GenomeNet

Database: UniProt
Entry: H0XGB0_OTOGA
LinkDB: H0XGB0_OTOGA
Original site: H0XGB0_OTOGA 
ID   H0XGB0_OTOGA            Unreviewed;       393 AA.
AC   H0XGB0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Cellular tumor antigen p53 {ECO:0000256|ARBA:ARBA00017135, ECO:0000256|RuleBase:RU003304};
GN   Name=TP53 {ECO:0000313|Ensembl:ENSOGAP00000015106.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000015106.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000015106.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
CC       growth arrest or apoptosis depending on the physiological circumstances
CC       and cell type. Involved in cell cycle regulation as a trans-activator
CC       that acts to negatively regulate cell division by controlling a set of
CC       genes required for this process. One of the activated genes is an
CC       inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be
CC       mediated either by stimulation of BAX and FAS antigen expression, or by
CC       repression of Bcl-2 expression. {ECO:0000256|RuleBase:RU003304}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602117-1,
CC         ECO:0000256|RuleBase:RU003304};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR602117-1,
CC       ECO:0000256|RuleBase:RU003304};
CC   -!- SUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU003304}. Nucleus
CC       {ECO:0000256|RuleBase:RU003304}. Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body
CC       {ECO:0000256|ARBA:ARBA00004322}.
CC   -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167,
CC       ECO:0000256|RuleBase:RU003304}.
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DR   EMBL; AAQR03080642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03080643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0XGB0; -.
DR   STRING; 30611.ENSOGAP00000015106; -.
DR   Ensembl; ENSOGAT00000016874.2; ENSOGAP00000015106.2; ENSOGAG00000016871.2.
DR   eggNOG; ENOG502QVY3; Eukaryota.
DR   GeneTree; ENSGT00950000183153; -.
DR   HOGENOM; CLU_019621_0_0_1; -.
DR   InParanoid; H0XGB0; -.
DR   OMA; HKKGEPC; -.
DR   TreeFam; TF106101; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0043073; C:germ cell nucleus; IEA:Ensembl.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR   GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0035033; F:histone deacetylase regulator activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0097371; F:MDM2/MDM4 family protein binding; IEA:Ensembl.
DR   GO; GO:0140677; F:molecular function activator activity; IEA:Ensembl.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0001094; F:TFIID-class transcription factor complex binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0002326; P:B cell lineage commitment; IEA:Ensembl.
DR   GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
DR   GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0060411; P:cardiac septum morphogenesis; IEA:Ensembl.
DR   GO; GO:0072717; P:cellular response to actinomycin D; IEA:Ensembl.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR   GO; GO:0071494; P:cellular response to UV-C; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR   GO; GO:0048512; P:circadian behavior; IEA:Ensembl.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IEA:Ensembl.
DR   GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR   GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR   GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IEA:Ensembl.
DR   GO; GO:0006983; P:ER overload response; IEA:Ensembl.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR   GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0019661; P:glucose catabolic process to lactate via pyruvate; IEA:Ensembl.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; IEA:Ensembl.
DR   GO; GO:0043504; P:mitochondrial DNA repair; IEA:Ensembl.
DR   GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR   GO; GO:0009299; P:mRNA transcription; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0008156; P:negative regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:1903451; P:negative regulation of G1 to G0 transition; IEA:Ensembl.
DR   GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
DR   GO; GO:1904024; P:negative regulation of glucose catabolic process to lactate via pyruvate; IEA:Ensembl.
DR   GO; GO:1903799; P:negative regulation of miRNA processing; IEA:Ensembl.
DR   GO; GO:1901525; P:negative regulation of mitophagy; IEA:Ensembl.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:1905856; P:negative regulation of pentose-phosphate shunt; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:Ensembl.
DR   GO; GO:0097252; P:oligodendrocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0090403; P:oxidative stress-induced premature senescence; IEA:Ensembl.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:2000774; P:positive regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
DR   GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; IEA:Ensembl.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0062100; P:positive regulation of programmed necrotic cell death; IEA:Ensembl.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:Ensembl.
DR   GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IEA:Ensembl.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR   GO; GO:2000269; P:regulation of fibroblast apoptotic process; IEA:Ensembl.
DR   GO; GO:1902253; P:regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR   GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0034103; P:regulation of tissue remodeling; IEA:Ensembl.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
DR   GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0002360; P:T cell lineage commitment; IEA:Ensembl.
DR   GO; GO:0002309; P:T cell proliferation involved in immune response; IEA:Ensembl.
DR   GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0060333; P:type II interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0016032; P:viral process; IEA:Ensembl.
DR   CDD; cd08367; P53; 1.
DR   Gene3D; 2.60.40.720; -; 1.
DR   Gene3D; 6.10.50.20; -; 1.
DR   Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR   InterPro; IPR011615; p53_DNA-bd.
DR   InterPro; IPR036674; p53_tetramer_sf.
DR   InterPro; IPR010991; p53_tetrameristn.
DR   InterPro; IPR013872; p53_transactivation_domain.
DR   InterPro; IPR002117; p53_tumour_suppressor.
DR   PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1.
DR   PANTHER; PTHR11447:SF6; CELLULAR TUMOR ANTIGEN P53; 1.
DR   Pfam; PF00870; P53; 1.
DR   Pfam; PF08563; P53_TAD; 1.
DR   Pfam; PF07710; P53_tetramer; 1.
DR   PRINTS; PR00386; P53SUPPRESSR.
DR   SUPFAM; SSF47719; p53 tetramerization domain; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   PROSITE; PS00348; P53; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU003304};
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|RuleBase:RU003304};
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU003304};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU003304};
KW   DNA-binding {ECO:0000256|RuleBase:RU003304};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602117-1}; Necrosis {ECO:0000256|ARBA:ARBA00022590};
KW   Nucleus {ECO:0000256|RuleBase:RU003304};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|RuleBase:RU003304};
KW   Transcription regulation {ECO:0000256|RuleBase:RU003304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602117-1}.
FT   DOMAIN          6..30
FT                   /note="p53 transactivation"
FT                   /evidence="ECO:0000259|Pfam:PF08563"
FT   DOMAIN          97..288
FT                   /note="p53 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00870"
FT   DOMAIN          319..358
FT                   /note="p53 tetramerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07710"
FT   REGION          281..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ   SEQUENCE   393 AA;  43843 MW;  118C6F5DA967E45D CRC64;
     MEETQSDLTI EPPLSQETFS DLWKLLPENN VLSSSLSPPV DDLMLSPDIV NWFDEGPDEA
     LRTLEDPAPV ASTTAALTPA ASAPVTGWPL SSCVPSQTTY PGSYGFRLGF LNSGTAKSVT
     CTYSPVLNKM FCQLAKTCPV QLWFDSTPPP GSRIRAMAIY KQSQHMTEVV RRCPHHERCS
     ESDGLAPPQH LIRVEGNLRV EYLDDKNTFR HSVVVPYEPP EVGSDCTTIH YNYMCNSSCM
     GGMNRRPILT IITLEDSRLG SGNLLGRNSF EVRVCACPGR DRRTEEENSR KKGETCSEPS
     LGSTKRSLPT STSSSPQPKK KLLEGEYFTL KIRGRERYEM FRELNEALEI KDAQAEKESD
     GNRAHSSQPK SKKEQSTSRH KKLMFKREGP DSD
//
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