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P13481 (P53_CHLAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cellular tumor antigen p53
Alternative name(s):
Tumor suppressor p53
Gene names
OrganismChlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Taxonomic identifier9534 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeChlorocebus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)


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. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation By similarity.


Binds 1 zinc ion per subunit By similarity.

Subunit structure

Binds DNA as a homotetramer. Found in a complex with CABLES1 and TP73. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. The C-terminus interacts with TAF1, when TAF1 is part of the TFIID complex. Interacts with HIPK1, HIPK2, AXIN1, and TP53INP1. Part of a complex consisting of TP53, HIPK2 and AXIN1. Interacts with WWOX. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with ARMD10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53. Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when monomethylated at Lys-382) with L3MBTL1. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA). Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion By similarity. Interacts with KAT6A By similarity. Interacts with UBC9 By similarity. Forms a complex with UBC9 and PRKRA By similarity. Interacts with ZNF385B; the interaction is direct By similarity. Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest By similarity. Interacts with ANKRD2 By similarity. Interacts with RFFL (via RING-type zinc finger); involved in p53/TP53 ubiquitination By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum By similarity. Mitochondrion matrix By similarity. Note: Interaction with BANP promotes nuclear localization. Translocates to mitochondria upon oxidative stress By similarity.


The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase By similarity.

Post-translational modification

Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter By similarity. Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Phosphorylated on Thr-55 by TAF1 which promotes MDM2-mediated TP53 degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated by HIPK1. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage By similarity.

Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence By similarity.

Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1 at Lys-291 and Lys-292, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24 and RFFL, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it By similarity.

Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370. Dimethylated at Lys-373 by EHMT1 and EHMT2. Monomethylated at Lys-382 by SETD8, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation By similarity.

Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9 By similarity.

Involvement in disease

p53 is found in increased amounts in a wide variety of transformed cells. p53 is frequently mutated or inactivated in many types of cancer.

Sequence similarities

Belongs to the p53 family.


   Biological processApoptosis
Cell cycle
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
   DiseaseTumor suppressor
   Molecular functionActivator
Isopeptide bond
Ubl conjugation
Gene Ontology (GO)
   Biological_processDNA strand renaturation

Inferred from sequence or structural similarity. Source: UniProtKB

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of release of cytochrome c from mitochondria

Inferred from sequence or structural similarity. Source: UniProtKB

protein tetramerization

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW


Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell


Inferred from sequence or structural similarity. Source: UniProtKB


Inferred from sequence or structural similarity. Source: UniProtKB


Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Cellular tumor antigen p53


DNA binding102 – 292191 By similarity
Region1 – 8383Interaction with HRMT1L2 By similarity
Region1 – 4444Transcription activation (acidic)
Region66 – 11045Interaction with WWOX By similarity
Region100 – 370271Interaction with HIPK1 By similarity
Region100 – 300201Required for interaction with ZNF385A By similarity
Region113 – 236124Required for interaction with FBXO42 By similarity
Region116 – 292177Interaction with AXIN1 By similarity
Region256 – 29439Interaction with E4F1 By similarity
Region273 – 2808Interaction with DNA By similarity
Region300 – 39394Interaction with CARM1 By similarity
Region319 – 36042Interaction with HIPK2 By similarity
Region325 – 35632Oligomerization
Region359 – 3635Interaction with USP7 By similarity
Region368 – 38720Basic (repression of DNA-binding)
Motif305 – 32117Bipartite nuclear localization signal By similarity
Motif339 – 35012Nuclear export signal By similarity
Motif370 – 3723[KR]-[STA]-K motif


Metal binding1761Zinc By similarity
Metal binding1791Zinc By similarity
Metal binding2381Zinc By similarity
Metal binding2421Zinc By similarity
Site1201Interaction with DNA By similarity

Amino acid modifications

Modified residue91Phosphoserine; by HIPK4 By similarity
Modified residue151Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM By similarity
Modified residue181Phosphothreonine; by CK1, VRK1 and VRK2 By similarity
Modified residue201Phosphoserine; by CHEK2, CK1 and PLK3 By similarity
Modified residue331Phosphoserine; by CDK5 and CDK7 By similarity
Modified residue371Phosphoserine; by MAPKAPK5 By similarity
Modified residue461Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG By similarity
Modified residue551Phosphothreonine; by TAF1 and GRK5; alternate By similarity
Modified residue551Phosphothreonine; by TAF1; alternate By similarity
Modified residue1201N6-acetyllysine; by KAT6A By similarity
Modified residue1831Phosphoserine; by AURKB By similarity
Modified residue2691Phosphoserine; by AURKB By similarity
Modified residue2841Phosphothreonine; by AURKB By similarity
Modified residue3051N6-acetyllysine By similarity
Modified residue3151Phosphoserine; by AURKA, CDK1 and CDK2 By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue3701N6,N6-dimethyllysine; alternate By similarity
Modified residue3701N6-methyllysine; by SMYD2; alternate By similarity
Modified residue3721N6-methyllysine; by SETD7 By similarity
Modified residue3731N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate By similarity
Modified residue3731N6-acetyllysine; alternate By similarity
Modified residue3811N6-acetyllysine By similarity
Modified residue3821N6,N6-dimethyllysine; alternate By similarity
Modified residue3821N6-acetyllysine; by KAT6A; alternate By similarity
Modified residue3821N6-methyllysine; by SETD8; alternate By similarity
Modified residue3921Phosphoserine; by CK2, CDK2 and NUAK1 By similarity
Cross-link291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity


Sequence LengthMass (Da)Tools
P13481 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 9ED285C9A7855D6E

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[1]"Nucleotide sequence of a cDNA encoding the monkey cellular phosphoprotein p53."
Rigaudy P., Eckhardt W.
Nucleic Acids Res. 17:8375-8375(1989) [PubMed] [Europe PMC] [Abstract]
Tissue: Liver.


Sequence databases

X16384 mRNA. Translation: CAA34420.1.

3D structure databases

SMRP13481. Positions 94-297, 325-356.

Protocols and materials databases


Phylogenomic databases


Family and domain databases

Gene3D2.60.40.720. 1 hit. 1 hit.
InterProIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR010991. p53_tetrameristn.
IPR013872. p53_transactivation_domain.
IPR002117. p53_tumour_suppressor.
[Graphical view]
PANTHERPTHR11447. PTHR11447. 1 hit.
PfamPF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]
SUPFAMSSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEPS00348. P53. 1 hit.
[Graphical view]

Entry information

Entry nameP53_CHLAE
AccessionPrimary (citable) accession number: P13481
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents


Index of protein domains and families