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Cellular tumor antigen p53

 Q549C9_MOUSE            Unreviewed;       390 AA.
Q549C9;
24-MAY-2005, integrated into UniProtKB/TrEMBL.
24-MAY-2005, sequence version 1.
20-JUN-2018, entry version 133.
RecName: Full=Cellular tumor antigen p53 {ECO:0000256|RuleBase:RU003304};
Name=Trp53 {ECO:0000313|EMBL:ABS81351.1,
ECO:0000313|Ensembl:ENSMUSP00000104298, ECO:0000313|MGI:MGI:98834};
Synonyms=p53 {ECO:0000313|EMBL:AAD44340.1};
ORFNames=mCG_20908 {ECO:0000313|EMBL:EDL10507.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000313|EMBL:AAD44340.1};
[1] {ECO:0000313|EMBL:AAD44340.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Radiosensitive breast carcinoma {ECO:0000313|EMBL:AAD44340.1};
Jiang G.C., Yuan L.Z., Wei K., Guo X.M.;
"Sequence of tumor supressor gene p53 in radiosensitive mouse breast
carcinoma cell line SX-9.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:EDL10507.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Mixed {ECO:0000313|EMBL:EDL10507.1};
PubMed=12040188; DOI=10.1126/science.1069193;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
"A comparison of whole-genome shotgun-derived mouse chromosome 16 and
the human genome.";
Science 296:1661-1671(2002).
[3] {ECO:0000313|EMBL:EDL10507.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Mixed {ECO:0000313|EMBL:EDL10507.1};
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:ABS81351.1}
NUCLEOTIDE SEQUENCE.
STRAIN=FVB/N {ECO:0000313|EMBL:ABS81351.1};
Cullen J.M., Brown D.L., Kissling G.E., Foley J.F., Buzzard J.,
Marion P.L., Parron V.I., French J.E.;
"Aflatoxin B1 and/or HBV induced tumor spectrum in a genetically-
engineered HBV expression and Trp53 mouse model for
hepatocarcinogenesis.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|Ensembl:ENSMUSP00000104298, ECO:0000313|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000104298,
ECO:0000313|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6] {ECO:0000313|Ensembl:ENSMUSP00000104298}
IDENTIFICATION.
STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000104298};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
[7] {ECO:0000213|PubMed:23806337}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
-!- 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. {ECO:0000256|RuleBase:RU003304}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|RuleBase:RU003304};
Note=Binds 1 zinc ion per subunit.
{ECO:0000256|RuleBase:RU003304};
-!- SUBUNIT: Binds DNA as a homotetramer.
{ECO:0000256|RuleBase:RU003304}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}.
Nucleus {ECO:0000256|RuleBase:RU003304}.
-!- SIMILARITY: Belongs to the p53 family.
{ECO:0000256|RuleBase:RU003401}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AL731687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF161020; AAD44340.1; -; mRNA.
EMBL; EU031806; ABS81351.1; -; mRNA.
EMBL; CH466601; EDL10507.1; -; Genomic_DNA.
RefSeq; NP_035770.2; NM_011640.3.
RefSeq; XP_006533220.1; XM_006533157.3.
UniGene; Mm.222; -.
Ensembl; ENSMUST00000108658; ENSMUSP00000104298; ENSMUSG00000059552.
GeneID; 22059; -.
KEGG; mmu:22059; -.
UCSC; uc007jqn.2; mouse.
CTD; 22059; -.
MGI; MGI:98834; Trp53.
eggNOG; ENOG410IITK; Eukaryota.
eggNOG; ENOG410ZSWV; LUCA.
GeneTree; ENSGT00390000015092; -.
HOVERGEN; HBG005201; -.
KO; K04451; -.
OMA; SFMCNSS; -.
OrthoDB; EOG091G0XY5; -.
TreeFam; TF106101; -.
ChiTaRS; Trp53; mouse.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000059552; -.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IEA:Ensembl.
GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
GO; GO:0002039; F:p53 binding; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001094; F:TFIID-class transcription factor binding; IEA:Ensembl.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0000990; F:transcription factor activity, core RNA polymerase binding; IEA:Ensembl.
GO; GO:0001074; F:transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding involved in preinitiation complex assembly; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0006914; P:autophagy; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
GO; GO:0072717; P:cellular response to actinomycin D; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0031497; P:chromatin assembly; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IEA:Ensembl.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
GO; GO:0000733; P:DNA strand renaturation; IEA:Ensembl.
GO; GO:0006983; P:ER overload response; IEA:Ensembl.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0009299; P:mRNA transcription; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0051974; P:negative regulation of telomerase activity; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0006289; P:nucleotide-excision repair; IEA:Ensembl.
GO; GO:0097252; P:oligodendrocyte apoptotic process; IEA:Ensembl.
GO; GO:0090403; P:oxidative stress-induced premature senescence; IEA:Ensembl.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0032461; P:positive regulation of protein oligomerization; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0008104; P:protein localization; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:1903205; P:regulation of hydrogen peroxide-induced cell death; IEA:Ensembl.
GO; GO:0051453; P:regulation of intracellular pH; IEA:Ensembl.
GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
GO; GO:0033552; P:response to vitamin B3; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
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_sf.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR036674; p53_tetramer_sf.
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;
Activator {ECO:0000256|RuleBase:RU003304};
Apoptosis {ECO:0000256|RuleBase:RU003304};
Cell cycle {ECO:0000256|RuleBase:RU003304};
Complete proteome {ECO:0000313|Proteomes:UP000000589};
Cytoplasm {ECO:0000256|RuleBase:RU003304};
DNA-binding {ECO:0000256|RuleBase:RU003304};
Metal-binding {ECO:0000256|RuleBase:RU003304};
Nucleus {ECO:0000256|RuleBase:RU003304};
Phosphoprotein {ECO:0000256|RuleBase:RU003304};
Proteomics identification {ECO:0000213|EPD:Q549C9,
ECO:0000213|MaxQB:Q549C9, ECO:0000213|PeptideAtlas:Q549C9};
Reference proteome {ECO:0000313|Proteomes:UP000000589};
Transcription {ECO:0000256|RuleBase:RU003304};
Transcription regulation {ECO:0000256|RuleBase:RU003304};
Zinc {ECO:0000256|RuleBase:RU003304}.
DOMAIN 8 30 P53_TAD. {ECO:0000259|Pfam:PF08563}.
DOMAIN 93 286 P53. {ECO:0000259|Pfam:PF00870}.
DOMAIN 316 353 P53_tetramer. {ECO:0000259|Pfam:PF07710}.
SEQUENCE 390 AA; 43458 MW; ED5A607378D921D7 CRC64;
MTAMEESQSD ISLELPLSQE TFSGLWKLLP PEDILPSPHC MDDLLLPQDV EEFFEGPSEA
LRVSGAPAAQ DPVTETPGPV APAPATPWPL SSFVPSQKTY QGNYGFHLGF LQSGTAKSVM
CTYSPPLNKL FCQLAKTCPV QLWVSATPPA GSRVRAMAIY KKSQHMTEVV RRCPHHERCS
DGDGLAPPQH LIRVEGNLYP EYLEDRQTFR HSVVVPYEPP EAGSEYTTIH YKYMCNSSCM
GGMNRRPILT IITLEDSSGN LLGRDSFEVR VCACPGRDRR TEEENFRKKE VLCPELPPGS
AKRALPTCTS ASPPQKKKPL DGEYFTLKIR GRKRFEMFRE LNEALELKDA HATEESGDSR
AHSSYLKTKK GQSTSRHKKT MVKKVGPDSD


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