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Conserved domains on  [gi|24639268|ref|NP_726793|]
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corkscrew, isoform C [Drosophila melanogaster]

Protein Classification

SH2 and PTPc-N11_6 domain-containing protein( domain architecture ID 13105711)

SH2 and PTPc-N11_6 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 93-489 9.32e-151

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: 436.89  E-value: 9.32e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  93 NRLKNRYRNILPYDHTRVKLLDVEHSVAGAEYINANYIRLPTDGDLYNMsssseslnssvpscpactaaqtqrncsncql 172
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRNENEGPTTDE------------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 173 qnktcvqcavksailpysncatcsrksdslskhkrsessassspssgsgsgpgssgtsgvssvngpgtptnltsgtagcl 252
Cdd:cd14544     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 253 vgllkrhsndssgavsismaerererereMFKTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCAR 332
Cdd:cd14544  50 -----------------------------NAKTYIATQGCLE----NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVR 96

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 333 YWPDEGRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQ--PARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHL 410
Cdd:cd14544  97 YWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQgdPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESL 176

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639268 411 AQagekPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQT 489
Cdd:cd14544 177 PH----AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIET 251
SH2 super family cl15255
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
 1-48 1.31e-22

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


The actual alignment was detected with superfamily member cd09931:

Pssm-ID: 472789  Cd Length: 99  Bit Score: 92.73  E-value: 1.31e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24639268   1 MIRWQDKKYDVGGGESFGTLSELIDHYKRNPMVETCGTVVHLRQPFNA 48
Cdd:cd09931  52 MIRCQGGKYDVGGGEEFDSLTDLVEHYKKNPMVETSGTVVHLKQPLNA 99
 
Name Accession Description Interval E-value
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 93-489 9.32e-151

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: 436.89  E-value: 9.32e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  93 NRLKNRYRNILPYDHTRVKLLDVEHSVAGAEYINANYIRLPTDGDLYNMsssseslnssvpscpactaaqtqrncsncql 172
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRNENEGPTTDE------------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 173 qnktcvqcavksailpysncatcsrksdslskhkrsessassspssgsgsgpgssgtsgvssvngpgtptnltsgtagcl 252
Cdd:cd14544     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 253 vgllkrhsndssgavsismaerererereMFKTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCAR 332
Cdd:cd14544  50 -----------------------------NAKTYIATQGCLE----NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVR 96

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 333 YWPDEGRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQ--PARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHL 410
Cdd:cd14544  97 YWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQgdPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESL 176

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639268 411 AQagekPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQT 489
Cdd:cd14544 177 PH----AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIET 251
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
67-485 8.96e-89

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 277.62  E-value: 8.96e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268     67 GFWEEFESLQQDSRDTFSRNEGYKQENRLKNRYRNILPYDHTRVKLLDVEHSVAGaeYINANYIRLPTDGdlynmsssse 146
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSD--YINASYIDGPNGP---------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    147 slnssvpscpactaaqtqrncsncqlqnktcvqcavksailpysncatcsrksdslskhkrsessassspssgsgsgpgs 226
Cdd:smart00194     --------------------------------------------------------------------------------

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    227 sgtsgvssvngpgtptnltsgtagclvgllkrhsndssgavsismaererereremfKTYIATQGCLltqqVNTVTDFWN 306
Cdd:smart00194  69 ---------------------------------------------------------KAYIATQGPL----PSTVEDFWR 87

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    307 MVWQENTRVIVMTTKEYERGKEKCARYWPDE-GRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQP-ARRIFHYHFQVW 384
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSeTRTVTHYHYTNW 167

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    385 PDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQIVRNGldtEIDIQRTIQMVRS 464
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTST------GPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRS 238

                          410       420
                   ....*....|....*....|.
gi 24639268    465 QRSGLVQTEAQYKFVYYAVQH 485
Cdd:smart00194 239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
284-483 2.44e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 244.46  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268   284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDE-GRSEQFGHARIQCVSENS-TSDYTL 361
Cdd:pfam00102  42 KKYIATQGPL----PNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEEeGESLEYGDFTVTLKKEKEdEKDYTV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268   362 REFLVSWRDQPA-RRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqagEKPGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:pfam00102 118 RTLEVSNGGSEEtRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLD-----GRSGPIVVHCSAGIGRTGTFIAIDIA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24639268   441 LDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:pfam00102 193 LQQLEAEG---EVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02738 PHA02738
hypothetical protein; Provisional
 284-488 6.11e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 138.13  E-value: 6.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPD-EGRSEQFGHARIQCVSENSTSDYTLR 362
Cdd:PHA02738  90 KKFICGQAPTR----QTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVKS 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  363 EFLVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLA----QAGEK---PGPICVHCSAGIGRTGTFI 435
Cdd:PHA02738 166 TLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAqeslQIGHNrlqPPPIVVHCNAGLGRTPCYC 245

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24639268  436 VIDMildQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:PHA02738 246 VVDI---SISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
284-490 6.63e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 116.73  E-value: 6.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLTQQVntvtDFWNMVWQENTRVIVMTT--KEYERGKEKCARYWPDEGRseqfgHARIQCVSENSTSDY-- 359
Cdd:COG5599  77 HRYIATQYPLEEQLE----DFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQDGE-----YGKYEVSSELTESIQlr 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 360 ---TLREFLVSWRD--QPARRIFHYHFQVWPDHGvPADPGCVLNFLQDVNtrqsHLAQAGEKP-GPICVHCSAGIGRTGT 433
Cdd:COG5599 148 dgiEARTYVLTIKGtgQKKIEIPVLHVKNWPDHG-AISAEALKNLADLID----KKEKIKDPDkLLPVVHCRAGVGRTGT 222

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24639268 434 FIVIdMILDQIVRNGLDTEIDIQRT-IQMVRSQRSGLVQTEAQY-KFVYYAVQHYIQTL 490
Cdd:COG5599 223 LIAC-LALSKSINALVQITLSVEEIvIDMRTSRNGGMVQTSEQLdVLVKLAEQQIRPLL 280
SH2_C-SH2_SHP_like cd09931
C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The ...
 1-48 1.31e-22

C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The SH2 domain phosphatases (SHP-1, SHP-2/Syp, Drosophila corkscrew (csw), and Caenorhabditis elegans Protein Tyrosine Phosphatase (Ptp-2)) are cytoplasmic signaling enzymes. They are both targeted and regulated by interactions of their SH2 domains with phosphotyrosine docking sites. These proteins contain two SH2 domains (N-SH2, C-SH2) followed by a tyrosine phosphatase (PTP) domain, and a C-terminal extension. Shp1 and Shp2 have two tyrosyl phosphorylation sites in their C-tails, which are phosphorylated differentially by receptor and nonreceptor PTKs. Csw retains the proximal tyrosine and Ptp-2 lacks both sites. Shp-binding proteins include receptors, scaffolding adapters, and inhibitory receptors. Some of these bind both Shp1 and Shp2 while others bind only one. Most proteins that bind a Shp SH2 domain contain one or more immuno-receptor tyrosine-based inhibitory motifs (ITIMs): [SIVL]xpYxx[IVL]. Shp1 N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, and is thus believed to regulate the phosphatase activity of SHP-1. Its C-SH2 domain is thought to be involved in searching for phosphotyrosine activators. The SHP2 N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. The C-SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation. Csw SH2 domain function is essential, but either SH2 domain can fulfill this requirement. The role of the csw SH2 domains during Sevenless receptor tyrosine kinase (SEV) signaling is to bind Daughter of Sevenless rather than activated SEV. Ptp-2 acts in oocytes downstream of sheath/oocyte gap junctions to promote major sperm protein (MSP)-induced MAP Kinase (MPK-1) phosphorylation. Ptp-2 functions in the oocyte cytoplasm, not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation. It is thought that MSP triggers PTP-2/Ras activation and ROS production to stimulate MPK-1 activity essential for oocyte maturation and that secreted MSP domains and Cu/Zn superoxide dismutases function antagonistically to control ROS and MAPK signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198185  Cd Length: 99  Bit Score: 92.73  E-value: 1.31e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24639268   1 MIRWQDKKYDVGGGESFGTLSELIDHYKRNPMVETCGTVVHLRQPFNA 48
Cdd:cd09931  52 MIRCQGGKYDVGGGEEFDSLTDLVEHYKKNPMVETSGTVVHLKQPLNA 99
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 3-31 1.33e-03

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 37.98  E-value: 1.33e-03
                           10        20
                   ....*....|....*....|....*....
gi 24639268      3 RWQDKKYDVGGGESFGTLSELIDHYKRNP 31
Cdd:smart00252  54 RNEDGKFYLEGGRKFPSLVELVEHYQKNS 82
 
Name Accession Description Interval E-value
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 93-489 9.32e-151

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: 436.89  E-value: 9.32e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  93 NRLKNRYRNILPYDHTRVKLLDVEHSVAGAEYINANYIRLPTDGDLYNMsssseslnssvpscpactaaqtqrncsncql 172
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRNENEGPTTDE------------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 173 qnktcvqcavksailpysncatcsrksdslskhkrsessassspssgsgsgpgssgtsgvssvngpgtptnltsgtagcl 252
Cdd:cd14544     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 253 vgllkrhsndssgavsismaerererereMFKTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCAR 332
Cdd:cd14544  50 -----------------------------NAKTYIATQGCLE----NTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVR 96

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 333 YWPDEGRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQ--PARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHL 410
Cdd:cd14544  97 YWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQgdPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESL 176

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639268 411 AQagekPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQT 489
Cdd:cd14544 177 PH----AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIET 251
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 284-489 9.16e-97

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: 298.47  E-value: 9.16e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14605  54 KSYIATQGCLQ----NTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRE 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQ--PARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGekpgPICVHCSAGIGRTGTFIVIDMIL 441
Cdd:cd14605 130 LKLSKVGQgnTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAG----PVVVHCSAGIGRTGTFIVIDILI 205

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24639268 442 DQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQT 489
Cdd:cd14605 206 DIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 76-489 6.89e-92

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: 286.39  E-value: 6.89e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  76 QQDSRDTFSRNEGYKQENRLKNRYRNILPYDHTRVKLLDVEHSVAGAEYINANYIRlptdgdlynmsssseslnssvpsc 155
Cdd:cd14606   1 KQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVK------------------------ 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 156 pactaaqtqrncsncqlqNKtcvqcavksailpysncatcsrksdslskhkrsessassspssgsgsgpgssgtsgvssV 235
Cdd:cd14606  57 ------------------NQ-----------------------------------------------------------L 59

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 236 NGPGTPTnltsgtagclvgllkrhsndssgavsismaererereremfKTYIATQGCLLTqqvnTVTDFWNMVWQENTRV 315
Cdd:cd14606  60 LGPDENA-----------------------------------------KTYIASQGCLEA----TVNDFWQMAWQENSRV 94

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 316 IVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFLVSW--RDQPARRIFHYHFQVWPDHGVPADP 393
Cdd:cd14606  95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPldNGELIREIWHYQYLSWPDHGVPSEP 174

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 394 GCVLNFLQDVNTRQSHLAQAGekpgPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTE 473
Cdd:cd14606 175 GGVLSFLDQINQRQESLPHAG----PIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTE 250

                       410
                ....*....|....*.
gi 24639268 474 AQYKFVYYAVQHYIQT 489
Cdd:cd14606 251 AQYKFIYVAIAQFIET 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
67-485 8.96e-89

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 277.62  E-value: 8.96e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268     67 GFWEEFESLQQDSRDTFSRNEGYKQENRLKNRYRNILPYDHTRVKLLDVEHSVAGaeYINANYIRLPTDGdlynmsssse 146
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSD--YINASYIDGPNGP---------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    147 slnssvpscpactaaqtqrncsncqlqnktcvqcavksailpysncatcsrksdslskhkrsessassspssgsgsgpgs 226
Cdd:smart00194     --------------------------------------------------------------------------------

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    227 sgtsgvssvngpgtptnltsgtagclvgllkrhsndssgavsismaererereremfKTYIATQGCLltqqVNTVTDFWN 306
Cdd:smart00194  69 ---------------------------------------------------------KAYIATQGPL----PSTVEDFWR 87

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    307 MVWQENTRVIVMTTKEYERGKEKCARYWPDE-GRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQP-ARRIFHYHFQVW 384
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSeTRTVTHYHYTNW 167

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    385 PDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQIVRNGldtEIDIQRTIQMVRS 464
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTST------GPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRS 238

                          410       420
                   ....*....|....*....|.
gi 24639268    465 QRSGLVQTEAQYKFVYYAVQH 485
Cdd:smart00194 239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
284-483 2.44e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 244.46  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268   284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDE-GRSEQFGHARIQCVSENS-TSDYTL 361
Cdd:pfam00102  42 KKYIATQGPL----PNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEEeGESLEYGDFTVTLKKEKEdEKDYTV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268   362 REFLVSWRDQPA-RRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqagEKPGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:pfam00102 118 RTLEVSNGGSEEtRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLD-----GRSGPIVVHCSAGIGRTGTFIAIDIA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 24639268   441 LDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:pfam00102 193 LQQLEAEG---EVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 284-481 9.92e-75

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: 238.72  E-value: 9.92e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSE-QFGHARIQCVSENSTSDYTLR 362
Cdd:cd00047  14 KEYIATQGPLP----NTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPlEYGDITVTLVSEEELSDYTIR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWRD-QPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqageKPGPICVHCSAGIGRTGTFIVIDMIL 441
Cdd:cd00047  90 TLELSPKGcSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK------PNGPIVVHCSAGVGRTGTFIAIDILL 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 442 DQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYY 481
Cdd:cd00047 164 ERLEAEG---EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 284-480 1.98e-63

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: 209.41  E-value: 1.98e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVS--ENSTSDYTL 361
Cdd:cd18533  15 KRYIATQGPL----PATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSeeENDDGGFIV 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 362 REFLVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNtrqsHLAQAGEKPGPICVHCSAGIGRTGTFIVIDMIL 441
Cdd:cd18533  91 REFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKR----ELNDSASLDPPIIVHCSAGVGRTGTFIALDSLL 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24639268 442 DQIVRNGLDT-----EID-IQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd18533 167 DELKRGLSDSqdledSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 284-480 2.59e-62

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: 206.43  E-value: 2.59e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14549  14 RAYIATQGPL----PSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEG-TETYGNIQVTLLSTEVLATYTVRT 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS------WRDQPA-RRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIV 436
Cdd:cd14549  89 FSLKnlklkkVKGRSSeRVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGA------GPIVVHCSAGVGRTGTYIV 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24639268 437 IDMILDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14549 163 IDSMLQQIQDKG---TVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 286-480 1.67e-58

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 196.81  E-value: 1.67e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14548  41 FIATQGPL----PGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFK 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQIV 445
Cdd:cd14548 117 LERGDE-VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQEK------GPTIVHCSAGVGRTGTFIALDRLLQQIE 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24639268 446 RNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14548 190 SEDY---VDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 284-481 1.81e-56

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: 191.46  E-value: 1.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERgKEKCARYWPDEgRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14547  41 KAYIATQGPL----PNTVADFWRMVWQEKTPIIVMITNLTEA-KEKCAQYWPEE-ENETYGDFEVTVQSVKETDGYTVRK 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNtrqsHLAQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14547 115 LTLKYGGE-KRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE----EARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQ 189

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24639268 444 IVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYY 481
Cdd:cd14547 190 LREEG---VVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 286-480 9.53e-56

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: 191.04  E-value: 9.53e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWP-DEGRSEQFGHARIQCVSENSTSDYTLREF 364
Cdd:cd14543  74 YIATQGPL----PKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPlEEGSSLRYGDLTVTNLSVENKEHYKKTTL 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 LV--SWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQA------GEKPG-PICVHCSAGIGRTGTFI 435
Cdd:cd14543 150 EIhnTETDE-SRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAmgdrwkGHPPGpPIVVHCSAGIGRTGTFC 228

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24639268 436 VIDMILDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14543 229 TLDICLSQLEDVG---TLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 286-483 3.02e-55

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: 187.58  E-value: 3.02e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQF--GHARIQCVSENSTSDYTLRE 363
Cdd:cd14538  18 YIACQGPLP----NTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLIcgGRLEVSLEKYQSLQDFVIRR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVswRDQPA---RRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:cd14538  94 ISL--RDKETgevHHITHLNFTTWPDHGTPQSADPLLRFIRYM--RRIHNS------GPIVVHCSAGIGRTGVLITIDVA 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24639268 441 LDQIVRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14538 164 LGLIER---DLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 286-483 9.40e-55

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: 186.38  E-value: 9.40e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14541  21 YIAAQGPL----PNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQITCVSEEVTPSFAFREFI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQP-ARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAQAgekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14541  97 LTNTNTGeERHITQMQYLAWPDHGVPDDSSDFLDFVKRV--RQNRVGMV----EPTVVHCSAGIGRTGVLITMETAMCLI 170

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLDTEIDIQRTIqmvRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14541 171 EANEPVYPLDIVRTM---RDQRAMLIQTPSQYRFVCEAI 206
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 284-480 1.60e-54

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: 185.32  E-value: 1.60e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSE-QFGHARIQCVSE-NSTSDYTL 361
Cdd:cd14542  14 KAYIATQGPL----PNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKISLEKEkRVGPDFLI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 362 REFLVSwRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqageKPGPICVHCSAGIGRTGTFIVIDMIL 441
Cdd:cd14542  90 RTLKVT-FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGS------EDVPICVHCSAGCGRTGTICAIDYVW 162

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 442 DQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14542 163 NLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 286-483 1.64e-53

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: 183.75  E-value: 1.64e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14553  48 YIATQGPLP----ETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQYWPTRG-TETYGLIQVTLLDTVELATYTVRTFA 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQPARR-IFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAQAgekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14553 123 LHKNGSSEKReVRQFQFTAWPDHGVPEHPTPFLAFLRRV--KACNPPDA----GPIVVHCSAGVGRTGCFIVIDSMLERI 196

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14553 197 KH---EKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 284-483 1.09e-50

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: 177.32  E-value: 1.09e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENS-TSDYTLR 362
Cdd:cd14603  73 RAYIATQGPL----SHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRlNEEVILR 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQshlaqaGEKPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14603 149 TLKVTFQKE-SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ------GSGPEPLCVHCSAGCGRTGVICTVDYVRQ 221

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24639268 443 QIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14603 222 LLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTV 262
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 284-480 1.47e-50

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: 175.66  E-value: 1.47e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWP-DEGRSEQFGHARIQC--VSENSTSDYT 360
Cdd:cd14545  39 RSYILTQGPL----PNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWPqGEGNAMIFEDTGLKVtlLSEEDKSYYT 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 361 LREF-LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAQAGEkpGPICVHCSAGIGRTGTFIVIDM 439
Cdd:cd14545 115 VRTLeLENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV--RESGSLSSDV--GPPVVHCSAGIGRSGTFCLVDT 190

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24639268 440 ILDQIVRNGLDtEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14545 191 CLVLIEKGNPS-SVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 284-482 3.85e-50

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: 174.63  E-value: 3.85e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14554  49 GAYIATQGPL----AETTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILRE 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS-WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntrQSHLAQAGEKpGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14554 124 FKVTdARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQV---HKTKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLE 199

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYA 482
Cdd:cd14554 200 RMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 286-483 6.13e-50

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: 173.18  E-value: 6.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14555  16 YIATQG----PMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD--TEVYGDIKVTLVETEPLAEYVVRTFA 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQPARR-IFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14555  90 LERRGYHEIReVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSA------GPIVVHCSAGAGRTGCYIVIDIMLDMA 163

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14555 164 EREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 286-487 1.45e-49

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 172.64  E-value: 1.45e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEG---RSEQFGHARIQCVSENSTSDYTLR 362
Cdd:cd14540  18 YIAAQGPL----QNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehDALTFGEYKVSTKFSVSSGCYTTT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVswRDQPARR---IFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAG---EKPGPICVHCSAGIGRTGTFIV 436
Cdd:cd14540  94 GLRV--KHTLSGQsrtVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVaghNRNPPTLVHCSAGVGRTGVVIL 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24639268 437 IDMILDQIVRNgldTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYI 487
Cdd:cd14540 172 ADLMLYCLDHN---EELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 286-484 2.74e-49

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: 171.30  E-value: 2.74e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14552  16 YIATQGPLD----HTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG-SVSSGDITVELKDQTDYEDYTLRDFL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSW-RDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14552  91 VTKgKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGN-----HPITVHCSAGAGRTGTFCALSTVLERV 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 445 VRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQ 484
Cdd:cd14552 166 KAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 284-488 6.27e-49

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: 173.58  E-value: 6.27e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSE-QFGHARIQCVSENSTSDYTLR 362
Cdd:cd14604 100 KAYIATQGPL----ANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPmTFGPFRISCEAEQARTDYFIR 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWrDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqageKPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14604 176 TLLLEF-QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEH------EDVPICIHCSAGCGRTGAICAIDYTWN 248

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24639268 443 QIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:cd14604 249 LLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 286-483 6.33e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 170.32  E-value: 6.33e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENS-TSDYTLREF 364
Cdd:cd14546  17 YIATQGPL----PHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEG-SEVYHIYEVHLVSEHIwCDDYLVRSF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 -LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQagekpgPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14546  92 yLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC------PIVVHCSDGAGRTGTYILIDMVLNR 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 444 IVRNGldTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14546 166 MAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 284-483 1.09e-48

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: 170.79  E-value: 1.09e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSE-QFGHARIQCVSENSTSDYTLR 362
Cdd:cd14602  41 RAYIATQGPL----STTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYWAEPGEMQlEFGPFSVTCEAEKRKSDYIIR 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqagEKPgPICVHCSAGIGRTGTFIVIDMILd 442
Cdd:cd14602 117 TLKVKFNSE-TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQED-----DSV-PICIHCSAGCGRTGVICAIDYTW- 188

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24639268 443 QIVRNGLDTE-IDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14602 189 MLLKDGIIPEnFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 284-480 1.82e-48

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 169.71  E-value: 1.82e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14617  40 REYIATQGPL----PGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIRE 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQ--PARRIFHYHFQVWPDHGVPADPGCVLNFlqdVNTRQSHLAQAgEKPGPICVHCSAGIGRTGTFIVIDMIL 441
Cdd:cd14617 116 FKICSEEQldAPRLVRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYINRT-PGSGPTVVHCSAGVGRTGTFIALDRIL 191

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 442 DQIVRNglDTeIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14617 192 QQLDSK--DS-VDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 284-479 2.20e-48

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: 169.61  E-value: 2.20e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14615  39 KEFIAAQGPL----PNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRD 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQPARR-IFHYHFQVWPDHGVPADPGCVLNFLQDVntrQSHLAQAgEKPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14615 114 FTVKNAQTNESRtVRHFHFTSWPDHGVPETTDLLINFRHLV---REYMKQN-PPNSPILVHCSAGVGRTGTFIAIDRLIY 189

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24639268 443 QIVRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFV 479
Cdd:cd14615 190 QIEN---ENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 286-483 5.20e-48

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: 168.86  E-value: 5.20e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLTqqvnTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQ--CVSENSTSDYTLRE 363
Cdd:cd14597  45 YIACQGPLPT----TVADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPEILGKTTMVDNRLQltLVRMQQLKNFVIRV 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 F-LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14597 121 LeLEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYM--RHIHKS------GPIITHCSAGIGRSGTLICIDVVLG 192

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24639268 443 QIVRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14597 193 LISK---DLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 286-480 2.98e-47

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: 165.47  E-value: 2.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14551  16 FIAAQG----PKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQG-CWTYGNLRVRVEDTVVLVDYTTRKFC 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VS-----WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:cd14551  91 IQkvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRA------GPIVVHCSAGVGRTGTFIVIDAM 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 441 LDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14551 165 LDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 284-490 8.08e-47

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: 167.60  E-value: 8.08e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14628  95 KAYIATQGPL----AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILRE 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS-WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQagekPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14628 170 FKVTdARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ----DGPISVHCSAGVGRTGVFITLSIVLE 245

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQTL 490
Cdd:cd14628 246 RMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSF 290
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 284-487 1.87e-46

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: 166.45  E-value: 1.87e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14627  96 KAYIATQGPL----AETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILRE 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS-WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQagekPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14627 171 FKVTdARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ----DGPISVHCSAGVGRTGVFITLSIVLE 246

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYI 487
Cdd:cd14627 247 RMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 284-480 2.54e-46

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: 164.29  E-value: 2.54e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14619  40 QEFIATQGPL----PQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVRE 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLV-SWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQsHLAQAGEKpGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14619 116 FLLkQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLL--RQ-WLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQ 191

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14619 192 QLQSEGL---LGPFSFVQKMRENRPLMVQTESQYVFLH 226
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 286-483 2.75e-46

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: 163.30  E-value: 2.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14632  16 FIATQG----PKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD--SDTYGDIKITLLKTETLAEYSVRTFA 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQPAR-RIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14632  90 LERRGYSARhEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDA------GPVVVHCSAGAGRTGCYIVLDVMLDMA 163

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14632 164 ECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 286-484 8.22e-46

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 163.14  E-value: 8.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14614  57 YIATQGPL----PETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFR 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQpARRIFHYHFQVWPDHGVPADPGC--VLNFLQDVntRQshlaQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14614 133 VSYADE-VQDVMHFNYTAWPDHGVPTANAAesILQFVQMV--RQ----QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQH 205

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24639268 444 IvrngLDTE-IDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQ 484
Cdd:cd14614 206 I----RDHEfVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 256-499 1.15e-45

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: 164.04  E-value: 1.15e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 256 LKRHSNDSSGAVSISMAERErereremfKTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWP 335
Cdd:cd14608  44 LHQEDNDYINASLIKMEEAQ--------RSYILTQGPL----PNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWP 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 336 DEGRSEQF---GHARIQCVSENSTSDYTLREF-LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQShlA 411
Cdd:cd14608 112 QKEEKEMIfedTNLKLTLISEDIKSYYTVRQLeLENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKV--RES--G 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 412 QAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQTLI 491
Cdd:cd14608 188 SLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIM 267


                ....*...
gi 24639268 492 ARKRAEEQ 499
Cdd:cd14608 268 GDSSVQDQ 275
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 284-486 1.28e-45

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: 162.70  E-value: 1.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERgKEKCARYWPD-EGRSEQFGhARIQCVSEnsTSDYTLR 362
Cdd:cd14612  60 KAYIATQGPML----NTVSDFWEMVWQEECPIIVMITKLKEK-KEKCVHYWPEkEGTYGRFE-IRVQDMKE--CDGYTIR 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQshlaQAGEKPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14612 132 DLTIQLEEE-SRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESR----QTAASPGPIVVHCSAGIGRTGCFIATSIGCQ 206

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24639268 443 QIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHY 486
Cdd:cd14612 207 QLKDTG---KVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLALY 247
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 286-483 2.01e-45

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: 161.65  E-value: 2.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14620  40 FIAAQG----PKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQYWPDQG-CWTYGNIRVAVEDCVVLVDYTIRKFC 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWR----DQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMIL 441
Cdd:cd14620 115 IQPQlpdgCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPVHA------GPIVVHCSAGVGRTGTFIVIDAMI 188

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24639268 442 DQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14620 189 DMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 284-483 2.75e-45

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: 160.53  E-value: 2.75e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLTqqvnTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd17668  14 KAYIAAQGPLKS----TAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADG-SEEYGNFLVTQKSVQVLAYYTVRN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLV--------SWRDQPARRIF-HYHFQVWPDHGVPADPGCVLNFLqdvntRQSHLAQAGEKpGPICVHCSAGIGRTGTF 434
Cdd:cd17668  89 FTLrntkikkgSQKGRPSGRVVtQYHYTQWPDMGVPEYTLPVLTFV-----RKASYAKRHAV-GPVVVHCSAGVGRTGTY 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24639268 435 IVIDMILDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd17668 163 IVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 286-483 6.91e-45

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: 159.80  E-value: 6.91e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14631  30 YIATQGPVH----ETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD--TEVYGDFKVTCVEMEPLAEYVVRTFT 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRD-QPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14631 104 LERRGyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA------GPIVVHCSAGAGRTGCYIVIDIMLDMA 177

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14631 178 EREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 284-487 7.40e-45

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: 161.74  E-value: 7.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLTqqvnTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd17667  72 KAYIATQGPLKS----TFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN-SEEYGNIIVTLKSTKIHACYTVRR 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRD------------QPARRIFHYHFQVWPDHGVPADPGCVLNFLqdvntRQSHLAQAGEKpGPICVHCSAGIGRT 431
Cdd:cd17667 147 FSIRNTKvkkgqkgnpkgrQNERTVIQYHYTQWPDMGVPEYALPVLTFV-----RRSSAARTPEM-GPVLVHCSAGVGRT 220

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24639268 432 GTFIVIDMILDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYI 487
Cdd:cd17667 221 GTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 286-486 1.07e-44

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: 158.63  E-value: 1.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14622  17 FIATQGPL----AHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG-SVTHGEITIEIKNDTLLETISIRDFL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSW-RDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQShlaQAGEKpgPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14622  92 VTYnQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQ---QTGNH--PIVVHCSAGAGRTGTFIALSNILERV 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24639268 445 VRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHY 486
Cdd:cd14622 167 KAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 286-487 1.11e-44

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: 161.73  E-value: 1.11e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14621  97 FIAAQG----PKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQG-CWTYGNIRVSVEDVTVLVDYTVRKFC 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSW-----RDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:cd14621 172 IQQvgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA------GAIVVHCSAGVGRTGTFIVIDAM 245

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24639268 441 LDQIvrnGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYA-VQHYI 487
Cdd:cd14621 246 LDMM---HAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAlLEHYL 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 284-490 1.85e-44

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: 161.05  E-value: 1.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14629  96 KAYIATQGPL----AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILRE 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS-WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQagekPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14629 171 FKVTdARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQ----DGPITVHCSAGVGRTGVFITLSIVLE 246

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQTL 490
Cdd:cd14629 247 RMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 284-483 2.30e-44

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 159.04  E-value: 2.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14630  46 RHYIATQGPMQ----ETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDD--TEVYGDIKVTLIETEPLAEYVIRT 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWR-DQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14630 120 FTVQKKgYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDA------GPIVVHCSAGAGRTGCFIAIDIMLD 193

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14630 194 MAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 286-480 3.39e-44

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 158.18  E-value: 3.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14618  42 FIATQGPL----KKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFK 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRD-QPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntrQSHLaQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14618 118 LWHEDlRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV---REHV-QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQL 193

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24639268 445 VRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14618 194 KE---EKVVDVFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 286-483 3.70e-44

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: 157.41  E-value: 3.70e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREF- 364
Cdd:cd14601  21 YIACQGPL----PNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVTCHSEEGNPAYVFREMt 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqageKPGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14601  97 LTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAG------KDEPVVVHCSAGIGRTGVLITMETAMCLI 170

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLDTEIDIQRTIqmvRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14601 171 ECNQPVYPLDIVRTM---RDQRAMMIQTPSQYRFVCEAI 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 286-480 3.86e-44

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: 157.24  E-value: 3.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGK-EKCARYWPD-EGRSEQFGHARIQCVSENSTSD-YTLR 362
Cdd:cd17658  18 FIATQGPL----PHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTNKKLKHSQHsITLR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWRD--QPARRIFHYHFQVWPDHGVPADPGCVLNFLQdvntRQSHLAQAGekpGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:cd17658  94 VLEVQYIEseEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK----RLYGIPPSA---GPIVVHCSAGIGRTGAYCTIHNT 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 441 LDQIVRNGLdTEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd17658 167 IRRILEGDM-SAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 284-484 8.39e-44

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: 157.13  E-value: 8.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14623  39 DSYIASQGPLQ----HTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDG-SVSYGDITIELKKEEECESYTVRD 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS-WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQShlaQAGEKpgPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14623 114 LLVTnTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ---QSGNH--PITVHCSAGAGRTGTFCALSTVLE 188

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQ 484
Cdd:cd14623 189 RVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 286-483 2.53e-43

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: 157.51  E-value: 2.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENS-TSDYTLREF 364
Cdd:cd14609  88 YIATQGPL----SHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG-SSLYHIYEVNLVSEHIwCEDFLVRSF 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 -LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNtrQSHLAQAgekpGPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14609 163 yLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVN--KCYRGRS----CPIIVHCSDGAGRTGTYILIDMVLNR 236

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 444 IVRnGLdTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14609 237 MAK-GV-KEIDIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 286-488 5.57e-43

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: 154.13  E-value: 5.57e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDE-GRSEQFGHARIQCVSENSTSDYTLREF 364
Cdd:cd14596  18 YIATQGPLP----STIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLENYQALQYFIIRII 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 -LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14596  94 kLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYM--RKVHNT------GPIVVHCSAGIGRAGVLICVDVLLSL 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24639268 444 IVRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:cd14596 166 IEK---DLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 286-483 1.48e-42

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: 155.19  E-value: 1.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14626  86 YIATQGPL----PETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRG-TETYGMIQVTLLDTVELATYSVRTFA 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQPARR-IFHYHFQVWPDHGVPADPGCVLNFLQDVNtrqshlAQAGEKPGPICVHCSAGIGRTGTFIVIDMILDqi 444
Cdd:cd14626 161 LYKNGSSEKReVRQFQFMAWPDHGVPEYPTPILAFLRRVK------ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE-- 232

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 vRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14626 233 -RMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 286-483 1.91e-42

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: 155.01  E-value: 1.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14600  84 YIATQGPL----PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREML 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VS-WRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQshlaQAGEkpgPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14600 160 LTnTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKR----VENE---PVLVHCSAGIGRTGVLVTMETAMCLT 232

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLDTEIDIQRTIqmvRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14600 233 ERNQPVYPLDIVRKM---RDQRAMMVQTSSQYKFVCEAI 268
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 284-480 1.93e-42

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: 152.29  E-value: 1.93e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPD-EGRSEQFGHARIQCVSENSTSDYTLR 362
Cdd:cd14557  14 RKYIAAQG----PKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEEKICPDYIIR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 EFLVSWRDQP--ARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMI 440
Cdd:cd14557  90 KLNINNKKEKgsGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFS------GPIVVHCSAGVGRTGTYIGIDAM 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 441 LDQIVRNGldtEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14557 164 LEGLEAEG---RVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 286-483 2.01e-42

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 154.82  E-value: 2.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEgrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14633  85 YIATQGPMQ----ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD--TEIYKDIKVTLIETELLAEYVIRTFA 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRD-QPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14633 159 VEKRGvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNA------GPLVVHCSAGAGRTGCFIVIDIMLDMA 232

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14633 233 EREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 286-490 2.35e-42

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: 154.83  E-value: 2.35e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLTqqvnTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENS-TSDYTLREF 364
Cdd:cd14610  90 YIATQGPLPA----TVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEG-SNLYHIYEVNLVSEHIwCEDFLVRSF 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 -LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTrqshlAQAGeKPGPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14610 165 yLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNK-----CYRG-RSCPIIVHCSDGAGRSGTYILIDMVLNK 238

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24639268 444 IVRNGldTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQTL 490
Cdd:cd14610 239 MAKGA--KEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 284-483 6.14e-42

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: 152.81  E-value: 6.14e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHA---RIQCVSENSTSDYT 360
Cdd:cd14607  63 RSYILTQGPL----PNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgfSVKLLSEDVKSYYT 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 361 LREF-LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQShlAQAGEKPGPICVHCSAGIGRTGTFIVIDM 439
Cdd:cd14607 139 VHLLqLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV--RES--GSLSPEHGPAVVHCSAGIGRSGTFSLVDT 214

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24639268 440 ILDQIVRNGLDTeIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14607 215 CLVLMEKKDPDS-VDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 284-486 1.33e-41

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: 151.94  E-value: 1.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGclltQQVNTVTDFWNMVWQENTRVIVMTTKeYERGKEKCARYWPDEgrSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14613  70 KVYIATQG----PTVNTVGDFWRMVWQERSPIIVMITN-IEEMNEKCTEYWPEE--QVTYEGIEITVKQVIHADDYRLRL 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSwRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVN-TRQshlaQAGEKPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14613 143 ITLK-SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEeARQ----QAEPNCGPVIVHCSAGIGRTGCFIATSICCK 217

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24639268 443 QIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHY 486
Cdd:cd14613 218 QLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 285-480 1.65e-40

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: 147.15  E-value: 1.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 285 TYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDE-GRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14539  16 RFIATQAPL----PGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQSVRTTPTHVERI 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQPARR-IFHYHFQVWPDHGVPADPGCVLNFLQDVntrQSHLAQAGEKPGPICVHCSAGIGRTGTF-IVIDMIL 441
Cdd:cd14539  92 ISIQHKDTRLSRsVVHLQFTTWPELGLPDSPNPLLRFIEEV---HSHYLQQRSLQTPIVVHCSSGVGRTGAFcLLYAAVQ 168

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 442 DQIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14539 169 EIEAGNGI---PDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 284-480 2.21e-39

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: 144.07  E-value: 2.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSeqFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14558  14 KSLIATQGPL----PDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTEKSPTYTVRV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQPA-RRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGEKPGPICVHCSAGIGRTGTFIVIDMILD 442
Cdd:cd14558  88 FEITHLKRKDsRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGRSVPIVVHCSDGSSRTGIFCALWNLLE 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24639268 443 QIvrnglDTE--IDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14558 168 SA-----ETEkvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 284-481 3.11e-39

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: 144.29  E-value: 3.11e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERgKEKCARYWPDegRSEQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14611  44 KAFIATQGPM----INTVNDFWQMVWQEDSPVIVMITKLKEK-NEKCVLYWPE--KRGIYGKVEVLVNSVKECDNYTIRN 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVSWRDQpARRIFHYHFQVWPDHGVPADPGCVLNFLQDVntRQSHLAQAGEkpGPICVHCSAGIGRTGTFIVIDMILDQ 443
Cdd:cd14611 117 LTLKQGSQ-SRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV--EEDRLASPGR--GPVVVHCSAGIGRTGCFIATTIGCQQ 191

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24639268 444 IVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYY 481
Cdd:cd14611 192 LKEEGV---VDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 286-483 5.33e-39

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: 145.64  E-value: 5.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREF- 364
Cdd:cd14624  92 YIATQGAL----PETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG-TETYGLIQVTLLDTVELATYCVRTFa 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 LVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14624 167 LYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDA------GPMVVHCSAGVGRTGCFIVIDAMLERI 240

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14624 241 KH---EKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 286-483 6.66e-39

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: 145.24  E-value: 6.66e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFL 365
Cdd:cd14625  92 YIATQGPL----PETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG-TETYGMIQVTLLDTIELATFCVRTFS 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 366 VSWRDQPARR-IFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAqagekpGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14625 167 LHKNGSSEKReVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDA------GPIVVHCSAGVGRTGCFIVIDAMLERI 240

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24639268 445 VRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd14625 241 KH---EKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 286-488 5.96e-38

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: 140.50  E-value: 5.96e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEG-RSEQFGHARIQCVSE-------NSTS 357
Cdd:cd14598  18 YIATQGPL----QNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsRHNTVTYGRFKITTRfrtdsgcYATT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 358 DYTLREFLVSWRdqpaRRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGEKPG---PICVHCSAGIGRTGTF 434
Cdd:cd14598  94 GLKIKHLLTGQE----RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSpnpPVLVHCSAGVGRTGVV 169

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24639268 435 IVIDMILDQIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:cd14598 170 ILSEIMIACLEHNEM---LDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 286-480 2.25e-36

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: 136.19  E-value: 2.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRS-EQFGHARIQCVSENSTSDYTLREF 364
Cdd:cd14616  42 FIATQGPL----PGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPEDNKPvTVFGDIVITKLMEDVQIDWTIRDL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 365 LVSwRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHlaqageKPGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:cd14616 118 KIE-RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRAH------DNTPMIVHCSAGVGRTGVFIALDHLTQHI 190

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24639268 445 vrNGLDTeIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14616 191 --NDHDF-VDIYGLVAELRSERMCMVQNLAQYIFLH 223
PHA02738 PHA02738
hypothetical protein; Provisional
 284-488 6.11e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 138.13  E-value: 6.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  284 KTYIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPD-EGRSEQFGHARIQCVSENSTSDYTLR 362
Cdd:PHA02738  90 KKFICGQAPTR----QTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVKS 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  363 EFLVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLA----QAGEK---PGPICVHCSAGIGRTGTFI 435
Cdd:PHA02738 166 TLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAqeslQIGHNrlqPPPIVVHCNAGLGRTPCYC 245

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24639268  436 VIDMildQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:PHA02738 246 VVDI---SISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 286-488 3.82e-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: 134.74  E-value: 3.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEG---RSEQFGHARIQCVSENSTSDYTLR 362
Cdd:cd14599  84 YIATQGPL----PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskhSSATYGKFKVTTKFRTDSGCYATT 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 363 ----EFLVSWRDqpaRRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSH----LAQAGEKPGPICVHCSAGIGRTGTF 434
Cdd:cd14599 160 glkvKHLLSGQE---RTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHtnsmLDSTKNCNPPIVVHCSAGVGRTGVV 236

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24639268 435 IVIDMILDQIVRNgldTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:cd14599 237 ILTELMIGCLEHN---EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
378-483 9.34e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.48  E-value: 9.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    378 HYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGekpgPICVHCSAGIGRTGTFIVIDMILDQIvRNGlDTEIDIQR 457
Cdd:smart00404   4 HYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSG----PVVVHCSAGVGRTGTFVAIDILLQQL-EAE-AGEVDIFD 77

                           90       100
                   ....*....|....*....|....*.
gi 24639268    458 TIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:smart00404  78 TVKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 378-483 9.34e-35

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: 127.48  E-value: 9.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268    378 HYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGekpgPICVHCSAGIGRTGTFIVIDMILDQIvRNGlDTEIDIQR 457
Cdd:smart00012   4 HYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSG----PVVVHCSAGVGRTGTFVAIDILLQQL-EAE-AGEVDIFD 77

                           90       100
                   ....*....|....*....|....*.
gi 24639268    458 TIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:smart00012  78 TVKELRSQRPGMVQTEEQYLFLYRAL 103
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 284-480 1.60e-33

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 127.52  E-value: 1.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTkEYERGKEKCARYWPDEGRSeQFGHARIQCVSENSTSDYTLRE 363
Cdd:cd14556  14 AAFIVTQHPL----PNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGSG-TYGPIQVEFVSTTIDEDVISRI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 364 FLVS--WRDQPARRIFHyHFQV--WPDHG-VPADPGCVLNFLQDVNTRQshlAQAGEkpGPICVHCSAGIGRTGTFIVID 438
Cdd:cd14556  88 FRLQntTRPQEGYRMVQ-QFQFlgWPRDRdTPPSKRALLKLLSEVEKWQ---EQSGE--GPIVVHCLNGVGRSGVFCAIS 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24639268 439 MILDQIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14556 162 SVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 292-487 3.11e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 127.45  E-value: 3.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  292 CLLTQQVNTVTDFWNMVWQENTRVIVMTTkEYERGKEKCARYWPDEGRSE-QFGH--ARIQCVSENSTSDYTlREFLVSW 368
Cdd:PHA02746 117 CAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTKEEDSElAFGRfvAKILDIIEELSFTKT-RLMITDK 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  369 RDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGE----KPGPICVHCSAGIGRTGTFIVIDMILDQI 444
Cdd:PHA02746 195 ISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADndpqTLGPIVVHCSAGIGRAGTFCAIDNALEQL 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24639268  445 VRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYI 487
Cdd:PHA02746 275 EK---EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 284-487 2.10e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 118.95  E-value: 2.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  284 KTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVM-TTKEYERGKEKCARYW-PDEGRSEQFGHARIQCVSENSTSDYTL 361
Cdd:PHA02747  93 KKFIATQGPF----AETCADFWKAVWQEHCSIIVMlTPTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYIL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  362 REFLVSWRD-QPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVN-TRQSHLAQAGEKPG---PICVHCSAGIGRTGTFIV 436
Cdd:PHA02747 169 TLIEITDKIlKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDiNRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCA 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24639268  437 IDMILDQIVrngLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVY--YAVQHYI 487
Cdd:PHA02747 249 VDICLNQLV---KRKAICLAKTAEKIREQRHAGIMNFDDYLFIQpgYEVLHYF 298
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
284-490 6.63e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 116.73  E-value: 6.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 284 KTYIATQGCLLTQQVntvtDFWNMVWQENTRVIVMTT--KEYERGKEKCARYWPDEGRseqfgHARIQCVSENSTSDY-- 359
Cdd:COG5599  77 HRYIATQYPLEEQLE----DFFQMLFDNNTPVLVVLAsdDEISKPKVKMPVYFRQDGE-----YGKYEVSSELTESIQlr 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 360 ---TLREFLVSWRD--QPARRIFHYHFQVWPDHGvPADPGCVLNFLQDVNtrqsHLAQAGEKP-GPICVHCSAGIGRTGT 433
Cdd:COG5599 148 dgiEARTYVLTIKGtgQKKIEIPVLHVKNWPDHG-AISAEALKNLADLID----KKEKIKDPDkLLPVVHCRAGVGRTGT 222

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24639268 434 FIVIdMILDQIVRNGLDTEIDIQRT-IQMVRSQRSGLVQTEAQY-KFVYYAVQHYIQTL 490
Cdd:COG5599 223 LIAC-LALSKSINALVQITLSVEEIvIDMRTSRNGGMVQTSEQLdVLVKLAEQQIRPLL 280
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 282-490 3.00e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 115.48  E-value: 3.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  282 MFKTYIATQGCLltqqVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSE-QFGHARIQCVSENSTSDYT 360
Cdd:PHA02742  91 AKGRFICTQAPL----EETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKaTHGEFKIKTKKIKSFRNYA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  361 LREFLVSWRDQPAR-RIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQS--HLAQAGE---KPGPICVHCSAGIGRTGTF 434
Cdd:PHA02742 167 VTNLCLTDTNTGASlDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLkaDVDIKGEnivKEPPILVHCSAGLDRAGAF 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24639268  435 IVIDMILDQIVRNGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQTL 490
Cdd:PHA02742 247 CAIDICISKYNERAI---IPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
SH2_C-SH2_SHP_like cd09931
C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The ...
 1-48 1.31e-22

C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The SH2 domain phosphatases (SHP-1, SHP-2/Syp, Drosophila corkscrew (csw), and Caenorhabditis elegans Protein Tyrosine Phosphatase (Ptp-2)) are cytoplasmic signaling enzymes. They are both targeted and regulated by interactions of their SH2 domains with phosphotyrosine docking sites. These proteins contain two SH2 domains (N-SH2, C-SH2) followed by a tyrosine phosphatase (PTP) domain, and a C-terminal extension. Shp1 and Shp2 have two tyrosyl phosphorylation sites in their C-tails, which are phosphorylated differentially by receptor and nonreceptor PTKs. Csw retains the proximal tyrosine and Ptp-2 lacks both sites. Shp-binding proteins include receptors, scaffolding adapters, and inhibitory receptors. Some of these bind both Shp1 and Shp2 while others bind only one. Most proteins that bind a Shp SH2 domain contain one or more immuno-receptor tyrosine-based inhibitory motifs (ITIMs): [SIVL]xpYxx[IVL]. Shp1 N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, and is thus believed to regulate the phosphatase activity of SHP-1. Its C-SH2 domain is thought to be involved in searching for phosphotyrosine activators. The SHP2 N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. The C-SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation. Csw SH2 domain function is essential, but either SH2 domain can fulfill this requirement. The role of the csw SH2 domains during Sevenless receptor tyrosine kinase (SEV) signaling is to bind Daughter of Sevenless rather than activated SEV. Ptp-2 acts in oocytes downstream of sheath/oocyte gap junctions to promote major sperm protein (MSP)-induced MAP Kinase (MPK-1) phosphorylation. Ptp-2 functions in the oocyte cytoplasm, not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation. It is thought that MSP triggers PTP-2/Ras activation and ROS production to stimulate MPK-1 activity essential for oocyte maturation and that secreted MSP domains and Cu/Zn superoxide dismutases function antagonistically to control ROS and MAPK signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198185  Cd Length: 99  Bit Score: 92.73  E-value: 1.31e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24639268   1 MIRWQDKKYDVGGGESFGTLSELIDHYKRNPMVETCGTVVHLRQPFNA 48
Cdd:cd09931  52 MIRCQGGKYDVGGGEEFDSLTDLVEHYKKNPMVETSGTVVHLKQPLNA 99
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 299-480 4.05e-20

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: 89.31  E-value: 4.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 299 NTVTDFWNMVWQENTRVIVMTTKEyeRGKEKCARYWPdEGRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQPA---RR 375
Cdd:cd14634  25 NTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWP-EKTSCCYGPIQVEFVSADIDEDIISRIFRICNMARPQdgyRI 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 376 IFHYHFQVWPDH-GVPADPGCVLNFLQDVNTRQShlaQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLdteID 454
Cdd:cd14634 102 VQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQE---QYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---ID 175

                       170       180
                ....*....|....*....|....*.
gi 24639268 455 IQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14634 176 VFHTVKTLRNNKSNMVETLEQYKFVY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 286-480 5.87e-19

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: 85.45  E-value: 5.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYErgKEKCARYWPDEGRSEQFGHARIQCVSE-----NSTSDYT 360
Cdd:cd14550  16 FIITQHPLE----HTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPTKEKPLECETFKVTLSGEdhsclSNEIRLI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 361 LREFLV-SWRDQPARRIFHYHFQVWPDHGVPadPGCVLNFLQDVntrQSHLAQageKPGPICVHCSAGIGRTGTFIVIDM 439
Cdd:cd14550  90 VRDFILeSTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTV---QEWAQQ---RDGPIVVHDRYGGVQAATFCALTT 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24639268 440 ILDQivrngLDTE--IDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14550 162 LHQQ-----LEHEssVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 299-480 2.75e-17

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: 80.84  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 299 NTVTDFWNMVWQENTRVIVMTTK-EYERGkekCARYWPDEGrSEQFGHARIQCVSENSTSDYTLREFLVSWRDQPAR--- 374
Cdd:cd14636  25 NTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWPEEG-MLRYGPIQVECMSCSMDCDVISRIFRICNLTRPQEgyl 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 375 RIFHYHFQVWPDH-GVPADPGCVLNFLQDVNTRQShlaQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLdteI 453
Cdd:cd14636 101 MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQE---ECDEGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---V 174

                       170       180
                ....*....|....*....|....*..
gi 24639268 454 DIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14636 175 DVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 299-480 1.91e-16

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 78.41  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 299 NTVTDFWNMVWQENTRVIVMTTKEYERGKE-KCARYWPDEGRsEQFGHARIQCVSENSTSDYTLREFLVS--WRDQPARR 375
Cdd:cd14637  25 NTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGL-QQYGPMEVEFVSGSADEDIVTRLFRVQniTRLQEGHL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 376 IF-HYHFQVW-PDHGVPADPGCVLNFLQDVNTRQshlAQAGEkpGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLdteI 453
Cdd:cd14637 104 MVrHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQ---RESGE--GRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---V 175

                       170       180
                ....*....|....*....|....*..
gi 24639268 454 DIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14637 176 DVFYAVKTLRNYKPNMVETLEQYRFCY 202
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 292-488 3.62e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 79.63  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  292 CLLTQQVNTVTDFWNMVWQENTRVIVMTTKEYErgKEKCARYWP-DEGRSEQFGHARIQCVSENSTSDYTLRefLVSWRD 370
Cdd:PHA02740  95 CIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCFNQFWSlKEGCVITSDKFQIETLEIIIKPHFNLT--LLSLTD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268  371 Q--PARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQ--AGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVR 446
Cdd:PHA02740 171 KfgQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKhkADGKIAPIIIDCIDGISSSAVFCVFDICATEFDK 250

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24639268  447 NGLdteIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQ 488
Cdd:PHA02740 251 TGM---LSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 286-483 1.48e-14

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: 73.10  E-value: 1.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 286 YIATQGCLLtqqvNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCArYWPDEGRS---EQFGHARI--QCVSENSTSDYT 360
Cdd:cd17669  16 FIITQHPLL----HTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPincETFKVTLIaeEHKCLSNEEKLI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 361 LREFLV-SWRDQPARRIFHYHFQVWPDHGVPADPGC-VLNFLQDvntrqshlaQAGEKPGPICVHCSAGIGRTGTFIVID 438
Cdd:cd17669  91 IQDFILeATQDDYVLEVRHFQCPKWPNPDSPISKTFeLISIIKE---------EAANRDGPMIVHDEHGGVTAGTFCALT 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24639268 439 MILDQIVRnglDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd17669 162 TLMHQLEK---ENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 282-480 4.22e-13

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: 68.95  E-value: 4.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 282 MFKTYIATQGCLLTQQV--NTVTDFWNMVWQENTRVIVMTTKEyeRGKEKCARYWPDEGrSEQFGHARIQCVSENSTSDY 359
Cdd:cd14635   6 LMDSYKQPSAFIVTQHPlpNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENG-VHRHGPIQVEFVSADLEEDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 360 TLREFLVSWRDQPA---RRIFHYHFQVWPDH-GVPADPGCVLNFLQDVNTRQSHLaQAGEkpGPICVHCSAGIGRTGTFI 435
Cdd:cd14635  83 ISRIFRIYNAARPQdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEY-NGGE--GRTVVHCLNGGGRSGTFC 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24639268 436 VIDMILDQIVRNgldTEIDIQRTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14635 160 AISIVCEMLRHQ---RAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
361-486 2.48e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.91  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 361 LREFLVSWRDQPARRIFHYHFqVWPDHGVPADpgcvlnflQDVNTRQSHLAQAGEKPGPICVHCSAGIGRTGTFIVidMI 440
Cdd:COG2453  33 TEEEELLLGLLEEAGLEYLHL-PIPDFGAPDD--------EQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAA--AY 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24639268 441 LdqiVRNGLDTEidiqRTIQMVRSQRSGLVQTEAQYKFVYYAVQHY 486
Cdd:COG2453 102 L---VLLGLSAE----EALARVRAARPGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 410-481 1.29e-09

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 56.20  E-value: 1.29e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639268 410 LAQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIvrngldteIDIQRTIQMVRSQR-SGLVQTEAQYKFVYY 481
Cdd:cd14494  49 LDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGG--------MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 374-479 3.30e-09

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 55.75  E-value: 3.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 374 RRIFHYHFQVwPDHGVPADPGcVLNFLQDVNtrqshlaQAGEKPGPICVHCSAGIGRTGTfividMILDQIVRNGLDTEI 453
Cdd:cd14504  48 PGLRYHHIPI-EDYTPPTLEQ-IDEFLDIVE-------EANAKNEAVLVHCLAGKGRTGT-----MLACYLVKTGKISAV 113

                        90       100
                ....*....|....*....|....*.
gi 24639268 454 DiqrTIQMVRSQRSGLVQTEAQYKFV 479
Cdd:cd14504 114 D---AINEIRRIRPGSIETSEQEKFV 136
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 299-483 3.46e-09

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: 57.38  E-value: 3.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 299 NTVTDFWNMVWQENTRVIVMTTKEYERGKEKCArYWPDEGRS---EQFGHARIQ----CVSenSTSDYTLREFLV-SWRD 370
Cdd:cd17670  25 HTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREESmncEAFTVTLISkdrlCLS--NEEQIIIHDFILeATQD 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 371 QPARRIFHYHFQVWPDHGVPADPGC-VLNFLQDvntrqshlaQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVRngl 449
Cdd:cd17670 102 DYVLEVRHFQCPKWPNPDAPISSTFeLINVIKE---------EALTRDGPTIVHDEFGAVSAGTLCALTTLSQQLEN--- 169

                       170       180       190
                ....*....|....*....|....*....|....
gi 24639268 450 DTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAV 483
Cdd:cd17670 170 ENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 373-479 9.08e-09

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 55.82  E-value: 9.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 373 ARRIFHYHFQvWPDHGVPAdpgcvLNFLQDVntrQSHLAQAGEKPGPICVHCSAGIGRTGTFIVIDMIldqivrngLDTE 452
Cdd:cd14506  74 RAGIYFYNFG-WKDYGVPS-----LTTILDI---VKVMAFALQEGGKVAVHCHAGLGRTGVLIACYLV--------YALR 136

                        90       100
                ....*....|....*....|....*..
gi 24639268 453 IDIQRTIQMVRSQRSGLVQTEAQYKFV 479
Cdd:cd14506 137 MSADQAIRLVRSKRPNSIQTRGQVLCV 163
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 377-480 1.38e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 48.80  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 377 FHYHFqvwPDHGVPADPGCVLNFLQDvntrqshLAQAGEKPGPICVHCSAGIGRTGTfiVIDMILDQivrngLDTEIDIQ 456
Cdd:cd14505  76 HHLPI---PDGGVPSDIAQWQELLEE-------LLSALENGKKVLIHCKGGLGRTGL--IAACLLLE-----LGDTLDPE 138

                        90       100
                ....*....|....*....|....
gi 24639268 457 RTIQMVRSQRSGLVQTEAQYKFVY 480
Cdd:cd14505 139 QAIAAVRALRPGAIQTPKQENFLH 162
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 379-477 1.26e-05

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 47.01  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 379 YHFQVWPDHG-VPADpgcVLNFLQD-VN-TRQSH---LAQAGE-------KPGPIcVHCSAGIGRTGTFIVIDMILDQiv 445
Cdd:cd14559 121 VHVTNWPDHTaISSE---GLKELADlVNkSAEEKrnfYKSKGSsaindknKLLPV-IHCRAGVGRTGQLAAAMELNKS-- 194

                        90       100       110
                ....*....|....*....|....*....|...
gi 24639268 446 rnglDTEIDIQRTIQMVRSQRSG-LVQTEAQYK 477
Cdd:cd14559 195 ----PNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
SH2_N-SH2_SHP_like cd10340
N-terminal Src homology 2 (N-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The ...
 9-47 2.12e-05

N-terminal Src homology 2 (N-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The SH2 domain phosphatases (SHP-1, SHP-2/Syp, Drosophila corkscrew (csw), and Caenorhabditis elegans Protein Tyrosine Phosphatase (Ptp-2)) are cytoplasmic signaling enzymes. They are both targeted and regulated by interactions of their SH2 domains with phosphotyrosine docking sites. These proteins contain two SH2 domains (N-SH2, C-SH2) followed by a tyrosine phosphatase (PTP) domain, and a C-terminal extension. Shp1 and Shp2 have two tyrosyl phosphorylation sites in their C-tails, which are phosphorylated differentially by receptor and nonreceptor PTKs. Csw retains the proximal tyrosine and Ptp-2 lacks both sites. Shp-binding proteins include receptors, scaffolding adapters, and inhibitory receptors. Some of these bind both Shp1 and Shp2 while others bind only one. Most proteins that bind a Shp SH2 domain contain one or more immuno-receptor tyrosine-based inhibitory motifs (ITIMs): [IVL]xpYxx[IVL]. Shp1 N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, and is thus believed to regulate the phosphatase activity of SHP-1. Its C-SH2 domain is thought to be involved in searching for phosphotyrosine activators. The SHP2 N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. The C-SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation. Csw SH2 domain function is essential, but either SH2 domain can fulfill this requirement. The role of the csw SH2 domains during Sevenless receptor tyrosine kinase (SEV) signaling is to bind Daughter of Sevenless rather than activated SEV. Ptp-2 acts in oocytes downstream of sheath/oocyte gap junctions to promote major sperm protein (MSP)-induced MAP Kinase (MPK-1) phosphorylation. Ptp-2 functions in the oocyte cytoplasm, not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation. It is thought that MSP triggers PTP-2/Ras activation and ROS production to stimulate MPK-1 activity essential for oocyte maturation and that secreted MSP domains and Cu/Zn superoxide dismutases function antagonistically to control ROS and MAPK signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198203  Cd Length: 99  Bit Score: 43.54  E-value: 2.12e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24639268   9 YDVGGGESFGTLSELIDHYKRNP--MVETCGTVVHLRQPFN 47
Cdd:cd10340  59 YDLYGGEKFATLSELVQYYMEQHgqLREKNGDVIELKYPLN 99
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 384-468 8.46e-05

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 43.36  E-value: 8.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 384 WP-DHGVPADPGCVLNFLQDVNTRqshLAQAGEKPGPICVHCSAGIGRTGTFIVIDMILDqivrnGLDTEidiqRTIQMV 462
Cdd:cd14500  64 WPfDDGSPPPDDVVDDWLDLLKTR---FKEEGKPGACIAVHCVAGLGRAPVLVAIALIEL-----GMKPE----DAVEFI 131


                ....*.
gi 24639268 463 RSQRSG 468
Cdd:cd14500 132 RKKRRG 137
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 385-435 1.08e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 40.51  E-value: 1.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24639268 385 PDHGVPADpGCVLNFLQDVNTRqshlaqagekPGPICVHCSAGIGRTGTFI 435
Cdd:cd14499  88 PDGSTPSD-DIVKKFLDICENE----------KGAIAVHCKAGLGRTGTLI 127
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 3-31 1.33e-03

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 37.98  E-value: 1.33e-03
                           10        20
                   ....*....|....*....|....*....
gi 24639268      3 RWQDKKYDVGGGESFGTLSELIDHYKRNP 31
Cdd:smart00252  54 RNEDGKFYLEGGRKFPSLVELVEHYQKNS 82
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 339-434 2.68e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 38.89  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 339 RSEQFGHARIQCVSE--NSTSDYTLREFL-VSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLqdvntrqsHLAQAGE 415
Cdd:cd14529  16 RSAQLSPDEDRALLKklGIKTVIDLRGADeRAASEEAAAKIDGVKYVNLPLSATRPTESDVQSFL--------LIMDLKL 87

                        90
                ....*....|....*....
gi 24639268 416 KPGPICVHCSAGIGRTGTF 434
Cdd:cd14529  88 APGPVLIHCKHGKDRTGLV 106
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 344-436 3.94e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 38.72  E-value: 3.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639268 344 GHARIQCVSENSTSDYTLREFLVSWRDqparrifhyhfqvWPDHGVPAdpgcvLNFLQD-VNTRQSHLAQagekpGP--- 419
Cdd:cd14497  41 DHYMIFNLSEEEYDDDSKFEGRVLHYG-------------FPDHHPPP-----LGLLLEiVDDIDSWLSE-----DPnnv 97

                        90
                ....*....|....*..
gi 24639268 420 ICVHCSAGIGRTGTFIV 436
Cdd:cd14497  98 AVVHCKAGKGRTGTVIC 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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