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Conserved domains on  [gi|12734656|gb|AAK06371|]
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cyclin-dependent kinase associated protein phosphatase [Homo sapiens]

Protein Classification

CDKN3 domain-containing protein( domain architecture ID 10529699)

CDKN3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 4.79e-118

Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner.


:

Pssm-ID: 399018  Cd Length: 168  Bit Score: 332.37  E-value: 4.79e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656     1 MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656    81 RGELSKYRVPKLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 12734656   161 TISPEQAI 168
Cdd:pfam05706 161 SISPEQAI 168
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 4.79e-118

Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner.


Pssm-ID: 399018  Cd Length: 168  Bit Score: 332.37  E-value: 4.79e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656     1 MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656    81 RGELSKYRVPKLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 12734656   161 TISPEQAI 168
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-191 1.64e-87

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: 254.88  E-value: 1.64e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  29 ISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPKLLDLYQQCGIITHHHPI 108
Cdd:cd14505   1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656 109 ADGGTPD-IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGsGAIQTIKQYN 187
Cdd:cd14505  81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPKQEN 159


                ....
gi 12734656 188 YLHE 191
Cdd:cd14505 160 FLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-196 3.08e-24

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 93.11  E-value: 3.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  62 KDTEELKSCGIQDIFVFCTRGELskyrvpkLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCY 141
Cdd:COG2453  16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12734656 142 GGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAIQTIKQYNYLHEFRDKL 196
Cdd:COG2453  89 GGIGRTGTVAAAYLVLLG--LSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
74-191 1.73e-08

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 53.05  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656     74 DIFVFCTRGELSKYRVPKLLDL-YQQCG---IITHHHPIA--DGGTPDIASCC-EIMEELTTCLKNYRK-TLIHCYGGLG 145
Cdd:smart00194 127 DITVTLKSVEKVDDYTIRTLEVtNTGCSetrTVTHYHYTNwpDHGVPESPESIlDLIRAVRKSQSTSTGpIVVHCSAGVG 206

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 12734656    146 RS-CLVAACLLLYL---SDTISPEQAIDSLRDLRgSGAIQTIKQYNYLHE 191
Cdd:smart00194 207 RTgTFIAIDILLQQleaGKEVDIFEIVKELRSQR-PGMVQTEEQYIFLYR 255
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 100-193 1.60e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 43.47  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  100 GIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTL----IHCYGGLGRS-CLVAACLLLYlsDTISPEQAIDSLRDL 174
Cdd:PTZ00242  61 GIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQSTPPetiaVHCVAGLGRApILVALALVEY--GGMEPLDAVGFVREK 138

                         90
                 ....*....|....*....
gi 12734656  175 RgSGAIQtIKQYNYLHEFR 193
Cdd:PTZ00242 139 R-KGAIN-QTQLQFLKKYK 155
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-168 4.79e-118

Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner.


Pssm-ID: 399018  Cd Length: 168  Bit Score: 332.37  E-value: 4.79e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656     1 MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656    81 RGELSKYRVPKLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD 160
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD 160


                  ....*...
gi 12734656   161 TISPEQAI 168
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-191 1.64e-87

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: 254.88  E-value: 1.64e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  29 ISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPKLLDLYQQCGIITHHHPI 108
Cdd:cd14505   1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656 109 ADGGTPD-IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGsGAIQTIKQYN 187
Cdd:cd14505  81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPKQEN 159


                ....
gi 12734656 188 YLHE 191
Cdd:cd14505 160 FLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-196 3.08e-24

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 93.11  E-value: 3.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  62 KDTEELKSCGIQDIFVFCTRGELskyrvpkLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCY 141
Cdd:COG2453  16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12734656 142 GGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAIQTIKQYNYLHEFRDKL 196
Cdd:COG2453  89 GGIGRTGTVAAAYLVLLG--LSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 41-191 2.46e-19

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: 79.70  E-value: 2.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  41 QFLGLCALPGCkfkdvrrNVQKDTEELKSCGIQDIFVFCTrgelskyrvpklldlyqqcgiithhhpiadggtpdiASCC 120
Cdd:cd14494   7 LRLIAGALPLS-------PLEADSRFLKQLGVTTIVDLTL------------------------------------AMVD 43

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12734656 121 EIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDtISPEQAIDSLRDLRGSGAIQTIKQYNYLHE 191
Cdd:cd14494  44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGG-MSAEEAVRIVRLIRPGGIPQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 65-192 2.14e-13

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: 66.22  E-value: 2.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  65 EELKSCGIQDIF--------VFCTRGELSKYRVPKLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKT 136
Cdd:cd14506  33 EQFKEKGIKTVInlqepgehASCGPGLEPESGFSYLPEAFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKV 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 12734656 137 LIHCYGGLGRSCLVAACLLLYLSDtISPEQAIDSLRDLRgSGAIQTIKQYNYLHEF 192
Cdd:cd14506 113 AVHCHAGLGRTGVLIACYLVYALR-MSADQAIRLVRSKR-PNSIQTRGQVLCVREF 166
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 87-192 4.61e-13

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: 63.84  E-value: 4.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  87 YRVPkLLDLYQQCGIITHHHPIADGGTP---DIASCCEIMEElttCLKNYRKTLIHCYGGLGRSCLVAACLLLYlSDTIS 163
Cdd:cd14504  37 EEPP-PEHSDTCPGLRYHHIPIEDYTPPtleQIDEFLDIVEE---ANAKNEAVLVHCLAGKGRTGTMLACYLVK-TGKIS 111

                        90       100
                ....*....|....*....|....*....
gi 12734656 164 PEQAIDSLRDLRGsGAIQTIKQYNYLHEF 192
Cdd:cd14504 112 AVDAINEIRRIRP-GSIETSEQEKFVIQF 139
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
74-191 1.73e-08

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 53.05  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656     74 DIFVFCTRGELSKYRVPKLLDL-YQQCG---IITHHHPIA--DGGTPDIASCC-EIMEELTTCLKNYRK-TLIHCYGGLG 145
Cdd:smart00194 127 DITVTLKSVEKVDDYTIRTLEVtNTGCSetrTVTHYHYTNwpDHGVPESPESIlDLIRAVRKSQSTSTGpIVVHCSAGVG 206

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 12734656    146 RS-CLVAACLLLYL---SDTISPEQAIDSLRDLRgSGAIQTIKQYNYLHE 191
Cdd:smart00194 207 RTgTFIAIDILLQQleaGKEVDIFEIVKELRSQR-PGMVQTEEQYIFLYR 255
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
104-191 1.85e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.44  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656    104 HHHPIADGGTPD----IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSC-LVAACLLLYL----SDTISPEQAIDSLRDL 174
Cdd:smart00404   6 HYTGWPDHGVPEspdsILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELRSQ 85

                           90
                   ....*....|....*..
gi 12734656    175 RgSGAIQTIKQYNYLHE 191
Cdd:smart00404  86 R-PGMVQTEEQYLFLYR 101
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 104-191 1.85e-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: 50.44  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656    104 HHHPIADGGTPD----IASCCEIMEELTTCLKNYRKTLIHCYGGLGRSC-LVAACLLLYL----SDTISPEQAIDSLRDL 174
Cdd:smart00012   6 HYTGWPDHGVPEspdsILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELRSQ 85

                           90
                   ....*....|....*..
gi 12734656    175 RgSGAIQTIKQYNYLHE 191
Cdd:smart00012  86 R-PGMVQTEEQYLFLYR 101
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 59-195 2.29e-08

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


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 51.45  E-value: 2.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  59 NVQKDTEELKSCGIQDIFVFCTRgelsKYRVPKLLDLyqqcGIITHHHPIADGGTPDIasccEIMEE----LTTCLKNYR 134
Cdd:cd14500  25 NLPLYIKELKKYNVTDLVRVCEP----TYDKEPLEKA----GIKVHDWPFDDGSPPPD----DVVDDwldlLKTRFKEEG 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12734656 135 KTL----IHCYGGLGRS-CLVAACLLLYlsdTISPEQAIDSLRDLRgSGAIqTIKQYNYLHEFRDK 195
Cdd:cd14500  93 KPGaciaVHCVAGLGRApVLVAIALIEL---GMKPEDAVEFIRKKR-RGAI-NSKQLQFLEKYKPK 153
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 62-175 2.48e-08

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: 50.62  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  62 KDTEELKSCGIQdiFVFCTRGELSKYRVPKlldlyqqcGIITHHHPIADGGTPDIAS----CCEIMEElttCLKNYRKTL 137
Cdd:cd14498  17 QDKELLKKLGIT--HILNVAGEPPPNKFPD--------GIKYLRIPIEDSPDEDILShfeeAIEFIEE---ALKKGGKVL 83

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 12734656 138 IHCYGGLGRSC-LVAACLLLYLSdtISPEQAIDSLRDLR 175
Cdd:cd14498  84 VHCQAGVSRSAtIVIAYLMKKYG--WSLEEALELVKSRR 120
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 96-195 4.06e-07

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: 47.64  E-value: 4.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  96 YQQCGIITHHHPIAD-GGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYlSDTISPEQAIDSLRDL 174
Cdd:cd14524  51 WKALGVEQLRLPTVDfTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQ-HKGWSPEEAQEFLRSK 129

                        90       100
                ....*....|....*....|.
gi 12734656 175 RGSGAIQTiKQYNYLHEFRDK 195
Cdd:cd14524 130 RPHILLRL-SQREVLEEFYRK 149
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 74-191 1.00e-06

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: 47.28  E-value: 1.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  74 DIFVFCTRGE-LSKYRVPKLLDLYQQCG---IITHHHPIA--DGGTPDIASccEIMEELTTCLKNYRK----TLIHCYGG 143
Cdd:cd00047  72 DITVTLVSEEeLSDYTIRTLELSPKGCSesrEVTHLHYTGwpDHGVPSSPE--DLLALVRRVRKEARKpngpIVVHCSAG 149

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12734656 144 LGRS----CLVAACLLLYLSDTISPEQAIDSLRDLRgSGAIQTIKQYNYLHE 191
Cdd:cd00047 150 VGRTgtfiAIDILLERLEAEGEVDVFEIVKALRKQR-PGMVQTLEQYEFIYE 200
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 100-193 1.60e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 43.47  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  100 GIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTL----IHCYGGLGRS-CLVAACLLLYlsDTISPEQAIDSLRDL 174
Cdd:PTZ00242  61 GIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFAKQSTPPetiaVHCVAGLGRApILVALALVEY--GGMEPLDAVGFVREK 138

                         90
                 ....*....|....*....
gi 12734656  175 RgSGAIQtIKQYNYLHEFR 193
Cdd:PTZ00242 139 R-KGAIN-QTQLQFLKKYK 155
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 65-195 1.74e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 44.15  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656   65 EELKSCGIQDIFVFCTRgelsKYRVPKLLDlyqqCGIITHHHPIADGGTP--DIAScceimEELTTC---LKNYRKTLIH 139
Cdd:PTZ00393 110 KEMKNYNVTDLVRTCER----TYNDGEITS----AGINVHELIFPDGDAPtvDIVS-----NWLTIVnnvIKNNRAVAVH 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 12734656  140 CYGGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAIQTiKQYNYLHEFRDK 195
Cdd:PTZ00393 177 CVAGLGRAPVLASIVLIEFG--MDPIDAIVFIRDRR-KGAINK-RQLQFLKAYKKK 228
PRK12361 PRK12361
hypothetical protein; Provisional
 107-195 3.70e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.84  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  107 PIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTiKQY 186
Cdd:PRK12361 149 PILDHSVPTLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIRKTARLNK-RQL 227


                 ....*....
gi 12734656  187 NYLHEFRDK 195
Cdd:PRK12361 228 RALEKMLEQ 236
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 89-175 6.48e-05

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: 41.49  E-value: 6.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  89 VPKLLDLYQQCGIITHHH-----PIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTIS 163
Cdd:cd14527  27 VPAVLDLTAELPRPRKRQayrcvPLLDLVAPTPEQLERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWLLAYGRAKS 106

                        90
                ....*....|..
gi 12734656 164 PEQAIDSLRDLR 175
Cdd:cd14527 107 VAEAEALIRAAR 118
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 131-191 1.61e-04

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 41.23  E-value: 1.61e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12734656 131 KNYRKTLIHCYGGLGRS-CLVAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTIKQYNYLHE 191
Cdd:cd14559 166 KNKLLPVIHCRAGVGRTgQLAAAMELNKSPNNLSVEDIVSDMRTSRNGKMVQKDEQLDTLKE 227
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
102-191 2.74e-04

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 40.69  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656   102 ITHHHPIA--DGGTPD----IASCCEIMEELTTCLKNyRKTLIHCYGGLGRS-CLVAACLLLYL---SDTISPEQAIDSL 171
Cdd:pfam00102 133 VKHFHYTGwpDHGVPEspnsLLDLLRKVRKSSLDGRS-GPIVVHCSAGIGRTgTFIAIDIALQQleaEGEVDIFQIVKEL 211

                          90       100
                  ....*....|....*....|
gi 12734656   172 RDLRGsGAIQTIKQYNYLHE 191
Cdd:pfam00102 212 RSQRP-GMVQTLEQYIFLYD 230
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
113-177 6.49e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.42  E-value: 6.49e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12734656    113 TPDIASCCEIMEElttCLKNYRKTLIHCYGGLGRS-CLVAACLLLYLSdtISPEQAIDSLRDLRGS 177
Cdd:smart00195  61 SPYFPEAVEFIED---AESKGGKVLVHCQAGVSRSaTLIIAYLMKTRN--MSLNDAYDFVKDRRPI 121
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 60-196 8.80e-04

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 38.44  E-value: 8.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  60 VQKDTEELKSCGIQDIFVFCTrgelSKYRVPklldLYQQCGIITHHHPIADGGTPDiascCEIMEELTTCLKN-YRK--- 135
Cdd:cd18536  27 LNKFTEELKKYGVTTLVRVCD----ATYDKA----PVEKEGIQVLDWPFDDGAPPP----NQIVDDWLNLLKTkFREepg 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12734656 136 --TLIHCYGGLGRSCLVAACLLLYLSdtISPEQAIDSLRDLRgSGAIQTiKQYNYLHEFRDKL 196
Cdd:cd18536  95 ccVAVHCVAGLGRAPVLVALALIECG--MKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 153
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 137-169 2.37e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.17  E-value: 2.37e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 12734656 137 LIHCYGGLGRSCLVAACLLLYLSDTISPEQAID 169
Cdd:cd14497  99 VVHCKAGKGRTGTVICAYLLYYGQYSTADEALE 131
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 136-190 2.71e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 37.89  E-value: 2.71e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 12734656 136 TLIHCYGGLGRS-CLVAA---CLLLYLSDTISPEQAIDSLRDLRGsGAIQTIKQYNYLH 190
Cdd:cd14612 184 IVVHCSAGIGRTgCFIATsigCQQLKDTGKVDILGIVCQLRLDRG-GMIQTSEQYQFLH 241
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 61-172 2.78e-03

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 36.97  E-value: 2.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  61 QKDTEELKSCGIQDIFVFCTRGELSKYRVPKLLDLyqqcGIITHHHPIaDGGTPDIA---SCCEIMEELTtclkNYRKTL 137
Cdd:cd14529  23 DEDRALLKKLGIKTVIDLRGADERAASEEAAAKID----GVKYVNLPL-SATRPTESdvqSFLLIMDLKL----APGPVL 93

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 12734656 138 IHCYGGLGRSCLVAA-CLLLYlsdTISPEQAIDSLR 172
Cdd:cd14529  94 IHCKHGKDRTGLVSAlYRIVY---GGSKEEANEDYR 126
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 110-190 2.95e-03

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 37.38  E-value: 2.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656 110 DGGTPDIASCCEIM-EELTTCLKNYRKT---LIHCYGGLGRS-CLVA---ACLLLylsdtiSPEQAID------SLRDLR 175
Cdd:cd14547 136 DHKTPEAAQPLLSLvQEVEEARQTEPHRgpiVVHCSAGIGRTgCFIAtsiGCQQL------REEGVVDvlgivcQLRLDR 209

                        90
                ....*....|....*
gi 12734656 176 GsGAIQTIKQYNYLH 190
Cdd:cd14547 210 G-GMVQTAEQYEFVH 223
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 136-190 5.36e-03

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 36.67  E-value: 5.36e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 12734656 136 TLIHCYGGLGRSCLVAAC-LLLYLSD---TISPEQAIDSLRDLRGSgAIQTIKQYNYLH 190
Cdd:cd14540 155 TLVHCSAGVGRTGVVILAdLMLYCLDhneELDIPRVLALLRHQRML-LVQTLAQYKFVY 212
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 58-175 5.75e-03

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 36.02  E-value: 5.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12734656  58 RNVQkDTEELKSCGIQDIFVFCTRGELSKYRVPK--LLDLYQQCGIITHHHPIADGGTPD----IASCCEIMEELttcLK 131
Cdd:cd14526  17 QNPE-DVDRLKKEGVTAVLNLQTDSDMEYWGVDIdsIRKACKESGIRYVRLPIRDFDTEDlrqkLPQAVALLYRL---LK 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 12734656 132 NYRKTLIHCYGGLGRSCLVaACLLLYLSDTISPEQAIDSLRDLR 175
Cdd:cd14526  93 NGGTVYVHCTAGLGRAPAT-VIAYLYWVLGYSLDEAYYLLTSKR 135
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 116-169 5.82e-03

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: 36.03  E-value: 5.82e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12734656 116 IASCCEIMEE-LTTCLKNYrkTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAID 169
Cdd:cd14509  78 IKPFCEDVDEwLKEDEKNV--AAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALD 130
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 128-177 6.79e-03

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: 35.32  E-value: 6.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 12734656   128 TCLKNYRKTLIHCYGGLGRS-CLVAACLLLYLSdtISPEQAIDSLRDLRGS 177
Cdd:pfam00782  64 DARQKGGKVLVHCQAGISRSaTLIIAYLMKTRN--LSLNEAYSFVKERRPG 112
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 136-191 6.91e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 36.15  E-value: 6.91e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12734656 136 TLIHCYGGLGRS-CLV----AACLLLYlSDTISPEQAIDSLRDLRGSgAIQTIKQYNYLHE 191
Cdd:cd14541 146 TVVHCSAGIGRTgVLItmetAMCLIEA-NEPVYPLDIVRTMRDQRAM-LIQTPSQYRFVCE 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 131-191 7.41e-03

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


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 36.18  E-value: 7.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12734656 131 KNYRKTLIHCYGGLGRSCLVAAclLLYLSDTISPEQAID------SLRDLRGSgAIQTIKQYNYLHE 191
Cdd:cd14548 159 QEKGPTIVHCSAGVGRTGTFIA--LDRLLQQIESEDYVDifgivyDLRKHRPL-MVQTEAQYIFLHQ 222
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 136-185 8.50e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 36.22  E-value: 8.50e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12734656 136 TLIHCYGGLGRS---CLVAACLLLYLSDTISPEQAIDSLRDLRGS--GAIQTIKQ 185
Cdd:cd14545 171 PVVHCSAGIGRSgtfCLVDTCLVLIEKGNPSSVDVKKVLLEMRKYrmGLIQTPDQ 225
 
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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