E9PFT5 · E9PFT5_HUMAN
- ProteinCellular tumor antigen p53
- GeneTP53
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids300 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | mitochondrial matrix | |
Cellular Component | PML body | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | metal ion binding | |
Molecular Function | transcription cis-regulatory region binding | |
Biological Process | apoptotic process | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | protein tetramerization | |
Biological Process | rhythmic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCellular tumor antigen p53
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionE9PFT5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,565 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 198 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Binds DNA as a homotetramer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-30 | p53 transactivation | ||||
Sequence: SDPSVEPPLSQETFSDLWKLLPENN | ||||||
Domain | 28-195 | p53 DNA-binding | ||||
Sequence: ENNVLYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEEN | ||||||
Compositional bias | 189-208 | Basic and acidic residues | ||||
Sequence: RRTEEENLRKKGEPHHELPP | ||||||
Region | 189-232 | Disordered | ||||
Sequence: RRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDG | ||||||
Compositional bias | 212-226 | Polar residues | ||||
Sequence: KRALPNNTSSSPQPK | ||||||
Domain | 226-264 | p53 tetramerisation | ||||
Sequence: KKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGK | ||||||
Region | 258-300 | Disordered | ||||
Sequence: KDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD | ||||||
Compositional bias | 273-287 | Basic residues | ||||
Sequence: SSHLKSKKGQSTSRH |
Sequence similarities
Belongs to the p53 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length300
- Mass (Da)33,979
- Last updated2024-01-24 v2
- Checksum07AB4CB91429F72D
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P04637 | P53_HUMAN | TP53 | 393 | ||
J3KP33 | J3KP33_HUMAN | TP53 | 343 | ||
A0A0U1RQC9 | A0A0U1RQC9_HUMAN | TP53 | 410 | ||
A0AAQ5BHZ9 | A0AAQ5BHZ9_HUMAN | TP53 | 411 | ||
A0AAQ5BHX5 | A0AAQ5BHX5_HUMAN | TP53 | 367 | ||
A0AAQ5BHY1 | A0AAQ5BHY1_HUMAN | TP53 | 347 | ||
E7EQX7 | E7EQX7_HUMAN | TP53 | 285 | ||
E7ESS1 | E7ESS1_HUMAN | TP53 | 199 | ||
E9PCY9 | E9PCY9_HUMAN | TP53 | 127 | ||
E7EMR6 | E7EMR6_HUMAN | TP53 | 165 | ||
S4R334 | S4R334_HUMAN | TP53 | 386 | ||
A0A386NBZ1 | A0A386NBZ1_HUMAN | TP53 | 35 | ||
A0A087X1Q1 | A0A087X1Q1_HUMAN | TP53 | 234 | ||
I3L0W9 | I3L0W9_HUMAN | TP53 | 344 | ||
A0A087WT22 | A0A087WT22_HUMAN | TP53 | 187 | ||
A0A087WXZ1 | A0A087WXZ1_HUMAN | TP53 | 182 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 189-208 | Basic and acidic residues | ||||
Sequence: RRTEEENLRKKGEPHHELPP | ||||||
Compositional bias | 212-226 | Polar residues | ||||
Sequence: KRALPNNTSSSPQPK | ||||||
Compositional bias | 273-287 | Basic residues | ||||
Sequence: SSHLKSKKGQSTSRH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC007421 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC087388 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |