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Conserved domains on  [gi|213972591|ref|NP_954863|]
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phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TPTE2 isoform gamma [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 206-382 1.09e-129

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


:

Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 374.78  E-value: 1.09e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 206 SENKRRYTRDGFDLDLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIM 285
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 286 IDDHNVPTLHEMVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKTHSNKFQ 365
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 213972591 366 GVETPSQNRYVGYFAQV 382
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 391-521 6.17e-43

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 148.96  E-value: 6.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591  391 PPRRILFIKRFIIYSI----RGDVCDLKVQVVMEKKVVFSStsLGNCSILHDIETDKILINVYDGPPLYDDVKVQFFSSN 466
Cdd:pfam10409   1 PPPKPLTLHSIILHGIpnfkSGGGCRPYIRIYQNKKKVFST--SGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 213972591  467 LPKYYDNCPFFFWFNTSFIQNNRLCLPRNELDNPHKQKAWKIYPPEFAVEILFGE 521
Cdd:pfam10409  79 SDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
 
Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 206-382 1.09e-129

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 374.78  E-value: 1.09e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 206 SENKRRYTRDGFDLDLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIM 285
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 286 IDDHNVPTLHEMVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKTHSNKFQ 365
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 213972591 366 GVETPSQNRYVGYFAQV 382
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 391-521 6.17e-43

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 148.96  E-value: 6.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591  391 PPRRILFIKRFIIYSI----RGDVCDLKVQVVMEKKVVFSStsLGNCSILHDIETDKILINVYDGPPLYDDVKVQFFSSN 466
Cdd:pfam10409   1 PPPKPLTLHSIILHGIpnfkSGGGCRPYIRIYQNKKKVFST--SGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 213972591  467 LPKYYDNCPFFFWFNTSFIQNNRLCLPRNELDNPHKQKAWKIYPPEFAVEILFGE 521
Cdd:pfam10409  79 SDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
224-381 3.22e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.14  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 224 VTERIIAMSFPSSGRQSFYRNPIEevvrfldkkhrnhyRVYNLCSERAYDPKHFHNR---VSRIMIDDHNVPTLHEMVVF 300
Cdd:COG2453    4 IPGLLAGGPLPGGGEADLKREGID--------------AVVSLTEEEELLLGLLEEAgleYLHLPIPDFGAPDDEQLQEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 301 TKEVNEWMAQDlENiVAIHCKGGKGRTGTMVCALLIASEifLTAEESLYYFGERRTnkthsnkfQGVETPSQNRYVGYFA 380
Cdd:COG2453   70 VDFIDEALREG-KK-VLVHCRGGIGRTGTVAAAYLVLLG--LSAEEALARVRAARP--------GAVETPAQRAFLERFA 137


                 .
gi 213972591 381 Q 381
Cdd:COG2453  138 K 138
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
288-346 6.92e-06

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 6.92e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972591   288 DHNVPTLHE-MVVFTKEVNEWMAQDLENI-VAIHCKGGKGRTGTMVCALLIASEIFLTAEE 346
Cdd:smart00404  12 DHGVPESPDsILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
262-372 8.59e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 37.99  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591  262 RVYNLCSERAYDPKHFHnrvsriMID--DHNVPTLHE-MVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTmVCALLIAS 338
Cdd:pfam00102 121 EVSNGGSEETRTVKHFH------YTGwpDHGVPESPNsLLDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGT-FIAIDIAL 193

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 213972591  339 EIfLTAEESLYYFGerrTNKT-HSNKFQGVETPSQ 372
Cdd:pfam00102 194 QQ-LEAEGEVDIFQ---IVKElRSQRPGMVQTLEQ 224
 
Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 206-382 1.09e-129

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 374.78  E-value: 1.09e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 206 SENKRRYTRDGFDLDLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIM 285
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 286 IDDHNVPTLHEMVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKTHSNKFQ 365
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 213972591 366 GVETPSQNRYVGYFAQV 382
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 220-381 1.55e-76

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 237.87  E-value: 1.55e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 220 DLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVV 299
Cdd:cd14509    1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 300 FTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNkthsNKfQGVETPSQNRYVGYF 379
Cdd:cd14509   81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTK----NK-KGVTIPSQRRYVYYY 155


                 ..
gi 213972591 380 AQ 381
Cdd:cd14509  156 SR 157
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 220-379 7.53e-65

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: 207.82  E-value: 7.53e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 220 DLTYVTERIIAMSFPSSG-RQSFYRNPIEEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVSRIMIDDHNVPTLHEMV 298
Cdd:cd14497    1 DLSYITPRIIAMSFPATGyPESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 299 VFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKthsnKFQGVETPSQNRYVGY 378
Cdd:cd14497   81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKE----GLPGVTIPSQLRYLQY 156


                 .
gi 213972591 379 F 379
Cdd:cd14497  157 F 157
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 220-380 4.11e-43

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 150.62  E-value: 4.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 220 DLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLcSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVV 299
Cdd:cd14508    1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNL-SERRHDLRSLNPKVLDFGWPELHAPPLEKLCS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 300 FTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRtnkTHSNKFQGVETPSQNRYVGYF 379
Cdd:cd14508   80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKR---FYDDKVGPLGQPSQKRYVGYF 156


                 .
gi 213972591 380 A 380
Cdd:cd14508  157 S 157
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 391-521 6.17e-43

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 148.96  E-value: 6.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591  391 PPRRILFIKRFIIYSI----RGDVCDLKVQVVMEKKVVFSStsLGNCSILHDIETDKILINVYDGPPLYDDVKVQFFSSN 466
Cdd:pfam10409   1 PPPKPLTLHSIILHGIpnfkSGGGCRPYIRIYQNKKKVFST--SGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 213972591  467 LPKYYDNCPFFFWFNTSFIQNNRLCLPRNELDNPHKQKAWKIYPPEFAVEILFGE 521
Cdd:pfam10409  79 SDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 218-382 3.16e-41

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 145.57  E-value: 3.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 218 DLDLTYVTERIIAMSFPSSGRQSFYR-NPIEEVVRFLDKKHRNHYRVYNLcSERAYDPKHFHNRVSRIMIDDHNVPTLHE 296
Cdd:cd14511    8 DLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNL-SPRSYPTLRLPSRVVECSWPYRRAPSLHA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 297 MVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTnkthsnkfQGVETPSQNRYV 376
Cdd:cd14511   87 LYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRC--------PPGLSPSELRYL 158


                 ....*.
gi 213972591 377 GYFAQV 382
Cdd:cd14511  159 YYFSDI 164
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 218-378 2.69e-38

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 137.73  E-value: 2.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 218 DLDLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLCsERAYDPKHFHNRVSRIMIDDHNVPTLHEM 297
Cdd:cd14564    8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLS-QRTYRPSRFHNRVSECGWPARRAPNLQNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 298 VVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKthsnkfqGVeTPSQNRYVG 377
Cdd:cd14564   87 YSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPP-------GI-WPSHKRYIE 158


                 .
gi 213972591 378 Y 378
Cdd:cd14564  159 Y 159
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 220-380 1.03e-33

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 125.09  E-value: 1.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 220 DLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLcSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVV 299
Cdd:cd14560    1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNL-SERRHDISKLHPKVLDFGWPDLHAPALEKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 300 FTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRtnkTHSNKFQGVETPSQNRYVGYF 379
Cdd:cd14560   80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKR---FYEDKVVPVGQPSQKRYVHYF 156


                 .
gi 213972591 380 A 380
Cdd:cd14560  157 S 157
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 218-382 1.12e-31

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 119.60  E-value: 1.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 218 DLDLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLcSERAYDPKHFHNRVSRIMIDDHNVPTLHEM 297
Cdd:cd14563    8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNL-SQKSYRSAKFHNRVSECSWPVRQAPSLHNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 298 VVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERRTNKthsnkfqgVETPSQNRYVG 377
Cdd:cd14563   87 FAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGI--------GLWPSHRRYIG 158


                 ....*
gi 213972591 378 YFAQV 382
Cdd:cd14563  159 YICDL 163
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 220-379 5.52e-31

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 117.74  E-value: 5.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 220 DLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLcSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVV 299
Cdd:cd14561    1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNL-SEKRYELTKLNPKIMDVGWPDLHAPPLDKMCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 300 FTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERrtnKTHSNKFQGVETPSQNRYVGYF 379
Cdd:cd14561   80 ICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMK---KFYDDKVSALMQPSQKRYVQFL 156
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 220-380 7.51e-29

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 111.96  E-value: 7.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 220 DLTYVTERIIAMSFPSSGRQSFYRNPIEEVVRFLDKKHRNHYRVYNLcSERAYDPKHFHNRVSRIMIDDHNVPTLHEMVV 299
Cdd:cd14562    1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNL-SEKRHDITRLNPKVQDFGWPDLHAPPLDKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 300 FTKEVNEWMAQDLENIVAIHCKGGKGRTGTMVCALLIASEIFLTAEESLYYFGERrtnKTHSNKFQGVETPSQNRYVGYF 379
Cdd:cd14562   80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMR---KFCEDKVATSLQPSQRRYISYF 156


                 .
gi 213972591 380 A 380
Cdd:cd14562  157 G 157
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
224-381 3.22e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.14  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 224 VTERIIAMSFPSSGRQSFYRNPIEevvrfldkkhrnhyRVYNLCSERAYDPKHFHNR---VSRIMIDDHNVPTLHEMVVF 300
Cdd:COG2453    4 IPGLLAGGPLPGGGEADLKREGID--------------AVVSLTEEEELLLGLLEEAgleYLHLPIPDFGAPDDEQLQEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 301 TKEVNEWMAQDlENiVAIHCKGGKGRTGTMVCALLIASEifLTAEESLYYFGERRTnkthsnkfQGVETPSQNRYVGYFA 380
Cdd:COG2453   70 VDFIDEALREG-KK-VLVHCRGGIGRTGTVAAAYLVLLG--LSAEEALARVRAARP--------GAVETPAQRAFLERFA 137


                 .
gi 213972591 381 Q 381
Cdd:COG2453  138 K 138
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 227-381 2.01e-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: 56.13  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 227 RIIAMSFPSSgrqsfyrnpiEEVVRFLDKKHRNHyrVYNLCSERAYDPKHFHNRVS--RIMIDDHNVPTLHEMVVFTKEV 304
Cdd:cd14504    8 KLAGMAFPRL----------PEHYAYLNENGIRH--VVTLTEEPPPEHSDTCPGLRyhHIPIEDYTPPTLEQIDEFLDIV 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972591 305 NEWMAQDLEniVAIHCKGGKGRTGTMVCALLIASEiFLTAEESLyyfgerrtNKTHSNKFQGVETPSQNRYVGYFAQ 381
Cdd:cd14504   76 EEANAKNEA--VLVHCLAGKGRTGTMLACYLVKTG-KISAVDAI--------NEIRRIRPGSIETSEQEKFVIQFAK 141
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 280-346 3.20e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 50.34  E-value: 3.20e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972591 280 RVSRIMIDDHNVPTLHEmvvFTKEVNEWMAQDLENI--VAIHCKGGKGRTGTMVCALLIASEIFLTAEE 346
Cdd:cd14505   74 TWHHLPIPDGGVPSDIA---QWQELLEELLSALENGkkVLIHCKGGLGRTGLIAACLLLELGDTLDPEQ 139
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
288-346 6.92e-06

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 6.92e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972591   288 DHNVPTLHE-MVVFTKEVNEWMAQDLENI-VAIHCKGGKGRTGTMVCALLIASEIFLTAEE 346
Cdd:smart00404  12 DHGVPESPDsILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 288-346 6.92e-06

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: 45.04  E-value: 6.92e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972591   288 DHNVPTLHE-MVVFTKEVNEWMAQDLENI-VAIHCKGGKGRTGTMVCALLIASEIFLTAEE 346
Cdd:smart00012  12 DHGVPESPDsILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 224-376 1.15e-05

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: 44.65  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 224 VTERIIAMSFPSSgrqsfyrnPIEEVVRFLDKKHRNHYrvynlcseraydpkhfhnrvsrIMIDDHNVptlHEMVVFTKE 303
Cdd:cd14494    5 DPLRLIAGALPLS--------PLEADSRFLKQLGVTTI----------------------VDLTLAMV---DRFLEVLDQ 51

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972591 304 VNEwmaqdLENIVAIHCKGGKGRTGTMVCALLIAsEIFLTAEESLYYFGERRTNKThsnkfqgVETPSQNRYV 376
Cdd:cd14494   52 AEK-----PGEPVLVHCKAGVGRTGTLVACYLVL-LGGMSAEEAVRIVRLIRPGGI-------PQTIEQLDFL 111
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 227-336 2.28e-04

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 41.88  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 227 RIIAMSFPSsgRQSFYRN-PIEEVVRFLDKKHRNHYRVYNL-------CSERAYDPKHFHNRV---SRIMIDDHNVP--- 292
Cdd:cd17665   16 RFIAFKVPL--RKSFFANlPPEQRFTPKDLVEQVEKRGEKLglvidltNTTRYYDPRDLTNHGvyyKKITCPGHQVPddk 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 213972591 293 TLHEmvvFTKEVNEWMAQDLEN--IVAIHCKGGKGRTGTMVCALLI 336
Cdd:cd17665   94 TIQS---FKDAVKDFLEKNKDNdkLIGVHCTHGLNRTGYLICRYLI 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 222-397 2.75e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 42.34  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 222 TYVTERIIAMSFPSSGrqsfyrnpIEEVVRFLDKKHRNHYR-VYNL--------C-------SERAYDPKHF---HNRVS 282
Cdd:cd14506    9 SWITDDILAMARPSTE--------LIDKYGIIEQFKEKGIKtVINLqepgehasCgpglepeSGFSYLPEAFmraGIYFY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 283 RIMIDDHNVPTLHEMVVFTKEVNewMAQDLENIVAIHCKGGKGRTGTMV-CALLIASEIflTAEESLYYFGERRTNkths 361
Cdd:cd14506   81 NFGWKDYGVPSLTTILDIVKVMA--FALQEGGKVAVHCHAGLGRTGVLIaCYLVYALRM--SADQAIRLVRSKRPN---- 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 213972591 362 nkfqGVETPSQNRYVGYFAQVkhlynwnLPPRRILF 397
Cdd:cd14506  153 ----SIQTRGQVLCVREFAQF-------LLPLRNVF 177
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 316-346 3.21e-04

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: 41.67  E-value: 3.21e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 213972591 316 VAIHCKGGKGRTGTMVCALLIASEIFlTAEE 346
Cdd:cd14499  112 IAVHCKAGLGRTGTLIACYLMKHYGF-TARE 141
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 267-357 3.21e-04

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 41.49  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 267 CSERAYDPKHFHN--RVSRIMIDDHNVPTLHEMV-VFTKEVNEWMAQDLENI-VAIHCKGGKGRTGTMVCALLIASEIFl 342
Cdd:cd14502   61 NTDRYYDPNDLDDdgYVYYKKVCVRKEPPDAEEVnKFIELVDKFLAEDNPDKlIAVHCTHGFNRTGFMIVSYLVERLGL- 139

                         90
                 ....*....|....*
gi 213972591 343 TAEESLYYFGERRTN 357
Cdd:cd14502  140 TVEQALEAFAQARPP 154
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 285-338 4.17e-04

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 40.71  E-value: 4.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972591 285 MIDDHNVPTL---HEMVVFTKEVNEwmaqdLENIVAIHCKGGKGRTGTMVCALLIAS 338
Cdd:cd14524   63 TVDFTGVPSLedlEKGVDFILKHRE-----KGKSVYVHCKAGRGRSATIVACYLIQH 114
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
233-340 6.91e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 41.49  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591   233 FPSSGRQSFYRNPIEevVRFLDKKHRNHYRVYNLCSERAYDP-----KHFHnrvsriMID--DHNVPTLHE-MVVFTKEV 304
Cdd:smart00194 115 WPDEEGEPLTYGDIT--VTLKSVEKVDDYTIRTLEVTNTGCSetrtvTHYH------YTNwpDHGVPESPEsILDLIRAV 186

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 213972591   305 NEWMAQDLENIVaIHCKGGKGRTGTMVCALLIASEI 340
Cdd:smart00194 187 RKSQSTSTGPIV-VHCSAGVGRTGTFIAIDILLQQL 221
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 262-331 1.32e-03

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: 40.29  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 213972591 262 RVYNLCSERAYDP----KHFHNRVsrimIDDHNVP-TLHEMVVFTKEVNEWMAQDLEN-IVAIHCKGGKGRTGTMV 331
Cdd:cd14617  114 REFKICSEEQLDAprlvRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRTPGSgPTVVHCSAGVGRTGTFI 185
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 254-331 3.11e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 39.67  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591 254 DKKHRNH---YRVYNLCSERAYDPKHFHNRVsRIMIDDHNVPTLHEM---VVFTKEV--NEWmaqdleniVAIHCKGGKG 325
Cdd:cd14495  128 KKKSPSQpktVKVESVRTEEELVKKKGAHYV-RIAATDHVWPDDEEIdafVAFYRSLpaDAW--------LHFHCRAGKG 198


                 ....*..
gi 213972591 326 RTGT-MV 331
Cdd:cd14495  199 RTTTfMV 205
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 275-331 7.73e-03

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: 37.95  E-value: 7.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213972591 275 KHFHNRVsrimIDDHNVP-TLHEMVVFTKEVNEWMAQDLEN-IVAIHCKGGKGRTGTMV 331
Cdd:cd14619  130 RHFHFTA----WPDHGVPsSTDTLLAFRRLLRQWLDQTMSGgPTVVHCSAGVGRTGTLI 184
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
262-372 8.59e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 37.99  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972591  262 RVYNLCSERAYDPKHFHnrvsriMID--DHNVPTLHE-MVVFTKEVNEWMAQDLENIVAIHCKGGKGRTGTmVCALLIAS 338
Cdd:pfam00102 121 EVSNGGSEETRTVKHFH------YTGwpDHGVPESPNsLLDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGT-FIAIDIAL 193

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 213972591  339 EIfLTAEESLYYFGerrTNKT-HSNKFQGVETPSQ 372
Cdd:pfam00102 194 QQ-LEAEGEVDIFQ---IVKElRSQRPGMVQTLEQ 224
 
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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