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Cellular tumor antigen p53 (Tumor suppressor p53)

 P53_MOUSE               Reviewed;         387 AA.
P02340; Q9QUP3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 3.
30-AUG-2017, entry version 219.
RecName: Full=Cellular tumor antigen p53;
AltName: Full=Tumor suppressor p53;
Name=Tp53; Synonyms=P53, Trp53;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6092064;
Bienz B., Zakut-Houri R., Givol D., Oren M.;
"Analysis of the gene coding for the murine cellular tumour antigen
p53.";
EMBO J. 3:2179-2183(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6646235; DOI=10.1038/306594a0;
Zakut-Houri R., Oren M., Bienz B., Lavie V., Hazum S., Givol D.;
"A single gene and a pseudogene for the cellular tumour antigen p53.";
Nature 306:594-597(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6379601; DOI=10.1093/nar/12.14.5609;
Jenkins J.R., Rudge K., Redmond S., Wade-Evans A.;
"Cloning and expression analysis of full length mouse cDNA sequences
encoding the transformation associated protein p53.";
Nucleic Acids Res. 12:5609-5626(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (CLONES PCD53; P53-M11 AND P53-M8).
PubMed=3023970; DOI=10.1128/MCB.6.9.3232;
Arai N., Nomura D., Yokota K., Wolf D., Brill E., Shohat O.,
Rotter V.;
"Immunologically distinct p53 molecules generated by alternative
splicing.";
Mol. Cell. Biol. 6:3232-3239(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-132.
PubMed=3329909;
Chumakov P.M.;
"Primary structure of DNA complementary to mRNA of murine oncoprotein
p53.";
Bioorg. Khim. 13:1691-1694(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=SCID;
Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.;
"Cell cycle in DNA-PKcs knock-out mice.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10403253; DOI=10.1038/21913;
Jimenez G.S., Bryntesson F., Torres-Arzayus M.I., Priestley A.,
Beeche M., Saito S., Sakaguchi K., Appella E., Jeggo P.A.,
Taccioli G.E., Wahl G.M., Hubank M.;
"DNA-dependent protein kinase is not required for the p53-dependent
response to DNA damage.";
Nature 400:81-83(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.;
"Characterization of DNA-PKcs null mutant SX9.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ; TISSUE=Lung fibroblast;
Fujimori A., Abe M.;
"p53 in 129-SVJ mice.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-255.
PubMed=1766680;
Burns P.A., Kemp C.J., Gannon J.V., Lane D.P., Bremner R., Balmain A.;
"Loss of heterozygosity and mutational alterations of the p53 gene in
skin tumours of interspecific hybrid mice.";
Oncogene 6:2363-2369(1991).
[12]
DISCOVERY OF P53.
PubMed=221923; DOI=10.1073/pnas.76.5.2420;
DeLeo A.B., Jay G., Appella E., Dubois G.C., Law L.W., Old L.J.;
"Detection of a transformation-related antigen in chemically induced
sarcomas and other transformed cells of the mouse.";
Proc. Natl. Acad. Sci. U.S.A. 76:2420-2424(1979).
[13]
INTERACTION WITH E4F1.
PubMed=10644996; DOI=10.1038/sj.onc.1203250;
Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J.,
Schneider C., Del Sal G.;
"p53 is involved in the p120E4F-mediated growth arrest.";
Oncogene 19:188-199(2000).
[14]
INTERACTION WITH HIPK1, AND PHOSPHORYLATION.
PubMed=12702766; DOI=10.1073/pnas.0530308100;
Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A.,
Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W.,
Mak T.W., Thukral S.K.;
"Characterization of cells and gene-targeted mice deficient for the
p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1).";
Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003).
[15]
INTERACTION WITH AXIN1, AND IDENTIFICATION IN A COMPLEX WITH HIPK2 AND
AXIN1.
PubMed=15526030; DOI=10.1038/sj.emboj.7600475;
Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M.,
Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.;
"Axin stimulates p53 functions by activation of HIPK2 kinase through
multimeric complex formation.";
EMBO J. 23:4583-4594(2004).
[16]
PHOSPHORYLATION AT SER-309 AND SER-386, AND RNA-BINDING.
PubMed=3006031; DOI=10.1073/pnas.83.4.897;
Samad A., Anderson C.W., Carroll R.B.;
"Mapping of phosphomonoester and apparent phosphodiester bonds of the
oncogene product p53 from simian virus 40-transformed 3T3 cells.";
Proc. Natl. Acad. Sci. U.S.A. 83:897-901(1986).
[17]
PHOSPHORYLATION AT SER-386.
PubMed=2145148;
Meek D.W., Simon S., Kikkawa U., Eckhart W.;
"The p53 tumour suppressor protein is phosphorylated at serine 389 by
casein kinase II.";
EMBO J. 9:3253-3260(1990).
[18]
PUTATIVE RNA-BINDING.
PubMed=1406686; DOI=10.1128/MCB.12.11.5145;
Fontoura B.M., Sorokina E.A., David E., Carroll R.B.;
"p53 is covalently linked to 5.8S rRNA.";
Mol. Cell. Biol. 12:5145-5151(1992).
[19]
DEACETYLATION BY SIRT1.
PubMed=11672522; DOI=10.1016/S0092-8674(01)00524-4;
Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A.,
Guarente L., Gu W.;
"Negative control of p53 by Sir2alpha promotes cell survival under
stress.";
Cell 107:137-148(2001).
[20]
INTERACTION WITH USP7.
PubMed=14719112;
Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.;
"Identification and characterization of murine mHAUSP encoding a
deubiquitinating enzyme that regulates the status of p53
ubiquitination.";
Int. J. Oncol. 24:357-364(2004).
[21]
IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP73.
PubMed=11706030; DOI=10.1074/jbc.M108535200;
Tsuji K., Mizumoto K., Yamochi T., Nishimoto I., Matsuoka M.;
"Differential effect of ik3-1/cables on p53- and p73-induced cell
death.";
J. Biol. Chem. 277:2951-2957(2002).
[22]
INTERACTION WITH BANP.
PubMed=12494467; DOI=10.1002/ijc.10881;
Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S.,
Chattopadhyay S.;
"Direct interaction with and activation of p53 by SMAR1 retards cell-
cycle progression at G2/M phase and delays tumor growth in mice.";
Int. J. Cancer 103:606-615(2003).
[23]
PHOSPHORYLATION AT SER-15, LYSINE ACETYLATION, UBIQUITINATION, AND
SUBCELLULAR LOCATION.
PubMed=15195100; DOI=10.1038/ncb1147;
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H.,
Pandolfi P.P.;
"PML regulates p53 stability by sequestering Mdm2 to the nucleolus.";
Nat. Cell Biol. 6:665-672(2004).
[24]
PHOSPHORYLATION AT SER-34.
PubMed=17254968; DOI=10.1016/j.cell.2006.11.050;
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., Han J.;
"PRAK is essential for ras-induced senescence and tumor suppression.";
Cell 128:295-308(2007).
[25]
INTERACTION WITH ZNF385A.
PubMed=17719541; DOI=10.1016/j.cell.2007.06.013;
Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A.,
Lee S.W.;
"Hzf Determines cell survival upon genotoxic stress by modulating p53
transactivation.";
Cell 130:624-637(2007).
[26]
PHOSPHORYLATION AT SER-9.
PubMed=18022393; DOI=10.1016/j.febslet.2007.11.022;
Arai S., Matsushita A., Du K., Yagi K., Okazaki Y., Kurokawa R.;
"Novel homeodomain-interacting protein kinase family member, HIPK4,
phosphorylates human p53 at serine 9.";
FEBS Lett. 581:5649-5657(2007).
[27]
INTERACTION WITH CHD8.
PubMed=19151705; DOI=10.1038/ncb1831;
Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S.,
Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.;
"CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment
during early embryogenesis.";
Nat. Cell Biol. 11:172-182(2009).
[28]
FUNCTION, UBIQUITINATION, AND INTERACTION WITH TRIM24.
PubMed=19556538; DOI=10.1073/pnas.0813177106;
Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J.,
Bergmann A., Johnson R.L., Barton M.C.;
"Trim24 targets endogenous p53 for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009).
[29]
FUNCTION.
PubMed=20673990; DOI=10.1016/j.cell.2010.06.040;
Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J.,
Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M.,
Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.;
"A large intergenic noncoding RNA induced by p53 mediates global gene
repression in the p53 response.";
Cell 142:409-419(2010).
[30]
FUNCTION.
PubMed=22726440; DOI=10.1016/j.cell.2012.05.014;
Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S.,
Moll U.M.;
"p53 opens the mitochondrial permeability transition pore to trigger
necrosis.";
Cell 149:1536-1548(2012).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[32]
FUNCTION, AND INDUCTION.
PubMed=24051492; DOI=10.1038/ncomms3444;
Miki T., Matsumoto T., Zhao Z., Lee C.C.;
"p53 regulates Period2 expression and the circadian clock.";
Nat. Commun. 4:2444-2444(2013).
[33]
UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
PubMed=25732823; DOI=10.1016/j.celrep.2015.01.066;
Qin B., Minter-Dykhouse K., Yu J., Zhang J., Liu T., Zhang H., Lee S.,
Kim J., Wang L., Lou Z.;
"DBC1 functions as a tumor suppressor by regulating p53 stability.";
Cell Rep. 10:1324-1334(2015).
[34]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-281.
PubMed=11152481; DOI=10.1074/jbc.M011644200;
Zhao K., Chai X., Johnston K., Clements A., Marmorstein R.;
"Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A
resolution.";
J. Biol. Chem. 276:12120-12127(2001).
[35]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 92-289.
PubMed=17139084; DOI=10.1107/S090744490603890X;
Ho W.C., Luo C., Zhao K., Chai X., Fitzgerald M.X., Marmorstein R.;
"High-resolution structure of the p53 core domain: implications for
binding small-molecule stabilizing compounds.";
Acta Crystallogr. D 62:1484-1493(2006).
[36]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 92-289 IN COMPLEX WITH DNA
AND ZINC IONS, AND SUBUNIT.
PubMed=16717092; DOI=10.1074/jbc.M603634200;
Ho W.C., Fitzgerald M.X., Marmorstein R.;
"Structure of the p53 core domain dimer bound to DNA.";
J. Biol. Chem. 281:20494-20502(2006).
[37]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-284.
PubMed=17876829; DOI=10.1002/prot.21608;
Kwon E., Kim D.Y., Suh S.W., Kim K.K.;
"Crystal structure of the mouse p53 core domain in zinc-free state.";
Proteins 70:280-283(2008).
[38]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-289 IN COMPLEX WITH DNA,
AND SUBUNIT.
PubMed=18978813; DOI=10.1038/onc.2008.400;
Malecka K.A., Ho W.C., Marmorstein R.;
"Crystal structure of a p53 core tetramer bound to DNA.";
Oncogene 28:325-333(2009).
-!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
growth arrest or apoptosis depending on the physiological
circumstances and cell type. Involved in cell cycle regulation as
a trans-activator that acts to negatively regulate cell division
by controlling a set of genes required for this process. One of
the activated genes is an inhibitor of cyclin-dependent kinases.
Apoptosis induction seems to be mediated either by stimulation of
BAX and FAS antigen expression, or by repression of Bcl-2
expression. In cooperation with mitochondrial PPIF is involved in
activating oxidative stress-induced necrosis; the function is
largely independent of transcription. Prevents CDK7 kinase
activity when associated to CAK complex in response to DNA damage,
thus stopping cell cycle progression (By similarity). Induces the
transcription of long intergenic non-coding RNA p21 (lincRNA-p21)
and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent
transcriptional repression leading to apoptosis, but seems to have
to effect on cell-cycle regulation. Regulates the circadian clock
by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional
activation of PER2 (PubMed:24051492).
{ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:19556538,
ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22726440,
ECO:0000269|PubMed:24051492}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Binds DNA as a homotetramer. Interacts with AXIN1
(PubMed:15526030). Probably part of a complex consisting of TP53,
HIPK2 and AXIN1 (PubMed:15526030). Interacts with histone
acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1,
and recruits them to promoters. Interacts (via C-terminus) with
TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4;
this interaction may be indirect (PubMed:12702766). Found in a
complex with CABLES1 and TP73 (PubMed:11706030). Interacts with
HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. Interacts with
USP7 and SYVN1 (PubMed:14719112). Interacts with HSP90AB1.
Interacts with CHD8; leading to recruit histone H1 and prevent
transactivation activity (PubMed:19151705). Interacts with ARMC10,
BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F
(PubMed:10644996). 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
(PubMed:19556538). Interacts (when monomethylated at Lys-376) with
L3MBTL1. 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 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 (PubMed:17719541).
Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in
p53/TP53 ubiquitination. Interacts with MTA1 and RFWD2. Interacts
with CCAR2 (via N-terminus). Interacts with MORC3. Interacts (via
C-terminus) with POU4F2 (via C-terminus). Interacts (via
oligomerization region) with NOP53; the interaction is direct and
may prevent the MDM2-mediated proteasomal degradation of TP53.
Interacts with AFG1L; mediates mitochondrial translocation of
TP53. Interacts with UBD (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:10644996,
ECO:0000269|PubMed:11706030, ECO:0000269|PubMed:12494467,
ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:14719112,
ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:17719541,
ECO:0000269|PubMed:19151705, ECO:0000269|PubMed:19556538}.
-!- INTERACTION:
P03070:- (xeno); NbExp=12; IntAct=EBI-474016, EBI-617698;
Q07817-1:BCL2L1 (xeno); NbExp=3; IntAct=EBI-474016, EBI-287195;
B2RWS6:Ep300; NbExp=4; IntAct=EBI-474016, EBI-3953360;
P23804:Mdm2; NbExp=5; IntAct=EBI-474016, EBI-641788;
P23804-1:Mdm2; NbExp=2; IntAct=EBI-474016, EBI-3386476;
Q9QUR7:Pin1; NbExp=3; IntAct=EBI-474016, EBI-2432975;
P54099:Polg; NbExp=2; IntAct=EBI-474016, EBI-863636;
Q99KR7:Ppif; NbExp=2; IntAct=EBI-474016, EBI-6455001;
O08586:Pten; NbExp=4; IntAct=EBI-474016, EBI-1186266;
Q61466:Smarcd1; NbExp=4; IntAct=EBI-474016, EBI-371529;
P09671:Sod2; NbExp=2; IntAct=EBI-474016, EBI-1635071;
P62991:Ubc; NbExp=2; IntAct=EBI-474016, EBI-413074;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}.
Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body
{ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix
{ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP
promotes nuclear localization. Recruited into PML bodies together
with CHEK2. Translocates to mitochondria upon oxidative stress.
Translocates to mitochondria in response to mitomycin C treatment
(By similarity). {ECO:0000250|UniProtKB:P04637}.
-!- INDUCTION: Expressed in a circadian manner in the suprachiasmatic
nucleus (SCN) of the brain with a peak seen at ZT8.
{ECO:0000269|PubMed:24051492}.
-!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the
SETD7 methyltransferase. {ECO:0000250}.
-!- PTM: Phosphorylated on Ser-15 upon ultraviolet irradiation; which
is enhanced by interaction with BANP (By similarity).
Phosphorylation on Ser residues mediates transcriptional
activation. Phosphorylation at Ser-9 by HIPK4 increases repression
activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1.
Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which
prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3
in response to reactive oxygen species (ROS), promoting p53/TP53-
mediated apoptosis. Probably phosphorylated on by CDK7 in a CAK
complex in response to DNA damage. Stabilized by CDK5-mediated
phosphorylation in response to genotoxic and oxidative stresses at
Ser-15 leading to accumulation of p53/TP53, particularly in the
nucleus, thus inducing the transactivation of p53/TP53 target
genes (By similarity). Phosphorylated on Ser-386 following UV but
not gamma irradiation. Phosphorylated by HIPK1. {ECO:0000250,
ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:15195100,
ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:18022393,
ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:2145148,
ECO:0000269|PubMed:3006031}.
-!- PTM: Deacetylation by SIRT2 impairs its ability to induce
transcription activation in a AKT-dependent manner (By
similarity). Acetylated. Its deacetylation by SIRT1 impairs its
ability to induce proapoptotic program and modulate cell
senescence. {ECO:0000250}.
-!- PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal
degradation. Ubiquitinated by RFWD3, which works in cooperation
with MDM2 and may catalyze the formation of short polyubiquitin
chains on p53/TP53 that are not targeted to the proteasome.
Ubiquitinated by MKRN1 at Lys-285 and Lys-286, which leads to
proteasomal degradation. Deubiquitinated by USP10, leading to
stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125,
which leads to proteasomal degradation. Ubiquitination by TOPORS
induces degradation. Deubiquitination by USP7, leading to
stabilize it. Ubiquitinated by RFWD2, which leads to proteasomal
degradation (By similarity). Ubiquitination and subsequent
proteasomal degradation is negatively regulated by CCAR2
(PubMed:25732823). {ECO:0000250|UniProtKB:P04637,
ECO:0000269|PubMed:25732823}.
-!- PTM: Monomethylated at Lys-366 by SETD7, leading to stabilization
and increased transcriptional activation. Monomethylated at Lys-
364 by SMYD2, leading to decreased DNA-binding activity and
subsequent transcriptional regulation activity. Lys-366
monomethylation prevents interaction with SMYD2 and subsequent
monomethylation at Lys-364. Dimethylated at Lys-367 EHMT1 and
EHMT2. Monomethylated at Lys-376 KMT5A, promoting interaction with
L3MBTL1 and leading to repress transcriptional activity.
Demethylation of dimethylated Lys-364 by KDM1A prevents
interaction with TP53BP1 and represses TP53-mediated
transcriptional activation (By similarity). {ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-380 by UBC9 (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=p53 is found in increased amounts in a wide variety
of transformed cells. p53 is frequently mutated or inactivated in
many types of cancer.
-!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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EMBL; X00876; CAA25420.1; -; Genomic_DNA.
EMBL; X00877; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00878; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00879; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00880; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00881; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00882; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00883; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00884; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X00885; CAA25420.1; JOINED; Genomic_DNA.
EMBL; X01237; CAA25625.1; -; mRNA.
EMBL; X00741; CAA25323.1; -; mRNA.
EMBL; M13872; AAA39881.1; -; mRNA.
EMBL; M13873; AAA39882.1; -; mRNA.
EMBL; M13874; AAA39883.1; ALT_SEQ; mRNA.
EMBL; AB021961; BAA82344.1; -; mRNA.
EMBL; AF151353; AAD39535.1; -; mRNA.
EMBL; AB017815; BAA82339.1; -; mRNA.
EMBL; AB017816; BAA82340.1; -; mRNA.
EMBL; AB020317; BAA82343.1; -; mRNA.
EMBL; BC005448; AAH05448.1; -; mRNA.
EMBL; S77930; AAB21108.2; -; Genomic_DNA.
PIR; A22739; DNMS53.
PIR; S38824; S38824.
RefSeq; NP_001120705.1; NM_001127233.1.
RefSeq; NP_035770.2; NM_011640.3.
RefSeq; XP_006533220.1; XM_006533157.3.
UniGene; Mm.222; -.
PDB; 1HU8; X-ray; 2.70 A; A/B/C=96-281.
PDB; 2GEQ; X-ray; 2.30 A; A/B=89-289.
PDB; 2IOI; X-ray; 1.55 A; A=89-289.
PDB; 2IOM; X-ray; 2.00 A; A=89-289.
PDB; 2IOO; X-ray; 2.02 A; A=89-289.
PDB; 2P52; X-ray; 1.50 A; A=89-284.
PDB; 3EXJ; X-ray; 2.00 A; A/B=93-289.
PDB; 3EXL; X-ray; 2.20 A; A=93-289.
PDBsum; 1HU8; -.
PDBsum; 2GEQ; -.
PDBsum; 2IOI; -.
PDBsum; 2IOM; -.
PDBsum; 2IOO; -.
PDBsum; 2P52; -.
PDBsum; 3EXJ; -.
PDBsum; 3EXL; -.
ProteinModelPortal; P02340; -.
SMR; P02340; -.
BioGrid; 204323; 90.
DIP; DIP-369N; -.
IntAct; P02340; 38.
MINT; MINT-120104; -.
STRING; 10090.ENSMUSP00000104298; -.
ChEMBL; CHEMBL4164; -.
iPTMnet; P02340; -.
PhosphoSitePlus; P02340; -.
SwissPalm; P02340; -.
EPD; P02340; -.
MaxQB; P02340; -.
PaxDb; P02340; -.
PRIDE; P02340; -.
Ensembl; ENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552.
GeneID; 22059; -.
KEGG; mmu:22059; -.
UCSC; uc007jql.2; mouse.
CTD; 22059; -.
MGI; MGI:98834; Trp53.
eggNOG; ENOG410IITK; Eukaryota.
eggNOG; ENOG410ZSWV; LUCA.
GeneTree; ENSGT00390000015092; -.
HOGENOM; HOG000039957; -.
HOVERGEN; HBG005201; -.
InParanoid; P02340; -.
KO; K04451; -.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
Reactome; R-MMU-2559585; Oncogene Induced Senescence.
Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-6804754; Regulation of TP53 Expression.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
Reactome; R-MMU-69481; G2/M Checkpoints.
Reactome; R-MMU-69541; Stabilization of p53.
Reactome; R-MMU-69895; Transcriptional activation of cell cycle inhibitor p21.
Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
EvolutionaryTrace; P02340; -.
PRO; PR:P02340; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000059552; -.
CleanEx; MM_TRP53; -.
ExpressionAtlas; P02340; baseline and differential.
Genevisible; P02340; MM.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0016605; C:PML body; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005657; C:replication fork; IDA:MGI.
GO; GO:0035861; C:site of double-strand break; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0035033; F:histone deacetylase regulator activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:BHF-UCL.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0043621; F:protein self-association; ISO:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0000990; F:transcription factor activity, core RNA polymerase binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0006914; P:autophagy; ISO:MGI.
GO; GO:0002326; P:B cell lineage commitment; IMP:MGI.
GO; GO:0060411; P:cardiac septum morphogenesis; IGI:MGI.
GO; GO:0007569; P:cell aging; IGI:MGI.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0034613; P:cellular protein localization; ISO:MGI.
GO; GO:0072717; P:cellular response to actinomycin D; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:MGI.
GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
GO; GO:0071479; P:cellular response to ionizing radiation; IDA:CAFA.
GO; GO:0034644; P:cellular response to UV; IDA:CAFA.
GO; GO:0071494; P:cellular response to UV-C; IGI:MGI.
GO; GO:0007417; P:central nervous system development; IGI:MGI.
GO; GO:0021549; P:cerebellum development; IDA:MGI.
GO; GO:0031497; P:chromatin assembly; ISO:MGI.
GO; GO:0051276; P:chromosome organization; IGI:MGI.
GO; GO:0048512; P:circadian behavior; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:BHF-UCL.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:MGI.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IGI:MGI.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:MGI.
GO; GO:0000733; P:DNA strand renaturation; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IMP:MGI.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:MGI.
GO; GO:0048568; P:embryonic organ development; IGI:MGI.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
GO; GO:0006983; P:ER overload response; ISO:MGI.
GO; GO:0007369; P:gastrulation; IGI:MGI.
GO; GO:0007507; P:heart development; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IMP:CAFA.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:CAFA.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:CAFA.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; IMP:MGI.
GO; GO:0043504; P:mitochondrial DNA repair; IMP:MGI.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:MGI.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; ISS:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
GO; GO:0070266; P:necroptotic process; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0008156; P:negative regulation of DNA replication; IDA:MGI.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI.
GO; GO:1904024; P:negative regulation of glucose catabolic process to lactate via pyruvate; IMP:MGI.
GO; GO:1901525; P:negative regulation of macromitophagy; IMP:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IGI:MGI.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IGI:MGI.
GO; GO:0045861; P:negative regulation of proteolysis; IMP:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:MGI.
GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
GO; GO:0090403; P:oxidative stress-induced premature senescence; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:MGI.
GO; GO:0090343; P:positive regulation of cell aging; IMP:BHF-UCL.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:MGI.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; IGI:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0032461; P:positive regulation of protein oligomerization; ISO:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:MGI.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IDA:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006461; P:protein complex assembly; ISO:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0000060; P:protein import into nucleus, translocation; IDA:MGI.
GO; GO:0008104; P:protein localization; ISO:MGI.
GO; GO:0050821; P:protein stabilization; IGI:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:2000772; P:regulation of cellular senescence; IGI:MGI.
GO; GO:2000269; P:regulation of fibroblast apoptotic process; IGI:MGI.
GO; GO:0072363; P:regulation of glycolytic process by positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:1902253; P:regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; IGI:MGI.
GO; GO:0070243; P:regulation of thymocyte apoptotic process; IGI:MGI.
GO; GO:0034103; P:regulation of tissue remodeling; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:MGI.
GO; GO:0090399; P:replicative senescence; ISO:MGI.
GO; GO:0042493; P:response to drug; IDA:MGI.
GO; GO:0010332; P:response to gamma radiation; IDA:MGI.
GO; GO:0002931; P:response to ischemia; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0009651; P:response to salt stress; IGI:MGI.
GO; GO:0009411; P:response to UV; IDA:MGI.
GO; GO:0010165; P:response to X-ray; IDA:MGI.
GO; GO:0009303; P:rRNA transcription; IGI:MGI.
GO; GO:0072331; P:signal transduction by p53 class mediator; ISO:MGI.
GO; GO:0001756; P:somitogenesis; IGI:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IGI:MGI.
GO; GO:0002360; P:T cell lineage commitment; IMP:MGI.
GO; GO:0002309; P:T cell proliferation involved in immune response; IGI:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:MGI.
GO; GO:0016032; P:viral process; ISO:MGI.
CDD; cd08367; P53; 1.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.170.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR010991; p53_tetrameristn.
InterPro; IPR013872; p53_transactivation_domain.
InterPro; IPR002117; p53_tumour_suppressor.
PANTHER; PTHR11447; PTHR11447; 1.
Pfam; PF00870; P53; 1.
Pfam; PF08563; P53_TAD; 1.
Pfam; PF07710; P53_tetramer; 1.
PRINTS; PR00386; P53SUPPRESSR.
SUPFAM; SSF47719; SSF47719; 1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS00348; P53; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Apoptosis; Biological rhythms;
Cell cycle; Complete proteome; Cytoplasm; Disease mutation;
DNA-binding; Endoplasmic reticulum; Isopeptide bond; Metal-binding;
Methylation; Mitochondrion; Necrosis; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
CHAIN 1 387 Cellular tumor antigen p53.
/FTId=PRO_0000185709.
DNA_BIND 96 286 {ECO:0000250}.
REGION 1 314 Interaction with CCAR2.
{ECO:0000250|UniProtKB:P04637}.
REGION 1 42 Transcription activation (acidic).
REGION 60 104 Interaction with WWOX. {ECO:0000250}.
REGION 94 364 Interaction with HIPK1.
{ECO:0000269|PubMed:12702766}.
REGION 94 294 Required for interaction with ZNF385A.
{ECO:0000250}.
REGION 107 230 Required for interaction with FBXO42.
{ECO:0000250}.
REGION 110 286 Interaction with AXIN1.
{ECO:0000269|PubMed:15526030}.
REGION 253 291 Interaction with E4F1. {ECO:0000250}.
REGION 267 274 Interaction with DNA.
REGION 313 354 Interaction with HIPK2. {ECO:0000250}.
REGION 319 350 Oligomerization.
REGION 353 357 Interaction with USP7. {ECO:0000250}.
REGION 362 381 Basic (repression of DNA-binding).
MOTIF 299 315 Bipartite nuclear localization signal.
{ECO:0000250}.
MOTIF 333 344 Nuclear export signal. {ECO:0000250}.
MOTIF 364 366 [KR]-[STA]-K motif.
METAL 170 170 Zinc.
METAL 173 173 Zinc.
METAL 232 232 Zinc.
METAL 236 236 Zinc.
SITE 114 114 Interaction with DNA.
MOD_RES 9 9 Phosphoserine; by HIPK4.
{ECO:0000269|PubMed:18022393}.
MOD_RES 15 15 Phosphoserine; by CDK5, PRPK, AMPK, NUAK1
and ATM. {ECO:0000269|PubMed:15195100}.
MOD_RES 18 18 Phosphothreonine; by CK1, VRK1 and VRK2.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 20 20 Phosphoserine; by CHEK2, CK1 and PLK3.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 34 34 Phosphoserine; by MAPKAPK5.
{ECO:0000269|PubMed:17254968}.
MOD_RES 114 114 N6-acetyllysine; by KAT6A.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 177 177 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 263 263 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 278 278 Phosphothreonine; by AURKB.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 309 309 Phosphoserine; by AURKA, CDK1 and CDK2.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 315 315 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 364 364 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 364 364 N6-methyllysine; by SMYD2; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 366 366 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 367 367 N6,N6-dimethyllysine; by EHMT1 and EHMT2;
alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 367 367 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 375 375 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 376 376 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 376 376 N6-acetyllysine; by KAT6A; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 376 376 N6-methyllysine; by KMT5A; alternate.
{ECO:0000250|UniProtKB:P04637}.
MOD_RES 386 386 Phosphoserine; by CK2, CDK2 and NUAK1.
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 286 286 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P04637}.
CROSSLNK 380 380 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VARIANT 132 132 A -> V (can cooperate with an activated
Ras to transform fibroblasts).
{ECO:0000269|PubMed:3329909}.
VARIANT 165 165 E -> G (in clone P53-M11).
VARIANT 188 188 L -> R.
CONFLICT 45 45 Q -> R (in Ref. 3; CAA25323).
{ECO:0000305}.
CONFLICT 76 78 PVA -> QW (in Ref. 3; CAA25323).
{ECO:0000305}.
HELIX 99 101 {ECO:0000244|PDB:2P52}.
STRAND 104 106 {ECO:0000244|PDB:2P52}.
HELIX 113 116 {ECO:0000244|PDB:3EXJ}.
STRAND 117 121 {ECO:0000244|PDB:2P52}.
TURN 122 125 {ECO:0000244|PDB:2P52}.
STRAND 126 129 {ECO:0000244|PDB:2P52}.
STRAND 134 140 {ECO:0000244|PDB:2P52}.
STRAND 150 159 {ECO:0000244|PDB:2P52}.
TURN 160 164 {ECO:0000244|PDB:2P52}.
HELIX 171 175 {ECO:0000244|PDB:2P52}.
STRAND 181 183 {ECO:0000244|PDB:2P52}.
STRAND 188 193 {ECO:0000244|PDB:2P52}.
STRAND 198 201 {ECO:0000244|PDB:2P52}.
TURN 203 205 {ECO:0000244|PDB:2P52}.
STRAND 208 213 {ECO:0000244|PDB:2P52}.
STRAND 222 230 {ECO:0000244|PDB:2P52}.
HELIX 235 237 {ECO:0000244|PDB:2P52}.
HELIX 239 242 {ECO:0000244|PDB:2P52}.
STRAND 245 252 {ECO:0000244|PDB:2P52}.
STRAND 258 268 {ECO:0000244|PDB:2P52}.
HELIX 272 283 {ECO:0000244|PDB:2P52}.
TURN 285 287 {ECO:0000244|PDB:3EXJ}.
SEQUENCE 387 AA; 43155 MW; B55EB7B463E1DD9D CRC64;
MEESQSDISL ELPLSQETFS GLWKLLPPED ILPSPHCMDD LLLPQDVEEF FEGPSEALRV
SGAPAAQDPV TETPGPVAPA PATPWPLSSF VPSQKTYQGN YGFHLGFLQS GTAKSVMCTY
SPPLNKLFCQ LAKTCPVQLW VSATPPAGSR VRAMAIYKKS QHMTEVVRRC PHHERCSDGD
GLAPPQHLIR VEGNLYPEYL EDRQTFRHSV VVPYEPPEAG SEYTTIHYKY MCNSSCMGGM
NRRPILTIIT LEDSSGNLLG RDSFEVRVCA CPGRDRRTEE ENFRKKEVLC PELPPGSAKR
ALPTCTSASP PQKKKPLDGE YFTLKIRGRK RFEMFRELNE ALELKDAHAT EESGDSRAHS
SYLKTKKGQS TSRHKKTMVK KVGPDSD


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