CPLM-002142

Genbank Nucleotide ID

Cellular tumor antigen p53

Protein Synonyms/Alias

Antigen NY-CO-13; Phosphoprotein p53; Tumor suppressor p53

Homo sapiens (Human)

Position	Peptide	Type	References
101	SSSVPSQKTYQGSYG	ubiquitination	[1, 2, 3]
120	FLHSGTAKSVTCTYS	acetylation	[4, 5, 6]
120	FLHSGTAKSVTCTYS	ubiquitination	[2, 7, 8]
132	TYSPALNKMFCQLAK	ubiquitination	[1, 3]
164	VRAMAIYKQSQHMTE	acetylation	[9]
164	VRAMAIYKQSQHMTE	ubiquitination	[1, 3]
291	TEEENLRKKGEPHHE	ubiquitination	[3]
292	EEENLRKKGEPHHEL	acetylation	[10, 11, 12]
292	EEENLRKKGEPHHEL	propionylation	[13]
292	EEENLRKKGEPHHEL	ubiquitination	[1, 3]
305	ELPPGSTKRALPNNT	acetylation	[10, 11, 14]
305	ELPPGSTKRALPNNT	ubiquitination	[1, 2, 3]
319	TSSSPQPKKKPLDGE	acetylation	[14]
319	TSSSPQPKKKPLDGE	butyrylation	[15]
319	TSSSPQPKKKPLDGE	propionylation	[15]
320	SSSPQPKKKPLDGEY	acetylation	[14, 16, 17]
320	SSSPQPKKKPLDGEY	butyrylation	[15]
320	SSSPQPKKKPLDGEY	propionylation	[15]
320	SSSPQPKKKPLDGEY	ubiquitination	[1, 3, 18, 19]
321	SSPQPKKKPLDGEYF	acetylation	[11]
321	SSPQPKKKPLDGEYF	ubiquitination	[1, 3, 8, 19]
351	LNEALELKDAQAGKE	ubiquitination	[19]
357	LKDAQAGKEPGGSRA	acetylation	[14]
357	LKDAQAGKEPGGSRA	ubiquitination	[2, 8, 19, 20]
370	RAHSSHLKSKKGQST	acetylation	[9, 10, 14, 21, 22]
370	RAHSSHLKSKKGQST	methylation	[23, 24]
370	RAHSSHLKSKKGQST	ubiquitination	[8]
372	HSSHLKSKKGQSTSR	acetylation	[9, 10, 14, 21]
372	HSSHLKSKKGQSTSR	butyrylation	[13]
372	HSSHLKSKKGQSTSR	methylation	[23, 24, 25]
373	SSHLKSKKGQSTSRH	acetylation	[9, 10, 14, 17, 21, 26]
373	SSHLKSKKGQSTSRH	butyrylation	[13]
373	SSHLKSKKGQSTSRH	methylation	[24, 27]
381	GQSTSRHKKLMFKTE	acetylation	[9, 10, 11, 14, 21]
382	QSTSRHKKLMFKTEG	acetylation	[9, 10, 11, 14, 21]
382	QSTSRHKKLMFKTEG	butyrylation	[13]
382	QSTSRHKKLMFKTEG	methylation	[24, 28]
386	RHKKLMFKTEGPDSD	acetylation	[9]
386	RHKKLMFKTEGPDSD	sumoylation	[29, 30, 31, 32]
386	RHKKLMFKTEGPDSD	ubiquitination	[20]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[4] Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis.
Tang Y, Luo J, Zhang W, Gu W.
Mol Cell. 2006 Dec 28;24(6):827-39. [PMID: 17189186]
[5] Acetylation of the p53 DNA-binding domain regulates apoptosis induction.
Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, Lane WS, McMahon SB.
Mol Cell. 2006 Dec 28;24(6):841-51. [PMID: 17189187]
[6] PDCD5 interacts with Tip60 and functions as a cooperator in acetyltransferase activity and DNA damage-induced apoptosis.
Xu L, Chen Y, Song Q, Xu D, Wang Y, Ma D.
Neoplasia. 2009 Apr;11(4):345-54. [PMID: 19308289]
[7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[9] Acetylation is indispensable for p53 activation.
Tang Y, Zhao W, Chen Y, Zhao Y, Gu W.
Cell. 2008 May 16;133(4):612-26. [PMID: 18485870]
[10] Identification and characterization of a novel p300-mediated p53 acetylation site, lysine 305.
Wang YH, Tsay YG, Tan BC, Lo WY, Lee SC.
J Biol Chem. 2003 Jul 11;278(28):25568-76. [PMID: 12724314]
[11] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[12] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[13] Molecular characterization of propionyllysines in non-histone proteins.
Cheng Z, Tang Y, Chen Y, Kim S, Liu H, Li SS, Gu W, Zhao Y.
Mol Cell Proteomics. 2009 Jan;8(1):45-52. [PMID: 18753126]
[14] Identification of new p53 acetylation sites in COS-1 cells.
Joubel A, Chalkley RJ, Medzihradszky KF, Hondermarck H, Burlingame AL.
Mol Cell Proteomics. 2009 Jun;8(6):1167-73. [PMID: 19155208]
[15] Lysine propionylation and butyrylation are novel post-translational modifications in histones.
Chen Y, Sprung R, Tang Y, Ball H, Sangras B, Kim SC, Falck JR, Peng J, Gu W, Zhao Y.
Mol Cell Proteomics. 2007 May;6(5):812-9. [PMID: 17267393]
[16] DNA damage activates p53 through a phosphorylation-acetylation cascade.
Sakaguchi K, Herrera JE, Saito S, Miki T, Bustin M, Vassilev A, Anderson CW, Appella E.
Genes Dev. 1998 Sep 15;12(18):2831-41. [PMID: 9744860]
[17] p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage.
Liu L, Scolnick DM, Trievel RC, Zhang HB, Marmorstein R, Halazonetis TD, Berger SL.
Mol Cell Biol. 1999 Feb;19(2):1202-9. [PMID: 9891054]
[18] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[19] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[20] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[21] Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain.
Gu W, Roeder RG.
Cell. 1997 Aug 22;90(4):595-606. [PMID: 9288740]
[22] p85α mediates p53 K370 acetylation by p300 and regulates its promoter-specific transactivity in the cellular UVB response.
Song L, Gao M, Dong W, Hu M, Li J, Shi X, Hao Y, Li Y, Huang C.
Oncogene. 2011 Mar 17;30(11):1360-71. [PMID: 21057544]
[23] Repression of p53 activity by Smyd2-mediated methylation.
Huang J, Perez-Burgos L, Placek BJ, Sengupta R, Richter M, Dorsey JA, Kubicek S, Opravil S, Jenuwein T, Berger SL.
Nature. 2006 Nov 30;444(7119):629-32. [PMID: 17108971]
[24] Update on activities at the Universal Protein Resource (UniProt) in 2013.
e="String">UniProt Consortium.
Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
[25] Regulation of p53 activity through lysine methylation.
Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D.
Nature. 2004 Nov 18;432(7015):353-60. [PMID: 15525938]
[26] Knockdown of CITED2 using short-hairpin RNA sensitizes cancer cells to cisplatin through stabilization of p53 and enhancement of p53-dependent apoptosis.
Wu ZZ, Sun NK, Chao CC.
J Cell Physiol. 2011 Sep;226(9):2415-28. [PMID: 21660965]
[27] G9a and Glp methylate lysine 373 in the tumor suppressor p53.
Huang J, Dorsey J, Chuikov S, Pérez-Burgos L, Zhang X, Jenuwein T, Reinberg D, Berger SL.
J Biol Chem. 2010 Mar 26;285(13):9636-41. [PMID: 20118233]
[28] Modulation of p53 function by SET8-mediated methylation at lysine 382.
Shi X, Kachirskaia I, Yamaguchi H, West LE, Wen H, Wang EW, Dutta S, Appella E, Gozani O.
Mol Cell. 2007 Aug 17;27(4):636-46. [PMID: 17707234]
[29] SUMO-1 modification activates the transcriptional response of p53.
Rodriguez MS, Desterro JM, Lain S, Midgley CA, Lane DP, Hay RT.
EMBO J. 1999 Nov 15;18(22):6455-61. [PMID: 10562557]
[30] Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity.
Schmidt D, Müller S.
Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2872-7. [PMID: 11867732]
[31] Ubc9 fusion-directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation.
Jakobs A, Koehnke J, Himstedt F, Funk M, Korn B, Gaestel M, Niedenthal R.
Nat Methods. 2007 Mar;4(3):245-50. [PMID: 17277783]
[32] Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that represses p53 and stimulates its nuclear export through interactions with promyelocytic leukemia nuclear bodies.
Pennella MA, Liu Y, Woo JL, Kim CA, Berk AJ.
J Virol. 2010 Dec;84(23):12210-25. [PMID: 20861261]

Functional Description

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.

DNA_BIND 102 292
REGION 1 83 Interaction with HRMT1L2.
REGION 1 44 Transcription activation (acidic).
REGION 66 110 Interaction with WWOX.
REGION 100 370 Interaction with HIPK1 (By similarity).
REGION 100 300 Required for interaction with ZNF385A.
REGION 113 236 Required for interaction with FBXO42.
REGION 116 292 Interaction with AXIN1 (By similarity).
REGION 241 248 Interacts with the 53BP2 SH3 domain.
REGION 256 294 Interaction with E4F1.
REGION 273 280 Interaction with DNA.
REGION 300 393 Interaction with CARM1.
REGION 319 360 Interaction with HIPK2.
REGION 325 356 Oligomerization.
REGION 359 363 Interaction with USP7.
REGION 368 387 Basic (repression of DNA-binding).
MOTIF 17 25 TADI.
MOTIF 48 56 TADII.
MOTIF 305 321 Bipartite nuclear localization signal.
MOTIF 339 350 Nuclear export signal.
MOTIF 370 372 [KR]-[STA]-K motif.
METAL 176 176 Zinc.
METAL 179 179 Zinc.
METAL 238 238 Zinc.
METAL 242 242 Zinc.
MOD_RES 9 9 Phosphoserine; by HIPK4.
MOD_RES 15 15 Phosphoserine; by CDK5, PRPK, AMPK, NUAK1
MOD_RES 18 18 Phosphothreonine; by CK1, VRK1 and VRK2.
MOD_RES 20 20 Phosphoserine; by CHEK2, CK1 and PLK3.
MOD_RES 33 33 Phosphoserine; by CDK5 and CDK7.
MOD_RES 37 37 Phosphoserine; by MAPKAPK5.
MOD_RES 46 46 Phosphoserine; by CDK5, DYRK2, HIPK2 and
MOD_RES 55 55 Phosphothreonine; by TAF1 and GRK5.
MOD_RES 120 120 N6-acetyllysine; by KAT6A.
MOD_RES 183 183 Phosphoserine; by AURKB.
MOD_RES 269 269 Phosphoserine; by AURKB.
MOD_RES 284 284 Phosphothreonine; by AURKB.
MOD_RES 305 305 N6-acetyllysine.
MOD_RES 315 315 Phosphoserine; by AURKA, CDK1 and CDK2.
MOD_RES 370 370 N6,N6-dimethyllysine; alternate.
MOD_RES 370 370 N6-methyllysine; by SMYD2; alternate.
MOD_RES 372 372 N6-methyllysine; by SETD7.
MOD_RES 373 373 N6,N6-dimethyllysine; by EHMT1 and EHMT2;
MOD_RES 373 373 N6-acetyllysine; alternate.
MOD_RES 381 381 N6-acetyllysine.
MOD_RES 382 382 N6,N6-dimethyllysine; alternate.
MOD_RES 382 382 N6-acetyllysine; by KAT6A; alternate.
MOD_RES 382 382 N6-methyllysine; by SETD8; alternate.
MOD_RES 392 392 Phosphoserine; by CK2, CDK2 and NUAK1.
CROSSLNK 291 291 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 292 292 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Activator; Alternative promoter usage; Alternative splicing; Apoptosis; Cell cycle; Complete proteome; Cytoplasm; Disease mutation; DNA-binding; Endoplasmic reticulum; Glycoprotein; Host-virus interaction; Isopeptide bond; Li-Fraumeni syndrome; Metal-binding; Methylation; Mitochondrion; Necrosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO:0005829; C:cytosol; IDA:UniProtKB.
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO:0005730; C:nucleolus; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0016605; C:PML body; IDA:UniProtKB.
GO:0043234; C:protein complex; IDA:BHF-UCL.
GO:0005657; C:replication fork; IBA:RefGenome.
GO:0005524; F:ATP binding; IDA:UniProtKB.
GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO:0003684; F:damaged DNA binding; IBA:RefGenome.
GO:0035033; F:histone deacetylase regulator activity; IEA:Compara.
GO:0002039; F:p53 binding; IBA:RefGenome.
GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Compara.
GO:0001228; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IDA:BHF-UCL.
GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO:0002326; P:B cell lineage commitment; IEA:Compara.
GO:0006284; P:base-excision repair; TAS:UniProtKB.
GO:0007596; P:blood coagulation; TAS:Reactome.
GO:0007050; P:cell cycle arrest; IMP:UniProtKB.
GO:0030154; P:cell differentiation; TAS:UniProtKB.
GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO:0034613; P:cellular protein localization; IDA:UniProtKB.
GO:0035690; P:cellular response to drug; IEP:UniProtKB.
GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
GO:0034644; P:cellular response to UV; IBA:RefGenome.
GO:0007417; P:central nervous system development; IEA:Compara.
GO:0051276; P:chromosome organization; IEA:Compara.
GO:0008340; P:determination of adult lifespan; ISS:BHF-UCL.
GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:BHF-UCL.
GO:0000733; P:DNA strand renaturation; IDA:UniProtKB.
GO:0006302; P:double-strand break repair; IEA:Compara.
GO:0006983; P:ER overload response; IDA:MGI.
GO:0007369; P:gastrulation; IEA:Compara.
GO:0001701; P:in utero embryonic development; IEA:Compara.
GO:0006917; P:induction of apoptosis; IEA:Compara.
GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB.
GO:0071850; P:mitotic cell cycle arrest; IEA:Compara.
GO:0035264; P:multicellular organism growth; IEA:Compara.
GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO:0008156; P:negative regulation of DNA replication; IEA:Compara.
GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB.
GO:0051097; P:negative regulation of helicase activity; TAS:UniProtKB.
GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Compara.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Compara.
GO:0051402; P:neuron apoptotic process; IEA:Compara.
GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
GO:0097252; P:oligodendrocyte apoptotic process; IDA:UniProtKB.
GO:0090403; P:oxidative stress-induced premature senescence; IMP:BHF-UCL.
GO:0090343; P:positive regulation of cell aging; IEA:Compara.
GO:0031065; P:positive regulation of histone deacetylation; IBA:RefGenome.
GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO:0043525; P:positive regulation of neuron apoptotic process; IBA:RefGenome.
GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO:0070245; P:positive regulation of thymocyte apoptotic process; ISS:BHF-UCL.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO:0000060; P:protein import into nucleus, translocation; IEA:Compara.
GO:0008104; P:protein localization; IDA:UniProtKB.
GO:0051262; P:protein tetramerization; TAS:UniProtKB.
GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
GO:0046902; P:regulation of mitochondrial membrane permeability; TAS:UniProtKB.
GO:0001836; P:release of cytochrome c from mitochondria; IEA:Compara.
GO:0090399; P:replicative senescence; IMP:BHF-UCL.
GO:0046677; P:response to antibiotic; IEP:UniProtKB.
GO:0010332; P:response to gamma radiation; IMP:BHF-UCL.
GO:0009651; P:response to salt stress; IEA:Compara.
GO:0010165; P:response to X-ray; IBA:RefGenome.
GO:0009303; P:rRNA transcription; IEA:Compara.
GO:0001756; P:somitogenesis; IEA:Compara.
GO:0033077; P:T cell differentiation in thymus; IEA:Compara.
GO:0002360; P:T cell lineage commitment; IEA:Compara.
GO:0002309; P:T cell proliferation involved in immune response; IEA:Compara.
GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Compara.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR008967; p53-like_TF_DNA-bd.
IPR012346; p53/RUNT-type_TF_DNA-bd.
IPR011615; p53_DNA-bd.
IPR010991; p53_tetrameristn.
IPR013872; p53_transactivation_domain.
IPR002117; p53_tumour_suppressor.

PF00870; P53
PF08563; P53_TAD
PF07710; P53_tetramer

PR00386; P53SUPPRESSR.