---LIYQ 190

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14615   191 IENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 2-203 4.62e-56

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: 177.65  E-value: 4.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   2 EEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQ--EEKEMVFDDtgLKLTLISEDVKSY 79
Cdd:cd14540    12 GGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggEHDALTFGE--YKVSTKFSVSSGC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  80 YTVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLE-------HGPIVVHCSAGIGRSGTF 152
Cdd:cd14540    90 YTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghnrNPPTLVHCSAGVGRTGVV 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907136856 153 CLADTCLLLMDKRKDpssVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14540   170 ILADLMLYCLDHNEE---LDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 8-196 1.05e-55

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: 178.51  E-value: 1.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEkemVFDDTGLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14600    84 YIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD---VMEYGGFRVQCHSEDCTIAYVFREMLL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVResgSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKRKD 167
Cdd:cd14600   161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQP 237

                         170       180
                  ....*....|....*....|....*....
gi 1907136856 168 PSSVDIKKvllEMRRFRMGLIQTADQLRF 196
Cdd:cd14600   238 VYPLDIVR---KMRDQRAMMVQTSSQYKF 263
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 8-203 1.37e-55

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: 176.10  E-value: 1.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqqEEKEMVFDDtgLKLTLISEDVKS-YYTVRQLE 86
Cdd:cd14546    17 YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYHI--YEVHLVSEHIWCdDYLVRSFY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESgslslEHG---PIVVHCSAGIGRSGTFCLADtcLLLMD 163
Cdd:cd14546    93 LKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS-----YRGrscPIVVHCSDGAGRTGTYILID--MVLNR 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 164 KRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14546   166 MAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 4-196 3.19e-55

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: 175.66  E-value: 3.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   4 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKgSLKCAQYWPqqEEKEMVFDDTGLklTLISEDVKSYYTVR 83
Cdd:cd14547    39 EEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-KEKCAQYWP--EEENETYGDFEV--TVQSVKETDGYTVR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENLTtkETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTClllMD 163
Cdd:cd14547   114 KLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIG---CQ 188

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907136856 164 KRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14547   189 QLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 8-202 1.10e-54

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: 174.63  E-value: 1.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTgLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14597    45 YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEILGKTTMVDNR-LQLTLVRMQQLKNFVIRVLEL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLslehGPIVVHCSAGIGRSGTFCLADTCLLLMDKRKD 167
Cdd:cd14597   124 EDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLD 199

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907136856 168 pssVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVI 202
Cdd:cd14597   200 ---FDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 3-203 2.92e-54

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: 172.62  E-value: 2.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMvfDDTGLKLTLISEDVKSYYTV 82
Cdd:cd14596    13 EEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPM--ELENYQLRLENYQALQYFII 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLslehGPIVVHCSAGIGRSGTFCLADTCLLLM 162
Cdd:cd14596    91 RIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGVLICVDVLLSLI 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 163 DKRkdpSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14596   167 EKD---LSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 6-196 6.49e-53

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: 170.07  E-value: 6.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDdtgLKLTLISEDVKSYYTVRQL 85
Cdd:cd14619    40 QEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWPLDYTPCTYGH---LRVTVVSEEVMENWTVREF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKR 165
Cdd:cd14619   117 LLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSE 196

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907136856 166 KdpsSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14619   197 G---LLGPFSFVQKMRENRPLMVQTESQYVF 224
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 6-203 9.58e-53

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: 168.97  E-value: 9.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVfddTGLKLTLISEDVKSYYTVRQL 85
Cdd:cd14601    19 NRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSY---GGFQVTCHSEEGNPAYVFREM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEhgPIVVHCSAGIGRSGTFCLADTCLLLMDKR 165
Cdd:cd14601    96 TLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIGRTGVLITMETAMCLIECN 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907136856 166 KDPSSVDIKKVlleMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14601   174 QPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 5-199 1.39e-51

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: 166.63  E-value: 1.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKeMVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14617    39 RREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGD--LIVQMLSESVLPEWTIRE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LEL---ENLTTKetREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd14617   116 FKIcseEQLDAP--RLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQ 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907136856 162 MDkRKDpsSVDIKKVLLEMRRFRMGLIQTADQlrFSYL 199
Cdd:cd14617   194 LD-SKD--SVDIYGAVHDLRLHRVHMVQTECQ--YVYL 226
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 7-198 5.73e-51

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 164.09  E-value: 5.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQLE 86
Cdd:cd14539    16 RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGA--ITVSLQSVRTTPTHVERIIS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSL-EHGPIVVHCSAGIGRSGTFCLADTCLLLMdkR 165
Cdd:cd14539    94 IQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRsLQTPIVVHCSSGVGRTGAFCLLYAAVQEI--E 171

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907136856 166 KDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd14539   172 AGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 5-201 1.72e-50

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: 164.42  E-value: 1.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQqeekEMVFDDTG-LKLTLISEDVKSYYTVR 83
Cdd:cd14605    53 KKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPD----EYALKEYGvMRVRNVKESAAHDYILR 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENLTTKET-REILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLM 162
Cdd:cd14605   129 ELKLSKVGQGNTeRTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDII 208

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 163 DKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:cd14605   209 REKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 5-205 2.04e-50

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: 164.82  E-value: 2.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQ--EEKEMVfddtglKLTLISEDVKSYYTV 82
Cdd:cd14626    83 QNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRgtETYGMI------QVTLLDTVELATYSV 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTcllLM 162
Cdd:cd14626   157 RTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACN--PPDAGPMVVHCSAGVGRTGCFIVIDA---ML 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907136856 163 DKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGA 205
Cdd:cd14626   232 ERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 5-204 2.60e-50

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: 164.88  E-value: 2.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFddtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14625    89 QNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGM----IQVTLLDTIELATFCVRT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTcllLMDK 164
Cdd:cd14625   165 FSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCN--PPDAGPIVVHCSAGVGRTGCFIVIDA---MLER 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEG 204
Cdd:cd14625   240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEA 279
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 3-208 4.14e-50

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: 163.90  E-value: 4.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVfddTGLKLTLISEDVKSYYTV 82
Cdd:cd14606    64 ENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAY---GPYSVTNCGEHDTTEYKL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENLTTKET-REILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd14606   141 RTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMEN 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907136856 162 MDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAViegAKFI 208
Cdd:cd14606   221 ISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAI---AQFI 264
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 6-198 2.08e-49

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: 159.90  E-value: 2.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSY-YTVRQ 84
Cdd:cd14542    14 KAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGP--FKISLEKEKRVGPdFLIRT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELEnlTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVR---ESGSLslehgPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd14542    92 LKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRdyqGSEDV-----PICVHCSAGCGRTGTICAIDYVWNL 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907136856 162 MDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd14542   165 LKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 8-196 4.15e-49

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: 160.07  E-value: 4.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14616    42 FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPEDNKPVTVFGD--IVITKLMEDVQIDWTIRDLKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENltTKETREILHFHYTTWPDFGVPESPASFLNFLFKVResGSLSLEHGPIVVHCSAGIGRSGTFCLADTcllLMDKRKD 167
Cdd:cd14616   120 ER--HGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR--ASRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHIND 192

                         170       180
                  ....*....|....*....|....*....
gi 1907136856 168 PSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14616   193 HDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 4-199 1.00e-48

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: 159.62  E-value: 1.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   4 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSlKCAQYWPQQEEkemvfddTGLKLTLISEDVKSY--YT 81
Cdd:cd14612    58 KEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEKKE-KCVHYWPEKEG-------TYGRFEIRVQDMKECdgYT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  82 VRQLELEnlTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADT-CLL 160
Cdd:cd14612   130 IRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQ 207

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 161 LmdkrKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYL 199
Cdd:cd14612   208 L----KDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 6-203 2.57e-48

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: 159.43  E-value: 2.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMvfddTGLKLTLISEDVKSYYTVRQL 85
Cdd:cd17667    72 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEY----GNIIVTLKSTKIHACYTVRRF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKE-----------TREILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSLEH-GPIVVHCSAGIGRSGTFC 153
Cdd:cd17667   148 SIRNTKVKKgqkgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARTPEmGPVLVHCSAGVGRTGTYI 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907136856 154 LADTcllLMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd17667   225 VIDS---MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 5-202 7.02e-48

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: 156.29  E-value: 7.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMvfddTGLKLTLISEDVKSYYTVRQ 84
Cdd:cd17668    13 PKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEY----GNFLVTQKSVQVLAYYTVRN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKE--------TREILHFHYTTWPDFGVPESPASFLNFLFKvrESGSLSLEHGPIVVHCSAGIGRSGTFCLAD 156
Cdd:cd17668    89 FTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK--ASYAKRHAVGPVVVHCSAGVGRTGTYIVLD 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907136856 157 TcllLMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVI 202
Cdd:cd17668   167 S---MLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 4-198 8.21e-48

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: 156.01  E-value: 8.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   4 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqqeEKEMVFDDTGLKLTliSEDVKSYYTVR 83
Cdd:cd14558    12 GPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG---DEKKTYGDIEVELK--DTEKSPTYTVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRES-GSLSLEHG---PIVVHCSAGIGRSGTFCladtCL 159
Cdd:cd14558    87 VFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKlPYKNSKHGrsvPIVVHCSDGSSRTGIFC----AL 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 160 L-LMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd14558   163 WnLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 6-203 1.89e-47

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: 155.07  E-value: 1.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEkemVFDDtgLKLTLISEDVKSYYTVRQL 85
Cdd:cd14555    14 NHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGD--IKVTLVETEPLAEYVVRTF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLehGPIVVHCSAGIGRSGTFCLADTcllLMDKR 165
Cdd:cd14555    89 ALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA--GPIVVHCSAGAGRTGCYIVIDI---MLDMA 163

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907136856 166 KDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14555   164 EREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 5-204 5.38e-47

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: 156.43  E-value: 5.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFddtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14624    89 QNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL----IQVTLLDTVELATYCVRT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTcllLMDK 164
Cdd:cd14624   165 FALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCN--PPDAGPMVVHCSAGVGRTGCFIVIDA---MLER 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEG 204
Cdd:cd14624   240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 5-203 2.14e-46

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: 154.21  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMV--FDDTGLKLTLISEDVksyyTV 82
Cdd:cd14603    72 SRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTgpFTITLVKEKRLNEEV----IL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELEnlTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEhgPIVVHCSAGIGRSGTFCLADTCLLLM 162
Cdd:cd14603   148 RTLKVT--FQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVRQLL 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 163 DKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14603   224 LTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 4-196 7.25e-46

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: 152.35  E-value: 7.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   4 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTglkLTLISEDVKSYYTVR 83
Cdd:cd14614    53 SPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDIT---VEMLSEEEQPDWAIR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELEnlTTKETREILHFHYTTWPDFGVPESPA--SFLNFLFKVRESGSLSleHGPIVVHCSAGIGRSGTFCLADTcllL 161
Cdd:cd14614   130 EFRVS--YADEVQDVMHFNYTAWPDHGVPTANAaeSILQFVQMVRQQAVKS--KGPMIIHCSAGVGRTGTFIALDR---L 202

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907136856 162 MDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14614   203 LQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 7-203 1.35e-45

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: 152.90  E-value: 1.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqqeekemvfdDTGLKL------TLISEDVKSY- 79
Cdd:cd14610    89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP----------DEGSNLyhiyevNLVSEHIWCEd 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  80 YTVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSLEHGPIVVHCSAGIGRSGTFCLADTCL 159
Cdd:cd14610   159 FLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYILIDMVL 236

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907136856 160 LLMdkRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14610   237 NKM--AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 8-198 1.64e-45

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: 150.06  E-value: 1.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKemvfddTGLKLTLISEDVKSY--YTVRQL 85
Cdd:cd14551    16 FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW------TYGNLRVRVEDTVVLvdYTTRKF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ----ELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVResGSLSLEHGPIVVHCSAGIGRSGTFCLADTcllL 161
Cdd:cd14551    90 ciqkVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK--SANPPRAGPIVVHCSAGVGRTGTFIVIDA---M 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907136856 162 MDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd14551   165 LDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 6-204 4.48e-45

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: 150.18  E-value: 4.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEkemVFDDtgLKLTLISEDVKSYYTVRQL 85
Cdd:cd14630    46 RHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDDTE---VYGD--IKVTLIETEPLAEYVIRTF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTcllLMDKR 165
Cdd:cd14630   121 TVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLN--PPDAGPIVVHCSAGAGRTGCFIAIDI---MLDMA 195

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 166 KDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEG 204
Cdd:cd14630   196 ENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 5-200 7.94e-45

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: 149.60  E-value: 7.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFddtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14554    48 RGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILRE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCladTCLLLMDK 164
Cdd:cd14554   124 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFI---TLSIVLER 200

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLA 200
Cdd:cd14554   201 MRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 7-201 1.10e-44

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: 147.80  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqqEEKEMVFDDtgLKLTLISEDVKSYYTVRQLE 86
Cdd:cd14552    15 AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGD--ITVELKDQTDYEDYTLRDFL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHgPIVVHCSAGIGRSGTFCLADTCLllmDKRK 166
Cdd:cd14552    91 VTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVL---ERVK 166

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907136856 167 DPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:cd14552   167 AEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 5-196 1.46e-44

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: 148.55  E-value: 1.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKemvFDDTGLKLTLISEDVKSYYTVRQ 84
Cdd:cd14618    39 PQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYWPSESTP---VSYGHITVHLLAQSSEDEWTRRE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDK 164
Cdd:cd14618   116 FKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKE 195

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907136856 165 RKdpsSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14618   196 EK---VVDVFNTVYILRMHRYLMIQTLSQYIF 224
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 6-193 1.50e-44

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: 147.67  E-value: 1.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTliSEDVKSYYTVRQL 85
Cdd:cd14557    14 RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN--EEKICPDYIIRKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKET-REILHFHYTTWPDFGVPESPasflNFLFKVRES-GSLS-LEHGPIVVHCSAGIGRSGTFCLADTcllLM 162
Cdd:cd14557    92 NINNKKEKGSgREVTHIQFTSWPDHGVPEDP----HLLLKLRRRvNAFNnFFSGPIVVHCSAGVGRTGTYIGIDA---ML 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907136856 163 DKRKDPSSVDIKKVLLEMRRFRMGLIQTADQ 193
Cdd:cd14557   165 EGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQ 195
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 4-208 2.12e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 150.15  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   4 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDdtglKLTLISEDVKS--YYT 81
Cdd:PHA02742   91 AKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHG----EFKIKTKKIKSfrNYA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  82 VRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRE---------SGSLSLEHGPIVVHCSAGIGRSGTF 152
Cdd:PHA02742  167 VTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAF 246

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136856 153 CLADTCLLLMDKRkdpSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFI 208
Cdd:PHA02742  247 CAIDICISKYNER---AIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 8-204 5.59e-44

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: 146.35  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqqEEKEMVFDdtgLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14632    16 FIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGD---IKITLLKTETLAEYSVRTFAL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVResGSLSLEHGPIVVHCSAGIGRSGTFCLADtclLLMDKRKD 167
Cdd:cd14632    91 ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVK--ASTPPDAGPVVVHCSAGAGRTGCYIVLD---VMLDMAEC 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907136856 168 PSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEG 204
Cdd:cd14632   166 EGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 5-203 5.59e-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: 147.01  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEekemVFDDTGLKLTLISEDVKSYYTVRQ 84
Cdd:cd14620    37 KNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQYWPDQG----CWTYGNIRVAVEDCVVLVDYTIRK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTT---KETREILHFHYTTWPDFGVPESPASFLNFLFKVResgSLSLEH-GPIVVHCSAGIGRSGTFCLADTCLL 160
Cdd:cd14620   113 FCIQPQLPdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK---SVNPVHaGPIVVHCSAGVGRTGTFIVIDAMID 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907136856 161 LMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14620   190 MMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 8-204 2.55e-43

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: 145.16  E-value: 2.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEkemVFDDtgLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14631    30 YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE---VYGD--FKVTCVEMEPLAEYVVRTFTL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLehGPIVVHCSAGIGRSGTFCLADtclLLMDKRKD 167
Cdd:cd14631   105 ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA--GPIVVHCSAGAGRTGCYIVID---IMLDMAER 179

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907136856 168 PSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEG 204
Cdd:cd14631   180 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 5-203 2.82e-43

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: 145.19  E-value: 2.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQqeEKEMVFDDTGLKLTliSEDVKSYYTVRQ 84
Cdd:cd14623    38 KDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPS--DGSVSYGDITIELK--KEEECESYTVRD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHgPIVVHCSAGIGRSGTFCLADTCLllmDK 164
Cdd:cd14623   114 LLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVL---ER 189

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14623   190 VKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 7-198 8.77e-43

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: 143.37  E-value: 8.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSL-KCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSyYTVRQL 85
Cdd:cd17658    17 KFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTNKKLKHSQHS-ITLRVL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKET-REILHFHYTTWPDFGVPESPASFLNFLfkvRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDK 164
Cdd:cd17658    96 EVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELL---KRLYGIPPSAGPIVVHCSAGIGRTGAYCTIHNTIRRILE 172

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907136856 165 rKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd17658   173 -GDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 7-203 1.03e-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: 145.18  E-value: 1.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPqqEEKEMVFDDtgLKLTLISEDVKSY-YTVRQL 85
Cdd:cd14609    87 AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHI--YEVNLVSEHIWCEdFLVRSF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMdkR 165
Cdd:cd14609   163 YLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRM--A 238

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907136856 166 KDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14609   239 KGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 5-203 3.27e-42

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: 144.49  E-value: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFddtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14628    94 QKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILRE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCladTCLLLMDK 164
Cdd:cd14628   170 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFI---TLSIVLER 246

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14628   247 MRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 8-204 3.40e-42

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: 143.64  E-value: 3.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEkemVFDDtgLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14633    85 YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLehGPIVVHCSAGIGRSGTFCLADtclLLMDKRKD 167
Cdd:cd14633   160 EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNA--GPLVVHCSAGAGRTGCFIVID---IMLDMAER 234

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907136856 168 PSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEG 204
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 5-196 8.70e-42

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: 141.21  E-value: 8.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSlKCAQYWPqqeEKEMVFDdtGLKLTLISEDVKSYYTVRQ 84
Cdd:cd14611    43 EKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWP---EKRGIYG--KVEVLVNSVKECDNYTIRN 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENltTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFcLADT--CLLLm 162
Cdd:cd14611   117 LTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASPGRGPVVVHCSAGIGRTGCF-IATTigCQQL- 192

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907136856 163 dkrKDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14611   193 ---KEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
97-203 1.18e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   97 EILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKRKDpsSVDIKKV 176
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1907136856  177 LLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 97-203 1.18e-41

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   97 EILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKRKDpsSVDIKKV 176
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1907136856  177 LLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 8-201 1.33e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 143.63  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRImEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDvkSYYTVRQLEL 87
Cdd:PHA02746  115 FICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFVAKILDIIEE--LSFTKTRLMI 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLSLEHGPIVVHCSAGIGRSGTFCLADTCL 159
Cdd:PHA02746  192 TDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPIVVHCSAGIGRAGTFCAIDNAL 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907136856 160 LLMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:PHA02746  272 EQLEKEK---EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 6-203 2.00e-41

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: 140.75  E-value: 2.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWpqQEEKEMVFDDTGLKLTLISEDVKSYYTVRQL 85
Cdd:cd14602    41 RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYW--AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLttKETREILHFHYTTWPDFGVPESPASFLNFLFKVResgslSLEHG---PIVVHCSAGIGRSGTFCLADTCLLLM 162
Cdd:cd14602   119 KVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR-----CYQEDdsvPICIHCSAGCGRTGVICAIDYTWMLL 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 163 DKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14602   192 KDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 5-203 4.72e-41

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: 141.41  E-value: 4.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFddtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14627    95 QKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILRE 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCladTCLLLMDK 164
Cdd:cd14627   171 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFI---TLSIVLER 247

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14627   248 MRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 6-201 4.97e-41

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: 141.22  E-value: 4.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTVRQL 85
Cdd:cd14604   100 KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGP--FRISCEAEQARTDYFIRTL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELEnlTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKR 165
Cdd:cd14604   178 LLE--FQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAG 253

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907136856 166 KDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:cd14604   254 KIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 3-196 5.00e-40

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: 137.69  E-value: 5.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSlKCAQYWPqqeEKEMVFDdtGLKLTLISEDVKSYYTV 82
Cdd:cd14613    67 GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP---EEQVTYE--GIEITVKQVIHADDYRL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELEnlTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRES-GSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLL 161
Cdd:cd14613   141 RLITLK--SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEArQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQ 218

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907136856 162 MdkrKDPSSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:cd14613   219 L---RNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 8-203 1.04e-39

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: 137.82  E-value: 1.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd14599    84 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLSLEHGPIVVHCSAGIGRSGTFCLADTCL 159
Cdd:cd14599   164 KHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmLDSTKNCNPPIVVHCSAGVGRTGVVILTELMI 243

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907136856 160 LLMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14599   244 GCLEHNE---KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 5-203 1.60e-39

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: 137.16  E-value: 1.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFddtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14629    95 QKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILRE 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCladTCLLLMDK 164
Cdd:cd14629   171 FKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFI---TLSIVLER 247

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 165 RKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14629   248 MRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 3-214 1.80e-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: 137.46  E-value: 1.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEekemVFDDTGLKLTLISEDVKSYYTV 82
Cdd:cd14621    92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQG----CWTYGNIRVSVEDVTVLVDYTV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENL----TTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLehGPIVVHCSAGIGRSGTFCLADTC 158
Cdd:cd14621   168 RKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA--GAIVVHCSAGVGRTGTFIVIDAM 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136856 159 LLLMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEgaKFIMGDSSV 214
Cdd:cd14621   246 LDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE--HYLYGDTEL 296
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 7-203 1.89e-39

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: 135.10  E-value: 1.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYYTVRQLE 86
Cdd:cd14598    17 DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKV----RESGSLSLEHG---PIVVHCSAGIGRSGTFCLADTCL 159
Cdd:cd14598    97 IKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTIDPKSpnpPVLVHCSAGVGRTGVVILSEIMI 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907136856 160 LLMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14598   177 ACLEHNE---MLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PHA02738 PHA02738
hypothetical protein; Provisional
 3-201 3.13e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 131.97  E-value: 3.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDtgLKLTLISEDVKSYYTV 82
Cdd:PHA02738   87 EYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGK--FKITTTQVETHPHYVK 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENlTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRES-----------GSLSLEHGPIVVHCSAGIGRSGT 151
Cdd:PHA02738  165 STLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqiGHNRLQPPPIVVHCNAGLGRTPC 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907136856 152 FCLADTCLLLMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:PHA02738  244 YCVVDISISRFDACA---TVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 5-198 1.28e-36

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: 127.14  E-value: 1.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRiMEKGSLKCAQYWPqqEEKEMVFDDtgLKLTLISEDVKSYYTVRQ 84
Cdd:cd14556    13 PAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWP--DEGSGTYGP--IQVEFVSTTIDEDVISRI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  85 LELENLT--TKETREILHFHYTTWPDFG-VPESPASFLNFLFKV----RESGSlslehGPIVVHCSAGIGRSGTFCladT 157
Cdd:cd14556    88 FRLQNTTrpQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVekwqEQSGE-----GPIVVHCLNGVGRSGVFC---A 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 158 CLLLMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY 198
Cdd:cd14556   160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 5-201 2.62e-36

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: 126.66  E-value: 2.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSY-ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQqeEKEMVFDDTGLKLTliSEDVKSYYTVR 83
Cdd:cd14622    13 QKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIK--NDTLLETISIR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHgPIVVHCSAGIGRSGTFCLADTcllLMD 163
Cdd:cd14622    89 DFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH-PIVVHCSAGAGRTGTFIALSN---ILE 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907136856 164 KRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAV 201
Cdd:cd14622   165 RVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 3-196 1.33e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 125.11  E-value: 1.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   3 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIME-KGSLKCAQYWPQQEEKEMvfDDTGLKLTLISEDVKSYYT 81
Cdd:PHA02747   90 EDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNI--DMEDFRIETLKTSVRAKYI 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  82 VRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKV----RESGSLSLEH----GPIVVHCSAGIGRSGTFC 153
Cdd:PHA02747  168 LTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFC 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907136856 154 LADTCLLLMDKRKdpsSVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:PHA02747  248 AVDICLNQLVKRK---AICLAKTAEKIREQRHAGIMNFDDYLF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
6-194 2.68e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 118.27  E-value: 2.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   6 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRIMEKGSLKCAQYWPQQEEKEmvfddtglKLTLISEDVKSYYTVR 83
Cdd:COG5599    77 HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLasDDEISKPKVKMPVYFRQDGEYG--------KYEVSSELTESIQLRD 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  84 QLELENL------TTKETREILHFHYTTWPDFGVPESPAsFLNFLFKVRESGSLSLEH-GPIVVHCSAGIGRSGTFcLAD 156
Cdd:COG5599   149 GIEARTYvltikgTGQKKIEIPVLHVKNWPDHGAISAEA-LKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTL-IAC 226

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907136856 157 TCLLLMDKRKDPSSVDIKKVLLEMRRFR-MGLIQTADQL 194
Cdd:COG5599   227 LALSKSINALVQITLSVEEIVIDMRTSRnGGMVQTSEQL 265
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 5-198 3.31e-29

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: 107.79  E-value: 3.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGslKCAQYWPqQEEKEMVFDdtGLKLTLISEDVKSY----- 79
Cdd:cd14550    13 SNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWP-TKEKPLECE--TFKVTLSGEDHSCLsneir 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  80 YTVRQLELENltTKETR--EILHFHYTTWPDfgvPESPAS-FLNFLFKVRESGSLSleHGPIVVHCSAGIGRSGTFCLAD 156
Cdd:cd14550    88 LIVRDFILES--TQDDYvlEVRQFQCPSWPN---PCSPIHtVFELINTVQEWAQQR--DGPIVVHDRYGGVQAATFCALT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907136856 157 TcllLMDKRKDPSSVDIKKV--LLEMRrfRMGLIQTADQLRFSY 198
Cdd:cd14550   161 T---LHQQLEHESSVDVYQVakLYHLM--RPGVFTSKEDYQFLY 199
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 7-203 4.22e-25

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: 97.67  E-value: 4.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSL-KCAQYWPQ---QEEKEMvfddtglKLTLISEDVKSYYTV 82
Cdd:cd14637    15 AFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEpglQQYGPM-------EVEFVSGSADEDIVT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 RQLELENLTTKETREIL--HFHYTTWPDF-GVPESPASFLNFLFKV----RESGSlslehGPIVVHCSAGIGRSGTFCla 155
Cdd:cd14637    88 RLFRVQNITRLQEGHLMvrHFQFLRWSAYrDTPDSKKAFLHLLASVekwqRESGE-----GRTVVHCLNGGGRSGTYC-- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907136856 156 dTCLLLMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14637   161 -ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 7-203 3.78e-24

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: 95.09  E-value: 3.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRiMEKGSLkCAQYWPqqEEKEMVFDDtgLKLTLISEDVKSYYTVRQLE 86
Cdd:cd14634    15 AFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWP--EKTSCCYGP--IQVEFVSADIDEDIISRIFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LENLTTKET--REILHFHYTTWPDF-GVPESPASFLNFLFKVRE-SGSLSLEHGPIVVHCSAGIGRSGTFC-LADTCLLL 161
Cdd:cd14634    89 ICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKwQEQYDGREGRTVVHCLNGGGRSGTFCaICSVCEMI 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907136856 162 MDKrkdpSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14634   169 QQQ----NIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 5-209 8.58e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 93.49  E-value: 8.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   5 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKgslKC-AQYWPQQEEKEMVFDDTGLK-LTLIsedVKSYYTv 82
Cdd:PHA02740   90 EQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCVITSDKFQIEtLEII---IKPHFN- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  83 rqLELENLTTK--ETREILHFHYTTWPDFGVPESPASFLNFLFKVrESGSLSLEH-------GPIVVHCSAGIGRSGTFC 153
Cdd:PHA02740  163 --LTLLSLTDKfgQAQKISHFQYTAWPADGFSHDPDAFIDFFCNI-DDLCADLEKhkadgkiAPIIIDCIDGISSSAVFC 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907136856 154 LADTCLLLMDKrkdPSSVDIKKVLLEMRRFRMGLIQTADQLRFSY--LAVIEGAKFIM 209
Cdd:PHA02740  240 VFDICATEFDK---TGMLSIANALKKVRQKKYGCMNCLDDYVFCYhlIAAYLKEKFDI 294
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 8-202 4.03e-22

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: 89.67  E-value: 4.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAqYWPQQEEKeMVFDdtGLKLTLISEDVKSYYTVRQLEL 87
Cdd:cd17669    16 FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEP-INCE--TFKVTLIAEEHKCLSNEEKLII 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  88 ENLTTKETR-----EILHFHYTTWPDfgvPESPAS-FLNFLFKVRESGslSLEHGPIVVHCSAGIGRSGTFCLADTcllL 161
Cdd:cd17669    92 QDFILEATQddyvlEVRHFQCPKWPN---PDSPISkTFELISIIKEEA--ANRDGPMIVHDEHGGVTAGTFCALTT---L 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907136856 162 MDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVI 202
Cdd:cd17669   164 MHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 7-203 4.32e-21

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: 87.05  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRImEKGSLkCAQYWPQQEekemVFDDTGLKLTLISEDVKSYYTVRQLE 86
Cdd:cd14635    15 AFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQL-CPQYWPENG----VHRHGPIQVEFVSADLEEDIISRIFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LENLTTKET--REILHFHYTTWPDFgvPESPASFLNFLFKVRESGSLSLEH----GPIVVHCSAGIGRSGTFC-LADTCL 159
Cdd:cd14635    89 IYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEYnggeGRTVVHCLNGGGRSGTFCaISIVCE 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907136856 160 LLMDKRkdpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14635   167 MLRHQR----AVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 8-202 4.98e-21

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: 86.66  E-value: 4.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   8 YILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRIMEKGSLkcaQYWPQQEEKemvFDDTGLKLTLISEDVKSYYTVRQL 85
Cdd:cd17670    16 FIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQGLAEDEF---VYWPSREES---MNCEAFTVTLISKDRLCLSNEEQI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETR-----EILHFHYTTWPDfgvPESPASFLNFLFKVRESGSLSLEhGPIVVHCSAGIGRSGTFCLADTcll 160
Cdd:cd17670    90 IIHDFILEATQddyvlEVRHFQCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEFGAVSAGTLCALTT--- 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907136856 161 LMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVI 202
Cdd:cd17670   163 LSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 7-203 1.22e-20

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: 85.85  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   7 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRI-MEKGslkCAQYWPqqEEKEMVFDDTGLKLTLISEDVKsyYTVRQL 85
Cdd:cd14636    15 AFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP--EEGMLRYGPIQVECMSCSMDCD--VISRIF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  86 ELENLTTKETREIL--HFHYTTWPDF-GVPESPASFLNFLFKVRESGSLSLE-HGPIVVHCSAGIGRSGTFClADTCLLL 161
Cdd:cd14636    88 RICNLTRPQEGYLMvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGGRSGMFC-AISIVCE 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907136856 162 MDKRKDpsSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIE 203
Cdd:cd14636   167 MIKRQN--VVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
71-196 2.29e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 59.21  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  71 LISEDVKSYYTVRQLELENLTTKETREILHFHYTtWPDFGVPEsPASFLNFLFKVREsgsLSLEHGPIVVHCSAGIGRSG 150
Cdd:COG2453    21 LKREGIDAVVSLTEEEELLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTG 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907136856 151 TFCLadtCLLLMDKrkdpssVDIKKVLLEMRRFRMGLIQTADQLRF 196
Cdd:COG2453    96 TVAA---AYLVLLG------LSAEEALARVRAARPGAVETPAQRAF 132
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 69-196 1.67e-10

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: 57.66  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  69 LTLISEDVKSYYTVRQLelenLTTKETREILHFHYTTwPDFGVPESPASFLNFLFKVRESgslsLEHGP-IVVHCSAGIG 147
Cdd:cd14505    48 VTLCTDGELEELGVPDL----LEQYQQAGITWHHLPI-PDGGVPSDIAQWQELLEELLSA----LENGKkVLIHCKGGLG 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907136856 148 RSGTFCladTCLLLMDKRKDPSSVDIKKVllemRRFRMGLIQTADQLRF 196
Cdd:cd14505   119 RTGLIA---ACLLLELGDTLDPEQAIAAV----RALRPGAIQTPKQENF 160
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 107-196 9.46e-10

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: 54.98  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856 107 PDFGVP--ESPASFLNFLFKVRESGslslehGPIVVHCSAGIGRSGTFcLAdtCLLLMdKRKDPSSVDIKKVllemRRFR 184
Cdd:cd14504    58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTM-LA--CYLVK-TGKISAVDAINEI----RRIR 123

                          90
                  ....*....|..
gi 1907136856 185 MGLIQTADQLRF 196
Cdd:cd14504   124 PGSIETSEQEKF 135
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 9-194 1.99e-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: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856   9 ILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRIMEKGSLKcaQYWPQqeekemvfDDTGLKLTLISEDVKSYYTVRQLE 86
Cdd:cd14559    32 IACQYPKNEQLEDHLKMLADNRTPCLVVLasNKDIQRKGLP--PYFRQ--------SGTYGSVTVKSKKTGKDELVDGLK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  87 LE--NLTTKE---TREILHFHYTTWPDFG-------------VPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGR 148
Cdd:cd14559   102 ADmyNLKITDgnkTITIPVVHVTNWPDHTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907136856 149 SGTFcLADTCLLlmdkrKDPSSVDIKKVLLEMRRFRMG-LIQTADQL 194
Cdd:cd14559   182 TGQL-AAAMELN-----KSPNNLSVEDIVSDMRTSRNGkMVQKDEQL 222
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 136-196 5.52e-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: 46.57  E-value: 5.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136856 136 GPIVVHCSAGIGRSGTFCladTCLLLMDKRKDPssvdiKKVLLEMRRFR-MGLIQTADQLRF 196
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLV---ACYLVLLGGMSA-----EEAVRIVRLIRpGGIPQTIEQLDF 110
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 101-196 4.20e-06

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: 45.80  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856 101 FHYTTWPDFGVPeSPASFLNFlfkVRESGSLSLEHGPIVVHCSAGIGRSGtfcLADTCLLLMDKRKDPSSVdIKKVllem 180
Cdd:cd14506    79 FYNFGWKDYGVP-SLTTILDI---VKVMAFALQEGGKVAVHCHAGLGRTG---VLIACYLVYALRMSADQA-IRLV---- 146

                          90
                  ....*....|....*.
gi 1907136856 181 RRFRMGLIQTADQLRF 196
Cdd:cd14506   147 RSKRPNSIQTRGQVLC 162
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 89-198 6.95e-06

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: 44.49  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136856  89 NLTTKETREILHFHyTTWPDFGVPESPASFLNFLFK-VRESGS-LSL-EHGPIVVHCSAGIGRSGTFCladTCLLLMDKR 165
Cdd:cd14497    47 NLSEEEYDDDSKFE-GRVLHYGFPDHHPPPLGLLLEiVDDIDSwLSEdPNNVAVVHCKAGKGRTGTVI---CAYLLYYGQ 122

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907136856 166 KdpSSVDIKKVLLEMRRFRMGL--IQTADQLRFSY 198
Cdd:cd14497   123 Y--STADEALEYFAKKRFKEGLpgVTIPSQLRYLQ 155
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 120-166 3.89e-05

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 41.86  E-value: 3.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907136856 120 NFLFKVRESGslslehGPIVVHCSAGIGRSGTFCLAdtclLLMDKRK 166
Cdd:pfam00782  60 EFIDDARQKG------GKVLVHCQAGISRSATLIIA----YLMKTRN 96
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
134-185 4.33e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.88  E-value: 4.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907136856  134 EHGPIVVHCSAGIGRSGTFCLAdtclLLMDKRKDPSSVDIKkvLLEMRRFRM 185
Cdd:smart00195  77 KGGKVLVHCQAGVSRSATLIIA----YLMKTRNMSLNDAYD--FVKDRRPII 122
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 100-155 7.03e-05

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 41.22  E-value: 7.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907136856 100 HFHYTTWP--DFGVPESPASF---LNFLFKVRESGslslehGPIVVHCSAGIGRSGTFCLA 155
Cdd:cd14565    44 HFQYKSIPveDSHNADISSWFeeaIGFIDKVKASG------GRVLVHCQAGISRSATICLA 98
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 100-155 7.57e-05

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 41.39  E-value: 7.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136856 100 HFHYTTWPDFGVPESPASfLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLA 155
Cdd:cd14572    51 QFEYVKVPLADMPHAPIS-LYFDSVADKIHSVGRKHGATLVHCAAGVSRSATLCIA 105
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 134-166 4.16e-04

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 39.07  E-value: 4.16e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907136856 134 EHGPIVVHCSAGIGRSGTFCLAdtclLLMDKRK 166
Cdd:cd14498    78 KGGKVLVHCQAGVSRSATIVIA----YLMKKYG 106
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 130-155 1.35e-03

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 37.53  E-value: 1.35e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907136856 130 SLSLEHGPIVVHCSAGIGRSGTFCLA 155
Cdd:cd14514    72 QVKRRGGRTLVHCVAGVSRSATLCLA 97
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 130-165 2.06e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 37.32  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907136856 130 SLSLEHGPIVVHCSAGIGRSGTFCLAdtcLLLMDKR 165
Cdd:cd14640    73 SVKDCNGRVLVHCQAGISRSATICLA---YLMMKKR 105
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 119-155 4.19e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350489 [Multi-domain]  Cd Length: 144  Bit Score: 36.38  E-value: 4.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907136856 119 LNFLFKVRESGslslehGPIVVHCSAGIGRSGTFCLA 155
Cdd:cd14641    71 IDFIDSVKNSG------GRVLVHCQAGISRSATICLA 101
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 119-166 4.66e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 36.05  E-value: 4.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907136856 119 LNFLFKVRESGslslehGPIVVHCSAGIGRSGTFCLAdtclLLMDKRK 166
Cdd:cd14639    68 IDFIDCVRRAG------GKVLVHCEAGISRSPTICMA----YLMKTKR 105
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 119-155 9.86e-03

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 35.09  E-value: 9.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907136856 119 LNFLFKVRESGslslehGPIVVHCSAGIGRSGTFCLA 155
Cdd:cd14568    69 VEFIEKARASN------KRVLVHCLAGISRSATIAIA 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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