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P04637

- P53_HUMAN

UniProt

P04637 - P53_HUMAN

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Protein

Cellular tumor antigen p53

Gene

TP53

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. 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

Zn2+Note: 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 heterodimerization activity Source: UniProtKB
  14. protein kinase binding Source: UniProtKB
  15. protein N-terminus binding Source: UniProtKB
  16. protein phosphatase 2A binding Source: UniProtKB
  17. protein phosphatase binding Source: UniProt
  18. receptor tyrosine kinase binding Source: BHF-UCL
  19. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  20. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  21. RNA polymerase II transcription factor binding Source: BHF-UCL
  22. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  23. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  24. transcription factor binding Source: UniProtKB
  25. transcription regulatory region DNA binding Source: BHF-UCL
  26. ubiquitin protein ligase binding Source: UniProtKB
  27. 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. cerebellum 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. necroptotic process Source: Ensembl
  36. negative regulation of apoptotic process Source: UniProtKB
  37. negative regulation of cell growth Source: UniProtKB
  38. negative regulation of cell proliferation Source: BHF-UCL
  39. negative regulation of DNA replication Source: Ensembl
  40. negative regulation of fibroblast proliferation Source: UniProtKB
  41. negative regulation of helicase activity Source: UniProtKB
  42. negative regulation of macromitophagy Source: Ensembl
  43. negative regulation of neuroblast proliferation Source: Ensembl
  44. negative regulation of reactive oxygen species metabolic process Source: Ensembl
  45. negative regulation of transcription, DNA-templated Source: BHF-UCL
  46. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  47. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  48. neuron apoptotic process Source: Ensembl
  49. Notch signaling pathway Source: Reactome
  50. nucleotide-excision repair Source: UniProtKB
  51. oligodendrocyte apoptotic process Source: UniProtKB
  52. oxidative stress-induced premature senescence Source: BHF-UCL
  53. positive regulation of apoptotic process Source: UniProtKB
  54. positive regulation of cardiac muscle cell apoptotic process Source: Ensembl
  55. positive regulation of cell aging Source: Ensembl
  56. positive regulation of cell cycle arrest Source: UniProtKB
  57. positive regulation of histone deacetylation Source: RefGenome
  58. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  59. positive regulation of mitochondrial membrane permeability Source: Ensembl
  60. positive regulation of neuron apoptotic process Source: RefGenome
  61. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  62. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  63. positive regulation of protein oligomerization Source: UniProtKB
  64. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  65. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  66. positive regulation of thymocyte apoptotic process Source: BHF-UCL
  67. positive regulation of transcription, DNA-templated Source: UniProtKB
  68. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  69. protein complex assembly Source: UniProtKB
  70. protein import into nucleus, translocation Source: Ensembl
  71. protein localization Source: UniProtKB
  72. protein tetramerization Source: UniProtKB
  73. Ras protein signal transduction Source: BHF-UCL
  74. regulation of apoptotic process Source: MGI
  75. regulation of mitochondrial membrane permeability Source: UniProtKB
  76. regulation of mitochondrial membrane permeability involved in apoptotic process Source: Ensembl
  77. regulation of tissue remodeling Source: Ensembl
  78. regulation of transcription, DNA-templated Source: UniProtKB
  79. release of cytochrome c from mitochondria Source: Ensembl
  80. replicative senescence Source: BHF-UCL
  81. response to antibiotic Source: UniProtKB
  82. response to gamma radiation Source: BHF-UCL
  83. response to ischemia Source: Ensembl
  84. response to salt stress Source: Ensembl
  85. response to X-ray Source: RefGenome
  86. rRNA transcription Source: Ensembl
  87. somitogenesis Source: Ensembl
  88. T cell differentiation in thymus Source: Ensembl
  89. T cell lineage commitment Source: Ensembl
  90. T cell proliferation involved in immune response Source: Ensembl
  91. transforming growth factor beta receptor signaling pathway Source: Ensembl
  92. viral process Source: UniProtKB-KW
Complete GO annotation...

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-KW
  5. mitochondrial matrix Source: Ensembl
  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
Complete GO annotation...

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

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 KAT6A1 Publication
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)1 Publication
Cross-linki292 – 292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei305 – 3051N6-acetyllysine1 Publication
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; alternate1 Publication
Modified residuei381 – 3811N6-acetyllysine1 Publication
Modified residuei382 – 3821N6,N6-dimethyllysine; alternate3 Publications
Modified residuei382 – 3821N6-acetyllysine; by KAT6A; alternate4 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, RFFL and RNF34, 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.2 Publications
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

BgeeiP04637.
ExpressionAtlasiP04637. baseline and differential.
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 and RNF34; 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
S100A4P264477EBI-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. 744 interactions.
DIPiDIP-368N.
IntActiP04637. 359 interactions.
MINTiMINT-91013.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 235Combined sources
Beta strandi27 – 293Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Helixi41 – 444Combined sources
Helixi47 – 559Combined sources
Turni105 – 1084Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi118 – 1203Combined sources
Turni121 – 1233Combined sources
Beta strandi124 – 1274Combined sources
Turni128 – 1314Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi156 – 16510Combined sources
Helixi166 – 1683Combined sources
Helixi177 – 1804Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi194 – 1996Combined sources
Beta strandi204 – 2074Combined sources
Turni209 – 2113Combined sources
Beta strandi214 – 2196Combined sources
Turni225 – 2273Combined sources
Beta strandi228 – 2369Combined sources
Helixi240 – 2423Combined sources
Turni243 – 2486Combined sources
Beta strandi251 – 2588Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi264 – 27411Combined sources
Helixi278 – 28710Combined sources
Helixi288 – 2903Combined sources
Helixi322 – 3243Combined sources
Beta strandi327 – 3348Combined sources
Helixi335 – 35420Combined sources
Helixi375 – 3806Combined sources
Turni382 – 3854Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1UNMR-A/C324-358[»]
1AIEX-ray1.50A326-356[»]
1C26X-ray1.70A325-356[»]
1DT7NMR-X/Y367-388[»]
1GZHX-ray2.60A/C95-292[»]
1H26X-ray2.24E376-386[»]
1HS5NMR-A/B324-357[»]
1JSPNMR-A367-386[»]
1KZYX-ray2.50A/B95-289[»]
1MA3X-ray2.00B372-389[»]
1OLGNMR-A/B/C/D319-360[»]
1OLHNMR-A/B/C/D319-360[»]
1PESNMR-A/B/C/D325-355[»]
1PETNMR-A/B/C/D325-355[»]
1SAENMR-A/B/C/D319-360[»]
1SAFNMR-A/B/C/D319-360[»]
1SAKNMR-A/B/C/D319-360[»]
1SALNMR-A/B/C/D319-360[»]
1TSRX-ray2.20A/B/C94-312[»]
1TUPX-ray2.20A/B/C94-312[»]
1UOLX-ray1.90A/B94-312[»]
1XQHX-ray1.75B/F369-377[»]
1YC5X-ray1.40B372-389[»]
1YCQX-ray2.30B13-29[»]
1YCRX-ray2.60B15-29[»]
1YCSX-ray2.20A94-292[»]
2AC0X-ray1.80A/B/C/D94-293[»]
2ADYX-ray2.50A/B94-293[»]
2AHIX-ray1.85A/B/C/D94-293[»]
2ATAX-ray2.20A/B/C/D94-293[»]
2B3GX-ray1.60B33-60[»]
2BIMX-ray1.98A/B94-312[»]
2BINX-ray1.90A94-312[»]
2BIOX-ray1.90A94-312[»]
2BIPX-ray1.80A94-312[»]
2BIQX-ray1.80A94-312[»]
2F1XX-ray2.30A/B359-368[»]
2FEJNMR-A94-297[»]
2FOJX-ray1.60B361-367[»]
2FOOX-ray2.20B358-363[»]
2GS0NMR-B20-73[»]
2H1LX-ray3.16M/N/O/P/Q/R/S/T/U/V/W/X92-292[»]
2H2DX-ray1.70B372-389[»]
2H2FX-ray2.20B372-389[»]
2H4FX-ray2.00D372-389[»]
2H4HX-ray1.99B372-389[»]
2H4JX-ray2.10D372-389[»]
2H59X-ray1.90D/E372-389[»]
2J0ZNMR-A/B/C/D326-356[»]
2J10NMR-A/B/C/D326-356[»]
2J11NMR-A/B/C/D326-356[»]
2J1WX-ray1.80A/B94-312[»]
2J1XX-ray1.65A/B94-312[»]
2J1YX-ray1.69A/B/C/D94-293[»]
2J1ZX-ray1.80A/B94-312[»]
2J20X-ray1.80A/B94-312[»]
2J21X-ray1.60A/B94-312[»]
2K8FNMR-B1-39[»]
2L14NMR-B13-61[»]
2LY4NMR-B1-93[»]
2MEJNMR-B96-312[»]
2OCJX-ray2.05A/B/C/D94-312[»]
2PCXX-ray1.54A94-292[»]
2VUKX-ray1.50A/B94-312[»]
2WGXX-ray1.75A/B94-312[»]
2X0UX-ray1.60A/B94-312[»]
2X0VX-ray1.80A/B94-312[»]
2X0WX-ray2.10A/B94-312[»]
2XWRX-ray1.68A/B89-293[»]
2YBGX-ray1.90A/B/C/D94-293[»]
2YDRX-ray2.75P144-154[»]
2Z5SX-ray2.30P/Q/R15-29[»]
2Z5TX-ray2.30P/Q/R15-29[»]
3D05X-ray1.70A94-293[»]
3D06X-ray1.20A94-293[»]
3D07X-ray2.20A/B94-293[»]
3D08X-ray1.40A94-293[»]
3D09X-ray1.90A94-293[»]
3D0AX-ray1.80A/B/C/D94-293[»]
3DABX-ray1.90B/D/F/H15-29[»]
3DACX-ray1.80B/P17-37[»]
3IGKX-ray1.70A94-293[»]
3IGLX-ray1.80A94-293[»]
3KMDX-ray2.15A/B/C/D92-291[»]
3KZ8X-ray1.91A/B94-293[»]
3LW1X-ray1.28P385-393[»]
3OQ5X-ray2.50D/E377-386[»]
3PDHX-ray1.80D372-389[»]
3Q01X-ray2.10A/B94-356[»]
3Q05X-ray2.40A/B/C/D94-356[»]
3Q06X-ray3.20A/B/C/D96-354[»]
3SAKNMR-A/B/C/D319-360[»]
3TG5X-ray2.30B365-375[»]
3TS8X-ray2.80A/B/C/D94-356[»]
3ZMEX-ray1.35A/B94-312[»]
4AGLX-ray1.70A/B94-312[»]
4AGMX-ray1.52A/B94-312[»]
4AGNX-ray1.60A/B94-312[»]
4AGOX-ray1.45A/B94-312[»]
4AGPX-ray1.50A/B94-312[»]
4AGQX-ray1.42A/B94-312[»]
4BUZX-ray1.90P379-386[»]
4BV2X-ray3.30E/H376-388[»]
4HFZX-ray2.69B/D15-29[»]
4HJEX-ray1.91A/B/C/D92-291[»]
4IBQX-ray1.80A/B/C/D94-293[»]
4IBSX-ray1.78A/B/C/D94-293[»]
4IBTX-ray1.70A/B/C/D94-293[»]
4IBUX-ray1.70A/B/C/D94-293[»]
4IBVX-ray2.10A94-293[»]
4IBWX-ray1.79A94-293[»]
4IBYX-ray1.45A/B94-293[»]
4IBZX-ray1.92A/B/C/D94-293[»]
4IJTX-ray1.78A94-293[»]
4KVPX-ray1.50A/B/C/D94-312[»]
4LO9X-ray2.50A/B/C/D94-312[»]
4LOEX-ray1.85A/B/C/D94-312[»]
4LOFX-ray2.00A94-312[»]
4MZIX-ray1.25A94-292[»]
4MZRX-ray2.90A/B/C/D94-388[»]
DisProtiDP00086.
ProteinModelPortaliP04637.
SMRiP04637. Positions 13-61, 91-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04637.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8383Interaction with HRMT1L2