Module talk:ImportProtein/p53

{{#invoke:ImportProtein | main | height=50 | width = 500|vtext=26| include = all | toprow = "ubiquitination site","acetylation","phosphorylation","methylation","neddylation site","proteolytic cleavage site"|exclude = | replaceregion = | usenotes = "other","modified","active","variant","binding" | substitute = "Transcription activation (acidic)":"TAD (transcription activation domain)","Basic (repression of DNA-binding)":"Basic-repress DNA binding","Required for interaction with FBXO42":"FBXO42 interaction"|file=LOCUS NP_000537 393 aa linear PRI 03-MAR-2013

DEFINITION cellular tumor antigen p53 isoform a [Homo sapiens].

ACCESSION NP_000537

VERSION NP_000537.3 GI:120407068

DBSOURCE REFSEQ: accession NM_000546.5

KEYWORDS .

SOURCE Homo sapiens (human)

ORGANISM Homo sapiens

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;

Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;

Catarrhini; Hominidae; Homo.

REFERENCE 1 (residues 1 to 393)

AUTHORS Marcel,V., Tran,P.L., Sagne,C., Martel-Planche,G., Vaslin,L.,

Teulade-Fichou,M.P., Hall,J., Mergny,J.L., Hainaut,P. and Van

Dyck,E.

TITLE G-quadruplex structures in TP53 intron 3: role in alternative

splicing and in production of p53 mRNA isoforms

JOURNAL Carcinogenesis 32 (3), 271-278 (2011)

PUBMED 21112961

REFERENCE 2 (residues 1 to 393)

AUTHORS Marcel,V., Perrier,S., Aoubala,M., Ageorges,S., Groves,M.J.,

Diot,A., Fernandes,K., Tauro,S. and Bourdon,J.C.

TITLE Delta160p53 is a novel N-terminal p53 isoform encoded by

Delta133p53 transcript

JOURNAL FEBS Lett. 584 (21), 4463-4468 (2010)

PUBMED 20937277

REMARK GeneRIF: Delta133p53 transcript generates two different p53

isoforms, Delta133p53 and Delta160p53

REFERENCE 3 (residues 1 to 393)

AUTHORS Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,

Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.

TITLE Does the nonsense-mediated mRNA decay mechanism prevent the

synthesis of truncated BRCA1, CHK2, and p53 proteins?

JOURNAL Hum. Mutat. 29 (1), 65-73 (2008)

PUBMED 17694537

REMARK GeneRIF: the p53 protein encoded by the 770delT allele is as

abundant as the wild-type protein, as removal of the C-terminal p53

domain leads to a stabilized mutant protein, whose abundance is

markedly increased when NMD is inhibited.

REFERENCE 4 (residues 1 to 393)

AUTHORS Bourdon,J.C.

TITLE p53 Family isoforms

JOURNAL Curr Pharm Biotechnol 8 (6), 332-336 (2007)

PUBMED 18289041

REMARK Review article

REFERENCE 5 (sites)

AUTHORS Matsuoka,S., Ballif,B.A., Smogorzewska,A., McDonald,E.R. III,

Hurov,K.E., Luo,J., Bakalarski,C.E., Zhao,Z., Solimini,N.,

Lerenthal,Y., Shiloh,Y., Gygi,S.P. and Elledge,S.J.

TITLE ATM and ATR substrate analysis reveals extensive protein networks

responsive to DNA damage

JOURNAL Science 316 (5828), 1160-1166 (2007)

PUBMED 17525332

REFERENCE 6 (sites)

AUTHORS Sun,P., Yoshizuka,N., New,L., Moser,B.A., Li,Y., Liao,R., Xie,C.,

Chen,J., Deng,Q., Yamout,M., Dong,M.Q., Frangou,C.G., Yates,J.R.

III, Wright,P.E. and Han,J.

TITLE PRAK is essential for ras-induced senescence and tumor suppression

JOURNAL Cell 128 (2), 295-308 (2007)

PUBMED 17254968

REFERENCE 7 (sites)

AUTHORS Li,H.H., Cai,X., Shouse,G.P., Piluso,L.G. and Liu,X.

TITLE A specific PP2A regulatory subunit, B56gamma, mediates DNA

damage-induced dephosphorylation of p53 at Thr55

JOURNAL EMBO J. 26 (2), 402-411 (2007)

PUBMED 17245430

REFERENCE 8 (sites)

AUTHORS Abida,W.M., Nikolaev,A., Zhao,W., Zhang,W. and Gu,W.

TITLE FBXO11 promotes the Neddylation of p53 and inhibits its

transcriptional activity

JOURNAL J. Biol. Chem. 282 (3), 1797-1804 (2007)

PUBMED 17098746

REFERENCE 9 (sites)

AUTHORS Huang,J., Perez-Burgos,L., Placek,B.J., Sengupta,R., Richter,M.,

Dorsey,J.A., Kubicek,S., Opravil,S., Jenuwein,T. and Berger,S.L.

TITLE Repression of p53 activity by Smyd2-mediated methylation

JOURNAL Nature 444 (7119), 629-632 (2006)

PUBMED 17108971

REFERENCE 10 (sites)

AUTHORS Le Cam,L., Linares,L.K., Paul,C., Julien,E., Lacroix,M., Hatchi,E.,

Triboulet,R., Bossis,G., Shmueli,A., Rodriguez,M.S., Coux,O. and

Sardet,C.

TITLE E4F1 is an atypical ubiquitin ligase that modulates p53 effector

functions independently of degradation

JOURNAL Cell 127 (4), 775-788 (2006)

PUBMED 17110336

REFERENCE 11 (residues 1 to 393)

AUTHORS Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,

Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.

TITLE Expression of p53 and p53/47 are controlled by alternative

mechanisms of messenger RNA translation initiation

JOURNAL Oncogene 25 (52), 6936-6947 (2006)

PUBMED 16983332

REMARK GeneRIF: harbouring alternative translation initiation sites, the

p53 mRNA gives rise to different levels of the p53 isoforms which

help to orchestrate the cell biological outcome of p53 activation

REFERENCE 12 (sites)

AUTHORS Pellegrini,M., Celeste,A., Difilippantonio,S., Guo,R., Wang,W.,

Feigenbaum,L. and Nussenzweig,A.

TITLE Autophosphorylation at serine 1987 is dispensable for murine Atm

activation in vivo

JOURNAL Nature 443 (7108), 222-225 (2006)

PUBMED 16906133

REFERENCE 13 (sites)

AUTHORS Chen,J., Dai,G., Wang,Y.Q., Wang,S., Pan,F.Y., Xue,B., Zhao,D.H.

and Li,C.J.

TITLE Polo-like kinase 1 regulates mitotic arrest after UV irradiation

through dephosphorylation of p53 and inducing p53 degradation

JOURNAL FEBS Lett. 580 (15), 3624-3630 (2006)

PUBMED 16753148

REFERENCE 14 (sites)

AUTHORS Radhakrishnan,S.K. and Gartel,A.L.

TITLE CDK9 phosphorylates p53 on serine residues 33, 315 and 392

JOURNAL Cell Cycle 5 (5), 519-521 (2006)

PUBMED 16552184

REFERENCE 15 (sites)

AUTHORS Couture,J.F., Collazo,E., Hauk,G. and Trievel,R.C.

TITLE Structural basis for the methylation site specificity of SET7/9

JOURNAL Nat. Struct. Mol. Biol. 13 (2), 140-146 (2006)

PUBMED 16415881

REFERENCE 16 (sites)

AUTHORS Dodson,G.E. and Tibbetts,R.S.

TITLE DNA replication stress-induced phosphorylation of cyclic AMP

response element-binding protein mediated by ATM

JOURNAL J. Biol. Chem. 281 (3), 1692-1697 (2006)

PUBMED 16293623

REFERENCE 17 (sites)

AUTHORS Di Stefano,V., Mattiussi,M., Sacchi,A. and D'Orazi,G.

TITLE HIPK2 inhibits both MDM2 gene and protein by, respectively,

p53-dependent and independent regulations

JOURNAL FEBS Lett. 579 (25), 5473-5480 (2005)

PUBMED 16212962

REFERENCE 18 (sites)

AUTHORS Chang,N.S., Schultz,L., Hsu,L.J., Lewis,J., Su,M. and Sze,C.I.

TITLE 17beta-Estradiol upregulates and activates WOX1/WWOXv1 and

WOX2/WWOXv2 in vitro: potential role in cancerous progression of

breast and prostate to a premetastatic state in vivo

JOURNAL Oncogene 24 (4), 714-723 (2005)

PUBMED 15580310

REFERENCE 19 (sites)

AUTHORS Fabbro,M., Savage,K., Hobson,K., Deans,A.J., Powell,S.N.,

McArthur,G.A. and Khanna,K.K.

TITLE BRCA1-BARD1 complexes are required for p53Ser-15 phosphorylation

and a G1/S arrest following ionizing radiation-induced DNA damage

JOURNAL J. Biol. Chem. 279 (30), 31251-31258 (2004)

PUBMED 15159397

REFERENCE 20 (sites)

AUTHORS Yeh,P.Y., Chuang,S.E., Yeh,K.H., Song,Y.C., Chang,L.L. and

Cheng,A.L.

TITLE Phosphorylation of p53 on Thr55 by ERK2 is necessary for

doxorubicin-induced p53 activation and cell death

JOURNAL Oncogene 23 (20), 3580-3588 (2004)

PUBMED 15116093

REFERENCE 21 (sites)

AUTHORS Schultz,L., Khera,S., Sleve,D., Heath,J. and Chang,N.S.

TITLE TIAF1 and p53 functionally interact in mediating apoptosis and

silencing of TIAF1 abolishes nuclear translocation of serine

15-phosphorylated p53

JOURNAL DNA Cell Biol. 23 (1), 67-74 (2004)

PUBMED 14965474

REFERENCE 22 (sites)

AUTHORS Wang,Y.H., Tsay,Y.G., Tan,B.C., Lo,W.Y. and Lee,S.C.

TITLE Identification and characterization of a novel p300-mediated p53

acetylation site, lysine 305

JOURNAL J. Biol. Chem. 278 (28), 25568-25576 (2003)

PUBMED 12724314

REFERENCE 23 (sites)

AUTHORS Uhle,S., Medalia,O., Waldron,R., Dumdey,R., Henklein,P.,

Bech-Otschir,D., Huang,X., Berse,M., Sperling,J., Schade,R. and

Dubiel,W.

TITLE Protein kinase CK2 and protein kinase D are associated with the

COP9 signalosome

JOURNAL EMBO J. 22 (6), 1302-1312 (2003)

PUBMED 12628923

REFERENCE 24 (sites)

AUTHORS Xie,S., Wu,H., Wang,Q., Kunicki,J., Thomas,R.O.,

Hollingsworth,R.E., Cogswell,J. and Dai,W.

TITLE Genotoxic stress-induced activation of Plk3 is partly mediated by

Chk2

JOURNAL Cell Cycle 1 (6), 424-429 (2002)

PUBMED 12548019

REFERENCE 25 (sites)

AUTHORS Zheng,H., You,H., Zhou,X.Z., Murray,S.A., Uchida,T., Wulf,G.,

Gu,L., Tang,X., Lu,K.P. and Xiao,Z.X.

TITLE The prolyl isomerase Pin1 is a regulator of p53 in genotoxic

response

JOURNAL Nature 419 (6909), 849-853 (2002)

PUBMED 12397361

REMARK Erratum:[Nature 2002 Nov 28;420(6914):445]

REFERENCE 26 (sites)

AUTHORS Bahassi el,M., Conn,C.W., Myer,D.L., Hennigan,R.F., McGowan,C.H.,

Sanchez,Y. and Stambrook,P.J.

TITLE Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein

involved in stress response pathways

JOURNAL Oncogene 21 (43), 6633-6640 (2002)

PUBMED 12242661

REFERENCE 27 (sites)

AUTHORS Kim,S.J., Hwang,S.G., Shin,D.Y., Kang,S.S. and Chun,J.S.

TITLE p38 kinase regulates nitric oxide-induced apoptosis of articular

chondrocytes by accumulating p53 via NFkappa B-dependent

transcription and stabilization by serine 15 phosphorylation

JOURNAL J. Biol. Chem. 277 (36), 33501-33508 (2002)

PUBMED 12091386

REFERENCE 28 (sites)

AUTHORS Jabbur,J.R. and Zhang,W.

TITLE p53 Antiproliferative function is enhanced by aspartate

substitution at threonine 18 and serine 20

JOURNAL Cancer Biol. Ther. 1 (3), 277-283 (2002)

PUBMED 12432277

REFERENCE 29 (sites)

AUTHORS Saito,S., Goodarzi,A.A., Higashimoto,Y., Noda,Y., Lees-Miller,S.P.,

Appella,E. and Anderson,C.W.

TITLE ATM mediates phosphorylation at multiple p53 sites, including

Ser(46), in response to ionizing radiation

JOURNAL J. Biol. Chem. 277 (15), 12491-12494 (2002)

PUBMED 11875057

REFERENCE 30 (sites)

AUTHORS Zhang,J., Krishnamurthy,P.K. and Johnson,G.V.

TITLE Cdk5 phosphorylates p53 and regulates its activity

JOURNAL J. Neurochem. 81 (2), 307-313 (2002)

PUBMED 12064478

REFERENCE 31 (sites)

AUTHORS Barcia,R., Lopez-Borges,S., Vega,F.M. and Lazo,P.A.

TITLE Kinetic properties of p53 phosphorylation by the human

vaccinia-related kinase 1

JOURNAL Arch. Biochem. Biophys. 399 (1), 1-5 (2002)

PUBMED 11883897

REFERENCE 32 (sites)

AUTHORS D'Orazi,G., Cecchinelli,B., Bruno,T., Manni,I., Higashimoto,Y.,

Saito,S., Gostissa,M., Coen,S., Marchetti,A., Del Sal,G.,

Piaggio,G., Fanciulli,M., Appella,E. and Soddu,S.

TITLE Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser

46 and mediates apoptosis

JOURNAL Nat. Cell Biol. 4 (1), 11-19 (2002)

PUBMED 11780126

REFERENCE 33 (sites)

AUTHORS Xie,S., Wu,H., Wang,Q., Cogswell,J.P., Husain,I., Conn,C.,

Stambrook,P., Jhanwar-Uniyal,M. and Dai,W.

TITLE Plk3 functionally links DNA damage to cell cycle arrest and

apoptosis at least in part via the p53 pathway

JOURNAL J. Biol. Chem. 276 (46), 43305-43312 (2001)

PUBMED 11551930

REFERENCE 34 (sites)

AUTHORS Vaziri,H., Dessain,S.K., Ng Eaton,E., Imai,S.I., Frye,R.A.,

Pandita,T.K., Guarente,L. and Weinberg,R.A.

TITLE hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

JOURNAL Cell 107 (2), 149-159 (2001)

PUBMED 11672523

REFERENCE 35 (sites)

AUTHORS Latonen,L., Taya,Y. and Laiho,M.

TITLE UV-radiation induces dose-dependent regulation of p53 response and

modulates p53-HDM2 interaction in human fibroblasts

JOURNAL Oncogene 20 (46), 6784-6793 (2001)

PUBMED 11709713

REMARK Erratum:[Oncogene 2001 Dec 6;20(56):8165]

REFERENCE 36 (sites)

AUTHORS Yeh,P.Y., Chuang,S.E., Yeh,K.H., Song,Y.C. and Cheng,A.L.

TITLE Nuclear extracellular signal-regulated kinase 2 phosphorylates p53

at Thr55 in response to doxorubicin

JOURNAL Biochem. Biophys. Res. Commun. 284 (4), 880-886 (2001)

PUBMED 11409876

REFERENCE 37 (sites)

AUTHORS Buschmann,T., Potapova,O., Bar-Shira,A., Ivanov,V.N., Fuchs,S.Y.,

Henderson,S., Fried,V.A., Minamoto,T., Alarcon-Vargas,D.,

Pincus,M.R., Gaarde,W.A., Holbrook,N.J., Shiloh,Y. and Ronai,Z.

TITLE Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is

important for p53 stabilization and transcriptional activities in

response to stress

JOURNAL Mol. Cell. Biol. 21 (8), 2743-2754 (2001)

PUBMED 11283254

REFERENCE 38 (sites)

AUTHORS Turenne,G.A. and Price,B.D.

TITLE Glycogen synthase kinase3 beta phosphorylates serine 33 of p53 and

activates p53's transcriptional activity

JOURNAL BMC Cell Biol. 2, 12 (2001)

PUBMED 11483158

REFERENCE 39 (sites)

AUTHORS Nakamura,S., Roth,J.A. and Mukhopadhyay,T.

TITLE Multiple lysine mutations in the C-terminal domain of p53 interfere

with MDM2-dependent protein degradation and ubiquitination

JOURNAL Mol. Cell. Biol. 20 (24), 9391-9398 (2000)

PUBMED 11094089

REFERENCE 40 (sites)

AUTHORS Rodriguez,M.S., Desterro,J.M., Lain,S., Lane,D.P. and Hay,R.T.

TITLE Multiple C-terminal lysine residues target p53 for

ubiquitin-proteasome-mediated degradation

JOURNAL Mol. Cell. Biol. 20 (22), 8458-8467 (2000)

PUBMED 11046142

REFERENCE 41 (sites)

AUTHORS Lopez-Borges,S. and Lazo,P.A.

TITLE The human vaccinia-related kinase 1 (VRK1) phosphorylates

threonine-18 within the mdm-2 binding site of the p53 tumour

suppressor protein

JOURNAL Oncogene 19 (32), 3656-3664 (2000)

PUBMED 10951572

REFERENCE 42 (sites)

AUTHORS Luciani,M.G., Hutchins,J.R., Zheleva,D. and Hupp,T.R.

TITLE The C-terminal regulatory domain of p53 contains a functional

docking site for cyclin A

JOURNAL J. Mol. Biol. 300 (3), 503-518 (2000)

PUBMED 10884347

REFERENCE 43 (sites)

AUTHORS Juan,L.J., Shia,W.J., Chen,M.H., Yang,W.M., Seto,E., Lin,Y.S. and

Wu,C.W.

TITLE Histone deacetylases specifically down-regulate p53-dependent gene

activation

JOURNAL J. Biol. Chem. 275 (27), 20436-20443 (2000)

PUBMED 10777477

REFERENCE 44 (sites)

AUTHORS Sayed,M., Kim,S.O., Salh,B.S., Issinger,O.G. and Pelech,S.L.

TITLE Stress-induced activation of protein kinase CK2 by direct

interaction with p38 mitogen-activated protein kinase

JOURNAL J. Biol. Chem. 275 (22), 16569-16573 (2000)

PUBMED 10747897

REFERENCE 45 (sites)

AUTHORS Delia,D., Mizutani,S., Panigone,S., Tagliabue,E., Fontanella,E.,

Asada,M., Yamada,T., Taya,Y., Prudente,S., Saviozzi,S., Frati,L.,

Pierotti,M.A. and Chessa,L.

TITLE ATM protein and p53-serine 15 phosphorylation in

ataxia-telangiectasia (AT) patients and at heterozygotes

JOURNAL Br. J. Cancer 82 (12), 1938-1945 (2000)

PUBMED 10864201

REFERENCE 46 (sites)

AUTHORS Shieh,S.Y., Ahn,J., Tamai,K., Taya,Y. and Prives,C.

TITLE The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2)

phosphorylate p53 at multiple DNA damage-inducible sites

JOURNAL Genes Dev. 14 (3), 289-300 (2000)

PUBMED 10673501

REMARK Erratum:[Genes Dev 2000 Mar 15;14(6):750]

REFERENCE 47 (sites)

AUTHORS Li,L., Ljungman,M. and Dixon,J.E.

TITLE The human Cdc14 phosphatases interact with and dephosphorylate the

tumor suppressor protein p53

JOURNAL J. Biol. Chem. 275 (4), 2410-2414 (2000)

PUBMED 10644693

REFERENCE 48 (sites)

AUTHORS Dumaz,N., Milne,D.M. and Meek,D.W.

TITLE Protein kinase CK1 is a p53-threonine 18 kinase which requires

prior phosphorylation of serine 15

JOURNAL FEBS Lett. 463 (3), 312-316 (1999)

PUBMED 10606744

REFERENCE 49 (sites)

AUTHORS Cuddihy,A.R., Wong,A.H., Tam,N.W., Li,S. and Koromilas,A.E.

TITLE The double-stranded RNA activated protein kinase PKR physically

associates with the tumor suppressor p53 protein and phosphorylates

human p53 on serine 392 in vitro

JOURNAL Oncogene 18 (17), 2690-2702 (1999)

PUBMED 10348343

REFERENCE 50 (sites)

AUTHORS Liu,L., Scolnick,D.M., Trievel,R.C., Zhang,H.B., Marmorstein,R.,

Halazonetis,T.D. and Berger,S.L.

TITLE p53 sites acetylated in vitro by PCAF and p300 are acetylated in

vivo in response to DNA damage

JOURNAL Mol. Cell. Biol. 19 (2), 1202-1209 (1999)

PUBMED 9891054

REFERENCE 51 (sites)

AUTHORS Khanna,K.K., Keating,K.E., Kozlov,S., Scott,S., Gatei,M.,

Hobson,K., Taya,Y., Gabrielli,B., Chan,D., Lees-Miller,S.P. and

Lavin,M.F.

TITLE ATM associates with and phosphorylates p53: mapping the region of

interaction

JOURNAL Nat. Genet. 20 (4), 398-400 (1998)

PUBMED 9843217

REFERENCE 52 (sites)

AUTHORS Giaccia,A.J. and Kastan,M.B.

TITLE The complexity of p53 modulation: emerging patterns from divergent

signals

JOURNAL Genes Dev. 12 (19), 2973-2983 (1998)

PUBMED 9765199

REFERENCE 53 (sites)

AUTHORS Sakaguchi,K., Herrera,J.E., Saito,S., Miki,T., Bustin,M.,

Vassilev,A., Anderson,C.W. and Appella,E.

TITLE DNA damage activates p53 through a phosphorylation-acetylation

cascade

JOURNAL Genes Dev. 12 (18), 2831-2841 (1998)

PUBMED 9744860

REFERENCE 54 (sites)

AUTHORS Youmell,M., Park,S.J., Basu,S. and Price,B.D.

TITLE Regulation of the p53 protein by protein kinase C alpha and protein

kinase C zeta

JOURNAL Biochem. Biophys. Res. Commun. 245 (2), 514-518 (1998)

PUBMED 9571186

REFERENCE 55 (sites)

AUTHORS Okorokov,A.L., Ponchel,F. and Milner,J.

TITLE Induced N- and C-terminal cleavage of p53: a core fragment of p53,

generated by interaction with damaged DNA, promotes cleavage of the

N-terminus of full-length p53, whereas ssDNA induces C-terminal

cleavage of p53

JOURNAL EMBO J. 16 (19), 6008-6017 (1997)

PUBMED 9312058

REFERENCE 56 (sites)

AUTHORS Gu,W. and Roeder,R.G.

TITLE Activation of p53 sequence-specific DNA binding by acetylation of

the p53 C-terminal domain

JOURNAL Cell 90 (4), 595-606 (1997)

PUBMED 9288740

REFERENCE 57 (sites)

AUTHORS Delphin,C., Huang,K.P., Scotto,C., Chapel,A., Vincon,M.,

Chambaz,E., Garin,J. and Baudier,J.

TITLE The in vitro phosphorylation of p53 by calcium-dependent protein

kinase C--characterization of a protein-kinase-C-binding site on

p53

JOURNAL Eur. J. Biochem. 245 (3), 684-692 (1997)

PUBMED 9183006

REFERENCE 58 (sites)

AUTHORS Baudier,J., Delphin,C., Grunwald,D., Khochbin,S. and Lawrence,J.J.

TITLE Characterization of the tumor suppressor protein p53 as a protein

kinase C substrate and a S100b-binding protein

JOURNAL Proc. Natl. Acad. Sci. U.S.A. 89 (23), 11627-11631 (1992)

PUBMED 1454855

REFERENCE 59 (residues 1 to 393)

AUTHORS Lamb,P. and Crawford,L.

TITLE Characterization of the human p53 gene

JOURNAL Mol. Cell. Biol. 6 (5), 1379-1385 (1986)

PUBMED 2946935

REFERENCE 60 (residues 1 to 393)

AUTHORS Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.

TITLE Localization of gene for human p53 tumour antigen to band 17p13

JOURNAL Nature 320 (6057), 84-85 (1986)

PUBMED 3456488

REFERENCE 61 (residues 1 to 393)

AUTHORS Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,

Bruns,G.A. and Peacock,J.

TITLE Transformation associated p53 protein is encoded by a gene on human

chromosome 17

JOURNAL Somat. Cell Mol. Genet. 11 (5), 505-510 (1985)

PUBMED 2994241

REFERENCE 62 (residues 1 to 393)

AUTHORS Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.

TITLE Molecular cloning and in vitro expression of a cDNA clone for human

cellular tumor antigen p53

JOURNAL Mol. Cell. Biol. 5 (7), 1601-1610 (1985)

PUBMED 3894933

REFERENCE 63 (residues 1 to 393)

AUTHORS Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.

TITLE Human p53 cellular tumor antigen: cDNA sequence and expression in

COS cells

JOURNAL EMBO J. 4 (5), 1251-1255 (1985)

PUBMED 4006916

REFERENCE 64 (sites)

AUTHORS Zhukov-Verezhnikov,N.N., Anisimov,P.I., Goncharova,N.S.,

Bochko,G.M. and Karaseva,Z.N.

TITLE [Study of the heterogenetic antigens in vaccinal preparations of V.

cholerae]

JOURNAL Biull Eksp Biol Med 82 (8), 961-962 (1976)

PUBMED 1088347

COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The

reference sequence was derived from DA453049.1, X02469.1,

AK223026.1 and DQ186650.1.

This sequence is a reference standard in the RefSeqGene project.

On Dec 29, 2006 this sequence version replaced gi:8400738.

Summary: This gene encodes a tumor suppressor protein containing

transcriptional activation, DNA binding, and oligomerization

domains. The encoded protein responds to diverse cellular stresses

to regulate expression of target genes, thereby inducing cell cycle

arrest, apoptosis, senescence, DNA repair, or changes in

metabolism. Mutations in this gene are associated with a variety of

human cancers, including hereditary cancers such as Li-Fraumeni

syndrome. Alternative splicing of this gene and the use of

alternate promoters result in multiple transcript variants and

isoforms. Additional isoforms have also been shown to result from

the use of alternate translation initiation codons (PMIDs:

12032546, 20937277). [provided by RefSeq, Feb 2013].

Transcript Variant: This variant (1) can initiate translation from

two in-frame AUG start codons. The isoform represented in this

variant (a, also known as p53alpha) results from translation

initiation at the upstream start codon. Both variants 1 and 2

encode isoform a, which is the longest isoform.

Publication Note: This RefSeq record includes a subset of the

publications that are available for this gene. Please see the Gene

record to access additional publications.

##RefSeq-Attributes-START##

Transcript_exon_combination_evidence :: DQ191317.1, DQ286964.1

[ECO:0000332]

##RefSeq-Attributes-END##

FEATURES Location/Qualifiers

source 1..393

/organism="Homo sapiens"

/db_xref="taxon:9606"

/chromosome="17"

/map="17p13.1"

Protein 1..393

/product="cellular tumor antigen p53 isoform a"

/note="cellular tumor antigen p53; phosphoprotein p53;

transformation-related protein 53; p53 tumor suppressor;

antigen NY-CO-13"

/calculated_mol_wt=43522

Region 1..83

/region_name="Interaction with HRMT1L2"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 1..44

/region_name="Transcription activation (acidic)"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 5..29

/region_name="P53_TAD"

/note="P53 transactivation motif; pfam08563"

/db_xref="CDD:149567"

Site 6

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[52]

/db_xref="HPRD:02739"

Site 9

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by HIPK4; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 9

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[29]

/citation=[52]

/db_xref="HPRD:02739"

Site 9

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[29]

/citation=[52]

/db_xref="HPRD:06347"

Site 15

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="dephosphorylation site"

/citation=[13]

/db_xref="HPRD:01146"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by CDK5, PRPK, AMPK, NUAK1 and ATM;

propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[21]

/citation=[27]

/db_xref="HPRD:01496"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[33]

/citation=[35]

/citation=[46]

/citation=[52]

/db_xref="HPRD:02941"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[33]

/citation=[35]

/citation=[46]

/citation=[52]

/db_xref="HPRD:04356"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[12]

/citation=[19]

/citation=[29]

/citation=[33]

/citation=[35]

/citation=[45]

/citation=[46]

/citation=[51]

/citation=[52]

/db_xref="HPRD:06347"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[16]

/citation=[19]

/citation=[33]

/citation=[35]

/citation=[46]

/citation=[52]

/db_xref="HPRD:08369"

Site 15

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[18]

/citation=[45]

Region 17..25

/region_name="TADI"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 18

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="proteolytic cleavage site"

/citation=[28]

/db_xref="HPRD:00253"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphothreonine, by CK1, VRK1 and VRK2; propagated

from UniProtKB/Swiss-Prot (P04637.4)"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[48]

/db_xref="HPRD:02920"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[31]

/citation=[35]

/citation=[41]

/citation=[44]

/db_xref="HPRD:02941"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[31]

/citation=[35]

/citation=[41]

/citation=[44]

/db_xref="HPRD:03701"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[31]

/citation=[33]

/citation=[35]

/citation=[41]

/citation=[44]

/citation=[46]

/db_xref="HPRD:08369"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[31]

/citation=[35]

/citation=[41]

/citation=[44]

/db_xref="HPRD:00277"

Site 18

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[31]

/citation=[35]

/citation=[41]

/citation=[44]

/db_xref="HPRD:00278"

Site 20

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="proteolytic cleavage site"

/citation=[28]

/db_xref="HPRD:00253"

Site 20

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by CHEK2, CK1 and PLK3; propagated

from UniProtKB/Swiss-Prot (P04637.4)"

Site 20

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[33]

/citation=[35]

/citation=[46]

/db_xref="HPRD:02941"

Site 20

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[24]

/citation=[26]

/citation=[33]

/citation=[35]

/citation=[46]

/db_xref="HPRD:04222"

Site 20

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[33]

/citation=[35]

/citation=[46]

/db_xref="HPRD:04356"

Site 20

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[29]

/citation=[33]

/citation=[35]

/citation=[46]

/db_xref="HPRD:06347"

Site 20

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[33]

/citation=[35]

/citation=[46]

/db_xref="HPRD:08369"

Site 23

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="proteolytic cleavage site"

/citation=[55]

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by CDK5 and CDK7; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[35]

/db_xref="HPRD:02941"

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[30]

/citation=[38]

/db_xref="HPRD:05418"

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[35]

/db_xref="HPRD:06347"

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[30]

/citation=[38]

/db_xref="HPRD:00449"

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[14]

/db_xref="HPRD:16016"

Site 33

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[25]

Site 37

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by MAPKAPK5; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 37

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[35]

/citation=[46]

/db_xref="HPRD:02941"

Site 37

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[35]

/citation=[46]

/db_xref="HPRD:04356"

Site 37

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[35]

/citation=[46]

/db_xref="HPRD:06347"

Site 37

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[35]

/citation=[46]

/db_xref="HPRD:08369"

Site 37

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[6]

/db_xref="HPRD:09467"

Region 40

/region_name="alternative start codon"

/note="delta40p53alpha"

Site 46

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by CDK5, DYRK2, HIPK2 and PKC/PRKCG;

propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 46

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[17]

/citation=[29]

/citation=[32]

/db_xref="HPRD:06039"

Site 46

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[29]

/citation=[32]

/db_xref="HPRD:06347"

Region 48..56

/region_name="TADII"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 55

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="dephosphorylation site"

/citation=[7]

Site 55

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphothreonine, by TAF1 and GRK5; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 55

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[20]

/citation=[36]

/db_xref="HPRD:01496"

Region 66..110

/region_name="Interaction with WWOX"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 81

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[37]

/db_xref="HPRD:03100"

Site 81

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[25]

Site 99

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine; propagated from UniProtKB/Swiss-Prot

(P04637.4)"

Site 99

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[5]

Region 100..370

/region_name="Interaction with HIPK1 (By similarity)"

/inference="non-experimental evidence, no additional

details recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 109..288

/region_name="P53"

/note="P53 DNA-binding domain; cd08367"

/db_xref="CDD:176262"

Region 113..236

/region_name="Required for interaction with FBXO42"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 116..292

/region_name="Interaction with AXIN1 (By similarity)"

/inference="non-experimental evidence, no additional

details recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 120

/site_type="other"

/experiment="experimental evidence, no additional details

recorded"

/note="Interaction with DNA; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 155

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[23]

/db_xref="HPRD:00277"

Site order(176,179,238,242)

/site_type="other"

/note="zinc binding site [ion binding]"

/db_xref="CDD:176262"

Site order(177..179,181)

/site_type="other"

/note="dimerization site [polypeptide binding]"

/db_xref="CDD:176262"

Site 183

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by AURKB; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site order(239,241,248,273,275..277,280)

/site_type="DNA binding"

/note="DNA binding site [nucleotide binding]"

/db_xref="CDD:176262"

Region 241..248

/region_name="Interacts with the 53BP2 SH3 domain"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 256..294

/region_name="Interaction with E4F1"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 269

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by AURKB; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Region 273..280

/region_name="Interaction with DNA"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 284

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphothreonine, by AURKB; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 292

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-acetyllysine; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 292

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[22]

/db_xref="HPRD:04078"

Region 300..393

/region_name="Interaction with CARM1"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 305..321

/region_name="Bipartite nuclear localization signal"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 305

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-acetyllysine; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 305

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[22]

/db_xref="HPRD:04078"

Site 313

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine; propagated from UniProtKB/Swiss-Prot

(P04637.4)"

Site 314

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine; propagated from UniProtKB/Swiss-Prot

(P04637.4)"

Site 315

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="dephosphorylation site"

/citation=[47]

/db_xref="HPRD:04614"

Site 315

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="dephosphorylation site"

/citation=[47]

/db_xref="HPRD:04615"

Site 315

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by AURKA, CDK1 and CDK2; propagated

from UniProtKB/Swiss-Prot (P04637.4)"

Site 315

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[30]

/citation=[42]

/db_xref="HPRD:00310"

Site 315

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[30]

/citation=[42]

/db_xref="HPRD:00449"

Site 315

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[14]

/db_xref="HPRD:16016"

Site 315

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[25]

Region 319..360

/region_name="Interaction with HIPK2"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 319..359

/region_name="P53_tetramer"

/note="P53 tetramerisation motif; pfam07710"

/db_xref="CDD:149007"

Site 319

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:04317"

Site 320

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[10]

/citation=[50]

/citation=[53]

/db_xref="HPRD:06780"

Site 320

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:04317"

Site 320

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 321

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:04317"

Site 321

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Region 325..356

/region_name="Oligomerization"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 339..350

/region_name="Nuclear export signal"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 351

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[40]

Site 357

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[40]

Region 359..363

/region_name="Interaction with USP7"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 366

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[57]

Region 368..387

/region_name="Basic (repression of DNA-binding)"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Region 370..372

/region_name="[KR]-[STA]-K motif"

/experiment="experimental evidence, no additional details

recorded"

/note="propagated from UniProtKB/Swiss-Prot (P04637.4)"

Site 370

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[56]

/db_xref="HPRD:04078"

Site 370

/site_type="methylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-methyllysine, by SMYD2, alternate;

N6,N6-dimethyllysine, alternate; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 370

/site_type="methylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[9]

/db_xref="HPRD:15406"

Site 370

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:01272"

Site 370

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 371

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[54]

/db_xref="HPRD:01498"

Site 372

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[56]

/db_xref="HPRD:04078"

Site 372

/site_type="methylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-methyllysine, by SETD7; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 372

/site_type="methylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[9]

/citation=[15]

/db_xref="HPRD:16226"

Site 372

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:01272"

Site 372

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 373

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-acetyllysine, alternate; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 373

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[56]

/db_xref="HPRD:04078"

Site 373

/site_type="methylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6,N6-dimethyllysine, by EHMT1 and EHMT2,

alternate; propagated from UniProtKB/Swiss-Prot

(P04637.4)"

Site 373

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/citation=[39]

/db_xref="HPRD:01272"

Site 373

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="deacetylation site"

/citation=[43]

/db_xref="HPRD:03143"

Site 373

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 378

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[58]

/db_xref="HPRD:01498"

Site 381

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-acetyllysine; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 381

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[56]

/db_xref="HPRD:04078"

Site 381

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:01272"

Site 381

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 382

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-acetyllysine, alternate; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 382

/site_type="acetylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[53]

/db_xref="HPRD:04078"

Site 382

/site_type="methylation"

/experiment="experimental evidence, no additional details

recorded"

/note="N6-methyllysine, by SETD8, alternate;

N6,N6-dimethyllysine, alternate; propagated from

UniProtKB/Swiss-Prot (P04637.4)"

Site 382

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="deacylation site"

/citation=[34]

/db_xref="HPRD:08381"

Site 382

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="deacetylation site"

/citation=[43]

/db_xref="HPRD:03143"

Site 382

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 386

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/citation=[40]

Site 386

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="ubiquitination site"

/citation=[10]

/db_xref="HPRD:01272"

Site 386

/site_type="modified"

/experiment="experimental evidence, no additional details

recorded"

/note="neddylation site"

/citation=[8]

/db_xref="HPRD:06985"

Site 392

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/note="Phosphoserine, by CK2, CDK2 and NUAK1; propagated

from UniProtKB/Swiss-Prot (P04637.4)"

Site 392

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[42]

/citation=[44]

/citation=[49]

/db_xref="HPRD:01468"

Site 392

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[42]

/citation=[44]

/citation=[49]

/citation=[64]

/db_xref="HPRD:02619"

Site 392

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[42]

/citation=[44]

/citation=[49]

/db_xref="HPRD:00277"

Site 392

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[42]

/citation=[44]

/citation=[49]

/db_xref="HPRD:00310"

Site 392

/site_type="phosphorylation"

/experiment="experimental evidence, no additional details

recorded"

/citation=[14]

/db_xref="HPRD:16016"

CDS 1..393

/gene="TP53"

/gene_synonym="BCC7; LFS1; P53; TRP53"

/coded_by="NM_000546.5:203..1384"

/note="isoform a is encoded by transcript variant 1"

/db_xref="CCDS:CCDS11118.1"

/db_xref="GeneID:7157"

/db_xref="HGNC:11998"

/db_xref="MIM:191170"

ORIGIN

1 meepqsdpsv epplsqetfs dlwkllpenn vlsplpsqam ddlmlspddi eqwftedpgp

61 deaprmpeaa ppvapapaap tpaapapaps wplsssvpsq ktyqgsygfr lgflhsgtak

121 svtctyspal nkmfcqlakt cpvqlwvdst pppgtrvram aiykqsqhmt evvrrcphhe

181 rcsdsdglap pqhlirvegn lrveylddrn tfrhsvvvpy eppevgsdct tihynymcns

241 scmggmnrrp iltiitleds sgnllgrnsf evrvcacpgr drrteeenlr kkgephhelp

301 pgstkralpn ntssspqpkk kpldgeyftl qirgrerfem frelnealel kdaqagkepg

361 gsrahsshlk skkgqstsrh kklmfktegp dsd

//}}