NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1041817975|ref|NP_001316079|]
View 

tumor protein 63 isoform 12 [Homo sapiens]

Protein Classification

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

P53 and P53_tetramer domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 14-179 8.84e-90

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: 266.06  E-value: 8.84e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  14 EYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEgqiAPPSHLIRVEgNSH 93
Cdd:cd08367    17 TYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDDGHT---APNSHVIRCE-NPQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  94 AQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDR 173
Cdd:cd08367    93 AEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRRVIEVRVCACPGRDR 172


                  ....*.
gi 1041817975 174 KADEDS 179
Cdd:cd08367   173 KNEEKA 178
P53_tetramer pfam07710
P53 tetramerization motif;
208-248 2.16e-17

P53 tetramerization motif;


:

Pssm-ID: 462238  Cd Length: 42  Bit Score: 74.63  E-value: 2.16e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1041817975 208 KKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHT 248
Cdd:pfam07710   2 KRPLSSDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 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 ...
 14-179 8.84e-90

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: 266.06  E-value: 8.84e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  14 EYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEgqiAPPSHLIRVEgNSH 93
Cdd:cd08367    17 TYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDDGHT---APNSHVIRCE-NPQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  94 AQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDR 173
Cdd:cd08367    93 AEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRRVIEVRVCACPGRDR 172


                  ....*.
gi 1041817975 174 KADEDS 179
Cdd:cd08367   173 KNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 5-179 1.50e-80

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: 242.96  E-value: 1.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975   5 ENNAQTQFSEYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPpsH 84
Cdd:pfam00870  18 SKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPNHRAKDDGNNDPIRE--H 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  85 LIRVEgNSHAQYV-EDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEA 163
Cdd:pfam00870  96 VIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTLEDPDGQVLGRQSISV 174

                         170
                  ....*....|....*.
gi 1041817975 164 RICACPGRDRKADEDS 179
Cdd:pfam00870 175 KVCSCPKRDRRKEEKA 190
P53_tetramer pfam07710
P53 tetramerization motif;
208-248 2.16e-17

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 74.63  E-value: 2.16e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1041817975 208 KKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHT 248
Cdd:pfam07710   2 KRPLSSDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 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 ...
 14-179 8.84e-90

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: 266.06  E-value: 8.84e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  14 EYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEgqiAPPSHLIRVEgNSH 93
Cdd:cd08367    17 TYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDDGHT---APNSHVIRCE-NPQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  94 AQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDR 173
Cdd:cd08367    93 AEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLGRRVIEVRVCACPGRDR 172


                  ....*.
gi 1041817975 174 KADEDS 179
Cdd:cd08367   173 KNEEKA 178
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 5-179 1.50e-80

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: 242.96  E-value: 1.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975   5 ENNAQTQFSEYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPpsH 84
Cdd:pfam00870  18 SKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPNHRAKDDGNNDPIRE--H 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041817975  85 LIRVEgNSHAQYV-EDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEA 163
Cdd:pfam00870  96 VIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVFTLEDPDGQVLGRQSISV 174

                         170
                  ....*....|....*.
gi 1041817975 164 RICACPGRDRKADEDS 179
Cdd:pfam00870 175 KVCSCPKRDRRKEEKA 190
P53_tetramer pfam07710
P53 tetramerization motif;
208-248 2.16e-17

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 74.63  E-value: 2.16e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1041817975 208 KKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHT 248
Cdd:pfam07710   2 KRPLSSDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQSQ 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH