ID G2HEX8_PANTR Unreviewed; 529 AA.
AC G2HEX8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Tumor protein p73 {ECO:0000256|RuleBase:RU003304};
GN Name=TP73 {ECO:0000313|Ensembl:ENSPTRP00000093155.1,
GN ECO:0000313|VGNC:VGNC:57117};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:BAK62286.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000093155.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:BAK62286.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAK62286.1};
RX PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA Kim D.S., Park H.S.;
RT "Major chimpanzee-specific structural changes in sperm development-
RT associated genes.";
RL Funct. Integr. Genomics 11:507-517(2011).
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000093155.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Participates in the apoptotic response to DNA damage.
CC Isoforms containing the transactivation domain are pro-apoptotic,
CC isoforms lacking the domain are anti-apoptotic and block the function
CC of p53 and transactivating p73 isoforms. May be a tumor suppressor
CC protein. {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: Found in a complex with p53/TP53 and CABLES1.
CC {ECO:0000256|RuleBase:RU003304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}.
CC Nucleus {ECO:0000256|RuleBase:RU003304}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167,
CC ECO:0000256|RuleBase:RU003304}.
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DR EMBL; AACZ04059709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK305292; BAK62286.1; -; mRNA.
DR Ensembl; ENSPTRT00000094362.1; ENSPTRP00000093155.1; ENSPTRG00000000062.5.
DR VGNC; VGNC:57117; TP73.
DR GeneTree; ENSGT00950000183153; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000000062; Expressed in cerebellar cortex and 3 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProt.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR CDD; cd09571; SAM_tumor-p73; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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; IPR002117; p53_tumour_suppressor.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037612; Tumour-p73_SAM.
DR PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1.
DR PANTHER; PTHR11447:SF21; TUMOR PROTEIN P73; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF07710; P53_tetramer; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47719; p53 tetramerization domain; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript level;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU003304};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|RuleBase:RU003304};
KW Cell cycle {ECO:0000256|RuleBase:RU003304};
KW Cytoplasm {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}; Nucleus {ECO:0000256|RuleBase:RU003304};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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 378..444
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 194..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ SEQUENCE 529 AA; 58332 MW; E3F86BB154CC6DE5 CRC64;
MVRGVELVSA GVPIPELPVS TFCFAPLPWH PHLQREYSPL LKKLYCQIAK TCPIQIKVST
PPPPGTAIRA MPVYKKAEHV TDVVKRCPNH ELGRDFNEGQ SAPASHLIRV EGNNLSQYVD
DPVTGRQSVV VPYEPPQVGT EFTTILYNFM CNSSCVGGMN RRPILIIITL EMRDGQVLGR
RSFEGRICAC PGRDRKADED HYREQQALNE SSAKNGAASK RAFKQSPPAV PALGAGVKKR
RHGDEDTYYL QVRGRENFEI LMKLKESLEL MELVPQPLVD SYRQQQQLLQ RPSHLQPPSY
GPVLSPMNKV HGGMNKLPSV NQLVGQPPPH SSAATPNLGP VGPGMLNNHG HAVPANGEMG
SSHSAQSMVS GSHCTPPPPY HADPSLVSFL TGLGCPNCIE YFTSQGLQSI YHLQNLTIED
LGALKIPEQY RMTIWRGLQD LKQGHDYSTT QQLLRSSNAA TISIGGSGEL QRQRVMEAVH
FRVRHTITIP NRGGPGGGPD EWADFGFDLP DCKARKQPIK EEFTEAEIH
//
