Cellular tumor antigen p53 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P10361 (P53_RAT)

Last modified February 9, 2010. Version 118. History...

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

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Names and origin

Protein names

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

Gene names

Name:	Tp53
Synonyms:	P53

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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 BANP. Interacts with ARMD10, E4F1 and CDKN2AIP. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity By similarity. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction By similarity. Interacts with HSP90AB1. Directly interacts with FBXO42; leading to ubiquination and degradation of TP53 By similarity. Ref.5
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	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 by HIPK1. Phosphorylated on Ser-390 following UV but not gamma irradiation. 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. Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence By similarity. Ubiquitinated by SYVN1, which leads to proteasomal degradation By similarity. Ubiquitinated by MKRN1 at Lys-289 and Lys-290, which leads to proteasomal degradation By similarity. Monomethylated at Lys-370 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-368 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-370 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-368 By similarity. Sumoylated by SUMO1 By similarity. Demethylation of di-methylated Lys-368 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.

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Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Disease	Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	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 multicellular organismal development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of smooth muscle cell proliferation Inferred from mutant phenotype. Source: RGD nucleotide-excision repair Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of apoptosis Inferred from mutant phenotype. Source: RGD positive regulation of cell cycle Inferred from mutant phenotype. Source: RGD positive regulation of gene-specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB positive regulation of leukocyte migration Inferred from mutant phenotype. Source: RGD regulation of intracellular pH Inferred from mutant phenotype. Source: RGD response to UV Inferred from expression pattern. Source: RGD response to X-ray Inferred from expression pattern. Source: RGD response to amino acid stimulus Inferred from expression pattern. Source: RGD response to caffeine Inferred from expression pattern. Source: RGD response to cytokine stimulus Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to hyperoxia Inferred from expression pattern. Source: RGD response to metal ion Inferred from expression pattern. Source: RGD response to oxidative stress Inferred from expression pattern. Source: RGD response to retinoic acid Inferred from expression pattern. Source: RGD response to tumor cell Inferred from electronic annotation. Source: InterPro response to vitamin B3 Inferred from expression pattern. Source: RGD transcription Inferred from electronic annotation. Source: UniProtKB-KW wound healing Inferred from expression pattern. Source: RGD
Cellular component	chromatin Inferred from direct assay. Source: RGD cytosol Inferred from direct assay. Source: RGD 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 transcription factor complex Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB DNA strand annealing activity Inferred from sequence or structural similarity. Source: UniProtKB RNA polymerase II transcription factor activity Traceable author statement. Source: RGD copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay. Source: RGD transcription factor activity Inferred from electronic annotation. Source: InterPro transcription repressor activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bard1	O70445	1	EBI-1790304,EBI-1790207	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 391

391

Cellular tumor antigen p53

PRO_0000185712

Regions

DNA binding

100 – 290

191

By similarity

Region

1 – 47

Transcription activation (acidic)

Region

64 – 108

Interaction with WWOX By similarity

Region

98 – 368

271

Interaction with HIPK1 By similarity

Region

111 – 234

124

Required for interaction with FBXO42 By similarity

Region

114 – 290

177

Interaction with AXIN1 By similarity

Region

254 – 292

Interaction with E4F1 By similarity

Region

317 – 358

Interaction with HIPK2 By similarity

Region

323 – 354

Oligomerization

Region

357 – 361

Interaction with USP7 By similarity

Region

366 – 385

Basic (repression of DNA-binding)

Motif

303 – 319

Bipartite nuclear localization signal By similarity

Motif

337 – 348

Nuclear export signal By similarity

Motif

368 – 370

[KR]-[STA]-K motif

Sites

Metal binding

174

Zinc By similarity

Metal binding

177

Zinc By similarity

Metal binding

236

Zinc By similarity

Metal binding

240

Zinc By similarity

Amino acid modifications

Modified residue

Phosphoserine; by HIPK4 By similarity

Modified residue

Phosphoserine; by PRPK By similarity

Modified residue

Phosphothreonine; by VRK1 By similarity

Modified residue

Phosphoserine By similarity

Modified residue

290

N6-acetyllysine By similarity

Modified residue

303

N6-acetyllysine By similarity

Modified residue

311

Phosphoserine By similarity

Modified residue

312

Phosphoserine By similarity

Modified residue

368

N6-methyllysine By similarity

Modified residue

370

N6-methyllysine By similarity

Modified residue

371

N6-acetyllysine By similarity

Modified residue

379

N6-acetyllysine By similarity

Modified residue

380

N6-acetyllysine By similarity

Modified residue

390

Phosphoserine; by CK2 By similarity

Cross-link

289

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

Cross-link

290

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

Cross-link

384

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

Natural variations

Natural variant

103

G → S

Natural variant

256

E → G

Experimental info

Sequence conflict

174

C → W in AAA41788. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P10361-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E62522313A5C872F
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FASTA

391

43,451

        10         20         30         40         50         60 
MEDSQSDMSI ELPLSQETFS CLWKLLPPDD ILPTTATGSP NSMEDLFLPQ DVAELLEGPE 

        70         80         90        100        110        120 
EALQVSAPAA QEPGTEAPAP VAPASATPWP LSSSVPSQKT YQGNYGFHLG FLQSGTAKSV 

       130        140        150        160        170        180 
MCTYSISLNK LFCQLAKTCP VQLWVTSTPP PGTRVRAMAI YKKSQHMTEV VRRCPHHERC 

       190        200        210        220        230        240 
SDGDGLAPPQ HLIRVEGNPY AEYLDDRQTF RHSVVVPYEP PEVGSDYTTI HYKYMCNSSC 

       250        260        270        280        290        300 
MGGMNRRPIL TIITLEDSSG NLLGRDSFEV RVCACPGRDR RTEEENFRKK EEHCPELPPG 

       310        320        330        340        350        360 
SAKRALPTST SSSPQQKKKP LDGEYFTLKI RGRERFEMFR ELNEALELKD ARAAEESGDS 

       370        380        390 
RAHSSYPKTK KGQSTSRHKK PMIKKVGPDS D

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA encoding the rat p53 nuclear oncoprotein." Soussi T. Nucleic Acids Res. 16:11384-11384(1988) [PubMed: 3060862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the rat p53 tumor suppressor gene." Hulla J.E., Schneider R.P. Nucleic Acids Res. 21:713-717(1993) [PubMed: 8441680] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Glucose catabolism in cancer cells. The type II hexokinase promoter contains functionally active response elements for the tumor suppressor p53." Mathupala S.P., Heese C., Pedersen P.L. J. Biol. Chem. 272:22776-22780(1997) [PubMed: 9278438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.
[4]	"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]. Tissue: Heart and Thymus.
[5]	"Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell." Sepehrnia B., Paz I.B., Dasgupta G., Momand J. J. Biol. Chem. 271:15084-15090(1996) [PubMed: 8663025] [Abstract] Cited for: INTERACTION WITH HSP90AB1. Tissue: Embryo.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X13058 mRNA. Translation: CAA31457.1. L07910 L07909 Genomic DNA. Translation: AAA41788.1. U90328 mRNA. Translation: AAB80959.1. BC081788 mRNA. Translation: AAH81788.2. BC098663 mRNA. Translation: AAH98663.1.
IPI	IPI00734784.
PIR	S02192.
RefSeq	NP_112251.2.
UniGene	Rn.54443
3D structure databases
SMR	P10361. Positions 93-288, 317-358.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10361. 1 interaction.
STRING	P10361.
PTM databases
PhosphoSite	P10361.
Genome annotation databases
Ensembl	ENSRNOT00000046490; ENSRNOP00000047840; ENSRNOG00000010756; Rattus norvegicus. [Genome view]
GeneID	24842.
KEGG	rno:24842.
UCSC	NM_030989. rat.
Organism-specific databases
CTD	24842.
RGD	3889. Tp53.
Phylogenomic databases
eggNOG	roNOG04248.
HOVERGEN	P10361.
InParanoid	P10361.
OMA	IHYNFMC.
OrthoDB	EOG92JRBM.
Gene expression databases
ArrayExpress	P10361.
Genevestigator	P10361.
GermOnline	ENSRNOG00000010756. Rattus norvegicus.
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
NextBio	604596.

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Entry information

Entry name

P53_RAT

Accession

Primary (citable) accession number: P10361
Secondary accession number(s): O09168, Q4KMA9, Q66HM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	February 9, 2010
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents