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P10361

- P53_RAT

UniProt

P10361 - P53_RAT

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Protein

Cellular tumor antigen p53

Gene

Tp53

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation (By similarity).By similarity

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei118 – 1181Interaction with DNABy similarity
Metal bindingi174 – 1741ZincBy similarity
Metal bindingi177 – 1771ZincBy similarity
Metal bindingi236 – 2361ZincBy similarity
Metal bindingi240 – 2401ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi100 – 290191By similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. chromatin binding Source: RefGenome
  3. copper ion binding Source: UniProtKB
  4. damaged DNA binding Source: RefGenome
  5. DNA binding Source: UniProtKB
  6. double-stranded DNA binding Source: RefGenome
  7. p53 binding Source: RefGenome
  8. protein C-terminus binding Source: RGD
  9. sequence-specific DNA binding Source: RGD
  10. sequence-specific DNA binding transcription factor activity Source: RefGenome
  11. transcription cofactor binding Source: RGD
  12. transcription regulatory region DNA binding Source: InterPro
  13. ubiquitin protein ligase binding Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. cell aging Source: UniProtKB
  3. cellular response to heat Source: RGD
  4. cellular response to organonitrogen compound Source: RGD
  5. cellular response to UV Source: RefGenome
  6. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
  7. DNA strand renaturation Source: UniProtKB
  8. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: RefGenome
  9. mitotic G1 DNA damage checkpoint Source: RefGenome
  10. multicellular organismal development Source: UniProtKB
  11. negative regulation of cell growth Source: UniProtKB
  12. negative regulation of DNA biosynthetic process Source: RGD
  13. negative regulation of smooth muscle cell proliferation Source: RGD
  14. negative regulation of transcription, DNA-templated Source: UniProtKB
  15. negative regulation of transcription from RNA polymerase II promoter Source: RefGenome
  16. nucleotide-excision repair Source: UniProtKB
  17. oligodendrocyte apoptotic process Source: UniProtKB
  18. positive regulation of apoptotic process Source: RGD
  19. positive regulation of cell cycle Source: RGD
  20. positive regulation of histone deacetylation Source: RefGenome
  21. positive regulation of leukocyte migration Source: RGD
  22. positive regulation of neuron apoptotic process Source: RefGenome
  23. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  24. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  25. protein tetramerization Source: InterPro
  26. regulation of intracellular pH Source: RGD
  27. regulation of transcription from RNA polymerase II promoter Source: RGD
  28. response to amino acid Source: RGD
  29. response to caffeine Source: RGD
  30. response to cytokine Source: RGD
  31. response to drug Source: RGD
  32. response to gamma radiation Source: RefGenome
  33. response to hyperoxia Source: RGD
  34. response to inorganic substance Source: RGD
  35. response to metal ion Source: RGD
  36. response to organic cyclic compound Source: RGD
  37. response to organonitrogen compound Source: RGD
  38. response to oxidative stress Source: RGD
  39. response to retinoic acid Source: RGD
  40. response to UV Source: RGD
  41. response to UV-B Source: RGD
  42. response to vitamin B3 Source: RGD
  43. response to X-ray Source: RGD
  44. transcription, DNA-templated Source: UniProtKB-KW
  45. wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Cell cycle, Necrosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular tumor antigen p53
Alternative name(s):
Tumor suppressor p53
Gene namesi
Name:Tp53
Synonyms:P53
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi3889. Tp53.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum By similarity. Mitochondrion matrix 1 Publication
Note: Interaction with BANP promotes nuclear localization. Translocates to mitochondria upon oxidative stress (By similarity).By similarity

GO - Cellular componenti

  1. chromatin Source: RGD
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: RGD
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. mitochondrion Source: UniProtKB
  6. nucleolus Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. replication fork Source: RefGenome
  9. transcription factor complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Cellular tumor antigen p53PRO_0000185712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by HIPK4By similarity
Modified residuei15 – 151Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATMBy similarity
Modified residuei18 – 181Phosphothreonine; by CK1, VRK1 and VRK2By similarity
Modified residuei20 – 201Phosphoserine; by CHEK2, CK1 and PLK3By similarity
Modified residuei39 – 391Phosphoserine; by MAPKAPK5By similarity
Modified residuei118 – 1181N6-acetyllysine; by KAT6ABy similarity
Modified residuei181 – 1811Phosphoserine; by AURKBBy similarity
Modified residuei267 – 2671Phosphoserine; by AURKBBy similarity
Modified residuei282 – 2821Phosphothreonine; by AURKBBy similarity
Cross-linki289 – 289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki290 – 290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei303 – 3031N6-acetyllysineBy similarity
Modified residuei313 – 3131Phosphoserine; by AURKA, CDK1 and CDK2By similarity
Modified residuei319 – 3191N6-acetyllysineBy similarity
Modified residuei368 – 3681N6,N6-dimethyllysine; alternateBy similarity
Modified residuei368 – 3681N6-methyllysine; by SMYD2; alternateBy similarity
Modified residuei370 – 3701N6-methyllysine; by SETD7By similarity
Modified residuei371 – 3711N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity
Modified residuei371 – 3711N6-acetyllysine; alternateBy similarity
Modified residuei379 – 3791N6-acetyllysineBy similarity
Modified residuei380 – 3801N6,N6-dimethyllysine; alternateBy similarity
Modified residuei380 – 3801N6-acetyllysine; by KAT6A; alternateBy similarity
Modified residuei380 – 3801N6-methyllysine; by SETD8; alternateBy similarity
Cross-linki384 – 384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei390 – 3901Phosphoserine; by CK2, CDK2 and NUAK1By similarity

Post-translational modificationi

Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Probably phosphorylated on by CDK7 in a CAK complex in response to DNA damage. Phosphorylated by HIPK1. Phosphorylated on Ser-390 following UV but not gamma irradiation. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated at Ser-313 and Ser-390 by CDK2 in response to DNA-damage (By similarity).By similarity
Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner (By similarity).By similarity
Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1 at Lys-289 and Lys-290, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL and RNF34, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by RFWD2, which leads to proteasomal degradation (By similarity).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. Dimethylated at Lys-371 by EHMT1 and EHMT2. Monomethylated at Lys-380 by SETD8, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-368 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP10361.
PRIDEiP10361.

PTM databases

PhosphoSiteiP10361.

Expressioni

Gene expression databases

ExpressionAtlasiP10361. baseline and differential.
GenevestigatoriP10361.

Interactioni

Subunit structurei

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 BANP. Interacts with ARMD10, E4F1, CDKN2AIP, NUAK1, UHRF2 and STK11/LKB1. 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 ubiquitination and degradation of TP53. Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when monomethylated at Lys-380) with L3MBTL1. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA). Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion (By similarity). Interacts with KAT6A (By similarity). Interacts with UBC9 (By similarity). Forms a complex with UBC9 and PRKRA (By similarity). Interacts with ZNF385B; the interaction is direct (By similarity). Interacts with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest (By similarity). Interacts with ANKRD2 (By similarity). Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and RFWD2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi246960. 9 interactions.
DIPiDIP-46016N.
IntActiP10361. 4 interactions.
MINTiMINT-4651801.
STRINGi10116.ENSRNOP00000047840.

Structurei

3D structure databases

ProteinModelPortaliP10361.
SMRiP10361. Positions 93-288, 317-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4747Transcription activation (acidic)Add
BLAST
Regioni64 – 10845Interaction with WWOXBy similarityAdd
BLAST
Regioni98 – 368271Interaction with HIPK1By similarityAdd
BLAST
Regioni98 – 298201Required for interaction with ZNF385ABy similarityAdd
BLAST
Regioni111 – 234124Required for interaction with FBXO42By similarityAdd
BLAST
Regioni114 – 290177Interaction with AXIN1By similarityAdd
BLAST
Regioni254 – 29239Interaction with E4F1By similarityAdd
BLAST
Regioni271 – 2788Interaction with DNABy similarity
Regioni317 – 35842Interaction with HIPK2By similarityAdd
BLAST
Regioni323 – 35432OligomerizationAdd
BLAST
Regioni357 – 3615Interaction with USP7By similarity
Regioni366 – 38520Basic (repression of DNA-binding)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi303 – 31917Bipartite nuclear localization signalBy similarityAdd
BLAST
Motifi337 – 34812Nuclear export signalBy similarityAdd
BLAST
Motifi368 – 3703[KR]-[STA]-K motif

Domaini

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

Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

eggNOGiNOG80479.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039957.
HOVERGENiHBG005201.
InParanoidiP10361.
KOiK04451.
OMAiVVSTRIC.
OrthoDBiEOG7JQBNW.
PhylomeDBiP10361.
TreeFamiTF106101.

Family and domain databases

Gene3Di2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProiIPR008967. 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]
PANTHERiPTHR11447. PTHR11447. 1 hit.
PfamiPF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]
PRINTSiPR00386. P53SUPPRESSR.
SUPFAMiSSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEiPS00348. P53. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10361-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDSQSDMSI ELPLSQETFS CLWKLLPPDD ILPTTATGSP NSMEDLFLPQ
60 70 80 90 100
DVAELLEGPE EALQVSAPAA QEPGTEAPAP VAPASATPWP LSSSVPSQKT
110 120 130 140 150
YQGNYGFHLG FLQSGTAKSV MCTYSISLNK LFCQLAKTCP VQLWVTSTPP
160 170 180 190 200
PGTRVRAMAI YKKSQHMTEV VRRCPHHERC SDGDGLAPPQ HLIRVEGNPY
210 220 230 240 250
AEYLDDRQTF RHSVVVPYEP PEVGSDYTTI HYKYMCNSSC MGGMNRRPIL
260 270 280 290 300
TIITLEDSSG NLLGRDSFEV RVCACPGRDR RTEEENFRKK EEHCPELPPG
310 320 330 340 350
SAKRALPTST SSSPQQKKKP LDGEYFTLKI RGRERFEMFR ELNEALELKD
360 370 380 390
ARAAEESGDS RAHSSYPKTK KGQSTSRHKK PMIKKVGPDS D
Length:391
Mass (Da):43,451
Last modified:July 1, 1989 - v1
Checksum:iE62522313A5C872F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741C → W in AAA41788. (PubMed:8441680)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031G → S.
Natural varianti256 – 2561E → G.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13058 mRNA. Translation: CAA31457.1.
L07910
, L07904, L07905, L07906, L07907, L07908, L07909 Genomic DNA. Translation: AAA41788.1.
U90328 mRNA. Translation: AAB80959.1.
BC081788 mRNA. Translation: AAH81788.2.
BC098663 mRNA. Translation: AAH98663.1.
PIRiS02192.
RefSeqiNP_112251.2. NM_030989.3.
XP_006246656.1. XM_006246594.2.
XP_006246657.1. XM_006246595.2.
UniGeneiRn.54443.

Genome annotation databases

EnsembliENSRNOT00000046490; ENSRNOP00000047840; ENSRNOG00000010756.
GeneIDi24842.
KEGGirno:24842.
UCSCiRGD:3889. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13058 mRNA. Translation: CAA31457.1 .
L07910
, L07904 , L07905 , L07906 , L07907 , L07908 , L07909 Genomic DNA. Translation: AAA41788.1 .
U90328 mRNA. Translation: AAB80959.1 .
BC081788 mRNA. Translation: AAH81788.2 .
BC098663 mRNA. Translation: AAH98663.1 .
PIRi S02192.
RefSeqi NP_112251.2. NM_030989.3.
XP_006246656.1. XM_006246594.2.
XP_006246657.1. XM_006246595.2.
UniGenei Rn.54443.

3D structure databases

ProteinModelPortali P10361.
SMRi P10361. Positions 93-288, 317-358.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246960. 9 interactions.
DIPi DIP-46016N.
IntActi P10361. 4 interactions.
MINTi MINT-4651801.
STRINGi 10116.ENSRNOP00000047840.

PTM databases

PhosphoSitei P10361.

Proteomic databases

PaxDbi P10361.
PRIDEi P10361.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000046490 ; ENSRNOP00000047840 ; ENSRNOG00000010756 .
GeneIDi 24842.
KEGGi rno:24842.
UCSCi RGD:3889. rat.

Organism-specific databases

CTDi 7157.
RGDi 3889. Tp53.

Phylogenomic databases

eggNOGi NOG80479.
GeneTreei ENSGT00390000015092.
HOGENOMi HOG000039957.
HOVERGENi HBG005201.
InParanoidi P10361.
KOi K04451.
OMAi VVSTRIC.
OrthoDBi EOG7JQBNW.
PhylomeDBi P10361.
TreeFami TF106101.

Miscellaneous databases

NextBioi 604596.
PROi P10361.

Gene expression databases

ExpressionAtlasi P10361. baseline and differential.
Genevestigatori P10361.

Family and domain databases

Gene3Di 2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProi 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_suppressor.
[Graphical view ]
PANTHERi PTHR11447. PTHR11447. 1 hit.
Pfami PF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view ]
PRINTSi PR00386. P53SUPPRESSR.
SUPFAMi SSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEi PS00348. P53. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA encoding the rat p53 nuclear oncoprotein."
    Soussi T.
    Nucleic Acids Res. 16:11384-11384(1988) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AB1.
    Tissue: Embryo.
  6. "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: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiP53_RAT
AccessioniPrimary (citable) accession number: P10361
Secondary accession number(s): O09168, Q4KMA9, Q66HM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3