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P02340

- P53_MOUSE

UniProt

P02340 - P53_MOUSE

Protein

Cellular tumor antigen p53

Gene

Tp53

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 187 (01 Oct 2014)
      Sequence version 3 (18 Mar 2008)
      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 By similarity. 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, but seems to have to effect on cell-cycle regulation.By similarity3 Publications

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei114 – 1141Interaction with DNA
    Metal bindingi170 – 1701Zinc
    Metal bindingi173 – 1731Zinc
    Metal bindingi232 – 2321Zinc
    Metal bindingi236 – 2361Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi96 – 286191By similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. chromatin binding Source: MGI
    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. histone deacetylase regulator activity Source: MGI
    8. MDM2/MDM4 family protein binding Source: BHF-UCL
    9. p53 binding Source: RefGenome
    10. protein binding Source: UniProtKB
    11. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    12. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
    13. sequence-specific DNA binding Source: RefGenome
    14. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. apoptotic process Source: MGI
    2. B cell lineage commitment Source: MGI
    3. cell aging Source: UniProtKB
    4. cellular response to DNA damage stimulus Source: MGI
    5. cellular response to ionizing radiation Source: MGI
    6. cellular response to UV Source: MGI
    7. central nervous system development Source: MGI
    8. cerebellum development Source: MGI
    9. chromosome organization Source: MGI
    10. determination of adult lifespan Source: BHF-UCL
    11. DNA damage response, signal transduction by p53 class mediator Source: MGI
    12. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: MGI
    13. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
    14. DNA strand renaturation Source: UniProtKB
    15. double-strand break repair Source: MGI
    16. embryo development ending in birth or egg hatching Source: MGI
    17. embryonic organ development Source: MGI
    18. gastrulation Source: MGI
    19. intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
    20. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    21. in utero embryonic development Source: MGI
    22. mitotic cell cycle arrest Source: MGI
    23. mitotic G1 DNA damage checkpoint Source: MGI
    24. multicellular organismal development Source: UniProtKB
    25. multicellular organism growth Source: MGI
    26. necroptotic process Source: MGI
    27. negative regulation of apoptotic process Source: MGI
    28. negative regulation of cell growth Source: UniProtKB
    29. negative regulation of cell proliferation Source: BHF-UCL
    30. negative regulation of DNA replication Source: MGI
    31. negative regulation of fibroblast proliferation Source: MGI
    32. negative regulation of macromitophagy Source: MGI
    33. negative regulation of neuroblast proliferation Source: MGI
    34. negative regulation of reactive oxygen species metabolic process Source: MGI
    35. negative regulation of transcription, DNA-templated Source: BHF-UCL
    36. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    37. negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
    38. neuron apoptotic process Source: MGI
    39. nucleotide-excision repair Source: UniProtKB
    40. oligodendrocyte apoptotic process Source: UniProtKB
    41. positive regulation of apoptotic process Source: MGI
    42. positive regulation of cardiac muscle cell apoptotic process Source: MGI
    43. positive regulation of cell aging Source: BHF-UCL
    44. positive regulation of histone deacetylation Source: MGI
    45. positive regulation of mitochondrial membrane permeability Source: MGI
    46. positive regulation of neuron apoptotic process Source: MGI
    47. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    48. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    49. positive regulation of thymocyte apoptotic process Source: BHF-UCL
    50. positive regulation of transcription, DNA-templated Source: MGI
    51. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    52. protein import into nucleus, translocation Source: MGI
    53. protein tetramerization Source: InterPro
    54. regulation of cell cycle Source: MGI
    55. regulation of cell proliferation Source: MGI
    56. regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
    57. regulation of neuron apoptotic process Source: MGI
    58. regulation of thymocyte apoptotic process Source: MGI
    59. regulation of tissue remodeling Source: MGI
    60. regulation of transcription, DNA-templated Source: MGI
    61. regulation of transcription from RNA polymerase II promoter Source: MGI
    62. release of cytochrome c from mitochondria Source: MGI
    63. response to drug Source: MGI
    64. response to gamma radiation Source: MGI
    65. response to ischemia Source: MGI
    66. response to oxidative stress Source: MGI
    67. response to salt stress Source: MGI
    68. response to UV Source: MGI
    69. response to X-ray Source: MGI
    70. rRNA transcription Source: MGI
    71. somitogenesis Source: MGI
    72. T cell differentiation in thymus Source: MGI
    73. T cell lineage commitment Source: MGI
    74. T cell proliferation involved in immune response Source: MGI
    75. transforming growth factor beta receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Apoptosis, Cell cycle, Necrosis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_188970. Oxidative Stress Induced Senescence.
    REACT_188971. Oncogene Induced Senescence.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cellular tumor antigen p53
    Alternative name(s):
    Tumor suppressor p53
    Gene namesi
    Name:Tp53
    Synonyms:P53, Trp53
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:98834. Trp53.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromatin Source: RefGenome
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: MGI
    4. endoplasmic reticulum Source: UniProtKB-SubCell
    5. mitochondrial matrix Source: MGI
    6. mitochondrion Source: UniProtKB
    7. nucleolus Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. replication fork Source: MGI
    10. transcription factor complex Source: RefGenome

    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

    Disease mutation, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Cellular tumor antigen p53PRO_0000185709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine; by HIPK42 Publications
    Modified residuei15 – 151Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM2 Publications
    Modified residuei18 – 181Phosphothreonine; by CK1, VRK1 and VRK2By similarity
    Modified residuei20 – 201Phosphoserine; by CHEK2, CK1 and PLK3By similarity
    Modified residuei34 – 341Phosphoserine; by MAPKAPK52 Publications
    Modified residuei114 – 1141N6-acetyllysine; by KAT6ABy similarity
    Modified residuei177 – 1771Phosphoserine; by AURKBBy similarity
    Modified residuei263 – 2631Phosphoserine; by AURKBBy similarity
    Modified residuei278 – 2781Phosphothreonine; by AURKBBy similarity
    Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki286 – 286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei299 – 2991N6-acetyllysineBy similarity
    Modified residuei309 – 3091Phosphoserine; by AURKA, CDK1 and CDK2By similarity
    Modified residuei315 – 3151N6-acetyllysine1 Publication
    Modified residuei364 – 3641N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei364 – 3641N6-methyllysine; by SMYD2; alternateBy similarity
    Modified residuei366 – 3661N6-methyllysine; by SETD7By similarity
    Modified residuei367 – 3671N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity
    Modified residuei367 – 3671N6-acetyllysine; alternateBy similarity
    Modified residuei375 – 3751N6-acetyllysineBy similarity
    Modified residuei376 – 3761N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei376 – 3761N6-acetyllysine; by KAT6A; alternateBy similarity
    Modified residuei376 – 3761N6-methyllysine; by SETD8; alternateBy similarity
    Cross-linki380 – 380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei386 – 3861Phosphoserine; by CK2, CDK2 and NUAK1By similarity

    Post-translational modificationi

    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. 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. 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 By similarity. Phosphorylated on Ser-386 following UV but not gamma irradiation. Phosphorylated by HIPK1.By similarity7 Publications
    Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner By similarity. Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence.By similarity1 Publication
    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-285 and Lys-286, 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-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. Dimethylated at Lys-367 EHMT1 and EHMT2. Monomethylated at Lys-376 SETD8, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-364 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation By similarity.By similarity
    Sumoylated with SUMO1. Sumoylated at Lys-380 by UBC9 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP02340.

    PTM databases

    PhosphoSiteiP02340.

    Expressioni

    Gene expression databases

    ArrayExpressiP02340.
    BgeeiP02340.
    CleanExiMM_TRP53.
    GenevestigatoriP02340.

    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 HSP90AB1. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts with AURKB, SETD2, UHRF2 and NOC2L By similarity. Interacts with PML (via C-terminus). Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53. Interacts with DAXX. Interacts (when monomethylated at Lys-376) with L3MBTL1. Interacts with BANP, CDKN2AIP, NUAK1, STK11/LKB1 and E4F1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity. Interacts with AURKA, TRIM24 and BRD7. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Phosphorylated at Ser-309 and Ser-386 by CDK2 in response to DNA-damage. 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 (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest. 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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P0307012EBI-474016,EBI-617698From a different organism.
    BCL2L1Q07817-13EBI-474016,EBI-287195From a different organism.
    Mdm2P238043EBI-474016,EBI-641788
    Mdm2P23804-12EBI-474016,EBI-3386476
    Pin1Q9QUR73EBI-474016,EBI-2432975
    PolgP540992EBI-474016,EBI-863636
    PpifQ99KR72EBI-474016,EBI-6455001
    PtenO085864EBI-474016,EBI-1186266
    Smarcd1Q614664EBI-474016,EBI-371529
    Sod2P096712EBI-474016,EBI-1635071
    UbcP629912EBI-474016,EBI-413074

    Protein-protein interaction databases

    BioGridi204323. 81 interactions.
    DIPiDIP-369N.
    IntActiP02340. 37 interactions.
    MINTiMINT-120104.
    STRINGi10090.ENSMUSP00000104298.

    Structurei

    Secondary structure

    1
    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi99 – 1013
    Beta strandi104 – 1063
    Helixi113 – 1164
    Beta strandi117 – 1215
    Turni122 – 1254
    Beta strandi126 – 1294
    Beta strandi134 – 1407
    Beta strandi150 – 15910
    Turni160 – 1645
    Helixi171 – 1755
    Beta strandi181 – 1833
    Beta strandi188 – 1936
    Beta strandi198 – 2014
    Turni203 – 2053
    Beta strandi208 – 2136
    Beta strandi222 – 2309
    Helixi235 – 2373
    Helixi239 – 2424
    Beta strandi245 – 2528
    Beta strandi258 – 26811
    Helixi272 – 28312
    Turni285 – 2873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HU8X-ray2.70A/B/C96-281[»]
    2GEQX-ray2.30A/B89-289[»]
    2IOIX-ray1.55A92-289[»]
    2IOMX-ray2.00A92-289[»]
    2IOOX-ray2.02A92-289[»]
    2P52X-ray1.50A89-284[»]
    3EXJX-ray2.00A/B93-289[»]
    3EXLX-ray2.20A93-289[»]
    ProteinModelPortaliP02340.
    SMRiP02340. Positions 88-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02340.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4242Transcription activation (acidic)Add
    BLAST
    Regioni60 – 10445Interaction with WWOXBy similarityAdd
    BLAST
    Regioni94 – 364271Interaction with HIPK1Add
    BLAST
    Regioni94 – 294201Required for interaction with ZNF385ABy similarityAdd
    BLAST
    Regioni107 – 230124Required for interaction with FBXO42By similarityAdd
    BLAST
    Regioni110 – 286177Interaction with AXIN1Add
    BLAST
    Regioni253 – 29139Interaction with E4F1By similarityAdd
    BLAST
    Regioni267 – 2748Interaction with DNA
    Regioni313 – 35442Interaction with HIPK2By similarityAdd
    BLAST
    Regioni319 – 35032OligomerizationAdd
    BLAST
    Regioni353 – 3575Interaction with USP7By similarity
    Regioni362 – 38120Basic (repression of DNA-binding)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi299 – 31517Bipartite nuclear localization signalBy similarityAdd
    BLAST
    Motifi333 – 34412Nuclear export signalBy similarityAdd
    BLAST
    Motifi364 – 3663[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.
    InParanoidiP02340.
    KOiK04451.
    OrthoDBiEOG7JQBNW.

    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.

    P02340-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEESQSDISL ELPLSQETFS GLWKLLPPED ILPSPHCMDD LLLPQDVEEF    50
    FEGPSEALRV SGAPAAQDPV TETPGPVAPA PATPWPLSSF VPSQKTYQGN 100
    YGFHLGFLQS GTAKSVMCTY SPPLNKLFCQ LAKTCPVQLW VSATPPAGSR 150
    VRAMAIYKKS QHMTEVVRRC PHHERCSDGD GLAPPQHLIR VEGNLYPEYL 200
    EDRQTFRHSV VVPYEPPEAG SEYTTIHYKY MCNSSCMGGM NRRPILTIIT 250
    LEDSSGNLLG RDSFEVRVCA CPGRDRRTEE ENFRKKEVLC PELPPGSAKR 300
    ALPTCTSASP PQKKKPLDGE YFTLKIRGRK RFEMFRELNE ALELKDAHAT 350
    EESGDSRAHS SYLKTKKGQS TSRHKKTMVK KVGPDSD 387
    Length:387
    Mass (Da):43,155
    Last modified:March 18, 2008 - v3
    Checksum:iB55EB7B463E1DD9D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451Q → R in CAA25323. (PubMed:6379601)Curated
    Sequence conflicti76 – 783PVA → QW in CAA25323. (PubMed:6379601)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321A → V Can cooperate with an activated Ras to transform fibroblasts. 1 Publication
    Natural varianti165 – 1651E → G in clone P53-M11.
    Natural varianti188 – 1881L → R.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA22739. DNMS53.
    S38824.
    RefSeqiNP_001120705.1. NM_001127233.1.
    NP_035770.2. NM_011640.3.
    XP_006533220.1. XM_006533157.1.
    XP_006533221.1. XM_006533158.1.
    UniGeneiMm.222.

    Genome annotation databases

    EnsembliENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552.
    GeneIDi22059.
    KEGGimmu:22059.
    UCSCiuc007jql.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A22739. DNMS53.
    S38824.
    RefSeqi NP_001120705.1. NM_001127233.1.
    NP_035770.2. NM_011640.3.
    XP_006533220.1. XM_006533157.1.
    XP_006533221.1. XM_006533158.1.
    UniGenei Mm.222.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HU8 X-ray 2.70 A/B/C 96-281 [» ]
    2GEQ X-ray 2.30 A/B 89-289 [» ]
    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 89-284 [» ]
    3EXJ X-ray 2.00 A/B 93-289 [» ]
    3EXL X-ray 2.20 A 93-289 [» ]
    ProteinModelPortali P02340.
    SMRi P02340. Positions 88-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204323. 81 interactions.
    DIPi DIP-369N.
    IntActi P02340. 37 interactions.
    MINTi MINT-120104.
    STRINGi 10090.ENSMUSP00000104298.

    Chemistry

    ChEMBLi CHEMBL4164.

    PTM databases

    PhosphoSitei P02340.

    Proteomic databases

    PRIDEi P02340.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005371 ; ENSMUSP00000005371 ; ENSMUSG00000059552 .
    GeneIDi 22059.
    KEGGi mmu:22059.
    UCSCi uc007jql.2. mouse.

    Organism-specific databases

    CTDi 22059.
    MGIi MGI:98834. Trp53.

    Phylogenomic databases

    eggNOGi NOG80479.
    GeneTreei ENSGT00390000015092.
    HOGENOMi HOG000039957.
    HOVERGENi HBG005201.
    InParanoidi P02340.
    KOi K04451.
    OrthoDBi EOG7JQBNW.

    Enzyme and pathway databases

    Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_188970. Oxidative Stress Induced Senescence.
    REACT_188971. Oncogene Induced Senescence.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.

    Miscellaneous databases

    EvolutionaryTracei P02340.
    NextBioi 301858.
    PROi P02340.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02340.
    Bgeei P02340.
    CleanExi MM_TRP53.
    Genevestigatori P02340.

    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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: DISCOVERY OF P53.
    13. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BANP.
    23. "PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
      Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
      Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15, LYSINE ACETYLATION, UBIQUITINATION, SUBCELLULAR LOCATION.
    24. Cited for: PHOSPHORYLATION AT SER-34.
    25. "Hzf Determines cell survival upon genotoxic stress by modulating p53 transactivation."
      Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A., Lee S.W.
      Cell 130:624-637(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF385A.
    26. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-9.
    27. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHD8.
    28. Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH TRIM24.
    29. "A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response."
      Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.
      Cell 142:409-419(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "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: FUNCTION.
    31. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    32. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-281.
    33. "High-resolution structure of the p53 core domain: implications for binding small-molecule stabilizing compounds."
      Ho W.C., Luo C., Zhao K., Chai X., Fitzgerald M.X., Marmorstein R.
      Acta Crystallogr. D 62:1484-1493(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 92-289.
    34. "Structure of the p53 core domain dimer bound to DNA."
      Ho W.C., Fitzgerald M.X., Marmorstein R.
      J. Biol. Chem. 281:20494-20502(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 92-289 IN COMPLEX WITH DNA AND ZINC IONS, SUBUNIT.
    35. "Crystal structure of the mouse p53 core domain in zinc-free state."
      Kwon E., Kim D.Y., Suh S.W., Kim K.K.
      Proteins 70:280-283(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-284.
    36. "Crystal structure of a p53 core tetramer bound to DNA."
      Malecka K.A., Ho W.C., Marmorstein R.
      Oncogene 28:325-333(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-289 IN COMPLEX WITH DNA, SUBUNIT.

    Entry informationi

    Entry nameiP53_MOUSE
    AccessioniPrimary (citable) accession number: P02340
    Secondary accession number(s): Q9QUP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 187 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3