P73_CHLAE
ID P73_CHLAE Reviewed; 637 AA.
AC Q9XSK8; Q9TSQ9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tumor protein p73;
DE AltName: Full=p53-like transcription factor;
DE AltName: Full=p53-related protein;
GN Name=TP73; Synonyms=P73;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC TISSUE=Kidney;
RA Caput D.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the apoptotic response to DNA damage. May be
CC a tumor suppressor protein (By similarity). Is an activator of FOXJ1
CC expression, essential for the positive regulation of lung ciliated cell
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q9JJP2}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Found in a complex with p53/TP53 and CABLES1. The C-terminal
CC oligomerization domain binds to the ABL1 tyrosine kinase SH3 domain.
CC Interacts with HECW2. Isoforms Alpha and Beta interact with HIPK2.
CC Isoform Alpha interacts with RANBP9. Interacts with WWOX (By
CC similarity). Isoform Beta interacts homotypically and with p53, whereas
CC isoform Alpha does not. Interacts (via SAM domain) with FBXO45 (via
CC B30.2/SPRY domain) (By similarity). Interacts with YAP1 (phosphorylated
CC form). Interacts with HCK (via SH3 domain); this inhibits TP73 activity
CC and degradation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Accumulates in the nucleus in response to DNA damage.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9XSK8-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9XSK8-2; Sequence=VSP_006537;
CC -!- DOMAIN: Possesses an acidic transactivation domain, a central DNA
CC binding domain and a C-terminal oligomerization domain that binds to
CC the ABL1 tyrosine kinase SH3 domain.
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}.
CC -!- PTM: Isoform Alpha (but not isoform Beta) is sumoylated on Lys-628,
CC which potentiates proteasomal degradation but does not affect
CC transcriptional activity. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by
CC the proteasome. {ECO:0000250}.
CC -!- MISCELLANEOUS: Activated and stabilized by interaction with RANBP9.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; Y11419; CAA72224.1; -; mRNA.
DR EMBL; Y11419; CAA72225.1; -; mRNA.
DR AlphaFoldDB; Q9XSK8; -.
DR SMR; Q9XSK8; -.
DR IntAct; Q9XSK8; 1.
DR MINT; Q9XSK8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
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:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR CDD; cd09571; SAM_tumor-p73; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
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; IPR032646; Tp73.
DR InterPro; IPR037612; Tumour-p73_SAM.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR PANTHER; PTHR11447:SF21; PTHR11447:SF21; 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; SSF47719; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Apoptosis; Cell cycle; Cytoplasm;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation;
KW Zinc.
FT CHAIN 1..637
FT /note="Tumor protein p73"
FT /id="PRO_0000185727"
FT DOMAIN 485..551
FT /note="SAM"
FT REGION 1..46
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT REGION 78..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..310
FT /note="DNA-binding"
FT /evidence="ECO:0000255"
FT REGION 301..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..386
FT /note="Oligomerization"
FT /evidence="ECO:0000255"
FT REGION 345..380
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250"
FT MOTIF 483..487
FT /note="PPxY motif"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT MOD_RES 28
FT /note="Phosphotyrosine; by SRC and HCK"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT MOD_RES 99
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); in isoform Alpha"
FT /evidence="ECO:0000250"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT VAR_SEQ 495..637
FT /note="SFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQ
FT DLKQGHDYGAAAQQLLRSSNAAAISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGA
FT GPDEWADFGFDLPDCKARKQPIKEEFTEAEIH -> RTWGP (in isoform
FT Beta)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_006537"
SQ SEQUENCE 637 AA; 69630 MW; 7CB200B919C9C70A CRC64;
MAQSTTTSPD GGTTFEHLWS SLEPDSTYFD LPQSSRGNNE VVGGTDSSMD VFHLEGMTTS
VMAQFNLLSS TMDQMSSRAA SASPYTPEHA ASVPTHSPYA QPSSTFDTMS PAPVIPSNTD
YPGPHHFEVT FQQSSTAKSA TWTYSPLLKK LYCQIAKTCP IQIKVSAPPP PGTAIRAMPV
YKKAEHVTDI VKRCPNHELG RDFNEGQSAP ASHLIRVEGN NLSQYVDDPV TGRQSVVVPY
EPPQVGTEFT TILYNFMCNS SCVGGMNRRP ILIIITLETR DGQVLGRRSF EGRICACPGR
DRKADEDHYR EQQALNESSA KNGAASKRAF KQSPPAVPAL GPGVKKRRHG DEDTYYLQVR
GRENFEILMK LKESLELMEL VPQPLVDSYR QQQQLLQRPS HLQPPSYGPV LSPMNKVHGG
VNKLPSVNQL VGQPPPHSSA ATPNLGPVGS GMLNNHGHAV PANSEMTSSH GTQSMVSGSH
CTPPPPYHAD PSLVSFLTGL GCPNCIEYFT SQGLQSIYHL QNLTIEDLGA LKIPEQYRMT
IWRGLQDLKQ GHDYGAAAQQ LLRSSNAAAI SIGGSGELQR QRVMEAVHFR VRHTITIPNR
GGPGAGPDEW ADFGFDLPDC KARKQPIKEE FTEAEIH
