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Conserved domains on  [gi|254692985|ref|NP_082498|]
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cyclin-dependent kinase inhibitor 3 isoform 2 [Mus musculus]

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 ...
 1-167 1.41e-110

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: 313.50  E-value: 1.41e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985    1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLAACLLLYLSD 159
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRScLVAACLLLYLSD 160


                  ....*...
gi 254692985  160 SISPQQAI 167
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 ...
 1-167 1.41e-110

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: 313.50  E-value: 1.41e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985    1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLAACLLLYLSD 159
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRScLVAACLLLYLSD 160


                  ....*...
gi 254692985  160 SISPQQAI 167
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-190 9.29e-73

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: 217.52  E-value: 9.29e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  29 ISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPI 108
Cdd:cd14505    1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985 109 PDGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLL-LYLSDSISPQQAIDSLRDVRGsGAIQTIKQYN 186
Cdd:cd14505   81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLlLELGDTLDPEQAIAAVRALRP-GAIQTPKQEN 159


                 ....
gi 254692985 187 YLHE 190
Cdd:cd14505  160 FLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-195 2.77e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.70  E-value: 2.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  62 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 141
Cdd:COG2453   16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254692985 142 GGLGRSclaaclllylSDSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 195
Cdd:COG2453   89 GGIGRTgtvaa-aylvLLGLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 65-194 1.73e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 47.24  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  65 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 138
Cdd:PTZ00393 110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254692985 139 HCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 194
Cdd:PTZ00393 176 HCVAGLGRAPVLASIVLIEF-GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 104-190 1.34e-05

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: 42.73  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   104 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRS------CLAACLLLYLSDSISPQQAIDSLR 171
Cdd:smart00012   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTgtfvaiDILLQQLEAEAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 254692985   172 DVRgSGAIQTIKQYNYLHE 190
Cdd:smart00012  84 SQR-PGMVQTEEQYLFLYR 101
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 1-167 1.41e-110

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: 313.50  E-value: 1.41e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985    1 MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT 80
Cdd:pfam05706   1 MKPPISIQASEFDSSDEEPIDDEQTPIHISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   81 RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLAACLLLYLSD 159
Cdd:pfam05706  81 RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRScLVAACLLLYLSD 160


                  ....*...
gi 254692985  160 SISPQQAI 167
Cdd:pfam05706 161 SISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 29-190 9.29e-73

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: 217.52  E-value: 9.29e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  29 ISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPI 108
Cdd:cd14505    1 IDWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985 109 PDGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLL-LYLSDSISPQQAIDSLRDVRGsGAIQTIKQYN 186
Cdd:cd14505   81 PDGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLlLELGDTLDPEQAIAAVRALRP-GAIQTPKQEN 159


                 ....
gi 254692985 187 YLHE 190
Cdd:cd14505  160 FLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
62-195 2.77e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.70  E-value: 2.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  62 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 141
Cdd:COG2453   16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254692985 142 GGLGRSclaaclllylSDSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 195
Cdd:COG2453   89 GGIGRTgtvaa-aylvLLGLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 41-190 3.61e-10

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: 55.43  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  41 QFLGLCALPGCkfkdvrrNIQKDTEELKSYGIQDVFVFCtrgelskyrvpnLLDLYqqygivthhhpipdggtpdigscw 120
Cdd:cd14494    7 LRLIAGALPLS-------PLEADSRFLKQLGVTTIVDLT------------LAMVD------------------------ 43

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985 121 EIMEELATCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHE 190
Cdd:cd14494   44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 87-191 2.69e-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: 53.44  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  87 YRVPNLlDLYQQYGIVTHHHPIPDGGTP---DIGSCWEIMEElatCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDSISP 163
Cdd:cd14504   37 EEPPPE-HSDTCPGLRYHHIPIEDYTPPtleQIDEFLDIVEE---ANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKISA 112

                         90       100
                 ....*....|....*....|....*...
gi 254692985 164 QQAIDSLRDVRGsGAIQTIKQYNYLHEF 191
Cdd:cd14504  113 VDAINEIRRIRP-GSIETSEQEKFVIQF 139
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 65-191 3.17e-08

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: 51.58  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  65 EELKSYGIQDVF--------VFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKT 136
Cdd:cd14506   33 EQFKEKGIKTVInlqepgehASCGPGLEPESGFSYLPEAFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKV 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254692985 137 LIHCYGGLGRSCLAACLLLYLSDSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEF 191
Cdd:cd14506  113 AVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKR-PNSIQTRGQVLCVREF 166
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 65-194 1.73e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 47.24  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  65 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 138
Cdd:PTZ00393 110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254692985 139 HCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 194
Cdd:PTZ00393 176 HCVAGLGRAPVLASIVLIEF-GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 104-190 1.34e-05

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: 42.73  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   104 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRS------CLAACLLLYLSDSISPQQAIDSLR 171
Cdd:smart00012   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTgtfvaiDILLQQLEAEAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 254692985   172 DVRgSGAIQTIKQYNYLHE 190
Cdd:smart00012  84 SQR-PGMVQTEEQYLFLYR 101
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
104-190 1.34e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 42.73  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   104 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRS------CLAACLLLYLSDSISPQQAIDSLR 171
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTgtfvaiDILLQQLEAEAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 254692985   172 DVRgSGAIQTIKQYNYLHE 190
Cdd:smart00404  84 SQR-PGMVQTEEQYLFLYR 101
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 59-194 2.12e-05

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


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 42.98  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  59 NIQKDTEELKSYGIQDVFVFCTRgelsKYRVPNLLDLyqqyGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKT 136
Cdd:cd14500   25 NLPLYIKELKKYNVTDLVRVCEP----TYDKEPLEKA----GIKVHDWPFDDGSPPpdDVVDDW--LDLLKTRFKEEGKP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254692985 137 L----IHCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDVRgSGAIqTIKQYNYLHEFRDK 194
Cdd:cd14500   95 GaciaVHCVAGLGRAPVLVAIALIEL-GMKPEDAVEFIRKKR-RGAI-NSKQLQFLEKYKPK 153
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 62-147 6.71e-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: 41.38  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  62 KDTEELKSYGIQdvFVFCTRGELSKYRVPNlldlyqqyGIVTHHHPIPDGGTPDIGS----CWEIMEElatCLKNNRKTL 137
Cdd:cd14498   17 QDKELLKKLGIT--HILNVAGEPPPNKFPD--------GIKYLRIPIEDSPDEDILShfeeAIEFIEE---ALKKGGKVL 83

                         90
                 ....*....|
gi 254692985 138 IHCYGGLGRS 147
Cdd:cd14498   84 VHCQAGVSRS 93
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
101-190 2.30e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 41.11  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985   101 IVTHHHPI--PDGGTP-DIGSCWEIMEELATCLKNNRK-TLIHCYGGLGRS-----CLAACLLLYLSDSISPQQAIDSLR 171
Cdd:smart00194 158 TVTHYHYTnwPDHGVPeSPESILDLIRAVRKSQSTSTGpIVVHCSAGVGRTgtfiaIDILLQQLEAGKEVDIFEIVKELR 237

                           90
                   ....*....|....*....
gi 254692985   172 DVRgSGAIQTIKQYNYLHE 190
Cdd:smart00194 238 SQR-PGMVQTEEQYIFLYR 255
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 83-192 2.98e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 40.01  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  83 ELSKYRVPNLL---------DLYQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTL----IHCYGGLGRS 147
Cdd:PTZ00242  35 ELQRYNVTHLVrvcgptydaELLEKNGIEVHDWPFDDGAPPpkAVIDNW--LRLLDQEFAKQSTPPetiaVHCVAGLGRA 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 254692985 148 CLAACLLLYLSDSISPQQAIDSLRDVRgSGAIQtIKQYNYLHEFR 192
Cdd:PTZ00242 113 PILVALALVEYGGMEPLDAVGFVREKR-KGAIN-QTQLQFLKKYK 155
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 58-147 3.01e-04

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: 39.49  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  58 RNIQkDTEELKSYGIQDVFVFCTRGELSKYRV--PNLLDLYQQYGIVTHHHPIPDGGTPD----IGSCWEIMEELatcLK 131
Cdd:cd14526   17 QNPE-DVDRLKKEGVTAVLNLQTDSDMEYWGVdiDSIRKACKESGIRYVRLPIRDFDTEDlrqkLPQAVALLYRL---LK 92

                         90
                 ....*....|....*.
gi 254692985 132 NNRKTLIHCYGGLGRS 147
Cdd:cd14526   93 NGGTVYVHCTAGLGRA 108
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 65-194 1.40e-03

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 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: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 37.70  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  65 EELKSYGIQDVFVFCtrgELSKYRVPnlldlYQQYGIVTHHHPIPDGGTP--DIGSCWEIMEELATCLKNNRKTLIHCYG 142
Cdd:cd18535   31 EDLKKYGATTVVRVC---EVTYDKTP-----LEKDGITVVDWPFDDGAPPpgKVVEDWLSLLKTKFCEDPGCCVAVHCVA 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254692985 143 GLGRSCLAACLLLYLSdSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDK 194
Cdd:cd18535  103 GLGRAPVLVALALIES-GMKYEDAIQFIRQKR-RGAINS-KQLTYLEKYRPK 151
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 101-190 2.33e-03

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: 37.65  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985 101 IVTHHHPI--PDGGTPDIGScwEIMEELA----TCLKNNRKTLIHCYGGLGRS-----CLAACLLLYLSDSISPQQAIDS 169
Cdd:cd00047  103 EVTHLHYTgwPDHGVPSSPE--DLLALVRrvrkEARKPNGPIVVHCSAGVGRTgtfiaIDILLERLEAEGEVDVFEIVKA 180

                         90       100
                 ....*....|....*....|.
gi 254692985 170 LRDVRgSGAIQTIKQYNYLHE 190
Cdd:cd00047  181 LRKQR-PGMVQTLEQYEFIYE 200
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 60-195 8.74e-03

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: 35.36  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692985  60 IQKDTEELKSYGIQDVFVFCTrgelSKYRVPnlldLYQQYGIVTHHHPIPDGGTP--DIGSCW------EIMEELATCLK 131
Cdd:cd18536   27 LNKFTEELKKYGVTTLVRVCD----ATYDKA----PVEKEGIQVLDWPFDDGAPPpnQIVDDWlnllktKFREEPGCCVA 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254692985 132 nnrktlIHCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDKL 195
Cdd:cd18536   99 ------VHCVAGLGRAPVLVALALIEC-GMKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 153
 
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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