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Conserved domains on  [gi|35210|emb|CAA26306|]
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unnamed protein product [Homo sapiens]

Protein Classification

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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 ...
 109-288 4.93e-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: 286.86  E-value: 4.93e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210    109 FRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCsDSDGL 188
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210    189 APPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRN 268
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158

                       170       180
                ....*....|....*....|
gi 35210    269 SFEVRVCACPGRDRRTEEEN 288
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
P53_tetramer pfam07710
P53 tetramerization motif;
319-358 2.26e-14

P53 tetramerization motif;


:

Pssm-ID: 462238  Cd Length: 42  Bit Score: 66.54  E-value: 2.26e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 35210      319 KKKPL--DGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE 358
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 42
TAD2 pfam18521
Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in ...
 35-59 2.86e-11

Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in p53 proteins. In p53 two TAD domains are found termed TAD1 (residues 1-39) and TAD2 (residues 40-61), both of which have been shown to be able to independently activate gene transcription and are intrinsically disordered protein domains that adopt a helical conformation for at least part of their length when bound. This inherent flexibility allows the TADs to adapt to and bind a broad range of proteins. This entry describes TAD2 which can independently interact with Taz2 domain of the histone acetyltransferase p300. It has also been shown to bind to OB-fold domain of replication protein 70 A (RPA) as well as the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH.


:

Pssm-ID: 375947  Cd Length: 25  Bit Score: 57.45  E-value: 2.86e-11
                          10        20
                  ....*....|....*....|....*
gi 35210       35 LPSQAMDDLMLSPDDIEQWFTEDPG 59
Cdd:pfam18521   1 LPSQAMDDLMLSPDDIEQWFTEDPG 25
P53_TAD pfam08563
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ...
 6-30 2.60e-08

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: 49.09  E-value: 2.60e-08
                          10        20
                  ....*....|....*....|....*
gi 35210        6 SDPSVEPPLSQETFSDLWKLLPENN 30
Cdd:pfam08563   1 SDLGLELPLSQETFSDLWNLLPPST 25
 
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 ...
 109-288 4.93e-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: 286.86  E-value: 4.93e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210    109 FRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCsDSDGL 188
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210    189 APPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRN 268
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158

                       170       180
                ....*....|....*....|
gi 35210    269 SFEVRVCACPGRDRRTEEEN 288
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 99-289 2.11e-85

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: 257.60  E-value: 2.11e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210       99 SQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPH 178
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210      179 HERCSDSDGLAPPQHLIRVEgNLRVEYL-DDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITL 257
Cdd:pfam00870  81 HRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTL 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 35210      258 EDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 289
Cdd:pfam00870 160 EDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
P53_tetramer pfam07710
P53 tetramerization motif;
319-358 2.26e-14

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 66.54  E-value: 2.26e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 35210      319 KKKPL--DGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE 358
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 42
TAD2 pfam18521
Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in ...
 35-59 2.86e-11

Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in p53 proteins. In p53 two TAD domains are found termed TAD1 (residues 1-39) and TAD2 (residues 40-61), both of which have been shown to be able to independently activate gene transcription and are intrinsically disordered protein domains that adopt a helical conformation for at least part of their length when bound. This inherent flexibility allows the TADs to adapt to and bind a broad range of proteins. This entry describes TAD2 which can independently interact with Taz2 domain of the histone acetyltransferase p300. It has also been shown to bind to OB-fold domain of replication protein 70 A (RPA) as well as the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH.


Pssm-ID: 375947  Cd Length: 25  Bit Score: 57.45  E-value: 2.86e-11
                          10        20
                  ....*....|....*....|....*
gi 35210       35 LPSQAMDDLMLSPDDIEQWFTEDPG 59
Cdd:pfam18521   1 LPSQAMDDLMLSPDDIEQWFTEDPG 25
P53_TAD pfam08563
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ...
 6-30 2.60e-08

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: 49.09  E-value: 2.60e-08
                          10        20
                  ....*....|....*....|....*
gi 35210        6 SDPSVEPPLSQETFSDLWKLLPENN 30
Cdd:pfam08563   1 SDLGLELPLSQETFSDLWNLLPPST 25
 
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 ...
 109-288 4.93e-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: 286.86  E-value: 4.93e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210    109 FRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCsDSDGL 188
Cdd:cd08367   1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQG-DDGHT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210    189 APPQHLIRVEgNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRN 268
Cdd:cd08367  80 APNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRR 158

                       170       180
                ....*....|....*....|
gi 35210    269 SFEVRVCACPGRDRRTEEEN 288
Cdd:cd08367 159 VIEVRVCACPGRDRKNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 99-289 2.11e-85

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: 257.60  E-value: 2.11e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210       99 SQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPH 178
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35210      179 HERCSDSDGLAPPQHLIRVEgNLRVEYL-DDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITL 257
Cdd:pfam00870  81 HRAKDDGNNDPIREHVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTL 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 35210      258 EDSSGNLLGRNSFEVRVCACPGRDRRTEEENL 289
Cdd:pfam00870 160 EDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
P53_tetramer pfam07710
P53 tetramerization motif;
319-358 2.26e-14

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 66.54  E-value: 2.26e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 35210      319 KKKPL--DGEYFTLQIRGRERFEMFRELNEALELKDAQAGKE 358
Cdd:pfam07710   1 KKRPLssDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 42
TAD2 pfam18521
Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in ...
 35-59 2.86e-11

Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in p53 proteins. In p53 two TAD domains are found termed TAD1 (residues 1-39) and TAD2 (residues 40-61), both of which have been shown to be able to independently activate gene transcription and are intrinsically disordered protein domains that adopt a helical conformation for at least part of their length when bound. This inherent flexibility allows the TADs to adapt to and bind a broad range of proteins. This entry describes TAD2 which can independently interact with Taz2 domain of the histone acetyltransferase p300. It has also been shown to bind to OB-fold domain of replication protein 70 A (RPA) as well as the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH.


Pssm-ID: 375947  Cd Length: 25  Bit Score: 57.45  E-value: 2.86e-11
                          10        20
                  ....*....|....*....|....*
gi 35210       35 LPSQAMDDLMLSPDDIEQWFTEDPG 59
Cdd:pfam18521   1 LPSQAMDDLMLSPDDIEQWFTEDPG 25
P53_TAD pfam08563
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ...
 6-30 2.60e-08

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: 49.09  E-value: 2.60e-08
                          10        20
                  ....*....|....*....|....*
gi 35210        6 SDPSVEPPLSQETFSDLWKLLPENN 30
Cdd:pfam08563   1 SDLGLELPLSQETFSDLWNLLPPST 25
 
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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