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P02340 (P53_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellular tumor antigen p53
Alternative name(s):
Tumor suppressor p53
Gene names
Name:Tp53
Synonyms:P53, Trp53
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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 By similarity. 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, but seems to have to effect on cell-cycle regulation. Ref.28 Ref.29 Ref.30

Cofactor

Binds 1 zinc ion per subunit.

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 YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts with AURKB, SETD2, UHRF2 and NOC2L By similarity. Interacts with PML (via C-terminus). Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53. Interacts with DAXX. Interacts (when monomethylated at Lys-376) with L3MBTL1. Interacts with BANP, CDKN2AIP, NUAK1, STK11/LKB1 and E4F1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity. Interacts with AURKA, TRIM24 and BRD7. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Phosphorylated at Ser-309 and Ser-386 by CDK2 in response to DNA-damage. 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. Interacts with ANKRD2 By similarity. Interacts with RFFL (via RING-type zinc finger); involved in p53/TP53 ubiquitination By similarity. Ref.13 Ref.14 Ref.15 Ref.20 Ref.21 Ref.22 Ref.25 Ref.27 Ref.28 Ref.34 Ref.36

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. Ref.23

Domain

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

Post-translational modification

Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP By similarity. Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1. 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. Probably phosphorylated on by CDK7 in a CAK complex in response to DNA damage. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15 leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes By similarity. Phosphorylated on Ser-386 following UV but not gamma irradiation. Phosphorylated by HIPK1. Ref.14 Ref.16 Ref.17 Ref.23 Ref.24 Ref.26

Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Ref.19 Ref.23

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-285 and Lys-286, 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. Ref.23 Ref.28

Monomethylated at Lys-366 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-364 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-366 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-364. Dimethylated at Lys-367 EHMT1 and EHMT2. Monomethylated at Lys-376 SETD8, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-364 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation By similarity.

Sumoylated with SUMO1. Sumoylated at Lys-380 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.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Necrosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Mitochondrion
Nucleus
   DiseaseDisease mutation
Tumor suppressor
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell lineage commitment

Inferred from mutant phenotype PubMed 8788039. Source: MGI

DNA damage response, signal transduction by p53 class mediator

Inferred from direct assay PubMed 11790307PubMed 11884608. Source: MGI

DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from genetic interaction PubMed 16107883. Source: MGI

DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA strand renaturation

Inferred from sequence or structural similarity. Source: UniProtKB

T cell differentiation in thymus

Inferred from genetic interaction PubMed 16357222. Source: MGI

T cell lineage commitment

Inferred from mutant phenotype PubMed 8788039. Source: MGI

T cell proliferation involved in immune response

Inferred from genetic interaction PubMed 16357222. Source: MGI

apoptotic process

Inferred from direct assay PubMed 16183742. Source: MGI

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 14744935PubMed 15383658. Source: MGI

cellular response to UV

Inferred from genetic interaction PubMed 14963330. Source: MGI

cellular response to ionizing radiation

Inferred from genetic interaction PubMed 16286009. Source: MGI

central nervous system development

Inferred from genetic interaction PubMed 16199867. Source: MGI

chromosome organization

Inferred from genetic interaction PubMed 17053789PubMed 17200209. Source: MGI

determination of adult lifespan

Inferred from mutant phenotype PubMed 20818388. Source: BHF-UCL

double-strand break repair

Inferred from mutant phenotype PubMed 17912366. Source: MGI

embryo development ending in birth or egg hatching

Inferred from genetic interaction PubMed 16702401. Source: MGI

embryonic organ development

Inferred from genetic interaction PubMed 17470788. Source: MGI

gastrulation

Inferred from genetic interaction PubMed 17000767. Source: MGI

in utero embryonic development

Inferred from genetic interaction PubMed 17325035PubMed 9288110. Source: MGI

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from direct assay PubMed 12135983PubMed 16107883. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 20818388. Source: BHF-UCL

mitotic G1 DNA damage checkpoint

Inferred from mutant phenotype PubMed 16107883. Source: MGI

mitotic cell cycle arrest

Inferred from direct assay PubMed 17515607. Source: MGI

multicellular organism growth

Inferred from genetic interaction PubMed 17325035. Source: MGI

multicellular organismal development

Inferred from sequence or structural similarity. Source: UniProtKB

necroptotic process

Inferred from genetic interaction Ref.30. Source: MGI

negative regulation of DNA replication

Inferred from direct assay PubMed 11884608. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17912366PubMed 8183579. Source: MGI

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 19749791. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 12952892PubMed 17332504. Source: MGI

negative regulation of macromitophagy

Inferred from mutant phenotype PubMed 22044588. Source: MGI

negative regulation of neuroblast proliferation

Inferred from genetic interaction PubMed 9608530. Source: MGI

negative regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 22044588. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19749791. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19749791. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 15657445. Source: MGI

neuron apoptotic process

Inferred from mutant phenotype PubMed 17591690. Source: MGI

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 apoptotic process

Inferred from mutant phenotype PubMed 17068116. Source: MGI

positive regulation of cardiac muscle cell apoptotic process

Inferred from mutant phenotype PubMed 22044588. Source: MGI

positive regulation of cell aging

Inferred from mutant phenotype PubMed 10562313. Source: BHF-UCL

positive regulation of histone deacetylation

Inferred from direct assay PubMed 15657445. Source: MGI

positive regulation of mitochondrial membrane permeability

Inferred from genetic interaction Ref.30. Source: MGI

positive regulation of neuron apoptotic process

Inferred from direct assay PubMed 10894779. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 19749791. Source: BHF-UCL

positive regulation of release of cytochrome c from mitochondria

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of thymocyte apoptotic process

Inferred from mutant phenotype PubMed 20818388. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16098148PubMed 16107883PubMed 19411634PubMed 20368352PubMed 7677753PubMed 8183579. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15735665PubMed 16044147. Source: MGI

protein import into nucleus, translocation

Inferred from direct assay PubMed 11799106. Source: MGI

protein tetramerization

Inferred from electronic annotation. Source: InterPro

rRNA transcription

Inferred from genetic interaction PubMed 18809582. Source: MGI

regulation of cell cycle

Inferred from mutant phenotype PubMed 15898111. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 12878730. Source: MGI

regulation of mitochondrial membrane permeability involved in apoptotic process

Inferred from genetic interaction PubMed 14963330. Source: MGI

regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 15483136. Source: MGI

regulation of thymocyte apoptotic process

Inferred from genetic interaction PubMed 17210642. Source: MGI

regulation of tissue remodeling

Inferred from mutant phenotype PubMed 22044588. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12135983. Source: MGI

release of cytochrome c from mitochondria

Inferred from direct assay PubMed 15483136. Source: MGI

response to UV

Inferred from direct assay PubMed 14744935. Source: MGI

response to X-ray

Inferred from direct assay PubMed 11884608. Source: MGI

response to drug

Inferred from direct assay PubMed 9098922. Source: MGI

response to gamma radiation

Inferred from direct assay PubMed 14744935. Source: MGI

response to ischemia

Inferred from mutant phenotype PubMed 22044588. Source: MGI

response to oxidative stress

Inferred from mutant phenotype PubMed 17591690. Source: MGI

response to salt stress

Inferred from genetic interaction PubMed 16571598. Source: MGI

somitogenesis

Inferred from genetic interaction PubMed 17320900. Source: MGI

transforming growth factor beta receptor signaling pathway

Inferred from genetic interaction PubMed 18212064. Source: MGI

   Cellular_componentchromatin

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 11799106. Source: MGI

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from direct assay Ref.30. Source: MGI

mitochondrion

Inferred from direct assay PubMed 12667443. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

replication fork

Inferred from direct assay PubMed 15364958. Source: MGI

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

MDM2/MDM4 family protein binding

Inferred from physical interaction PubMed 20818388. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 21300779. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 22737085PubMed 24013501. Source: MGI

chromatin binding

Inferred from direct assay PubMed 15657445PubMed 18212064PubMed 20434500. Source: MGI

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

damaged DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

double-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

histone deacetylase regulator activity

Inferred from direct assay PubMed 15657445. Source: MGI

p53 binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.28. Source: UniProtKB

sequence-specific DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12135983PubMed 16044147PubMed 16098148. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Cellular tumor antigen p53
PRO_0000185709

Regions

DNA binding96 – 286191 By similarity
Region1 – 4242Transcription activation (acidic)
Region60 – 10445Interaction with WWOX By similarity
Region94 – 364271Interaction with HIPK1
Region94 – 294201Required for interaction with ZNF385A By similarity
Region107 – 230124Required for interaction with FBXO42 By similarity
Region110 – 286177Interaction with AXIN1
Region253 – 29139Interaction with E4F1 By similarity
Region267 – 2748Interaction with DNA
Region313 – 35442Interaction with HIPK2 By similarity
Region319 – 35032Oligomerization
Region353 – 3575Interaction with USP7 By similarity
Region362 – 38120Basic (repression of DNA-binding)
Motif299 – 31517Bipartite nuclear localization signal By similarity
Motif333 – 34412Nuclear export signal By similarity
Motif364 – 3663[KR]-[STA]-K motif

Sites

Metal binding1701Zinc
Metal binding1731Zinc
Metal binding2321Zinc
Metal binding2361Zinc
Site1141Interaction with DNA

Amino acid modifications

Modified residue91Phosphoserine; by HIPK4 Ref.26
Modified residue151Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM Ref.23
Modified residue181Phosphothreonine; by CK1, VRK1 and VRK2 By similarity
Modified residue201Phosphoserine; by CHEK2, CK1 and PLK3 By similarity
Modified residue341Phosphoserine; by MAPKAPK5 Ref.24
Modified residue1141N6-acetyllysine; by KAT6A By similarity
Modified residue1771Phosphoserine; by AURKB By similarity
Modified residue2631Phosphoserine; by AURKB By similarity
Modified residue2781Phosphothreonine; by AURKB By similarity
Modified residue2991N6-acetyllysine By similarity
Modified residue3091Phosphoserine; by AURKA, CDK1 and CDK2 By similarity
Modified residue3151N6-acetyllysine Ref.31
Modified residue3641N6,N6-dimethyllysine; alternate By similarity
Modified residue3641N6-methyllysine; by SMYD2; alternate By similarity
Modified residue3661N6-methyllysine; by SETD7 By similarity
Modified residue3671N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate By similarity
Modified residue3671N6-acetyllysine; alternate By similarity
Modified residue3751N6-acetyllysine By similarity
Modified residue3761N6,N6-dimethyllysine; alternate By similarity
Modified residue3761N6-acetyllysine; by KAT6A; alternate By similarity
Modified residue3761N6-methyllysine; by SETD8; alternate By similarity
Modified residue3861Phosphoserine; by CK2, CDK2 and NUAK1 By similarity
Cross-link285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Natural variant1321A → V Can cooperate with an activated Ras to transform fibroblasts. Ref.5
Natural variant1651E → G in clone P53-M11.
Natural variant1881L → R.

Experimental info

Sequence conflict451Q → R in CAA25323. Ref.3
Sequence conflict76 – 783PVA → QW in CAA25323. Ref.3

Secondary structure

......................................... 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02340 [UniParc].

Last modified March 18, 2008. Version 3.
Checksum: B55EB7B463E1DD9D

FASTA38743,155
        10         20         30         40         50         60 
MEESQSDISL ELPLSQETFS GLWKLLPPED ILPSPHCMDD LLLPQDVEEF FEGPSEALRV 

        70         80         90        100        110        120 
SGAPAAQDPV TETPGPVAPA PATPWPLSSF VPSQKTYQGN YGFHLGFLQS GTAKSVMCTY 

       130        140        150        160        170        180 
SPPLNKLFCQ LAKTCPVQLW VSATPPAGSR VRAMAIYKKS QHMTEVVRRC PHHERCSDGD 

       190        200        210        220        230        240 
GLAPPQHLIR VEGNLYPEYL EDRQTFRHSV VVPYEPPEAG SEYTTIHYKY MCNSSCMGGM 

       250        260        270        280        290        300 
NRRPILTIIT LEDSSGNLLG RDSFEVRVCA CPGRDRRTEE ENFRKKEVLC PELPPGSAKR 

       310        320        330        340        350        360 
ALPTCTSASP PQKKKPLDGE YFTLKIRGRK RFEMFRELNE ALELKDAHAT EESGDSRAHS 

       370        380 
SYLKTKKGQS TSRHKKTMVK KVGPDSD 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the gene coding for the murine cellular tumour antigen p53."
Bienz B., Zakut-Houri R., Givol D., Oren M.
EMBO J. 3:2179-2183(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A single gene and a pseudogene for the cellular tumour antigen p53."
Zakut-Houri R., Oren M., Bienz B., Lavie V., Hazum S., Givol D.
Nature 306:594-597(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and expression analysis of full length mouse cDNA sequences encoding the transformation associated protein p53."
Jenkins J.R., Rudge K., Redmond S., Wade-Evans A.
Nucleic Acids Res. 12:5609-5626(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Immunologically distinct p53 molecules generated by alternative splicing."
Arai N., Nomura D., Yokota K., Wolf D., Brill E., Shohat O., Rotter V.
Mol. Cell. Biol. 6:3232-3239(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (CLONES PCD53; P53-M11 AND P53-M8).
[5]"Primary structure of DNA complementary to mRNA of murine oncoprotein p53."
Chumakov P.M.
Bioorg. Khim. 13:1691-1694(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-132.
[6]"Cell cycle in DNA-PKcs knock-out mice."
Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SCID.
[7]"DNA-dependent protein kinase is not required for the p53-dependent response to DNA damage."
Jimenez G.S., Bryntesson F., Torres-Arzayus M.I., Priestley A., Beeche M., Saito S., Sakaguchi K., Appella E., Jeggo P.A., Taccioli G.E., Wahl G.M., Hubank M.
Nature 400:81-83(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]"Characterization of DNA-PKcs null mutant SX9."
Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[9]"p53 in 129-SVJ mice."
Fujimori A., Abe M.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvJ.
Tissue: Lung fibroblast.
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[11]"Loss of heterozygosity and mutational alterations of the p53 gene in skin tumours of interspecific hybrid mice."
Burns P.A., Kemp C.J., Gannon J.V., Lane D.P., Bremner R., Balmain A.
Oncogene 6:2363-2369(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-255.
[12]"Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse."
DeLeo A.B., Jay G., Appella E., Dubois G.C., Law L.W., Old L.J.
Proc. Natl. Acad. Sci. U.S.A. 76:2420-2424(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCOVERY OF P53.
[13]"p53 is involved in the p120E4F-mediated growth arrest."
Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J., Schneider C., Del Sal G.
Oncogene 19:188-199(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E4F1.
[14]"Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)."
Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A., Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W., Mak T.W., Thukral S.K.
Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK1, PHOSPHORYLATION.
[15]"Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation."
Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.
EMBO J. 23:4583-4594(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1, IDENTIFICATION IN A COMPLEX WITH HIPK2 AND AXIN1.
[16]"Mapping of phosphomonoester and apparent phosphodiester bonds of the oncogene product p53 from simian virus 40-transformed 3T3 cells."
Samad A., Anderson C.W., Carroll R.B.
Proc. Natl. Acad. Sci. U.S.A. 83:897-901(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-309 AND SER-386, RNA-BINDING.
[17]"The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II."
Meek D.W., Simon S., Kikkawa U., Eckhart W.
EMBO J. 9:3253-3260(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-386.
[18]"p53 is covalently linked to 5.8S rRNA."
Fontoura B.M., Sorokina E.A., David E., Carroll R.B.
Mol. Cell. Biol. 12:5145-5151(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PUTATIVE RNA-BINDING.
[19]"Negative control of p53 by Sir2alpha promotes cell survival under stress."
Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., Gu W.
Cell 107:137-148(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEACETYLATION BY SIRT1.
[20]"Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of p53 ubiquitination."
Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.
Int. J. Oncol. 24:357-364(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP7.
[21]"Differential effect of ik3-1/cables on p53- and p73-induced cell death."
Tsuji K., Mizumoto K., Yamochi T., Nishimoto I., Matsuoka M.
J. Biol. Chem. 277:2951-2957(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP73.
[22]"Direct interaction with and activation of p53 by SMAR1 retards cell-cycle progression at G2/M phase and delays tumor growth in mice."
Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S., Chattopadhyay S.
Int. J. Cancer 103:606-615(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BANP.
[23]"PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-15, LYSINE ACETYLATION, UBIQUITINATION, SUBCELLULAR LOCATION.
[24]"PRAK is essential for ras-induced senescence and tumor suppression."
Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C., Chen J., Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III, Wright P.E., Han J.
Cell 128:295-308(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-34.
[25]"Hzf Determines cell survival upon genotoxic stress by modulating p53 transactivation."
Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A., Lee S.W.
Cell 130:624-637(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF385A.
[26]"Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9."
Arai S., Matsushita A., Du K., Yagi K., Okazaki Y., Kurokawa R.
FEBS Lett. 581:5649-5657(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-9.
[27]"CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment during early embryogenesis."
Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S., Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.
Nat. Cell Biol. 11:172-182(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHD8.
[28]"Trim24 targets endogenous p53 for degradation."
Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A., Johnson R.L., Barton M.C.
Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH TRIM24.
[29]"A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response."
Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.
Cell 142:409-419(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"p53 opens the mitochondrial permeability transition pore to trigger necrosis."
Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S., Moll U.M.
Cell 149:1536-1548(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[32]"Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution."
Zhao K., Chai X., Johnston K., Clements A., Marmorstein R.
J. Biol. Chem. 276:12120-12127(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-281.
[33]"High-resolution structure of the p53 core domain: implications for binding small-molecule stabilizing compounds."
Ho W.C., Luo C., Zhao K., Chai X., Fitzgerald M.X., Marmorstein R.
Acta Crystallogr. D 62:1484-1493(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 92-289.
[34]"Structure of the p53 core domain dimer bound to DNA."
Ho W.C., Fitzgerald M.X., Marmorstein R.
J. Biol. Chem. 281:20494-20502(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 92-289 IN COMPLEX WITH DNA AND ZINC IONS, SUBUNIT.
[35]"Crystal structure of the mouse p53 core domain in zinc-free state."
Kwon E., Kim D.Y., Suh S.W., Kim K.K.
Proteins 70:280-283(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-284.
[36]"Crystal structure of a p53 core tetramer bound to DNA."
Malecka K.A., Ho W.C., Marmorstein R.
Oncogene 28:325-333(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-289 IN COMPLEX WITH DNA, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00876 expand/collapse EMBL AC list , X00877, X00878, X00879, X00880, X00881, X00882, X00883, X00884, X00885 Genomic DNA. Translation: CAA25420.1.
X01237 mRNA. Translation: CAA25625.1.
X00741 mRNA. Translation: CAA25323.1.
M13872 mRNA. Translation: AAA39881.1.
M13873 mRNA. Translation: AAA39882.1.
M13874 mRNA. Translation: AAA39883.1. Sequence problems.
AB021961 mRNA. Translation: BAA82344.1.
AF151353 mRNA. Translation: AAD39535.1.
AB017815 mRNA. Translation: BAA82339.1.
AB017816 mRNA. Translation: BAA82340.1.
AB020317 mRNA. Translation: BAA82343.1.
BC005448 mRNA. Translation: AAH05448.1.
S77930 Genomic DNA. Translation: AAB21108.2.
PIRDNMS53. A22739.
S38824.
RefSeqNP_001120705.1. NM_001127233.1.
NP_035770.2. NM_011640.3.
XP_006533220.1. XM_006533157.1.
XP_006533221.1. XM_006533158.1.
UniGeneMm.222.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C96-281[»]
2GEQX-ray2.30A/B89-289[»]
2IOIX-ray1.55A92-289[»]
2IOMX-ray2.00A92-289[»]
2IOOX-ray2.02A92-289[»]
2P52X-ray1.50A89-284[»]
3EXJX-ray2.00A/B93-289[»]
3EXLX-ray2.20A93-289[»]
ProteinModelPortalP02340.
SMRP02340. Positions 88-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204323. 79 interactions.
DIPDIP-369N.
IntActP02340. 35 interactions.
MINTMINT-120104.
STRING10090.ENSMUSP00000104298.

Chemistry

ChEMBLCHEMBL4164.

PTM databases

PhosphoSiteP02340.

Proteomic databases

PRIDEP02340.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552.
GeneID22059.
KEGGmmu:22059.
UCSCuc007jql.2. mouse.

Organism-specific databases

CTD22059.
MGIMGI:98834. Trp53.

Phylogenomic databases

eggNOGNOG80479.
GeneTreeENSGT00390000015092.
HOGENOMHOG000039957.
HOVERGENHBG005201.
InParanoidP02340.
KOK04451.
OrthoDBEOG7JQBNW.

Gene expression databases

ArrayExpressP02340.
BgeeP02340.
CleanExMM_TRP53.
GenevestigatorP02340.

Family and domain databases

Gene3D2.60.40.720. 1 hit.
4.10.170.10. 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]
PRINTSPR00386. P53SUPPRESSR.
SUPFAMSSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEPS00348. P53. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02340.
NextBio301858.
PROP02340.
SOURCESearch...

Entry information

Entry nameP53_MOUSE
AccessionPrimary (citable) accession number: P02340
Secondary accession number(s): Q9QUP3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 18, 2008
Last modified: July 9, 2014
This is version 185 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot