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Reviewed, UniProtKB/Swiss-Prot P02340 (P53_MOUSE)

Last modified February 9, 2010. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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.

Cofactor

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 P53DINP1. 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 By similarity. Directly interacts with FBXO42; leading to ubiquination and degradation of TP53 By similarity. Interacts with BANP, CDKN2AIP and E4F1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity. Ref.13 Ref.14 Ref.15 Ref.20 Ref.22 Ref.25

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum By similarity. Note: Interaction with BANP promotes nuclear localization By similarity.

Domain

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

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. 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, which may prevent the interaction with MDM2. Phosphorylated on Ser-386 following UV but not gamma irradiation. Phosphorylated by HIPK1. Ref.14 Ref.16 Ref.17 Ref.23

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

Ubiquitinated by SYVN1, which leads to proteasomal degradation By similarity. Ubiquitinated by MKRN1 at Lys-285 and Lys-286, which leads to proteasomal degradation By similarity.

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 By similarity.

Sumoylated by SUMO1 By similarity.

Demethylation of di-methylated Lys-364 by KDM1/LSD1 prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation 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
Transcription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   DiseaseDisease mutation
Tumor suppressor
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Gene Ontology (GO)
   Biological processB cell lineage commitment

Inferred from mutant phenotype. Source: MGI

DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis

Inferred from mutant phenotype. Source: MGI

G1/S DNA damage checkpoint

Inferred from mutant phenotype. Source: MGI

T cell differentiation in the thymus

Inferred from genetic interaction. Source: MGI

T cell lineage commitment

Inferred from mutant phenotype. Source: MGI

T cell proliferation during immune response

Inferred from genetic interaction. Source: MGI

activation of caspase activity by cytochrome c

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

cellular response to UV

Inferred from genetic interaction. Source: MGI

central nervous system development

Inferred from genetic interaction. Source: MGI

chromosome organization

Inferred from genetic interaction. Source: MGI

double-strand break repair

Inferred from mutant phenotype. Source: MGI

gastrulation

Inferred from genetic interaction. Source: MGI

in utero embryonic development

Inferred from genetic interaction. Source: MGI

multicellular organism growth

Inferred from genetic interaction. Source: MGI

negative regulation of DNA replication

Inferred from direct assay. Source: MGI

negative regulation of apoptosis

Inferred from mutant phenotype. Source: MGI

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fibroblast proliferation

Inferred from direct assay. Source: MGI

negative regulation of neuroblast proliferation

Inferred from genetic interaction. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay. Source: MGI

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype. Source: MGI

nucleotide-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of histone deacetylation

Inferred from direct assay. Source: MGI

positive regulation of neuron apoptosis

Inferred from direct assay. Source: MGI

protein import into nucleus, translocation

Inferred from direct assay. Source: MGI

rRNA transcription

Inferred from genetic interaction. Source: MGI

regulation of mitochondrial membrane permeability

Inferred from genetic interaction. Source: MGI

release of cytochrome c from mitochondria

Inferred from direct assay. Source: MGI

response to X-ray

Inferred from direct assay. Source: MGI

response to drug

Inferred from direct assay. Source: MGI

response to gamma radiation

Inferred from direct assay. Source: MGI

response to salt stress

Inferred from genetic interaction. Source: MGI

response to tumor cell

Inferred from electronic annotation. Source: InterPro

somitogenesis

Inferred from genetic interaction. Source: MGI

transforming growth factor beta receptor signaling pathway

Inferred from genetic interaction. Source: MGI

   Cellular componentcytosol

Inferred from direct assay. Source: MGI

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

replication fork

Inferred from direct assay. Source: MGI

   Molecular functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA strand annealing activity

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from direct assay. Source: MGI

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase regulator activity

Inferred from direct assay. Source: MGI

transcription factor activity

Inferred from direct assay. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P030706EBI-474016,EBI-617698From a different organism.
ATMQ133151EBI-474016,EBI-495465From a different organism.
Bard1O704451EBI-474016,EBI-1790207
BCL2L1Q07817-12EBI-474016,EBI-287195From a different organism.
CHEK2O960171EBI-474016,EBI-1180783From a different organism.
EP300Q094721EBI-474016,EBI-447295From a different organism.
Mapkapk5O549921EBI-474016,EBI-1202132
Mdm2P238041EBI-474016,EBI-641788
PIAS4Q8N2W92EBI-474016,EBI-473160From a different organism.
Ppp1ccP63087-11EBI-474016,EBI-450267
Smarcd1Q614661EBI-474016,EBI-371529
VRK1Q999861EBI-474016,EBI-1769146From a different organism.

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
Region107 – 230124Required for interaction with FBXO42 By similarity
Region110 – 286177Interaction with AXIN1
Region253 – 29139Interaction with E4F1 By similarity
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

Amino acid modifications

Modified residue91Phosphoserine; by HIPK4 Ref.23
Modified residue151Phosphoserine; by PRPK By similarity
Modified residue181Phosphothreonine; by VRK1 By similarity
Modified residue931Phosphoserine By similarity
Modified residue2861N6-acetyllysine By similarity
Modified residue2991N6-acetyllysine By similarity
Modified residue3071Phosphoserine By similarity
Modified residue3091Phosphoserine Ref.16
Modified residue3641N6-methyllysine By similarity
Modified residue3661N6-methyllysine By similarity
Modified residue3671N6-acetyllysine By similarity
Modified residue3751N6-acetyllysine By similarity
Modified residue3761N6-acetyllysine By similarity
Modified residue3861Phosphoserine; by CK2 Ref.16 Ref.17
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
P02340-1 [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: 6092064] [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: 6646235] [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: 6379601] [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: 3023970] [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: 3329909] [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: 10403253] [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: 15489334] [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: 1766680] [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: 221923] [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: 10644996] [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: 12702766] [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: 15526030] [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: 3006031] [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: 2145148] [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: 1406686] [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: 11672522] [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: 14719112] [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: 11706030] [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: 12494467] [Abstract]
Cited for: INTERACTION WITH BANP.
[23]"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: 18022393] [Abstract]
Cited for: PHOSPHORYLATION AT SER-9.
[24]"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: 11152481] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-281.
[25]"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: 19151705] [Abstract]
Cited for: INTERACTION WITH CHD8.
+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.
IPIIPI00406306.
PIRDNMS53. A22739.
S38824.
RefSeqNP_001120705.1.
NP_035770.2.
UniGeneMm.222

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C96-281[»]
2GEQX-ray2.30A/B92-289[»]
2IOIX-ray1.55A92-289[»]
2IOMX-ray2.00A92-289[»]
2IOOX-ray2.02A92-289[»]
2P52X-ray1.50A92-284[»]
3EXJX-ray2.00A/B93-289[»]
3EXLX-ray2.20A93-289[»]
SMRP02340. Positions 313-354.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-369N.
IntActP02340. 20 interactions.
STRINGP02340.

PTM databases

PhosphoSiteP02340.

Genome annotation databases

EnsemblENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552; Mus musculus. [Genome view]
ENSMUST00000108658; ENSMUSP00000104298; ENSMUSG00000059552; Mus musculus. [Genome view]
GeneID22059.
KEGGmmu:22059.
UCSCuc007jqn.1. mouse.

Organism-specific databases

CTD22059.
MGIMGI:98834. Trp53.

Phylogenomic databases

HOVERGENP02340.
InParanoidP02340.
OrthoDBEOG92JRBM.
PhylomeDBP02340.

Gene expression databases

ArrayExpressP02340.
BgeeP02340.
CleanExMM_TRP53.
GenevestigatorP02340.
GermOnlineENSMUSG00000059552. Mus musculus.

Family and domain databases

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_Ag.
IPR015551. Trp53.
[Graphical view]
Gene3DG3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit.
G3DSA:4.10.170.10. p53_tetrameristn. 1 hit.
PANTHERPTHR11447. Trp53. 1 hit.
PfamPF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]
PRINTSPR00386. P53SUPPRESSR.
PROSITEPS00348. P53. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: February 9, 2010
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents