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Conserved domains on  [gi|568973603|ref|XP_006533220|]
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cellular tumor antigen p53 isoform X1 [Mus musculus]

Protein Classification

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 ...
 106-286 1.69e-97

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: 288.01  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603 106 FHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGdGL 185
Cdd:cd08367    1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDDG-HT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603 186 APPQHLIRVEgNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRD 265
Cdd:cd08367   80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158

                        170       180
                 ....*....|....*....|.
gi 568973603 266 SFEVRVCACPGRDRRTEEENF 286
Cdd:cd08367  159 VIEVRVCACPGRDRKNEEKAA 179
P53_tetramer pfam07710
P53 tetramerization motif;
316-350 2.80e-12

P53 tetramerization motif;


:

Pssm-ID: 462238  Cd Length: 42  Bit Score: 60.76  E-value: 2.80e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568973603  316 KKKPL--DGEYFTLKIRGRKRFEMFRELNEALELKDA 350
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDM 37
P53_TAD pfam08563
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ...
 9-31 1.27e-06

P53 transactivation motif; The binding of the p53 transactivation domain by regulatory proteins regulates p53 transcription activation. This motif is comprised of a single amphipathic alpha helix and contains a highly conserved sequence.


:

Pssm-ID: 462520  Cd Length: 25  Bit Score: 44.47  E-value: 1.27e-06
                          10        20
                  ....*....|....*....|...
gi 568973603    9 SDISLELPLSQETFSGLWKLLPP 31
Cdd:pfam08563   1 SDLGLELPLSQETFSDLWNLLPP 23
 
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 ...
 106-286 1.69e-97

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: 288.01  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603 106 FHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGdGL 185
Cdd:cd08367    1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDDG-HT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603 186 APPQHLIRVEgNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRD 265
Cdd:cd08367   80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158

                        170       180
                 ....*....|....*....|.
gi 568973603 266 SFEVRVCACPGRDRRTEEENF 286
Cdd:cd08367  159 VIEVRVCACPGRDRKNEEKAA 179
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 96-286 2.44e-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: 252.21  E-value: 2.44e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603   96 SQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPH 175
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603  176 HERCSDGDGLAPPQHLIRVEGNLyPEYL-EDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITL 254
Cdd:pfam00870  81 HRAKDDGNNDPIREHVIRCENPD-AEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTL 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568973603  255 EDSSGNLLGRDSFEVRVCACPGRDRRTEEENF 286
Cdd:pfam00870 160 EDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
P53_tetramer pfam07710
P53 tetramerization motif;
316-350 2.80e-12

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 60.76  E-value: 2.80e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568973603  316 KKKPL--DGEYFTLKIRGRKRFEMFRELNEALELKDA 350
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDM 37
P53_TAD pfam08563
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ...
 9-31 1.27e-06

P53 transactivation motif; The binding of the p53 transactivation domain by regulatory proteins regulates p53 transcription activation. This motif is comprised of a single amphipathic alpha helix and contains a highly conserved sequence.


Pssm-ID: 462520  Cd Length: 25  Bit Score: 44.47  E-value: 1.27e-06
                          10        20
                  ....*....|....*....|...
gi 568973603    9 SDISLELPLSQETFSGLWKLLPP 31
Cdd:pfam08563   1 SDLGLELPLSQETFSDLWNLLPP 23
 
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 ...
 106-286 1.69e-97

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: 288.01  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603 106 FHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGdGL 185
Cdd:cd08367    1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDDG-HT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603 186 APPQHLIRVEgNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRD 265
Cdd:cd08367   80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158

                        170       180
                 ....*....|....*....|.
gi 568973603 266 SFEVRVCACPGRDRRTEEENF 286
Cdd:cd08367  159 VIEVRVCACPGRDRKNEEKAA 179
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 96-286 2.44e-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: 252.21  E-value: 2.44e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603   96 SQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPH 175
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973603  176 HERCSDGDGLAPPQHLIRVEGNLyPEYL-EDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITL 254
Cdd:pfam00870  81 HRAKDDGNNDPIREHVIRCENPD-AEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTL 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568973603  255 EDSSGNLLGRDSFEVRVCACPGRDRRTEEENF 286
Cdd:pfam00870 160 EDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
P53_tetramer pfam07710
P53 tetramerization motif;
316-350 2.80e-12

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 60.76  E-value: 2.80e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568973603  316 KKKPL--DGEYFTLKIRGRKRFEMFRELNEALELKDA 350
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDM 37
P53_TAD pfam08563
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ...
 9-31 1.27e-06

P53 transactivation motif; The binding of the p53 transactivation domain by regulatory proteins regulates p53 transcription activation. This motif is comprised of a single amphipathic alpha helix and contains a highly conserved sequence.


Pssm-ID: 462520  Cd Length: 25  Bit Score: 44.47  E-value: 1.27e-06
                          10        20
                  ....*....|....*....|...
gi 568973603    9 SDISLELPLSQETFSGLWKLLPP 31
Cdd:pfam08563   1 SDLGLELPLSQETFSDLWNLLPP 23
 
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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