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Conserved domains on  [gi|60594460]
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Chain A, CELLULAR TUMOR ANTIGEN P53

Protein Classification

P53 domain-containing protein( domain architecture ID 10170125)

P53 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
16-195 8.00e-95

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


:

Pssm-ID: 176262  Cd Length: 179  Bit Score: 274.53  E-value: 8.00e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460  16 FRLGFLHSGTAKSVACTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQRMTEVVRRCPHHERCsDSDGL 95
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460  96 APPQHLIRVEgNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRSPILTIITLEDSSGNLLGRD 175
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158
                       170       180
                ....*....|....*....|
gi 60594460 176 SFEVRVCACPGRDRRTEEEN 195
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
 
Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
16-195 8.00e-95

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


Pssm-ID: 176262  Cd Length: 179  Bit Score: 274.53  E-value: 8.00e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460  16 FRLGFLHSGTAKSVACTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQRMTEVVRRCPHHERCsDSDGL 95
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460  96 APPQHLIRVEgNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRSPILTIITLEDSSGNLLGRD 175
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158
                       170       180
                ....*....|....*....|
gi 60594460 176 SFEVRVCACPGRDRRTEEEN 195
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
6-196 6.45e-83

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


Pssm-ID: 459972 [Multi-domain]  Cd Length: 191  Bit Score: 244.89  E-value: 6.45e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460     6 SQKTYQGSYGFRLGFLHSGTAKSVACTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQRMTEVVRRCPH 85
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460    86 HERCSDSDGLAPPQHLIRVEgNLRAEYL-DDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRSPILTIITL 164
Cdd:pfam00870  81 HRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTL 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 60594460   165 EDSSGNLLGRDSFEVRVCACPGRDRRTEEENL 196
Cdd:pfam00870 160 EDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
 
Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
16-195 8.00e-95

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


Pssm-ID: 176262  Cd Length: 179  Bit Score: 274.53  E-value: 8.00e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460  16 FRLGFLHSGTAKSVACTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQRMTEVVRRCPHHERCsDSDGL 95
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460  96 APPQHLIRVEgNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRSPILTIITLEDSSGNLLGRD 175
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158
                       170       180
                ....*....|....*....|
gi 60594460 176 SFEVRVCACPGRDRRTEEEN 195
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
6-196 6.45e-83

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


Pssm-ID: 459972 [Multi-domain]  Cd Length: 191  Bit Score: 244.89  E-value: 6.45e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460     6 SQKTYQGSYGFRLGFLHSGTAKSVACTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQRMTEVVRRCPH 85
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60594460    86 HERCSDSDGLAPPQHLIRVEgNLRAEYL-DDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRSPILTIITL 164
Cdd:pfam00870  81 HRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTL 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 60594460   165 EDSSGNLLGRDSFEVRVCACPGRDRRTEEENL 196
Cdd:pfam00870 160 EDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
 
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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