Reviewed, UniProtKB/Swiss-Prot P02340 (P53_MOUSE)

Names and origin

Protein names

Recommended name:
    Cellular tumor antigen p53
Alternative name(s):
    Tumor suppressor p53

Gene names

Name:	Tp53
Synonyms:	P53, Trp53

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Disease	Disease mutation Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	B 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 component	cytosol 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 function	ATP 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
	P03070	6	EBI-474016,EBI-617698	From a different organism.
ATM	Q13315	1	EBI-474016,EBI-495465	From a different organism.
Bard1	O70445	1	EBI-474016,EBI-1790207
BCL2L1	Q07817-1	2	EBI-474016,EBI-287195	From a different organism.
CHEK2	O96017	1	EBI-474016,EBI-1180783	From a different organism.
EP300	Q09472	1	EBI-474016,EBI-447295	From a different organism.
Mapkapk5	O54992	1	EBI-474016,EBI-1202132
Mdm2	P23804	1	EBI-474016,EBI-641788
PIAS4	Q8N2W9	2	EBI-474016,EBI-473160	From a different organism.
Ppp1cc	P63087-1	1	EBI-474016,EBI-450267
Smarcd1	Q61466	1	EBI-474016,EBI-371529
VRK1	Q99986	1	EBI-474016,EBI-1769146	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 387

387

Cellular tumor antigen p53

PRO_0000185709

Regions

DNA binding

96 – 286

191

By similarity

Region

1 – 42

42

Transcription activation (acidic)

Region

60 – 104

45

Interaction with WWOX By similarity

Region

94 – 364

271

Interaction with HIPK1

Region

107 – 230

124

Required for interaction with FBXO42 By similarity

Region

110 – 286

177

Interaction with AXIN1

Region

253 – 291

39

Interaction with E4F1 By similarity

Region

313 – 354

42

Interaction with HIPK2 By similarity

Region

319 – 350

32

Oligomerization

Region

353 – 357

5

Interaction with USP7 By similarity

Region

362 – 381

20

Basic (repression of DNA-binding)

Motif

299 – 315

17

Bipartite nuclear localization signal By similarity

Motif

333 – 344

12

Nuclear export signal By similarity

Motif

364 – 366

3

[KR]-[STA]-K motif

Sites

Metal binding

170

1

Zinc

Metal binding

173

1

Zinc

Metal binding

232

1

Zinc

Metal binding

236

1

Zinc

Amino acid modifications

Modified residue

9

1

Phosphoserine; by HIPK4 Ref.23

Modified residue

15

1

Phosphoserine; by PRPK By similarity

Modified residue

18

1

Phosphothreonine; by VRK1 By similarity

Modified residue

93

1

Phosphoserine By similarity

Modified residue

286

1

N6-acetyllysine By similarity

Modified residue

299

1

N6-acetyllysine By similarity

Modified residue

307

1

Phosphoserine By similarity

Modified residue

309

1

Phosphoserine Ref.16

Modified residue

364

1

N6-methyllysine By similarity

Modified residue

366

1

N6-methyllysine By similarity

Modified residue

367

1

N6-acetyllysine By similarity

Modified residue

375

1

N6-acetyllysine By similarity

Modified residue

376

1

N6-acetyllysine By similarity

Modified residue

386

1

Phosphoserine; by CK2 Ref.16 Ref.17

Cross-link

285

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

286

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

380

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Natural variant

132

1

A → V Can cooperate with an activated Ras to transform fibroblasts. Ref.5

Natural variant

165

1

E → G in clone P53-M11.

Natural variant

188

1

L → R

Experimental info

Sequence conflict

45

1

Q → R in CAA25323. Ref.3

Sequence conflict

76 – 78

3

PVA → QW in CAA25323. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

387

Helix Strand Turn

Details...

Helix

102 – 104

3

Beta strand

107 – 109

3

Beta strand

121 – 124

4

Turn

125 – 128

4

Beta strand

129 – 132

4

Beta strand

138 – 143

6

Beta strand

153 – 162

10

Turn

163 – 167

5

Helix

174 – 177

4

Beta strand

184 – 186

3

Beta strand

191 – 196

6

Beta strand

201 – 204

4

Turn

206 – 208

3

Beta strand

211 – 216

6

Beta strand

225 – 233

9

Turn

240 – 245

6

Beta strand

248 – 255

8

Beta strand

261 – 271

11

Helix

275 – 284

10

Sequences

	Sequence		Length	Mass (Da)
	P02340-1 [UniParc]. Last modified March 18, 2008. Version 3. Checksum: B55EB7B463E1DD9D	FASTA	387	43,155
	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

References

	« Hide 'large scale' referencesShow '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 , 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.

IPI

IPI00406306.

PIR

DNMS53. A22739.
S38824.

RefSeq

NP_001120705.1.
NP_035770.2.

UniGene

Mm.222

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HU8	X-ray	2.70	A/B/C	96-281	[»]
2GEQ	X-ray	2.30	A/B	92-289	[»]
2IOI	X-ray	1.55	A	92-289	[»]
2IOM	X-ray	2.00	A	92-289	[»]
2IOO	X-ray	2.02	A	92-289	[»]
2P52	X-ray	1.50	A	92-284	[»]
3EXJ	X-ray	2.00	A/B	93-289	[»]
3EXL	X-ray	2.20	A	93-289	[»]

SMR

P02340. Positions 313-354.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-369N.

IntAct

P02340. 20 interactions.

STRING

P02340.

PTM databases

PhosphoSite

P02340.

Genome annotation databases

Ensembl

ENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552; Mus musculus. [Genome view]
ENSMUST00000108658; ENSMUSP00000104298; ENSMUSG00000059552; Mus musculus. [Genome view]

GeneID

22059.

KEGG

mmu:22059.

UCSC

uc007jqn.1. mouse.

Organism-specific databases

CTD

22059.

MGI

MGI:98834. Trp53.

Phylogenomic databases

HOVERGEN

P02340.

InParanoid

P02340.

OrthoDB

EOG92JRBM.

PhylomeDB

P02340.

Gene expression databases

ArrayExpress

P02340.

Bgee

P02340.

CleanEx

MM_TRP53.

Genevestigator

P02340.

GermOnline

ENSMUSG00000059552. Mus musculus.

Family and domain databases

InterPro

IPR008967. 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]

Gene3D

G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit.
G3DSA:4.10.170.10. p53_tetrameristn. 1 hit.

PANTHER

PTHR11447. Trp53. 1 hit.

Pfam

PF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]

PRINTS

PR00386. P53SUPPRESSR.

PROSITE

PS00348. P53. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

P53_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)