NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217276606|ref|XP_047280966|]
View 

tyrosine-protein phosphatase non-receptor type 20 isoform X10 [Homo sapiens]

Protein Classification

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 ...
 127-261 1.72e-75

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 cd14596:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 207  Bit Score: 228.48  E-value: 1.72e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 NYQILQYFIIRMFQVVEK-------------------------------------------------------------- 224
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKetgenrlikhlqfttwpdhgtpqssdqlvkficymrkvhntgpivvhcsagigragvlicvd 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217276606 225 ----------SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 261
Cdd:cd14596   161 vllsliekdlSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PHA02742 super family cl31501
protein tyrosine phosphatase; Provisional
 63-188 1.64e-19

protein tyrosine phosphatase; Provisional


The actual alignment was detected with superfamily member PHA02742:

Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 85.82  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  63 KDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNCG 139
Cdd:PHA02742   13 KNCEQLIEESNLAEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVDGHNAK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217276606 140 EEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYW 188
Cdd:PHA02742   93 GRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW 139
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 127-261 1.72e-75

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: 228.48  E-value: 1.72e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 NYQILQYFIIRMFQVVEK-------------------------------------------------------------- 224
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKetgenrlikhlqfttwpdhgtpqssdqlvkficymrkvhntgpivvhcsagigragvlicvd 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217276606 225 ----------SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 261
Cdd:cd14596   161 vllsliekdlSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
78-258 1.05e-64

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 202.89  E-value: 1.05e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606   78 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLL 152
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  153 STIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVV---------- 222
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTntgcsetrtv 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  223 ----------------------------------------------------------------EKSFNIMDIVAQMREQ 238
Cdd:smart00194 160 thyhytnwpdhgvpespesildliravrksqststgpivvhcsagvgrtgtfiaidillqqleaGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 2217276606  239 RSGMVQTKEQYHFCYDIVLE 258
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
102-258 2.79e-59

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 187.83  E-value: 2.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 178
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 179 GGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVV----------------------------------- 222
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSnggseetrtvkhfhytgwpdhgvpespnslldllr 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217276606 223 ----------------------------------------EKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:pfam00102 159 kvrkssldgrsgpivvhcsagigrtgtfiaidialqqleaEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
98-265 2.09e-22

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 93.23  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  98 NQPSNREKNRYRDILPYDSTRVplGKSKDYINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 177
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 178 EGG--IIKCYHYWPIS-----------LKKPLELK---HFRVFL-------ENYQILQYFIIR---------------MF 219
Cdd:COG5599   113 EISkpKVKMPVYFRQDgeygkyevsseLTESIQLRdgiEARTYVltikgtgQKKIEIPVLHVKnwpdhgaisaealknLA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 220 QVVEKS------------------------------------------FNIMDIVAQMREQR-SGMVQTKEQYHFCYDIV 256
Cdd:COG5599   193 DLIDKKekikdpdkllpvvhcragvgrtgtliaclalsksinalvqitLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLA 272


                  ....*....
gi 2217276606 257 LEVLRKLLT 265
Cdd:COG5599   273 EQQIRPLLR 281
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 78-227 2.28e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 88.52  E-value: 2.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  78 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLS 153
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 154 TIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSFN 227
Cdd:PHA02747  105 TCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK 179
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 63-188 1.64e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 85.82  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  63 KDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNCG 139
Cdd:PHA02742   13 KNCEQLIEESNLAEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVDGHNAK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217276606 140 EEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYW 188
Cdd:PHA02742   93 GRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW 139
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 127-261 1.72e-75

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: 228.48  E-value: 1.72e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 NYQILQYFIIRMFQVVEK-------------------------------------------------------------- 224
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKetgenrlikhlqfttwpdhgtpqssdqlvkficymrkvhntgpivvhcsagigragvlicvd 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217276606 225 ----------SFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 261
Cdd:cd14596   161 vllsliekdlSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 127-260 3.31e-71

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: 217.63  E-value: 3.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL-ELKHFRVFL 205
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 206 ENYQILQYFIIRMFQVVEKS------------------------------------------------------------ 225
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKEtgevhhithlnfttwpdhgtpqsadpllrfirymrrihnsgpivvhcsagigrtgvliti 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217276606 226 ------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 260
Cdd:cd14538   161 dvalglierdlpFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
78-258 1.05e-64

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 202.89  E-value: 1.05e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606   78 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLL 152
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  153 STIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVV---------- 222
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTntgcsetrtv 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  223 ----------------------------------------------------------------EKSFNIMDIVAQMREQ 238
Cdd:smart00194 160 thyhytnwpdhgvpespesildliravrksqststgpivvhcsagvgrtgtfiaidillqqleaGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 2217276606  239 RSGMVQTKEQYHFCYDIVLE 258
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
102-258 2.79e-59

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 187.83  E-value: 2.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 178
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 179 GGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVV----------------------------------- 222
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSnggseetrtvkhfhytgwpdhgvpespnslldllr 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217276606 223 ----------------------------------------EKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:pfam00102 159 kvrkssldgrsgpivvhcsagigrtgtfiaidialqqleaEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 102-260 4.76e-56

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


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 179.64  E-value: 4.76e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRVPLGKSKDYINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 182 IKCYHYWPISLKKPLEL-KHFRVFLENYQILQYFIIRMFQV--------------------------------------- 221
Cdd:cd14597    83 IKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELediqtrevrhithlnftawpdhdtpsqpeqlltfisymr 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217276606 222 -VEKS--------------------------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 260
Cdd:cd14597   163 hIHKSgpiithcsagigrsgtlicidvvlgliskdldFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 127-254 2.14e-41

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: 140.88  E-value: 2.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd00047     1 YINASYIDGYRGPKEY--IATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 NYQILQYFIIRMFQVV---------------------------------------------------------------- 222
Cdd:cd00047    79 SEEELSDYTIRTLELSpkgcsesrevthlhytgwpdhgvpsspedllalvrrvrkearkpngpivvhcsagvgrtgtfia 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217276606 223 ----------EKSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 254
Cdd:cd00047   159 idillerleaEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 78-253 2.84e-38

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: 135.18  E-value: 2.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  78 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIrivncgEEY----FYIATQ 148
Cdd:cd14543     5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdeRTDYINANFM------DGYkqknAYIATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 149 GPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQV------- 221
Cdd:cd14543    79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhntetde 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 222 ----------------VEKS------------------------------------------------------------ 225
Cdd:cd14543   159 srqvthfqftswpdfgVPSSaaalldflgevrqqqalavkamgdrwkghppgppivvhcsagigrtgtfctldiclsqle 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2217276606 226 ----FNIMDIVAQMREQRSGMVQTKEQYHFCY 253
Cdd:cd14543   239 dvgtLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 67-189 1.23e-35

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: 128.58  E-value: 1.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  67 KILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSKD----YINASYIRIVNCGEEY 142
Cdd:cd14599     3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKEnntgYINASHIKVTVGGEEW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217276606 143 FYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 189
Cdd:cd14599    83 HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWP 129
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 95-259 2.46e-35

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: 127.25  E-value: 2.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  95 NSGNQPSNREKNRYRDILPYDSTRVPL------GKSkDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSN 168
Cdd:cd14603    23 VAGGRKENVKKNRYKDILPYDQTRVILsllqeeGHS-DYINANFIKGVD--GSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 169 VIAMITREIEGGIIKCYHYWPiSLKKPLELKHF----------------RVFLENYQI-------LQYF----------- 214
Cdd:cd14603   100 VILMACREIEMGKKKCERYWA-QEQEPLQTGPFtitlvkekrlneevilRTLKVTFQKesrsvshFQYMawpdhgipdsp 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 215 --IIRMFQVVEK----------------------------------------SFNIMDIVAQMREQRSGMVQTKEQYHFC 252
Cdd:cd14603   179 dcMLAMIELARRlqgsgpeplcvhcsagcgrtgvictvdyvrqllltqrippDFSIFDVVLEMRKQRPAAVQTEEQYEFL 258


                  ....*..
gi 2217276606 253 YDIVLEV 259
Cdd:cd14603   259 YHTVAQM 265
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 107-221 2.03e-34

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: 123.62  E-value: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 107 RYRDILPYDSTRVPLGKS-----KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14548     1 RYTNILPYDHSRVKLIPIneeegSDYINANYIPGYNSPREF--IATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217276606 182 IKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQV 221
Cdd:cd14548    79 VKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKL 117
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 98-251 5.65e-33

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: 120.32  E-value: 5.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  98 NQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivncGEEY--FYIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd14554     2 NLPCNKFKNRLVNILPYESTRVCLQpirgvEGSDYINASFID----GYRQrgAYIATQGPLAETTEDFWRMLWEHNSTII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 171 AMITREIEGGIIKCYHYWPislkkplelkhfrvfLENYQILQYFII------RMFQVVEKSFNIMDIvaqmreqRSGMVQ 244
Cdd:cd14554    78 VMLTKLREMGREKCHQYWP---------------AERSARYQYFVVdpmaeyNMPQYILREFKVTDA-------RDGQSR 135


                  ....*..
gi 2217276606 245 TKEQYHF 251
Cdd:cd14554   136 TVRQFQF 142
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 105-253 7.39e-33

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: 119.80  E-value: 7.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 105 KNRYRDILPYDSTRVPL---GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVklkQGDNDYINASLVEVEEAKRSY--ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217276606 182 IKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSFNimdivaqmreqrsgmvQTKEQYHFCY 253
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQ----------------ETREVLHFHY 136
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 99-262 1.10e-32

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: 120.73  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  99 QPSNREKNRYRDILPYDSTRVPLGKSKDYINASYIRI----VNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMIT 174
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMeipsANIVNKY--IATQGPLPHTCAQFWQVVWEQKLSLIVMLT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 175 REIEGGIIKCYHYWPiSLKKPLELKHFRVFL--ENYQI----------------------LQY----------------- 213
Cdd:cd14600   115 TLTERGRTKCHQYWP-DPPDVMEYGGFRVQChsEDCTIayvfremlltntqtgeertvthLQYvawpdhgvpddssdfle 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 214 FIIRMFQ--------VVEKSFNI------------------------MDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 261
Cdd:cd14600   194 FVNYVRSkrvenepvLVHCSAGIgrtgvlvtmetamclternqpvypLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYE 273


                  .
gi 2217276606 262 K 262
Cdd:cd14600   274 E 274
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 106-251 1.68e-32

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: 118.65  E-value: 1.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 106 NRYRDILPYDSTRVPLGKSKD-----YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIRGYD-GEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 181 iIKCYHYWPI----------------------SLKKpLELKHF--RVFLENY---------------QILQY-------- 213
Cdd:cd14547    80 -EKCAQYWPEeenetygdfevtvqsvketdgyTVRK-LTLKYGgeKRYLKHYwytswpdhktpeaaqPLLSLvqeveear 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217276606 214 ----------------------FI---IRMFQVVEKSF-NIMDIVAQMREQRSGMVQTKEQYHF 251
Cdd:cd14547   158 qtephrgpivvhcsagigrtgcFIatsIGCQQLREEGVvDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 102-253 1.86e-32

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: 119.49  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRVPLG------KSKDYINASYIRIVNCGEEYF-----YIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKdrdpnvPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 171 AMITREIEGGIIKCYHYWPISLKKPlELKHFRVFLENYQILQYFIIRMFQVV---------------------------- 222
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVSkldqgdpireiwhyqylswpdhgvpsdp 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 223 -------------EKSFN------------------------IMDIVA--------------QM-REQRSGMVQTKEQYH 250
Cdd:cd14544   160 ggvlnfledvnqrQESLPhagpivvhcsagigrtgtfividmLLDQIKrkgldcdidiqktiQMvRSQRSGMVQTEAQYK 239


                  ...
gi 2217276606 251 FCY 253
Cdd:cd14544   240 FIY 242
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 127-254 2.09e-32

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: 118.12  E-value: 2.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FL 205
Cdd:cd18533     1 YINASYI-TLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 206 ENYQI-LQYFIIRMFQV--------------------------------------------------------------- 221
Cdd:cd18533    79 SEEENdDGGFIVREFELskedgkvkkvyhiqykswpdfgvpdspedlltliklkrelndsasldppiivhcsagvgrtgt 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217276606 222 --------------------VEKSF-NIMDIVAQMREQRSGMVQTKEQYHFCYD 254
Cdd:cd18533   159 fialdslldelkrglsdsqdLEDSEdPVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 102-258 3.08e-30

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: 113.26  E-value: 3.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRVPLGKSK-----DYINASYI---RIVNCgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMI 173
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgvpgsDYINANYCdgyRKQNA-----YIATQGPLPETFGDFWRMVWEQRSATIVMM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 174 TREIEGGIIKCYHYWP-----------ISLKKPLELKHF--RVFL-------ENYQILQY-------------------F 214
Cdd:cd14553    78 TKLEERSRVKCDQYWPtrgtetygliqVTLLDTVELATYtvRTFAlhkngssEKREVRQFqftawpdhgvpehptpflaF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217276606 215 IIRM------------------------FQVV---------EKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14553   158 LRRVkacnppdagpivvhcsagvgrtgcFIVIdsmlerikhEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 106-224 4.04e-30

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: 112.67  E-value: 4.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 106 NRYRDILPYDSTRVPLGKSK-----DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHeepgsDYINANYMPGYWSSQEF--IATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217276606 181 IIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEK 224
Cdd:cd14619    79 RVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQV 121
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 95-264 6.75e-30

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: 113.87  E-value: 6.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  95 NSGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNV 169
Cdd:cd14604    50 ATGEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKGVYGPKAY--IATQGPLANTVIDFWRMIWEYNVAI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 170 IAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQI-LQYFI--------------------------------- 215
Cdd:cd14604   128 IVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQArTDYFIrtlllefqnetrrlyqfhyvnwpdhdvpssfds 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 216 -------IRMFQ----------------------------------VVEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 254
Cdd:cd14604   208 ildmislMRKYQehedvpicihcsagcgrtgaicaidytwnllkagKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 287

                         250
                  ....*....|
gi 2217276606 255 IVLEVLRKLL 264
Cdd:cd14604   288 AIAQLFEKQL 297
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 106-221 1.86e-29

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: 110.78  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 106 NRYRDILPYDSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNvdddpCSDYINASYIPGNNFRREY--IATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2217276606 181 IIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQV 221
Cdd:cd14617    79 RVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKI 118
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 96-257 4.83e-29

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: 110.36  E-value: 4.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  96 SGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd14614     6 AADLPVNRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANYIPGYNSPQEY--IATQGPLPETRNDFWKMVLQQKSQII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 171 AMITREIEGGIIKCYHYWPISlKKPLE------------------LKHFRVFLE---------NY--------------- 208
Cdd:cd14614    84 VMLTQCNEKRRVKCDHYWPFT-EEPVAygditvemlseeeqpdwaIREFRVSYAdevqdvmhfNYtawpdhgvptanaae 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 209 QILQYF-IIR------------------------------MFQVVEKSF-NIMDIVAQMREQRSGMVQTKEQYHFCYDIV 256
Cdd:cd14614   163 SILQFVqMVRqqavkskgpmiihcsagvgrtgtfialdrlLQHIRDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                  .
gi 2217276606 257 L 257
Cdd:cd14614   243 Q 243
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 102-253 1.33e-28

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: 109.34  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRV------PLGKSKDYINASYI------RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNV 169
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVvlhdgdPNEPVSDYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 170 IAMITREIEGGIIKCYHYWP--ISLKK------------PL------ELK----------------HFRV---------- 203
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPdeYALKEygvmrvrnvkesAAhdyilrELKlskvgqgntertvwqyHFRTwpdhgvpsdp 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 204 -----FLENYQILQYFIIRMFQVV---------EKSFNIMDI-------------------VAQMREQRSGMVQTKEQYH 250
Cdd:cd14605   162 ggvldFLEEVHHKQESIMDAGPVVvhcsagigrTGTFIVIDIlidiirekgvdcdidvpktIQMVRSQRSGMVQTEAQYR 241


                  ...
gi 2217276606 251 FCY 253
Cdd:cd14605   242 FIY 244
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 127-260 3.08e-28

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 107.54  E-value: 3.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP---------------IS 191
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggehdaltfgeykVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 192 LKK--------------------------------------PLELKHFRVFLENYQILQYFIIRMFQ--------VVEKS 225
Cdd:cd14540    81 TKFsvssgcytttglrvkhtlsgqsrtvwhlqytdwpdhgcPEDVSGFLDFLEEINSVRRHTNQDVAghnrnpptLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217276606 226 ------------------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 260
Cdd:cd14540   161 agvgrtgvviladlmlycldhneeLDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 98-221 8.94e-28

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: 107.81  E-value: 8.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  98 NQPSNREKNRYRDILPYDSTRVPL-------GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVI 170
Cdd:cd17667    23 NHPDNKHKNRYINILAYDHSRVKLrplpgkdSKHSDYINANYVDGYNKAKAY--IATQGPLKSTFEDFWRMIWEQNTGII 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217276606 171 AMITREIEGGIIKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQV 221
Cdd:cd17667   101 VMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSI 149
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 97-258 9.28e-28

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: 107.27  E-value: 9.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  97 GNQPSNREKNRYRDILPYDSTRVPLGKS------KDYINASYIR---IVNCGEEYFYIATQGPLLSTIDDFWQMVLENNS 167
Cdd:cd14606    13 GQRPENKSKNRYKNILPFDHSRVILQGRdsnipgSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 168 NVIAMITREIEGGIIKCYHYWPI----------------------------------SLKKPLELKHFRV---------- 203
Cdd:cd14606    93 RVIVMTTREVEKGRNKCVPYWPEvgmqraygpysvtncgehdtteyklrtlqvspldNGELIREIWHYQYlswpdhgvps 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 204 -------FLENYQILQ----------------------YFIIRMF------QVVEKSFNIMDIVAQMREQRSGMVQTKEQ 248
Cdd:cd14606   173 epggvlsFLDQINQRQeslphagpiivhcsagigrtgtIIVIDMLmenistKGLDCDIDIQKTIQMVRAQRSGMVQTEAQ 252

                         250
                  ....*....|
gi 2217276606 249 YHFCYDIVLE 258
Cdd:cd14606   253 YKFIYVAIAQ 262
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 100-253 2.65e-27

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: 105.69  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 100 PSNREKNRYRDILPYDSTRVPLGKSK------DYINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMI 173
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLRRAGsqeeegSYINANYIRGYD-GKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 174 TREIEGGiIKCYHYWP--------------------------ISLKKPLELKHFRVFL----------ENYQILqyfiIR 217
Cdd:cd14612    92 TKLKEKK-EKCVHYWPekegtygrfeirvqdmkecdgytirdLTIQLEEESRSVKHYWfsswpdhqtpESAGPL----LR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 218 MFQVVEKS---------------------------------------FNIMDIVAQMREQRSGMVQTKEQYHFCY 253
Cdd:cd14612   167 LVAEVEESrqtaaspgpivvhcsagigrtgcfiatsigcqqlkdtgkVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 83-260 4.14e-27

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: 106.36  E-value: 4.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  83 MALELKNLP------GEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14627    28 MELEFKRLAnskahtSRFISANLPCNKFKNRLVNIMPYETTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYFI--------------- 215
Cdd:cd14627   106 AETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQYILrefkvtdardgqsrt 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 216 IRMFQVV------------------------------------------------------------EKSFNIMDIVAQM 235
Cdd:cd14627   184 VRQFQFTdwpeqgvpksgegfidfigqvhktkeqfgqdgpisvhcsagvgrtgvfitlsivlermryEGVVDIFQTVKML 263

                         250       260
                  ....*....|....*....|....*
gi 2217276606 236 REQRSGMVQTKEQYHFCYDIVLEVL 260
Cdd:cd14627   264 RTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 105-259 1.23e-26

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: 103.77  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 105 KNRYRDILPYDSTRVPLG-----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG 179
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKGVYGPRAY--IATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 180 GIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQV-------------------------------------- 221
Cdd:cd14602    79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVkfnsetrtiyqfhyknwpdhdvpssidpileliwdvrc 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 222 -------------------------------------VEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 259
Cdd:cd14602   159 yqeddsvpicihcsagcgrtgvicaidytwmllkdgiIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 100-253 1.30e-26

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: 104.72  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 100 PSNREKNRYRDILPYDSTRVPLGKS-KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 178
Cdd:cd14608    23 PKNKNRNRYRDVSPFDHSRIKLHQEdNDYINASLIKMEEAQRSY--ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217276606 179 GGIIKCYHYWPISLKKPL--ELKHFRVFLENYQILQYFIIRmfqvveksfnimdivaQMREQRSGMVQTKEQYHFCY 253
Cdd:cd14608   101 KGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVR----------------QLELENLTTQETREILHFHY 161
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 83-251 7.82e-26

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: 102.89  E-value: 7.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  83 MALELKNLPG------EFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14628    27 MELEFKRLASskahtsRFISANLPCNKFKNRLVNIMPYESTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKsfnimd 230
Cdd:cd14628   105 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDA------ 175

                         170       180
                  ....*....|....*....|.
gi 2217276606 231 ivaqmreqRSGMVQTKEQYHF 251
Cdd:cd14628   176 --------RDGQSRTVRQFQF 188
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 127-254 8.59e-26

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: 100.50  E-value: 8.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 206
Cdd:cd14549     1 YINANYVDGYNKARAY--IATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 NYQILQYFIIRMFQV----------------------------------------------------------------- 221
Cdd:cd14549    77 STEVLATYTVRTFSLknlklkkvkgrsservvyqyhytqwpdhgvpdytlpvlsfvrkssaanppgagpivvhcsagvgr 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217276606 222 ---------------VEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 254
Cdd:cd14549   157 tgtyividsmlqqiqDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 85-253 8.91e-26

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: 101.97  E-value: 8.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  85 LELKNLPGE--FNSGNQPSNREKNRYRDILPYDSTRVPLGKSK-DYINASYIRIVNCgeEYFYIATQGPLLSTIDDFWQM 161
Cdd:cd14607     5 LEIRNESHDypHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEnDYINASLVVIEEA--QRSYILTQGPLPNTCCHFWLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 162 VLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFqvveksfnimdivaQMREQR 239
Cdd:cd14607    83 VWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLL--------------QLENIN 148

                         170
                  ....*....|....
gi 2217276606 240 SGmvQTKEQYHFCY 253
Cdd:cd14607   149 SG--ETRTISHFHY 160
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 106-221 2.79e-25

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: 99.89  E-value: 2.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 106 NRYRDILPYDSTRVPLG----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14615     1 NRYNNVLPYDISRVKLSvqshSTDDYINANYMPGYNSKKEF--IAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217276606 182 IKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQV 221
Cdd:cd14615    79 TKCEEYWPSKQKK--DYGDITVTMTSEIVLPEWTIRDFTV 116
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 91-258 1.08e-24

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: 99.75  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  91 PGEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLEN 165
Cdd:cd14610    33 PNATNVAQREENVQKNRSLAVLPYDHSRIILKaenshSHSDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWES 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 166 NSNVIAMITREIEGGIIKCYHYWP--------------IS--------LKKPLELK-------------HF--------- 201
Cdd:cd14610   112 GCVVIVMLTPLAENGVKQCYHYWPdegsnlyhiyevnlVSehiwcedfLVRSFYLKnlqtnetrtvtqfHFlswndqgvp 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 202 ---RVFLENYQILQ-----------------------YFIIRM-FQVVEKSFNIMDIVA---QMREQRSGMVQTKEQYHF 251
Cdd:cd14610   192 astRSLLDFRRKVNkcyrgrscpiivhcsdgagrsgtYILIDMvLNKMAKGAKEIDIAAtleHLRDQRPGMVQTKEQFEF 271


                  ....*..
gi 2217276606 252 CYDIVLE 258
Cdd:cd14610   272 ALTAVAE 278
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 83-251 8.11e-24

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: 97.49  E-value: 8.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  83 MALELKNLPG------EFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14629    28 MELEFKLLANskahtsRFISANLPCNKFKNRLVNIMPYELTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKsfnimd 230
Cdd:cd14629   106 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDA------ 176

                         170       180
                  ....*....|....*....|.
gi 2217276606 231 ivaqmreqRSGMVQTKEQYHF 251
Cdd:cd14629   177 --------RDGQSRTIRQFQF 189
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 91-251 2.27e-23

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: 95.87  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  91 PGEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLEN 165
Cdd:cd14609    31 PNTCSTAQGEANVKKNRNPDFVPYDHARIKLKaesnpSRSDYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWEN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 166 NSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRmfqvvekSFNIMDIvaQMREQRsgmv 243
Cdd:cd14609   110 GCTVIVMLTPLVEDGVKQCDRYWP---DEGSSLYHiYEVNLVSEHIwCEDFLVR-------SFYLKNV--QTQETR---- 173


                  ....*...
gi 2217276606 244 qTKEQYHF 251
Cdd:cd14609   174 -TLTQFHF 180
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 80-258 6.27e-23

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: 94.72  E-value: 6.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  80 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14626    20 QEYESID----PGQqftWENSNLEVNKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID--GYRKQNAYIATQGPL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP-----------ISLKKPLELKHF--RVF------------LE 206
Cdd:cd14626    94 PETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPirgtetygmiqVTLLDTVELATYsvRTFalykngssekreVR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 NYQILQY--------------FIIRM------------------------FQVV---------EKSFNIMDIVAQMREQR 239
Cdd:cd14626   174 QFQFMAWpdhgvpeyptpilaFLRRVkacnppdagpmvvhcsagvgrtgcFIVIdamlermkhEKTVDIYGHVTCMRSQR 253

                         250
                  ....*....|....*....
gi 2217276606 240 SGMVQTKEQYHFCYDIVLE 258
Cdd:cd14626   254 NYMVQTEDQYIFIHEALLE 272
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 126-259 7.57e-23

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: 92.78  E-value: 7.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 126 DYINASYIR-------IVNcgeeyFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP----ISLKK 194
Cdd:cd14541     1 DYINANYVNmeipgsgIVN-----RYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdlgeTMQFG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 195 PLELKH----------FRVFL-------ENYQI--LQY-----------------FIIRMFQ---------VVEKSFNI- 228
Cdd:cd14541    76 NLQITCvseevtpsfaFREFIltntntgEERHItqMQYlawpdhgvpddssdfldFVKRVRQnrvgmveptVVHCSAGIg 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217276606 229 -----------------------MDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 259
Cdd:cd14541   156 rtgvlitmetamclieanepvypLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 102-251 8.03e-23

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: 93.55  E-value: 8.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 102 NREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITRE 176
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLqlldgDPHSDYINANYIDGYH--RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 177 IEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSFNimdivaQMREQRsgmvqtkeQYHF 251
Cdd:cd14630    81 VEVGRVKCVRYWPDDTEVYGDIK---VTLIETEPLAEYVIRTFTVQKKGYH------EIREIR--------QFHF 138
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 106-221 8.10e-23

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: 93.47  E-value: 8.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 106 NRYRDILPYDSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlggepHSDYINANFIPGYTSPQEF--IATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2217276606 181 IIKCYHYWPISLkKPLELKHFRVFLENYQILQYFIIRMFQV 221
Cdd:cd14618    79 RVLCDHYWPSES-TPVSYGHITVHLLAQSSEDEWTRREFKL 118
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 127-253 1.96e-22

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: 91.76  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG-GIIKCYHYWPISLKKPLELKHFRV-- 203
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVtn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 204 -------------FLENYQI-----------LQYF----------------IIRMFQVVEKSF----------------- 226
Cdd:cd17658    81 kklkhsqhsitlrVLEVQYIeseepplsvlhIQYPewpdhgvpkdtrsvreLLKRLYGIPPSAgpivvhcsagigrtgay 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217276606 227 ------------------NIMDIVAQMREQRSGMVQTKEQYHFCY 253
Cdd:cd17658   161 ctihntirrilegdmsavDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
98-265 2.09e-22

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 93.23  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  98 NQPSNREKNRYRDILPYDSTRVplGKSKDYINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 177
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 178 EGG--IIKCYHYWPIS-----------LKKPLELK---HFRVFL-------ENYQILQYFIIR---------------MF 219
Cdd:COG5599   113 EISkpKVKMPVYFRQDgeygkyevsseLTESIQLRdgiEARTYVltikgtgQKKIEIPVLHVKnwpdhgaisaealknLA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 220 QVVEKS------------------------------------------FNIMDIVAQMREQR-SGMVQTKEQYHFCYDIV 256
Cdd:COG5599   193 DLIDKKekikdpdkllpvvhcragvgrtgtliaclalsksinalvqitLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLA 272


                  ....*....
gi 2217276606 257 LEVLRKLLT 265
Cdd:COG5599   273 EQQIRPLLR 281
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 127-253 2.69e-22

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: 91.33  E-value: 2.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14542     1 YINANFIKGVS--GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 207 N------------------------YQiLQYF-------------IIRMFQVVEK------------------------- 224
Cdd:cd14542    79 KekrvgpdflirtlkvtfqkesrtvYQ-FHYTawpdhgvpssvdpILDLVRLVRDyqgsedvpicvhcsagcgrtgtica 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217276606 225 ---------------SFNIMDIVAQMREQRSGMVQTKEQYHFCY 253
Cdd:cd14542   158 idyvwnllktgkipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 127-189 4.12e-22

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: 91.19  E-value: 4.12e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217276606 127 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 189
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP 63
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 106-189 1.50e-21

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: 89.97  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 106 NRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 180
Cdd:cd14616     1 NRFPNIKPYNNNRVKLiadagVPGSDYINASYISGYLCPNEF--IATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78


                  ....*....
gi 2217276606 181 IIKCYHYWP 189
Cdd:cd14616    79 RIRCHQYWP 87
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 94-251 1.89e-21

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: 90.49  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  94 FNSGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSN 168
Cdd:cd14633    32 WDSAKKDENRMKNRYGNIIAYDHSRVRLqpiegETSSDYINGNYIDGYH--RPNHYIATQGPMQETIYDFWRMVWHENTA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 169 VIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSfnimdiVAQMREQRsgmvqtkeQ 248
Cdd:cd14633   110 SIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRG------VHEIREIR--------Q 172


                  ...
gi 2217276606 249 YHF 251
Cdd:cd14633   173 FHF 175
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 105-256 2.05e-21

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: 90.31  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 105 KNRYRDILPYDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEI 177
Cdd:cd14613    28 KNRYKTILPNPHSRVCL-TSPDqddplssYINANYIRGYG-GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 178 EGGIIKCYHYWP----------ISLKKPLELKHFRVFL------ENYQILQYF----------------IIRMFQVVEKS 225
Cdd:cd14613   105 EEMNEKCTEYWPeeqvtyegieITVKQVIHADDYRLRLitlksgGEERGLKHYwytswpdqktpdnappLLQLVQEVEEA 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217276606 226 ----------------------------------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 256
Cdd:cd14613   185 rqqaepncgpvivhcsagigrtgcfiatsicckqlrnegvVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 80-219 2.80e-21

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: 90.47  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  80 QEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPLLST 154
Cdd:cd14621    30 EEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPvegvpDSDYINASFIN--GYQEKNKFIAAQGPKEET 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 155 IDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMF 219
Cdd:cd14621   108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPD--QGCWTYGNIRVSVEDVTVLVDYTVRKF 170
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 80-260 7.85e-21

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: 89.00  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  80 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14625    26 QEYESID----PGQqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPiegimGSDYINANYID--GYRKQNAYIATQGPL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP-----------ISLKKPLELKHF--RVF-------LENYQIL 211
Cdd:cd14625   100 PETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPsrgtetygmiqVTLLDTIELATFcvRTFslhkngsSEKREVR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 212 QY-------------------FIIRM------------------------FQVV---------EKSFNIMDIVAQMREQR 239
Cdd:cd14625   180 QFqftawpdhgvpeyptpflaFLRRVktcnppdagpivvhcsagvgrtgcFIVIdamlerikhEKTVDIYGHVTLMRSQR 259

                         250       260
                  ....*....|....*....|.
gi 2217276606 240 SGMVQTKEQYHFCYDIVLEVL 260
Cdd:cd14625   260 NYMVQTEDQYSFIHDALLEAV 280
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 105-253 8.23e-21

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: 88.05  E-value: 8.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 105 KNRYRDILPYDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 177
Cdd:cd14611     2 KNRYKTILPNPHSRVCL-KPKNsndslstYINANYIRGYG-GKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 178 EGGiIKCYHYWPislKKPLELKHFRVFLENYQILQYFIIR------------------------------------MFQV 221
Cdd:cd14611    80 EKN-EKCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRnltlkqgsqsrsvkhywytswpdhktpdsaqpllqlMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 222 VEKSFN--------------------------------------IMDIVAQMREQRSGMVQTKEQYHFCY 253
Cdd:cd14611   156 EEDRLAspgrgpvvvhcsagigrtgcfiattigcqqlkeegvvdVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 78-227 2.28e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 88.52  E-value: 2.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  78 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLS 153
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 154 TIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSFN 227
Cdd:PHA02747  105 TCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK 179
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 127-256 9.57e-20

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: 84.63  E-value: 9.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP-----------ISLKKP 195
Cdd:cd14552     1 YINASFIDGYR--QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPedgsvssgditVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 196 LELKHF--RVFL------ENYQILQYF----------------IIRMFQVVEKS-------------------------- 225
Cdd:cd14552    79 TDYEDYtlRDFLvtkgkgGSTRTVRQFhfhgwpevgipdngkgMIDLIAAVQKQqqqsgnhpitvhcsagagrtgtfcal 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217276606 226 ------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 256
Cdd:cd14552   159 stvlervkaegvLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 127-254 1.02e-19

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: 84.37  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP----------ISLKKP- 195
Cdd:cd14558     1 YINASFIDGYWGPKSL--IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGdekktygdieVELKDTe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 196 ---------LELKHFRVF----LENYQILQYF----------IIRMFQVVEKSF-------------------------- 226
Cdd:cd14558    79 ksptytvrvFEITHLKRKdsrtVYQYQYHKWKgeelpekpkdLVDMIKSIKQKLpyknskhgrsvpivvhcsdgssrtgi 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217276606 227 -----NIMD------------IVAQMREQRSGMVQTKEQYHFCYD 254
Cdd:cd14558   159 fcalwNLLEsaetekvvdvfqVVKALRKQRPGMVSTLEQYQFLYD 203
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 63-188 1.64e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 85.82  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  63 KDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNCG 139
Cdd:PHA02742   13 KNCEQLIEESNLAEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVDGHNAK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217276606 140 EEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYW 188
Cdd:PHA02742   93 GRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW 139
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 127-221 2.65e-19

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: 83.49  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 206
Cdd:cd17668     1 YINANYVDGYN--KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQK 76

                          90
                  ....*....|....*
gi 2217276606 207 NYQILQYFIIRMFQV 221
Cdd:cd17668    77 SVQVLAYYTVRNFTL 91
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 108-258 9.34e-19

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: 82.30  E-value: 9.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 108 YRDILPYDSTRVPL-----GKSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGII 182
Cdd:cd14620     1 YPNILPYDHSRVILsqldgIPCSDYINASYID--GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 183 KCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQV----------------------------------------- 221
Cdd:cd14620    79 KCYQYWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIqpqlpdgckaprlvtqlhftswpdfgvpftpigmlkflkkv 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217276606 222 ------------------------------------VEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14620   157 ksvnpvhagpivvhcsagvgrtgtfividamidmmhAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 80-260 2.78e-18

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 82.09  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  80 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 151
Cdd:cd14624    26 QEYESID----PGQqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAiegipGSDYINANYID--GYRKQNAYIATQGAL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP-----------ISLKKPLELKHF--RVFL-------ENYQIL 211
Cdd:cd14624   100 PETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPsrgtetygliqVTLLDTVELATYcvRTFAlykngssEKREVR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 212 QY-------------------FIIRM------------------------FQVV---------EKSFNIMDIVAQMREQR 239
Cdd:cd14624   180 QFqftawpdhgvpehptpflaFLRRVktcnppdagpmvvhcsagvgrtgcFIVIdamlerikhEKTVDIYGHVTLMRAQR 259

                         250       260
                  ....*....|....*....|.
gi 2217276606 240 SGMVQTKEQYHFCYDIVLEVL 260
Cdd:cd14624   260 NYMVQTEDQYIFIHDALLEAV 280
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 126-189 3.24e-18

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: 80.76  E-value: 3.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217276606 126 DYINASYI--RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP 189
Cdd:cd14601     1 DYINANYInmEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP 66
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 127-258 4.73e-17

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: 77.48  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRV-- 203
Cdd:cd14546     1 YINASTI-YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVhl 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 204 ---------------FLENYQILQYFIIRMFQV---------------------VEKSF--------------------- 226
Cdd:cd14546    77 vsehiwcddylvrsfYLKNLQTSETRTVTQFHFlswpdegipasakpllefrrkVNKSYrgrscpivvhcsdgagrtgty 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217276606 227 -------NIM-------DIVA---QMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14546   157 ilidmvlNRMakgakeiDIAAtleHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 127-224 4.82e-17

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: 77.17  E-value: 4.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 206
Cdd:cd14557     1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN 78

                          90
                  ....*....|....*...
gi 2217276606 207 NYQILQYFIIRMFQVVEK 224
Cdd:cd14557    79 EEKICPDYIIRKLNINNK 96
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 127-251 5.05e-17

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: 77.26  E-value: 5.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLE 206
Cdd:cd14555     1 YINANYIDGYH--RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217276606 207 NYQILQYFIIRMFQVVEKSFNimdivaQMREQRsgmvqtkeQYHF 251
Cdd:cd14555    76 ETEPLAEYVVRTFALERRGYH------EIREVR--------QFHF 106
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 127-254 5.16e-17

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: 77.04  E-value: 5.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIR-IVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFL 205
Cdd:cd14539     1 YINASLIEdLTPYCPRF--IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 206 ENYQILQYFIIRMFQVVEK-----------------------------SF------------------------------ 226
Cdd:cd14539    79 QSVRTTPTHVERIISIQHKdtrlsrsvvhlqfttwpelglpdspnpllRFieevhshylqqrslqtpivvhcssgvgrtg 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217276606 227 -------------------NIMDIVAQMREQRSGMVQTKEQYHFCYD 254
Cdd:cd14539   159 afcllyaavqeieagngipDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 107-258 8.45e-17

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: 77.01  E-value: 8.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 107 RYRDILPYDSTRV--PLGKSK---DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 181
Cdd:cd14623     1 RVLQIIPYEFNRViiPVKRGEentDYVNASFID--GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 182 IKCYHYWP-----------ISLKKPLELKHFRV-------FLEN--YQILQYF---------------IIRMFQVVEKS- 225
Cdd:cd14623    79 EKCAQYWPsdgsvsygditIELKKEEECESYTVrdllvtnTRENksRQIRQFHfhgwpevgipsdgkgMINIIAAVQKQq 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 226 -------------------------------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14623   159 qqsgnhpitvhcsagagrtgtfcalstvlervkaegiLDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 124-251 3.40e-16

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: 75.06  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 124 SKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkKPLEL-KHFR 202
Cdd:cd14631    12 SSDYINANYID--GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP----DDTEVyGDFK 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217276606 203 VFLENYQILQYFIIRMFQVVEKSFNimdivaQMREQRsgmvqtkeQYHF 251
Cdd:cd14631    86 VTCVEMEPLAEYVVRTFTLERRGYN------EIREVK--------QFHF 120
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 126-256 1.80e-15

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: 73.12  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 126 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWP-----------ISLKK 194
Cdd:cd14622     1 DYINASFID--GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPsegsvthgeitIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 195 P--LELKHFRVFLENY-QILQYFIIRMFQ---------------------VVEKS------------------------- 225
Cdd:cd14622    79 DtlLETISIRDFLVTYnQEKQTRLVRQFHfhgwpeigipaegkgmidliaAVQKQqqqtgnhpivvhcsagagrtgtfia 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217276606 226 -------------FNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 256
Cdd:cd14622   159 lsnilervkaeglLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PHA02738 PHA02738
hypothetical protein; Provisional
 57-215 1.72e-14

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 71.88  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  57 HEQTAIKDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSgnQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYI 133
Cdd:PHA02738    6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNA--EKKNRKLNRYLDAVCFDHSRVILPAERnrgDYINANYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 134 RivncGEEYF--YIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQIL 211
Cdd:PHA02738   84 D----GFEYKkkFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETH 159


                  ....
gi 2217276606 212 QYFI 215
Cdd:PHA02738  160 PHYV 163
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 127-241 2.93e-14

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: 69.27  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGiiKCYHYWPISlKKPLELKHFRVFL- 205
Cdd:cd14550     1 YINASYLQGYRRSNEF--IITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECETFKVTLs 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217276606 206 ---------ENYQILQYFII-----------RMFQV---------VEKSFNIMDIVAQMREQRSG 241
Cdd:cd14550    76 gedhsclsnEIRLIVRDFILestqddyvlevRQFQCpswpnpcspIHTVFELINTVQEWAQQRDG 140
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 127-219 4.00e-14

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: 69.17  E-value: 4.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLE 206
Cdd:cd14551     1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVE 76

                          90
                  ....*....|...
gi 2217276606 207 NYQILQYFIIRMF 219
Cdd:cd14551    77 DTVVLVDYTTRKF 89
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 127-234 9.90e-14

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: 68.15  E-value: 9.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 206
Cdd:cd14632     1 YINANYIDGYH--RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIK---ITLL 75

                          90       100
                  ....*....|....*....|....*...
gi 2217276606 207 NYQILQYFIIRMFQVVEKSFNIMDIVAQ 234
Cdd:cd14632    76 KTETLAEYSVRTFALERRGYSARHEVKQ 103
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 53-188 5.56e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 64.66  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  53 IFNFHEQT-AIKDCLKILEEKTAAYDImqefmalelkNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-------- 123
Cdd:PHA02746   11 AFDFFDKTnHAKFCEFVLLEHAEVMDI----------PIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 124 ------------SKD----YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHY 187
Cdd:PHA02746   81 vgdsdgkkievtSEDnaenYIHANFVD--GFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFEL 157


                  .
gi 2217276606 188 W 188
Cdd:PHA02746  158 W 158
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 127-249 1.17e-10

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: 59.62  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYhYWPiSLKKPLELKHFRVFL- 205
Cdd:cd17669     1 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLi 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217276606 206 ---------ENYQILQYFI-----------IRMFQV---------VEKSFNIMDIVAQMREQRSGMVQTKEQY 249
Cdd:cd17669    77 aeehkclsnEEKLIIQDFIleatqddyvleVRHFQCpkwpnpdspISKTFELISIIKEEAANRDGPMIVHDEH 149
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 127-254 1.78e-10

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: 58.96  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIrivncgEEY----FYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPI------------ 190
Cdd:cd14556     1 YINAALL------DSYkqpaAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDegsgtygpiqve 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 191 ----SLKKPLELKHFRV-----FLENYQILQYF-----------------IIRMFQVVEK-------------------- 224
Cdd:cd14556    74 fvstTIDEDVISRIFRLqnttrPQEGYRMVQQFqflgwprdrdtppskraLLKLLSEVEKwqeqsgegpivvhclngvgr 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217276606 225 --SFNIMDIVAQM----------------REQRSGMVQTKEQYHFCYD 254
Cdd:cd14556   154 sgVFCAISSVCERikvenvvdvfqavktlRNHRPNMVETEEQYKFCYD 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
213-258 1.33e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 54.29  E-value: 1.33e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217276606  213 YFIIRMFQVVEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:smart00404  60 DILLQQLEAEAGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 213-258 1.33e-09

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: 54.29  E-value: 1.33e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217276606  213 YFIIRMFQVVEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:smart00012  60 DILLQQLEAEAGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 127-258 4.00e-08

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: 52.22  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINA----SYIRIVNcgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGIIKCYHYWP---ISLKKPLEL 198
Cdd:cd14637     1 YINAaltdSYTRSAA------FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPepgLQQYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 199 KHF----------RVF-LENYQILQ--YFIIRMFQVV-----------EKSF---------------------------- 226
Cdd:cd14637    75 EFVsgsadedivtRLFrVQNITRLQegHLMVRHFQFLrwsayrdtpdsKKAFlhllasvekwqresgegrtvvhclnggg 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217276606 227 ------------------NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14637   155 rsgtycasamilemirchNIVDVfyaVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 127-258 5.47e-08

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: 51.95  E-value: 5.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWPISLK---KPLELKHF-- 201
Cdd:cd14634     1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQL-CMQYWPEKTSccyGPIQVEFVsa 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 202 --------RVFL--------ENYQILQYF-----------------IIRMFQVVEK------------------------ 224
Cdd:cd14634    77 didediisRIFRicnmarpqDGYRIVQHLqyigwpayrdtppskrsILKVVRRLEKwqeqydgregrtvvhclngggrsg 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217276606 225 SF-------------NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14634   157 TFcaicsvcemiqqqNIIDVfhtVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 127-205 4.35e-07

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: 49.29  E-value: 4.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217276606 127 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPiSLKKPLELKHFRVFL 205
Cdd:cd17670     1 YINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTL 75
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 78-224 6.43e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 43.42  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606  78 IMQEFMALelknLPGEFNSGNQPSNREKNRYRD------ILPYDSTRVPLGKSKDYINASYIRIVNcgEEYFYIATQGPL 151
Cdd:PHA02740   27 IIKEYRAI----VPEHEDEANKACAQAENKAKDenlalhITRLLHRRIKLFNDEKVLDARFVDGYD--FEQKFICIINLC 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217276606 152 LSTIDDFWQMVLENNSNVIAMITREIEGgiiKCYH-YWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEK 224
Cdd:PHA02740  101 EDACDKFLQALSDNKVQIIVLISRHADK---KCFNqFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDK 171
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 127-258 3.10e-04

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: 40.78  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGiikCYHYWP---------------- 189
Cdd:cd14636     1 YINAALMDSYR--QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWPeegmlrygpiqvecms 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 190 ISLKKPLELKHFRVFLENYQILQYFIIRMFQVV-----------EKSF-------------------------------- 226
Cdd:cd14636    76 CSMDCDVISRIFRICNLTRPQEGYLMVQQFQYLgwashrevpgsKRSFlklilqvekwqeecdegegrtiihclngggrs 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217276606 227 ----------------NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 258
Cdd:cd14636   156 gmfcaisivcemikrqNVVDVfhaVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 127-216 2.14e-03

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: 38.52  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276606 127 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWP---ISLKKPLELKHFRV 203
Cdd:cd14635     1 YINAALMD--SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPengVHRHGPIQVEFVSA 76

                          90
                  ....*....|...
gi 2217276606 204 FLENYQILQYFII 216
Cdd:cd14635    77 DLEEDIISRIFRI 89
 
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