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Conserved domains on  [gi|145477609|ref|XP_001424827|]
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uncharacterized protein GSPATT00028464001 [Paramecium tetraurelia]

Protein Classification

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN family protein( domain architecture ID 12997976)

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN family protein similar to Dictyostelium discoideum protein phosphatase CnrN that negatively regulates PI3K-dependent pathways, regulates cAMP signal transduction to control territory size, acts as a negative regulator of proliferation, and mediates AprA-induced chemorepulsion

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 23-181 1.20e-80

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: 246.34  E-value: 1.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGI-EGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCWIWKDHHSPPLDLLF 101
Cdd:cd14497    1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 102 EICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEGLGVNQPCQVKYVEYFYKL 181
Cdd:cd14497   81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPGVTIPSQLRYLQYFERL 160
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 188-328 4.60e-31

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: 116.22  E-value: 4.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  188 IYPTVVTLKRITFQGKaPAFNMNGSCKPYMQVIQVKNDKElystqKEAKKYKGVSHDVLNLCelKLKLDKLMPIYGDILI 267
Cdd:pfam10409   1 PPPKPLTLHSIILHGI-PNFKSGGGCRPYIRIYQNKKKVF-----STSGKYKKLKEYQQDDC--VILFPKGIPVQGDVLV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145477609  268 KVFNEGI--LKKEKMFRLAFNTAFIDetaQNSLEFSLQDLD-PSQIIKDERFDKNFKVIITIEP 328
Cdd:pfam10409  73 EFYHKGSdlLSEEKMFRFWFNTSFIE---DNTLTLPKNELDkADKDKKDKRFPKDFKVELLFSE 133
 
Name Accession Description Interval E-value
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 23-181 1.20e-80

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: 246.34  E-value: 1.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGI-EGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCWIWKDHHSPPLDLLF 101
Cdd:cd14497    1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 102 EICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEGLGVNQPCQVKYVEYFYKL 181
Cdd:cd14497   81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPGVTIPSQLRYLQYFERL 160
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 188-328 4.60e-31

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: 116.22  E-value: 4.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  188 IYPTVVTLKRITFQGKaPAFNMNGSCKPYMQVIQVKNDKElystqKEAKKYKGVSHDVLNLCelKLKLDKLMPIYGDILI 267
Cdd:pfam10409   1 PPPKPLTLHSIILHGI-PNFKSGGGCRPYIRIYQNKKKVF-----STSGKYKKLKEYQQDDC--VILFPKGIPVQGDVLV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145477609  268 KVFNEGI--LKKEKMFRLAFNTAFIDetaQNSLEFSLQDLD-PSQIIKDERFDKNFKVIITIEP 328
Cdd:pfam10409  73 EFYHKGSdlLSEEKMFRFWFNTSFIE---DNTLTLPKNELDkADKDKKDKRFPKDFKVELLFSE 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
30-182 7.71e-13

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 65.38  E-value: 7.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  30 RIIAMSYPGEGIEGLYRNPIDQVAGyLNTQHNADYMVFNLSGRKYdfskfrgvvqdCWI-WKDHHSPPLDLLFEICDLIH 108
Cdd:COG2453    7 LLAGGPLPGGGEADLKREGIDAVVS-LTEEEELLLGLLEEAGLEY-----------LHLpIPDFGAPDDEQLQEAVDFID 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145477609 109 GYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGkfKSVKDVLyyygkKRFEEEGLGVNQ-PCQVKYVEYFYKLL 182
Cdd:COG2453   75 EALREGK--KVLVHCRGGIGRTGTVAAAYLVLLG--LSAEEAL-----ARVRAARPGAVEtPAQRAFLERFAKRL 140
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
86-158 8.82e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.05  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609    86 CWIWKDHHSPPL-DLLFEICDLIHGYLKGDKIN-VVVIHCLAGKGRTGTIICCYLL-----YTGKFKSVKDVLYYYGKKR 158
Cdd:smart00404   7 YTGWPDHGVPESpDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILlqqleAEAGEVDIFDTVKELRSQR 86
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 56-158 3.09e-05

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 43.40  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609   56 LNTQHNADYmVFNLSGRKYDFSKFRgvvQDCWIW-KDHH-SPPLDLLFEICDLIHGYL-KGDKinvVVIHCLAGKGRTGT 132
Cdd:pfam00782  13 FLSKLGITA-VINVTREVDLYNSGI---LYLRIPvEDNHeTNISKYLEEAVEFIDDARqKGGK---VLVHCQAGISRSAT 85

                          90       100
                  ....*....|....*....|....*.
gi 145477609  133 IICCYLLYTGKFKSvkDVLYYYGKKR 158
Cdd:pfam00782  86 LIIAYLMKTRNLSL--NEAYSFVKER 109
PRK12361 PRK12361
hypothetical protein; Provisional
 91-151 2.42e-04

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.46  E-value: 2.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145477609  91 DHHSPPLDLLFEICDLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVL 151
Cdd:PRK12361 152 DHSVPTLAQLNQAINWIHRQVRANK--SVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVL 210
 
Name Accession Description Interval E-value
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 23-181 1.20e-80

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: 246.34  E-value: 1.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGI-EGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCWIWKDHHSPPLDLLF 101
Cdd:cd14497    1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 102 EICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEGLGVNQPCQVKYVEYFYKL 181
Cdd:cd14497   81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPGVTIPSQLRYLQYFERL 160
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 23-181 2.16e-62

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: 199.35  E-value: 2.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNL-SGRKYDFSKFRGVVQdCWIWKDHHSPPLDLLF 101
Cdd:cd14509    1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVA-EYPFDDHNPPPLELIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 102 EICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRfEEEGLGVNQPCQVKYVEYFYKL 181
Cdd:cd14509   80 PFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKR-TKNKKGVTIPSQRRYVYYYSRL 158
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 9-181 9.56e-60

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: 193.35  E-value: 9.56e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609   9 SGKKKRLIQEGYNLDLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNL-SGRKYDFSKFRGVVQDCW 87
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  88 IwKDHHSPPLDLLFEICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKR--FEEEGL- 164
Cdd:cd14510   81 I-DDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRtdKSVSSKf 159

                        170
                 ....*....|....*...
gi 145477609 165 -GVNQPCQVKYVEYFYKL 181
Cdd:cd14510  160 qGVETPSQSRYVGYFEKL 177
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 23-181 1.43e-45

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: 155.62  E-value: 1.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDcWIWKDHHSPPLDLLFE 102
Cdd:cd14508    1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLD-FGWPELHAPPLEKLCS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 103 ICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEGLG-VNQPCQVKYVEYFYKL 181
Cdd:cd14508   80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKVGpLGQPSQKRYVGYFSGL 159
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 22-178 4.26e-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: 144.03  E-value: 4.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  22 LDLTYVTKRIIAMSYPGEGIEGLYR-NPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCwIWKDHHSPPLDLL 100
Cdd:cd14511    9 LDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVEC-SWPYRRAPSLHAL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145477609 101 FEICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEglgvNQPCQVKYVEYF 178
Cdd:cd14511   88 YALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPG----LSPSELRYLYYF 161
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 23-181 9.40e-37

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: 132.41  E-value: 9.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDcWIWKDHHSPPLDLLFE 102
Cdd:cd14560    1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLD-FGWPDLHAPALEKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 103 ICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRF-EEEGLGVNQPCQVKYVEYFYKL 181
Cdd:cd14560   80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFyEDKVVPVGQPSQKRYVHYFSGL 159
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 21-177 3.02e-35

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: 128.48  E-value: 3.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  21 NLDLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCWiWKDHHSPPLDLL 100
Cdd:cd14564    8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECG-WPARRAPNLQNL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145477609 101 FEICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRfEEEGLGvnqPCQVKYVEY 177
Cdd:cd14564   87 YSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKR-CPPGIW---PSHKRYIEY 159
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 23-181 6.04e-34

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: 124.67  E-value: 6.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCWiWKDHHSPPLDLLFE 102
Cdd:cd14561    1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVG-WPDLHAPPLDKMCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 103 ICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEGL-GVNQPCQVKYVEYFYKL 181
Cdd:cd14561   80 ICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVsALMQPSQKRYVQFLSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 23-178 6.29e-34

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: 124.68  E-value: 6.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  23 DLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDcWIWKDHHSPPLDLLFE 102
Cdd:cd14562    1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQD-FGWPDLHAPPLDKICS 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145477609 103 ICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRFEEEGLGVN-QPCQVKYVEYF 178
Cdd:cd14562   80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDKVATSlQPSQRRYISYF 156
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 188-328 4.60e-31

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: 116.22  E-value: 4.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  188 IYPTVVTLKRITFQGKaPAFNMNGSCKPYMQVIQVKNDKElystqKEAKKYKGVSHDVLNLCelKLKLDKLMPIYGDILI 267
Cdd:pfam10409   1 PPPKPLTLHSIILHGI-PNFKSGGGCRPYIRIYQNKKKVF-----STSGKYKKLKEYQQDDC--VILFPKGIPVQGDVLV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145477609  268 KVFNEGI--LKKEKMFRLAFNTAFIDetaQNSLEFSLQDLD-PSQIIKDERFDKNFKVIITIEP 328
Cdd:pfam10409  73 EFYHKGSdlLSEEKMFRFWFNTSFIE---DNTLTLPKNELDkADKDKKDKRFPKDFKVELLFSE 133
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 22-181 2.52e-27

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: 106.89  E-value: 2.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  22 LDLTYVTKRIIAMSYPGEGIEGLYRNPIDQVAGYLNTQHNADYMVFNLSGRKYDFSKFRGVVQDCwIWKDHHSPPLDLLF 101
Cdd:cd14563    9 LDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSEC-SWPVRQAPSLHNLF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609 102 EICDLIHGYLKGDKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRfeeEGLGVnQPCQVKYVEYFYKL 181
Cdd:cd14563   88 AVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKR---PGIGL-WPSHRRYIGYICDL 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
30-182 7.71e-13

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 65.38  E-value: 7.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  30 RIIAMSYPGEGIEGLYRNPIDQVAGyLNTQHNADYMVFNLSGRKYdfskfrgvvqdCWI-WKDHHSPPLDLLFEICDLIH 108
Cdd:COG2453    7 LLAGGPLPGGGEADLKREGIDAVVS-LTEEEELLLGLLEEAGLEY-----------LHLpIPDFGAPDDEQLQEAVDFID 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145477609 109 GYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGkfKSVKDVLyyygkKRFEEEGLGVNQ-PCQVKYVEYFYKLL 182
Cdd:COG2453   75 EALREGK--KVLVHCRGGIGRTGTVAAAYLVLLG--LSAEEAL-----ARVRAARPGAVEtPAQRAFLERFAKRL 140
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 25-199 2.97e-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: 56.59  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  25 TYVTKRIIAMSYPGEGIEGLYrNPIDQVAGYLNTqhnadyMVFNL----------------SGRKYDFSKF--RGVVQDC 86
Cdd:cd14506    9 SWITDDILAMARPSTELIDKY-GIIEQFKEKGIK------TVINLqepgehascgpglepeSGFSYLPEAFmrAGIYFYN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  87 WIWKDHHSPPLDLLFEICDLIHGYLKgdKINVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVLYYYGKKRfeeegLGV 166
Cdd:cd14506   82 FGWKDYGVPSLTTILDIVKVMAFALQ--EGGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRP-----NSI 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 145477609 167 NQPCQVKYVEYFYKLLTLGYIIYPTVVTLKRIT 199
Cdd:cd14506  155 QTRGQVLCVREFAQFLLPLRNVFACPDPKAAVT 187
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 90-148 4.75e-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: 54.59  E-value: 4.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  90 KDHHSPPLDLLFEICDLIHgylKGDKIN-VVVIHCLAGKGRTGTIICCYLLYTGKFKSVK 148
Cdd:cd14504   58 EDYTPPTLEQIDEFLDIVE---EANAKNeAVLVHCLAGKGRTGTMLACYLVKTGKISAVD 114
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 21-144 1.20e-08

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: 54.38  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  21 NLDLTYVT-KRIIAMSYP---GEGIEGLYRNPIDQVAGYLNtQHNADyMVFNLSGRKYDFSKF--RGVvqdcwiwkDHH- 93
Cdd:cd14499   15 NGDLNWIVpGKFLAFSGPhdtRKDENGYPTHTPEDYIPYFK-KLGVT-TVVRLNKKLYDAKRFtdAGI--------RHYd 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145477609  94 -------SPPLDLL---FEICDLIHGylkgdkinVVVIHCLAGKGRTGTIICCYLLYTGKF 144
Cdd:cd14499   85 lyfpdgsTPSDDIVkkfLDICENEKG--------AIAVHCKAGLGRTGTLIACYLMKHYGF 137
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
86-158 8.82e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.05  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609    86 CWIWKDHHSPPL-DLLFEICDLIHGYLKGDKIN-VVVIHCLAGKGRTGTIICCYLL-----YTGKFKSVKDVLYYYGKKR 158
Cdd:smart00404   7 YTGWPDHGVPESpDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILlqqleAEAGEVDIFDTVKELRSQR 86
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 86-158 8.82e-08

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: 50.05  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609    86 CWIWKDHHSPPL-DLLFEICDLIHGYLKGDKIN-VVVIHCLAGKGRTGTIICCYLL-----YTGKFKSVKDVLYYYGKKR 158
Cdd:smart00012   7 YTGWPDHGVPESpDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILlqqleAEAGEVDIFDTVKELRSQR 86
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 97-158 5.19e-07

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 48.11  E-value: 5.19e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145477609  97 LDLLFEICDLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKfKSVKDVLYYYGKKR 158
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGE--PVLVHCKAGVGRTGTLVACYLVLLGG-MSAEEAVRIVRLIR 97
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 91-151 6.02e-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: 46.10  E-value: 6.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145477609  91 DHHSPPLDLLF-EICDLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVL 151
Cdd:cd14505   82 DGGVPSDIAQWqELLEELLSALENGK--KVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAI 141
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
89-151 8.51e-06

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 47.39  E-value: 8.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145477609  89 WKDHHSPPLDLLFEICDLIHGYLK---GDKiNVVVIHCLAGKGRTGTIICCYLLY------TGKFKSVKDVL 151
Cdd:COG5599  177 WPDHGAISAEALKNLADLIDKKEKikdPDK-LLPVVHCRAGVGRTGTLIACLALSksinalVQITLSVEEIV 247
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 65-159 1.44e-05

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


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 44.46  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  65 MVFNLSGRKYDFSKFRGVVQDCWIWKDHHSPPLDLLF-EICDLIHGYLKgdKINVVVIHCLAGKGRTGTIICCYLLYTGK 143
Cdd:cd14498   29 HILNVAGEPPPNKFPDGIKYLRIPIEDSPDEDILSHFeEAIEFIEEALK--KGGKVLVHCQAGVSRSATIVIAYLMKKYG 106

                         90
                 ....*....|....*.
gi 145477609 144 FkSVKDVLYYYGKKRF 159
Cdd:cd14498  107 W-SLEEALELVKSRRP 121
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 56-158 3.09e-05

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 43.40  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609   56 LNTQHNADYmVFNLSGRKYDFSKFRgvvQDCWIW-KDHH-SPPLDLLFEICDLIHGYL-KGDKinvVVIHCLAGKGRTGT 132
Cdd:pfam00782  13 FLSKLGITA-VINVTREVDLYNSGI---LYLRIPvEDNHeTNISKYLEEAVEFIDDARqKGGK---VLVHCQAGISRSAT 85

                          90       100
                  ....*....|....*....|....*.
gi 145477609  133 IICCYLLYTGKFKSvkDVLYYYGKKR 158
Cdd:pfam00782  86 LIIAYLMKTRNLSL--NEAYSFVKER 109
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 91-140 3.85e-05

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: 43.79  E-value: 3.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145477609  91 DH-HSPPLDLLFEICDLIHGYLKgdKINVVVIHCLAGKGRTGTIICCYLLY 140
Cdd:cd14524   65 DFtGVPSLEDLEKGVDFILKHRE--KGKSVYVHCKAGRGRSATIVACYLIQ 113
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
91-159 6.90e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 42.65  E-value: 6.90e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609    91 DHHSPPLDLLFEIC-DLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKFkSVKDVLYYYGKKRF 159
Cdd:smart00195  54 DNTETKISPYFPEAvEFIEDAESKGG--KVLVHCQAGVSRSATLIIAYLMKTRNM-SLNDAYDFVKDRRP 120
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 89-134 1.30e-04

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: 43.27  E-value: 1.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145477609  89 WKDHHSP-PLDLLFEICDLIHGYLKGDKINV-VVIHCLAGKGRTGTII 134
Cdd:cd14615  135 WPDHGVPeTTDLLINFRHLVREYMKQNPPNSpILVHCSAGVGRTGTFI 182
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 89-135 1.59e-04

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: 42.75  E-value: 1.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 145477609  89 WKDHHSP--PLDLLFEICDLIHGYLKGDkinvVVIHCLAGKGRTGTIIC 135
Cdd:cd14538  115 WPDHGTPqsADPLLRFIRYMRRIHNSGP----IVVHCSAGIGRTGVLIT 159
PRK12361 PRK12361
hypothetical protein; Provisional
 91-151 2.42e-04

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.46  E-value: 2.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145477609  91 DHHSPPLDLLFEICDLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDVL 151
Cdd:PRK12361 152 DHSVPTLAQLNQAINWIHRQVRANK--SVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVL 210
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 89-134 3.10e-04

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: 41.85  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145477609  89 WKDHHSPPL-DLLFEICDLIHGYLKGDKI-NVVVIHCLAGKGRTGTII 134
Cdd:cd18533  113 WPDFGVPDSpEDLLTLIKLKRELNDSASLdPPIIVHCSAGVGRTGTFI 160
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 89-135 3.79e-04

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: 41.74  E-value: 3.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 145477609  89 WKDHHSP--PLDLLFEICDLIHGYLKGDkinvVVIHCLAGKGRTGTIIC 135
Cdd:cd14597  142 WPDHDTPsqPEQLLTFISYMRHIHKSGP----IITHCSAGIGRSGTLIC 186
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 56-135 9.11e-04

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: 40.35  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  56 LNTQHNADYMVFNLSGRKYDFSKFRGVVQDCWI-WKDHHSPP-----LDLLFEICDLihgylKGDKINVVVIHCLAGKGR 129
Cdd:cd00047   78 VSEEELSDYTIRTLELSPKGCSESREVTHLHYTgWPDHGVPSspedlLALVRRVRKE-----ARKPNGPIVVHCSAGVGR 152


                 ....*.
gi 145477609 130 TGTIIC 135
Cdd:cd00047  153 TGTFIA 158
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 74-180 1.60e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 39.24  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  74 YDFSKFR--GVVQDCWIWKDHHSPPLDLL---FEICDLIHGYLKGDKINVVViHCLAGKGRTGTIICCYLLYTGKFKSVK 148
Cdd:PTZ00242  52 YDAELLEknGIEVHDWPFDDGAPPPKAVIdnwLRLLDQEFAKQSTPPETIAV-HCVAGLGRAPILVALALVEYGGMEPLD 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 145477609 149 DVLYYYGKKRfeeeGlGVNQPcQVKYVEYFYK 180
Cdd:PTZ00242 131 AVGFVREKRK----G-AINQT-QLQFLKKYKP 156
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 91-158 2.35e-03

dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, and similar proteins; This family is composed of fungal dual specificity protein phosphatases (DUSPs) including Saccharomyces cerevisiae SDP1 and MSG5, and Schizosaccharomyces pombe Pmp1. function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. SDP1 is oxidative stress-induced and dephosphorylates MAPK substrates such as SLT2. MSG5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity (CWI) pathways, respectively. Pmp1 is responsible for dephosphorylating the CWI MAPK Pmk1. These phosphatases bind to their target MAPKs through a conserved IYT motif located outside of the dual specificity phosphatase domain.


Pssm-ID: 350371 [Multi-domain]  Cd Length: 155  Bit Score: 38.46  E-value: 2.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145477609  91 DHHSPPLDLLFEICDLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKfKSVKDVlYYYGKKR 158
Cdd:cd14521   71 DHNSQIQKDLPKLTSIIEDATQSGK--KVLIHCQCGVSRSASLIIAYIMKKLG-LSLNDA-YDLLKSR 134
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 89-141 2.95e-03

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: 38.96  E-value: 2.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145477609  89 WKDHHSP--PLDLLFEICDLIHGYLKGDkinvVVIHCLAGKGRTGTIICCYLLYT 141
Cdd:cd14596  114 WPDHGTPqsSDQLVKFICYMRKVHNTGP----IVVHCSAGIGRAGVLICVDVLLS 164
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
58-151 3.46e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 38.76  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609   58 TQHNADYMVFNLSGRKYDFSKFRGVVQDCWI-WKDHHSP--PLDLLfeicDLIHgYLKGDKINV----VVIHCLAGKGRT 130
Cdd:pfam00102 109 KEDEKDYTVRTLEVSNGGSEETRTVKHFHYTgWPDHGVPesPNSLL----DLLR-KVRKSSLDGrsgpIVVHCSAGIGRT 183

                          90       100
                  ....*....|....*....|....*
gi 145477609  131 GTII----CCYLLYTGKFKSVKDVL 151
Cdd:pfam00102 184 GTFIaidiALQQLEAEGEVDIFQIV 208
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 87-141 4.67e-03

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: 38.17  E-value: 4.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145477609  87 WIWKDHHSPPL-DLLFEICDLIHGYLKGDKINVVViHCLAGKGRTGTIicCYLLYT 141
Cdd:cd14542  109 TAWPDHGVPSSvDPILDLVRLVRDYQGSEDVPICV-HCSAGCGRTGTI--CAIDYV 161
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 91-150 6.09e-03

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 36.87  E-value: 6.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145477609  91 DHHSPPLDLLFEICDLIHGYLKGDKinVVVIHCLAGKGRTGTIICCYLLYTGKFKSVKDV 150
Cdd:cd14527   53 DLVAPTPEQLERAVAWIEELRAQGG--PVLVHCALGYGRSATVVAAWLLAYGRAKSVAEA 110
 
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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