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P10361

- P53_RAT

UniProt

P10361 - P53_RAT

Protein

Cellular tumor antigen p53

Gene

Tp53

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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 binding Source: UniProtKB
    9. protein C-terminus binding Source: RGD
    10. sequence-specific DNA binding Source: RGD
    11. sequence-specific DNA binding transcription factor activity Source: RefGenome
    12. transcription cofactor binding Source: RGD
    13. transcription regulatory region DNA binding Source: InterPro
    14. 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

    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-SubCell
    5. mitochondrial matrix Source: UniProtKB-SubCell
    6. mitochondrion Source: UniProtKB
    7. nucleolus Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. replication fork Source: RefGenome
    10. transcription factor complex Source: RGD

    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 and RFFL, 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

    ArrayExpressiP10361.
    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 (via RING-type zinc finger); 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

    MEDSQSDMSI ELPLSQETFS CLWKLLPPDD ILPTTATGSP NSMEDLFLPQ    50
    DVAELLEGPE EALQVSAPAA QEPGTEAPAP VAPASATPWP LSSSVPSQKT 100
    YQGNYGFHLG FLQSGTAKSV MCTYSISLNK LFCQLAKTCP VQLWVTSTPP 150
    PGTRVRAMAI YKKSQHMTEV VRRCPHHERC SDGDGLAPPQ HLIRVEGNPY 200
    AEYLDDRQTF RHSVVVPYEP PEVGSDYTTI HYKYMCNSSC MGGMNRRPIL 250
    TIITLEDSSG NLLGRDSFEV RVCACPGRDR RTEEENFRKK EEHCPELPPG 300
    SAKRALPTST SSSPQQKKKP LDGEYFTLKI RGRERFEMFR ELNEALELKD 350
    ARAAEESGDS RAHSSYPKTK KGQSTSRHKK PMIKKVGPDS D 391
    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_006246594.1.
    XP_006246657.1. XM_006246595.1.
    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_006246594.1.
    XP_006246657.1. XM_006246595.1.
    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

    ArrayExpressi P10361.
    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

    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 1, 2014
    This is version 169 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