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Conserved domains on  [gi|454544715|ref|NP_001263626|]
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cellular tumor antigen p53 isoform j [Homo sapiens]

Protein Classification

P53 and P53_tetramer domain-containing protein( domain architecture ID 10170140)

P53 and P53_tetramer 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 ...
1-129 1.11e-68

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: 208.66  E-value: 1.11e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 454544715   1 MAIYKQSQHMTEVVRRCPHHERCsDSDGLAPPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCN 80
Cdd:cd08367   52 MLVYKDPEHVKEPVERCPNHRQG-DDGHTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQ 129
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 454544715  81 SSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEEN 129
Cdd:cd08367  130 NSCPGGINRRPIQLVFTLEDENGNVLGRRVIEVRVCACPGRDRKNEEKA 178
P53_tetramer pfam07710
P53 tetramerization motif;
160-199 7.39e-14

P53 tetramerization motif;


:

Pssm-ID: 462238  Cd Length: 42  Bit Score: 63.46  E-value: 7.39e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 454544715  160 KKKPL--DGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE 199
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 42
 
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 ...
1-129 1.11e-68

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: 208.66  E-value: 1.11e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 454544715   1 MAIYKQSQHMTEVVRRCPHHERCsDSDGLAPPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCN 80
Cdd:cd08367   52 MLVYKDPEHVKEPVERCPNHRQG-DDGHTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQ 129
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 454544715  81 SSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEEN 129
Cdd:cd08367  130 NSCPGGINRRPIQLVFTLEDENGNVLGRRVIEVRVCACPGRDRKNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
1-130 5.78e-60

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: 187.11  E-value: 5.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 454544715    1 MAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEgNLRVEYL-DDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMC 79
Cdd:pfam00870  62 MLVYSKSEHANDPVERCPNHRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMC 140
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 454544715   80 NSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 130
Cdd:pfam00870 141 KSSCPGGINRRPTALVFTLEDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
P53_tetramer pfam07710
P53 tetramerization motif;
160-199 7.39e-14

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 63.46  E-value: 7.39e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 454544715  160 KKKPL--DGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE 199
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 42
 
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 ...
1-129 1.11e-68

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: 208.66  E-value: 1.11e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 454544715   1 MAIYKQSQHMTEVVRRCPHHERCsDSDGLAPPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCN 80
Cdd:cd08367   52 MLVYKDPEHVKEPVERCPNHRQG-DDGHTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQ 129
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 454544715  81 SSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEEN 129
Cdd:cd08367  130 NSCPGGINRRPIQLVFTLEDENGNVLGRRVIEVRVCACPGRDRKNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
1-130 5.78e-60

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: 187.11  E-value: 5.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 454544715    1 MAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEgNLRVEYL-DDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMC 79
Cdd:pfam00870  62 MLVYSKSEHANDPVERCPNHRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMC 140
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 454544715   80 NSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 130
Cdd:pfam00870 141 KSSCPGGINRRPTALVFTLEDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
P53_tetramer pfam07710
P53 tetramerization motif;
160-199 7.39e-14

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 63.46  E-value: 7.39e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 454544715  160 KKKPL--DGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE 199
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 42
 
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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