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Cellular tumor antigen p53

 H2QC53_PANTR            Unreviewed;       393 AA.
H2QC53;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
27-SEP-2017, entry version 48.
RecName: Full=Cellular tumor antigen p53 {ECO:0000256|RuleBase:RU003304};
Name=TP53 {ECO:0000313|EMBL:JAA11113.1,
ECO:0000313|Ensembl:ENSPTRP00000014836};
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000014836, ECO:0000313|Proteomes:UP000002277};
[1] {ECO:0000313|Ensembl:ENSPTRP00000014836, ECO:0000313|Proteomes:UP000002277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16136131; DOI=10.1038/nature04072;
Chimpanzee sequencing and analysis consortium;
"Initial sequence of the chimpanzee genome and comparison with the
human genome.";
Nature 437:69-87(2005).
[2] {ECO:0000313|Proteomes:UP000002277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16136134; DOI=10.1038/nature04101;
Hughes J.F., Skaletsky H., Pyntikova T., Minx P.J., Graves T.,
Rozen S., Wilson R.K., Page D.C.;
"Conservation of Y-linked genes during human evolution revealed by
comparative sequencing in chimpanzee.";
Nature 437:100-103(2005).
[3] {ECO:0000313|Ensembl:ENSPTRP00000014836}
IDENTIFICATION.
Ensembl;
Submitted (FEB-2012) to UniProtKB.
[4] {ECO:0000313|EMBL:JAA11113.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA11113.1},
Skeletal muscle {ECO:0000313|EMBL:JAA44609.1},
Skin {ECO:0000313|EMBL:JAA26397.1}, and
Smooth vascular {ECO:0000313|EMBL:JAA14208.1};
Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
"De novo assembly of the reference chimpanzee transcriptome from
NextGen mRNA sequences.";
Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
-!- 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; AACZ03109503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AACZ03109504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; GABC01000225; JAA11113.1; -; mRNA.
EMBL; GABC01000224; JAA11114.1; -; mRNA.
EMBL; GABC01000223; JAA11115.1; -; mRNA.
EMBL; GABC01000222; JAA11116.1; -; mRNA.
EMBL; GABC01000221; JAA11117.1; -; mRNA.
EMBL; GABF01007937; JAA14208.1; -; mRNA.
EMBL; GABF01007936; JAA14209.1; -; mRNA.
EMBL; GABF01007935; JAA14210.1; -; mRNA.
EMBL; GABF01007934; JAA14211.1; -; mRNA.
EMBL; GABD01006703; JAA26397.1; -; mRNA.
EMBL; GABE01000130; JAA44609.1; -; mRNA.
RefSeq; XP_001172077.2; XM_001172077.4.
SMR; H2QC53; -.
STRING; 9598.ENSPTRP00000014836; -.
Ensembl; ENSPTRT00000016033; ENSPTRP00000014836; ENSPTRG00000008703.
GeneID; 455214; -.
KEGG; ptr:455214; -.
CTD; 7157; -.
eggNOG; ENOG410IITK; Eukaryota.
eggNOG; ENOG410ZSWV; LUCA.
GeneTree; ENSGT00390000015092; -.
KO; K04451; -.
OMA; PATSWPL; -.
OrthoDB; EOG091G0XY5; -.
TreeFam; TF106101; -.
Proteomes; UP000002277; Chromosome 17.
Bgee; ENSPTRG00000008703; -.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0005657; C:replication fork; IBA:GO_Central.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
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:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
GO; GO:0002039; F:p53 binding; IBA:GO_Central.
GO; GO:0002020; F:protease 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:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000990; F:transcription factor activity, core RNA polymerase binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific 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:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IBA:GO_Central.
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:0051974; P:negative regulation of telomerase activity; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
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:0031065; P:positive regulation of histone deacetylation; IBA:GO_Central.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IBA:GO_Central.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; 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:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
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:0090399; P:replicative senescence; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IBA:GO_Central.
GO; GO:0010165; P:response to X-ray; IBA:GO_Central.
GO; GO:0016032; P:viral process; 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.
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.
2: Evidence at transcript level;
Activator {ECO:0000256|RuleBase:RU003304};
Apoptosis {ECO:0000256|RuleBase:RU003304};
Cell cycle {ECO:0000256|RuleBase:RU003304};
Complete proteome {ECO:0000313|Proteomes:UP000002277};
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};
Reference proteome {ECO:0000313|Proteomes:UP000002277};
Transcription {ECO:0000256|RuleBase:RU003304};
Transcription regulation {ECO:0000256|RuleBase:RU003304};
Zinc {ECO:0000256|RuleBase:RU003304}.
DOMAIN 5 29 P53_TAD. {ECO:0000259|Pfam:PF08563}.
DOMAIN 95 288 P53. {ECO:0000259|Pfam:PF00870}.
DOMAIN 319 357 P53_tetramer. {ECO:0000259|Pfam:PF07710}.
SEQUENCE 393 AA; 43653 MW; AD5C149FD8106131 CRC64;
MEEPQSDPSV EPPLSQETFS DLWKLLPENN VLSPLPSQAM DDLMLSPDDI EQWFTEDPGP
DEAPRMPEAA PPVAPAPAAP TPAAPAPAPS WPLSSSVPSQ KTYQGSYGFR LGFLHSGTAK
SVTCTYSPAL NKMFCQLAKT CPVQLWVDST PPPGTRVRAM AIYKQSQHMT EVVRRCPHHE
RCSDSDGLAP PQHLIRVEGN LRVEYLDDRN TFRHSVVVPY EPPEVGSDCT TIHYNYMCNS
SCMGGMNRRP ILTIITLEDS SGNLLGRNSF EVRVCACPGR DRRTEEENLR KKGEPHHELP
PGSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL KDAQAGKEPG
GSRAHSSHLK SKKGQSTSRH KKLMFKTEGP DSD


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