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P04637

- P53_HUMAN

UniProt

P04637 - P53_HUMAN

Protein

Cellular tumor antigen p53

Gene

TP53

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 224 (01 Oct 2014)
      Sequence version 4 (24 Nov 2009)
      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. 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. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis.11 Publications

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei120 – 1201Interaction with DNA
    Metal bindingi176 – 1761Zinc
    Metal bindingi179 – 1791Zinc
    Metal bindingi238 – 2381Zinc
    Metal bindingi242 – 2421Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi102 – 292191Add
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. chaperone binding Source: UniProtKB
    3. chromatin binding Source: UniProtKB
    4. copper ion binding Source: UniProtKB
    5. damaged DNA binding Source: RefGenome
    6. DNA binding Source: UniProtKB
    7. enzyme binding Source: UniProtKB
    8. histone acetyltransferase binding Source: UniProtKB
    9. histone deacetylase regulator activity Source: Ensembl
    10. identical protein binding Source: IntAct
    11. p53 binding Source: RefGenome
    12. protease binding Source: UniProtKB
    13. protein binding Source: IntAct
    14. protein heterodimerization activity Source: UniProtKB
    15. protein kinase binding Source: UniProtKB
    16. protein N-terminus binding Source: UniProtKB
    17. protein phosphatase 2A binding Source: UniProtKB
    18. protein phosphatase binding Source: UniProt
    19. receptor tyrosine kinase binding Source: BHF-UCL
    20. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    21. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    22. RNA polymerase II transcription factor binding Source: BHF-UCL
    23. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    24. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    25. transcription factor binding Source: UniProtKB
    26. transcription regulatory region DNA binding Source: BHF-UCL
    27. ubiquitin protein ligase binding Source: UniProtKB
    28. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. base-excision repair Source: UniProtKB
    3. B cell lineage commitment Source: Ensembl
    4. blood coagulation Source: Reactome
    5. cell aging Source: UniProtKB
    6. cell cycle arrest Source: UniProtKB
    7. cell differentiation Source: UniProtKB
    8. cell proliferation Source: UniProtKB
    9. cellular protein localization Source: UniProtKB
    10. cellular response to DNA damage stimulus Source: UniProtKB
    11. cellular response to drug Source: UniProtKB
    12. cellular response to glucose starvation Source: UniProtKB
    13. cellular response to hypoxia Source: UniProtKB
    14. cellular response to ionizing radiation Source: BHF-UCL
    15. cellular response to UV Source: RefGenome
    16. central nervous system development Source: Ensembl
    17. chromatin assembly Source: UniProtKB
    18. determination of adult lifespan Source: BHF-UCL
    19. DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    20. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    21. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
    22. DNA strand renaturation Source: UniProtKB
    23. double-strand break repair Source: Ensembl
    24. embryonic organ development Source: Ensembl
    25. ER overload response Source: MGI
    26. gastrulation Source: Ensembl
    27. intrinsic apoptotic signaling pathway Source: HGNC
    28. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    29. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    30. in utero embryonic development Source: Ensembl
    31. mitotic cell cycle arrest Source: Ensembl
    32. mitotic G1 DNA damage checkpoint Source: BHF-UCL
    33. multicellular organismal development Source: UniProtKB
    34. multicellular organism growth Source: Ensembl
    35. negative regulation of apoptotic process Source: UniProtKB
    36. negative regulation of cell growth Source: UniProtKB
    37. negative regulation of cell proliferation Source: BHF-UCL
    38. negative regulation of DNA replication Source: Ensembl
    39. negative regulation of fibroblast proliferation Source: UniProtKB
    40. negative regulation of helicase activity Source: UniProtKB
    41. negative regulation of macromitophagy Source: Ensembl
    42. negative regulation of neuroblast proliferation Source: Ensembl
    43. negative regulation of reactive oxygen species metabolic process Source: Ensembl
    44. negative regulation of transcription, DNA-templated Source: BHF-UCL
    45. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    46. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    47. neuron apoptotic process Source: Ensembl
    48. Notch signaling pathway Source: Reactome
    49. nucleotide-excision repair Source: UniProtKB
    50. oligodendrocyte apoptotic process Source: UniProtKB
    51. oxidative stress-induced premature senescence Source: BHF-UCL
    52. positive regulation of apoptotic process Source: UniProtKB
    53. positive regulation of cardiac muscle cell apoptotic process Source: Ensembl
    54. positive regulation of cell aging Source: Ensembl
    55. positive regulation of cell cycle arrest Source: UniProtKB
    56. positive regulation of histone deacetylation Source: RefGenome
    57. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    58. positive regulation of neuron apoptotic process Source: RefGenome
    59. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    60. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    61. positive regulation of protein oligomerization Source: UniProtKB
    62. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
    63. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    64. positive regulation of thymocyte apoptotic process Source: BHF-UCL
    65. positive regulation of transcription, DNA-templated Source: UniProtKB
    66. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    67. protein complex assembly Source: UniProtKB
    68. protein import into nucleus, translocation Source: Ensembl
    69. protein localization Source: UniProtKB
    70. protein tetramerization Source: UniProtKB
    71. Ras protein signal transduction Source: BHF-UCL
    72. regulation of apoptotic process Source: MGI
    73. regulation of mitochondrial membrane permeability Source: UniProtKB
    74. regulation of mitochondrial membrane permeability involved in apoptotic process Source: Ensembl
    75. regulation of tissue remodeling Source: Ensembl
    76. regulation of transcription, DNA-templated Source: UniProtKB
    77. release of cytochrome c from mitochondria Source: Ensembl
    78. replicative senescence Source: BHF-UCL
    79. response to antibiotic Source: UniProtKB
    80. response to gamma radiation Source: BHF-UCL
    81. response to ischemia Source: Ensembl
    82. response to salt stress Source: Ensembl
    83. response to X-ray Source: RefGenome
    84. rRNA transcription Source: Ensembl
    85. somitogenesis Source: Ensembl
    86. T cell differentiation in thymus Source: Ensembl
    87. T cell lineage commitment Source: Ensembl
    88. T cell proliferation involved in immune response Source: Ensembl
    89. transforming growth factor beta receptor signaling pathway Source: Ensembl
    90. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Apoptosis, Cell cycle, Host-virus interaction, Necrosis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_1194. Activation of NOXA and translocation to mitochondria.
    REACT_121. Activation of PUMA and translocation to mitochondria.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_309. Stabilization of p53.
    SignaLinkiP04637.

    Protein family/group databases

    TCDBi1.C.110.1.1. the pore-forming pnc-27 peptide of 32 aas from the p53 tumor suppressor protein (pnc-27) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cellular tumor antigen p53
    Alternative name(s):
    Antigen NY-CO-13
    Phosphoprotein p53
    Tumor suppressor p53
    Gene namesi
    Name:TP53
    Synonyms:P53
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11998. TP53.

    Subcellular locationi

    Cytoplasm. Nucleus. NucleusPML body. Endoplasmic reticulum. Mitochondrion matrix
    Note: Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress.
    Isoform 1 : Nucleus. Cytoplasm
    Note: Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4.
    Isoform 2 : Nucleus. Cytoplasm
    Note: Localized mainly in the nucleus with minor staining in the cytoplasm.
    Isoform 3 : Nucleus. Cytoplasm
    Note: Localized in the nucleus in most cells but found in the cytoplasm in some cells.
    Isoform 4 : Nucleus. Cytoplasm
    Note: Predominantly nuclear but translocates to the cytoplasm following cell stress.
    Isoform 7 : Nucleus. Cytoplasm
    Note: Localized mainly in the nucleus with minor staining in the cytoplasm.
    Isoform 8 : Nucleus. Cytoplasm
    Note: Localized in both nucleus and cytoplasm in most cells. In some cells, forms foci in the nucleus that are different from nucleoli.

    GO - Cellular componenti

    1. chromatin Source: RefGenome
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. endoplasmic reticulum Source: UniProtKB-SubCell
    5. mitochondrial matrix Source: UniProtKB-SubCell
    6. mitochondrion Source: UniProtKB
    7. nuclear chromatin Source: BHF-UCL
    8. nuclear matrix Source: UniProtKB
    9. nucleolus Source: UniProtKB
    10. nucleoplasm Source: UniProtKB
    11. nucleus Source: UniProtKB
    12. PML body Source: UniProtKB
    13. protein complex Source: BHF-UCL
    14. replication fork Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers. TP53 defects are found in Barrett metaplasia a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma.
    Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Li-Fraumeni syndrome (LFS) [MIM:151623]: Autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (PubMed:8118819 and PubMed:8718514) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821P → L in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044621
    Natural varianti97 – 971V → I in familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_044650
    Natural varianti105 – 1051G → C in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044661
    Natural varianti106 – 1061S → R in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044667
    Natural varianti110 – 1101R → L in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation.
    VAR_005861
    Natural varianti126 – 1261Y → C in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044716
    Natural varianti132 – 1321K → E in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044740
    Natural varianti133 – 1331M → R in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044747
    Natural varianti133 – 1331M → T in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    Corresponds to variant rs28934873 [ dbSNP | Ensembl ].
    VAR_005875
    Natural varianti138 – 1381A → P in LFS; germline mutation and in sporadic cancers; somatic mutation.
    Corresponds to variant rs28934875 [ dbSNP | Ensembl ].
    VAR_005881
    Natural varianti138 – 1381A → S in LFS; germline mutation.
    VAR_044764
    Natural varianti141 – 1411C → Y in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005886
    Natural varianti144 – 1441Q → L in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044790
    Natural varianti151 – 1511P → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    Corresponds to variant rs28934874 [ dbSNP | Ensembl ].
    VAR_005895
    Natural varianti151 – 1511P → T in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005896
    Natural varianti152 – 1521P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005897
    Natural varianti155 – 1551T → N in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044836
    Natural varianti156 – 1561R → H in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044841
    Natural varianti158 – 1581R → G in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005906
    Natural varianti158 – 1581R → H in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005907
    Natural varianti163 – 1631Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 Publications
    VAR_033035
    Natural varianti167 – 1671Q → K in LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_044885
    Natural varianti172 – 1721V → F in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044906
    Natural varianti173 – 1731V → M in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005926
    Natural varianti174 – 1741R → G in LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_044911
    Natural varianti175 – 1751R → G in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005929
    Natural varianti175 – 1751R → H in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation; reduces interaction with ZNF385A. 4 Publications
    Corresponds to variant rs28934578 [ dbSNP | Ensembl ].
    VAR_005932
    Natural varianti175 – 1751R → L in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005930
    Natural varianti179 – 1791H → Y in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044939
    Natural varianti180 – 1801E → K in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044943
    Natural varianti181 – 1811R → C in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044946
    Natural varianti181 – 1811R → H in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044948
    Natural varianti181 – 1811R → L in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005937
    Natural varianti181 – 1811R → P in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044949
    Natural varianti189 – 1891A → V in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_044978
    Natural varianti193 – 1931H → R in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 Publications
    VAR_005948
    Natural varianti196 – 1961R → P in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045007
    Natural varianti197 – 1971V → E in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045010
    Natural varianti197 – 1971V → M in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045013
    Natural varianti210 – 2101N → Y in a familial cancer not matching LFS; germline mutation.
    VAR_045073
    Natural varianti213 – 2131R → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_036506
    Natural varianti213 – 2131R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005955
    Natural varianti219 – 2191P → S in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045114
    Natural varianti220 – 2201Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 Publications
    VAR_005957
    Natural varianti227 – 2271S → T in LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_045151
    Natural varianti233 – 2331H → D in LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_045175
    Natural varianti234 – 2341Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005963
    Natural varianti235 – 2351N → S in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045186
    Natural varianti236 – 2361Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045189
    Natural varianti237 – 2371M → I in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005965
    Natural varianti238 – 2381C → G in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045200
    Natural varianti238 – 2381C → S in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045202
    Natural varianti238 – 2381C → Y in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005967
    Natural varianti241 – 2411S → F in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 Publications
    Corresponds to variant rs28934573 [ dbSNP | Ensembl ].
    VAR_005969
    Natural varianti241 – 2411S → T in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_047183
    Natural varianti242 – 2421C → Y in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045224
    Natural varianti244 – 2441G → D in LFS; germline mutation and in sporadic cancers; somatic mutation.
    Corresponds to variant rs28934572 [ dbSNP | Ensembl ].
    VAR_045232
    Natural varianti244 – 2441G → V in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045236
    Natural varianti245 – 2451G → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 Publications
    VAR_005972
    Natural varianti245 – 2451G → D in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005973
    Natural varianti245 – 2451G → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    Corresponds to variant rs28934575 [ dbSNP | Ensembl ].
    VAR_005974
    Natural varianti245 – 2451G → V in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005975
    Natural varianti246 – 2461M → V in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005978
    Natural varianti248 – 2481R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. 4 Publications
    Corresponds to variant rs11540652 [ dbSNP | Ensembl ].
    VAR_005983
    Natural varianti248 – 2481R → W in LFS; germline mutation and in sporadic cancers; somatic mutation. 3 Publications
    VAR_005984
    Natural varianti251 – 2511I → M in LFS; germline mutation.
    VAR_045258
    Natural varianti252 – 2521L → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005988
    Natural varianti257 – 2571L → Q in LFS; germline mutation and in sporadic cancers; somatic mutation.
    Corresponds to variant rs28934577 [ dbSNP | Ensembl ].
    VAR_045284
    Natural varianti258 – 2581E → K in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005991
    Natural varianti265 – 2651L → P in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045321
    Natural varianti267 – 2671R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045330
    Natural varianti272 – 2721V → A in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045351
    Natural varianti272 – 2721V → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005992
    Natural varianti273 – 2731R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 4 Publications
    VAR_005993
    Natural varianti273 – 2731R → G in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_005994
    Natural varianti273 – 2731R → H in LFS; germline mutation and in sporadic cancers; somatic mutation; abolishes sequence-specific DNA binding; does not induce SNAI1 degradation. 7 Publications
    Corresponds to variant rs28934576 [ dbSNP | Ensembl ].
    VAR_005995
    Natural varianti273 – 2731R → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_036509
    Natural varianti273 – 2731R → S in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045357
    Natural varianti275 – 2751C → Y in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_005998
    Natural varianti278 – 2781P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_006003
    Natural varianti278 – 2781P → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 3 Publications
    VAR_006004
    Natural varianti278 – 2781P → T in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_006005
    Natural varianti280 – 2801R → K in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_006007
    Natural varianti281 – 2811D → N in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_047202
    Natural varianti281 – 2811D → V in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_006014
    Natural varianti282 – 2821R → G in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045384
    Natural varianti282 – 2821R → Q in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_045387
    Natural varianti282 – 2821R → W in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation. 1 Publication
    Corresponds to variant rs28934574 [ dbSNP | Ensembl ].
    VAR_006016
    Natural varianti283 – 2831R → C in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_006017
    Natural varianti285 – 2851E → Q in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_006024
    Natural varianti286 – 2861E → A in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_006026
    Natural varianti290 – 2901R → H in LFS; germline mutation and in sporadic cancers; somatic mutation.
    Corresponds to variant rs55819519 [ dbSNP | Ensembl ].
    VAR_045411
    Natural varianti290 – 2901R → L in LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045412
    Natural varianti292 – 2921K → I in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1 Publication
    VAR_015819
    Natural varianti305 – 3051K → M in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.
    VAR_045471
    Natural varianti306 – 3061R → P in LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_045475
    Natural varianti309 – 3091P → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_006038
    Natural varianti325 – 3251G → V in LFS; germline mutation. 1 Publication
    Corresponds to variant rs28934271 [ dbSNP | Ensembl ].
    VAR_006039
    Natural varianti337 – 3371R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_006041
    Natural varianti337 – 3371R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    VAR_035016
    Natural varianti344 – 3441L → P in LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_045546
    Natural varianti365 – 3651H → Y in a familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation.
    VAR_045568
    Natural varianti366 – 3661S → A in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication
    Corresponds to variant rs17881470 [ dbSNP | Ensembl ].
    VAR_022317
    Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
    Note: The gene represented in this entry is involved in disease pathogenesis.
    Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Papilloma of choroid plexus (CPP) [MIM:260500]: A benign tumor of neuroectodermal origin that generally occurs in childhood, but has also been reported in adults. Although generally found within the ventricular system, choroid plexus papillomas can arise ectopically in the brain parenchyma or disseminate throughout the neuraxis. Patients present with signs and symptoms of increased intracranial pressure including headache, hydrocephalus, papilledema, nausea, vomiting, cranial nerve deficits, gait impairment, and seizures.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Adrenocortical carcinoma (ADCC) [MIM:202300]: A malignant neoplasm of the adrenal cortex and a rare childhood tumor. It occurs with increased frequency in patients with Beckwith-Wiedemann syndrome and Li-Fraumeni syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Basal cell carcinoma 7 (BCC7) [MIM:614740]: A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. It is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151S → A: Loss of interaction with PPP2R5C, PPP2CA AND PPP2R1A. 2 Publications
    Mutagenesisi18 – 181T → A: No effect on interaction with MDM2 and increase in protein levels after DNA damage. 2 Publications
    Mutagenesisi20 – 201S → A: Abolishes phosphorylation site. Abolishes increase in protein levels after DNA damage. 2 Publications
    Mutagenesisi20 – 201S → D: Constitutively increased TP53 protein levels. 2 Publications
    Mutagenesisi22 – 232LW → QS: Loss of interaction with MDM2, leading to constitutively increased TP53 protein levels. 1 Publication
    Mutagenesisi37 – 371S → D: Abolihes phosphorylation by MAPKAPK5. 2 Publications
    Mutagenesisi46 – 461S → A: Abolishes phosphorylation by DYRK2 and HIPK2 and acetylation of K-382 by CREBBP. 4 Publications
    Mutagenesisi46 – 461Missing: Alters interaction with WWOX. 4 Publications
    Mutagenesisi55 – 551T → A: Blocks phosphorylation by TAF1. 2 Publications
    Mutagenesisi183 – 1831S → A: Abolishes strongly phosphorylation. 2 Publications
    Mutagenesisi183 – 1831S → E: Inhibits slightly its transcriptional activity. 2 Publications
    Mutagenesisi248 – 2481R → S: Does not induce SNAI1 degradation. 2 Publications
    Mutagenesisi269 – 2691S → A: Abolishes phosphorylation. 2 Publications
    Mutagenesisi269 – 2691S → E: Inhibits strongly its transcriptional activity. 2 Publications
    Mutagenesisi284 – 2841T → E: Inhibits strongly its transcriptional activity. 1 Publication
    Mutagenesisi291 – 2922KK → RR: Abolishes polyubiquitination by MKRN1. 1 Publication
    Mutagenesisi319 – 3191K → A: Loss of nuclear localization; when associated with A-320 and A-321. 2 Publications
    Mutagenesisi320 – 3201K → A: Loss of nuclear localization; when associated with A-319 and A-321. 2 Publications
    Mutagenesisi321 – 3211K → A: Loss of nuclear localization; when associated with A-319 and A-320. 2 Publications
    Mutagenesisi359 – 3591P → D: Abolishes binding to USP7. 2 Publications
    Mutagenesisi361 – 3611G → E: Abolishes binding to USP7. 2 Publications
    Mutagenesisi362 – 3621S → A: Abolishes binding to USP7. 2 Publications
    Mutagenesisi370 – 3701K → R: Induces a decrease in methylation by SMYD2. 2 Publications
    Mutagenesisi372 – 3721K → R: Induces a decrease in protein stabilization. 2 Publications
    Mutagenesisi373 – 3731K → R: Abolishes dimethylation by EHMT1 and EHMT2. 2 Publications
    Mutagenesisi382 – 3821K → A: Abolishes acetylation by CREBBP. 5 Publications
    Mutagenesisi382 – 3821K → R: Abolishes monomethylation by SETD8. 5 Publications
    Mutagenesisi383 – 3831L → A: Abolishes S-315 phosphorylation by CDK2/cyclin A. 2 Publications
    Mutagenesisi385 – 3851F → A: Reduced SUMO1 conjugation. 3 Publications
    Mutagenesisi386 – 3861K → A: Abolishes SUMO1 conjugation, in vitro and in vivo. 3 Publications
    Mutagenesisi387 – 3871T → A: No effect SUMO1 conjugation. 2 Publications
    Mutagenesisi388 – 3881E → A: Abolishes SUMO1 conjugation. 2 Publications

    Keywords - Diseasei

    Disease mutation, Li-Fraumeni syndrome, Tumor suppressor

    Organism-specific databases

    MIMi133239. phenotype.
    151623. phenotype.
    191170. gene+phenotype.
    202300. phenotype.
    211980. phenotype.
    260500. phenotype.
    275355. phenotype.
    614740. phenotype.
    Orphaneti1501. Adrenocortical carcinoma.
    67038. B-cell chronic lymphocytic leukemia.
    3318. Essential thrombocythemia.
    1333. Familial pancreatic carcinoma.
    251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    524. Li-Fraumeni syndrome.
    2807. Papilloma of choroid plexus.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA36679.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Cellular tumor antigen p53PRO_0000185703Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine; by HIPK41 Publication
    Modified residuei15 – 151Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM8 Publications
    Modified residuei18 – 181Phosphothreonine; by CK1, VRK1 and VRK23 Publications
    Modified residuei20 – 201Phosphoserine; by CHEK2, CK1 and PLK35 Publications
    Modified residuei33 – 331Phosphoserine; by CDK5 and CDK72 Publications
    Modified residuei37 – 371Phosphoserine; by MAPKAPK51 Publication
    Modified residuei46 – 461Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG5 Publications
    Modified residuei55 – 551Phosphothreonine; by TAF1 and GRK52 Publications
    Modified residuei120 – 1201N6-acetyllysine; by KAT6A2 Publications
    Modified residuei183 – 1831Phosphoserine; by AURKB1 Publication
    Modified residuei269 – 2691Phosphoserine; by AURKB1 Publication
    Modified residuei284 – 2841Phosphothreonine; by AURKB1 Publication
    Cross-linki291 – 291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)13 Publications
    Cross-linki292 – 292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)13 Publications
    Modified residuei305 – 3051N6-acetyllysine2 Publications
    Modified residuei315 – 3151Phosphoserine; by AURKA, CDK1 and CDK22 Publications
    Modified residuei321 – 3211N6-acetyllysineBy similarity
    Modified residuei370 – 3701N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei370 – 3701N6-methyllysine; by SMYD2; alternate2 Publications
    Modified residuei372 – 3721N6-methyllysine; by SETD72 Publications
    Modified residuei373 – 3731N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate1 Publication
    Modified residuei373 – 3731N6-acetyllysine; alternate2 Publications
    Modified residuei381 – 3811N6-acetyllysine2 Publications
    Modified residuei382 – 3821N6,N6-dimethyllysine; alternate3 Publications
    Modified residuei382 – 3821N6-acetyllysine; by KAT6A; alternate5 Publications
    Modified residuei382 – 3821N6-methyllysine; by SETD8; alternate3 Publications
    Cross-linki386 – 386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei392 – 3921Phosphoserine; by CK2, CDK2 and NUAK15 Publications

    Post-translational modificationi

    Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Deacetylation of Lys-382 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.4 Publications
    Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 By similarity. 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. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was intially thought to be mediated by STK11/LKB1 but it was later shown that it is indirect and that STK11/LKB1-dependent phosphorylation is probably mediated by downstream NUAK1 (PubMed:21317932). It is unclear whether AMP directly mediates phosphorylation at Ser-15. Phosphorylated on Thr-18 by isoform 1 and isoform 2 of VRK2. Phosphorylation on Thr-18 by isoform 2 of VRK2 results in a reduction in ubiquitination by MDM2 and an increase in acetylation by EP300. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage.By similarity32 Publications
    Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.
    May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line.1 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-291 and Lys-292, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to its stabilization. Ubiquitinated by TRIM24 and RFFL, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilization. Isoform 4 is monoubiquitinated in an MDM2-independent manner. Ubiquitinated by RFWD2, which leads to proteasomal degradation.1 Publication
    Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370. Dimethylated at Lys-373 by EHMT1 and EHMT2. Monomethylated at Lys-382 by SETD8, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20. Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation.
    Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9.3 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP04637.
    PaxDbiP04637.
    PRIDEiP04637.

    2D gel databases

    SWISS-2DPAGEP04637.

    PTM databases

    PhosphoSiteiP04637.

    Miscellaneous databases

    PMAP-CutDBP04637.

    Expressioni

    Tissue specificityi

    Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine.1 Publication

    Inductioni

    Up-regulated in response to DNA damage. Isoform 2 is not induced in tumor cells in response to stress.2 Publications

    Gene expression databases

    ArrayExpressiP04637.
    BgeeiP04637.
    GenevestigatoriP04637.

    Organism-specific databases

    HPAiCAB002973.
    CAB039238.
    CAB039239.
    HPA051244.

    Interactioni

    Subunit structurei

    Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 By similarity. Binds DNA as a homotetramer. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. In vitro, the interaction of TP53 with cancer-associated/HPV (E6) viral proteins leads to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6. Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4; this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. May interact with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity By similarity. Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F1. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts (via DNA-binding domain) with MAML1 (via N-terminus). Interacts with MKRN1. 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 (phosphorylated at Ser-15 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent inhibition of cell proliferation. Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when monomethylated at Lys-382) with L3MBTL1. Isoform 1 interacts with isoform 2 and with isoform 4. 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 human cytomegalovirus/HHV-5 protein UL123. Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the interaction is direct. 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. Interacts with RFFL (via RING-type zinc finger); involved in p53/TP53 ubiquitination. Interacts with MTA1 and RFWD2.By similarity66 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-366083,EBI-366083
    P0307018EBI-366083,EBI-617698From a different organism.
    P266639EBI-366083,EBI-6838571From a different organism.
    Q7L7W22EBI-366083,EBI-7210801
    Q8QW272EBI-366083,EBI-6863726From a different organism.
    ARIH2O953765EBI-366083,EBI-711158
    ASH2LQ9UBL35EBI-366083,EBI-540797
    AXIN1O151694EBI-366083,EBI-710484
    BANPQ8N9N53EBI-366083,EBI-744695
    BCL2P104155EBI-366083,EBI-77694
    BCL2L1Q07817-118EBI-366083,EBI-287195
    BCRP112742EBI-366083,EBI-712838
    BHLHE40O145035EBI-366083,EBI-711810
    BRD7Q9NPI18EBI-366083,EBI-711221
    BTBD2Q9BX702EBI-366083,EBI-710091
    Cables1Q9ESJ13EBI-366083,EBI-604411From a different organism.
    CCDC106Q9BWC93EBI-366083,EBI-711501
    CDKN1AP389363EBI-366083,EBI-375077
    CEBPBP176764EBI-366083,EBI-969696
    CREBBPQ927938EBI-366083,EBI-81215
    CrebbpP454816EBI-366083,EBI-296306From a different organism.
    CSE1LP550605EBI-366083,EBI-286709
    CSNK2A1P684002EBI-366083,EBI-347804
    CUL7Q149994EBI-366083,EBI-308606
    CUL9Q8IWT33EBI-366083,EBI-311123
    CXXC1Q9P0U47EBI-366083,EBI-949911
    DAXXQ9UER712EBI-366083,EBI-77321
    DDX17Q928413EBI-366083,EBI-746012
    DDX5P178446EBI-366083,EBI-351962
    DUSP26Q9BV479EBI-366083,EBI-2924519
    E6P031263EBI-366083,EBI-1177242From a different organism.
    E6P064632EBI-366083,EBI-1186926From a different organism.
    EP300Q0947210EBI-366083,EBI-447295
    FBXO11Q86XK24EBI-366083,EBI-1047804
    FOXO3O435242EBI-366083,EBI-1644164
    GSK3BP498413EBI-366083,EBI-373586
    GTF2H1P327805EBI-366083,EBI-715539
    HDAC1Q135477EBI-366083,EBI-301834
    HIPK1Q86Z022EBI-366083,EBI-692891
    HNRNPKP619782EBI-366083,EBI-304185
    HNRNPKP61978-22EBI-366083,EBI-7060731
    HSPA1LP349312EBI-366083,EBI-354912
    HSPA9P386466EBI-366083,EBI-354932
    HSPB1P047923EBI-366083,EBI-352682
    HTTP428584EBI-366083,EBI-466029
    HUWE1Q7Z6Z73EBI-366083,EBI-625934
    IFI16Q16666-23EBI-366083,EBI-6273540
    Ifi205bQ086192EBI-366083,EBI-8064290From a different organism.
    KAT5Q929933EBI-366083,EBI-399080
    KAT8Q9H7Z62EBI-366083,EBI-896414
    KMT2EQ8IZD24EBI-366083,EBI-2689959
    LAMA4Q163632EBI-366083,EBI-711505
    MAGEA2BP433566EBI-366083,EBI-5650739
    MAGEC2Q9UBF13EBI-366083,EBI-5651487
    MAP1BP468216EBI-366083,EBI-764611
    MAPK11Q157592EBI-366083,EBI-298304
    MAPKAPK5Q8IW412EBI-366083,EBI-1201460
    MDM2Q0098763EBI-366083,EBI-389668
    MDM4O1515113EBI-366083,EBI-398437
    MKRN1Q9UHC78EBI-366083,EBI-373524
    MPDZO759703EBI-366083,EBI-821405
    MT1AP047313EBI-366083,EBI-8045030
    NCLP193382EBI-366083,EBI-346967
    NFYAP2351111EBI-366083,EBI-389739
    NFYBP252086EBI-366083,EBI-389728
    NOC2LQ9Y3T98EBI-366083,EBI-751547
    NPM1P067486EBI-366083,EBI-78579
    NPM1P06748-13EBI-366083,EBI-354150
    NR0B2Q154663EBI-366083,EBI-3910729
    NR4A1P227366EBI-366083,EBI-721550
    NRD1O438476EBI-366083,EBI-2371631
    NUAK1O602855EBI-366083,EBI-1046789
    OTUB1Q96FW18EBI-366083,EBI-1058491
    PARD3Q8TEW03EBI-366083,EBI-81968
    PARP1P098743EBI-366083,EBI-355676
    PBKQ96KB57EBI-366083,EBI-536853
    PIAS1O759254EBI-366083,EBI-629434
    PIAS2O759282EBI-366083,EBI-348555
    PIAS4Q8N2W92EBI-366083,EBI-473160
    PIN1Q1352612EBI-366083,EBI-714158
    PLK1P533506EBI-366083,EBI-476768
    PMLP295904EBI-366083,EBI-295890
    PPIFP304054EBI-366083,EBI-5544229
    PPP1CCP36873-12EBI-366083,EBI-356289
    PPP1R13LQ8WUF511EBI-366083,EBI-5550163
    PPP2R1AP301533EBI-366083,EBI-302388
    PPP2R5CQ133624EBI-366083,EBI-1266156
    PSME3P612897EBI-366083,EBI-355546
    PTK2Q0539713EBI-366083,EBI-702142
    RAD51Q066092EBI-366083,EBI-297202
    RCHY1Q96PM57EBI-366083,EBI-947779
    RYBPQ8N4883EBI-366083,EBI-752324
    S100A1P232972EBI-366083,EBI-743686
    S100A2P290342EBI-366083,EBI-752230
    S100A4P264473EBI-366083,EBI-717058
    S100BP042712EBI-366083,EBI-458391
    SAFBQ154245EBI-366083,EBI-348298
    SETD7Q8WTS66EBI-366083,EBI-1268586
    SFNP319474EBI-366083,EBI-476295
    SIN3AQ96ST32EBI-366083,EBI-347218
    SIRT1Q96EB613EBI-366083,EBI-1802965
    Sirt1Q923E44EBI-366083,EBI-1802585From a different organism.
    SMAD2Q157964EBI-366083,EBI-1040141
    SNAI1O958632EBI-366083,EBI-1045459
    SREBF2Q127723EBI-366083,EBI-465059
    SRPK1Q96SB43EBI-366083,EBI-539478
    SYVN1Q86TM65EBI-366083,EBI-947849
    TBPP202262EBI-366083,EBI-355371
    TOE1Q96GM83EBI-366083,EBI-717460
    TP53BP1Q128882EBI-366083,EBI-396540
    TP53BP2Q136252EBI-366083,EBI-77642
    TP63Q9H3D45EBI-366083,EBI-2337775
    Tp63O888982EBI-366083,EBI-2338025From a different organism.
    TPT1P136935EBI-366083,EBI-1783169
    TWIST1Q156729EBI-366083,EBI-1797287
    Twist1P266874EBI-366083,EBI-6123119From a different organism.
    UBCP0CG4815EBI-366083,EBI-3390054
    UBE3AQ050863EBI-366083,EBI-954357
    UHRF2Q96PU43EBI-366083,EBI-625304
    USP42Q9H9J42EBI-366083,EBI-2513638
    USP42Q9H9J4-22EBI-366083,EBI-9118105
    USP7Q9300917EBI-366083,EBI-302474
    VDRP114736EBI-366083,EBI-286357
    VRK1Q999869EBI-366083,EBI-1769146
    WRNQ141915EBI-366083,EBI-368417
    XRCC6P129562EBI-366083,EBI-353208
    YWHAGP619815EBI-366083,EBI-359832
    YWHAZP631042EBI-366083,EBI-347088
    ZNF420Q8TAQ54EBI-366083,EBI-3923307
    znf585bQ9PST73EBI-366083,EBI-1782562From a different organism.

    Protein-protein interaction databases

    BioGridi113010. 560 interactions.
    DIPiDIP-368N.
    IntActiP04637. 359 interactions.
    MINTiMINT-91013.

    Structurei

    Secondary structure

    1
    393
    Legend: HelixTurnBeta strand
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    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 235
    Beta strandi27 – 293
    Beta strandi33 – 353
    Helixi36 – 383
    Helixi41 – 444
    Helixi47 – 559
    Turni105 – 1084
    Beta strandi110 – 1123
    Beta strandi118 – 1203
    Turni121 – 1233
    Beta strandi124 – 1274
    Turni128 – 1314
    Beta strandi132 – 1354
    Beta strandi141 – 1466
    Beta strandi156 – 16510
    Helixi166 – 1683
    Helixi177 – 1804
    Beta strandi181 – 1833
    Beta strandi187 – 1893
    Beta strandi194 – 1996
    Beta strandi204 – 2074
    Turni209 – 2113
    Beta strandi214 – 2196
    Turni225 – 2273
    Beta strandi228 – 2369
    Helixi240 – 2423
    Turni243 – 2486
    Beta strandi251 – 2588
    Beta strandi260 – 2623