P73_MOUSE
ID P73_MOUSE Reviewed; 631 AA.
AC Q9JJP2; B1AX89; B1AX90; Q3UT91; Q9CU77; Q9JJP1; Q9WUJ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tumor protein p73 {ECO:0000250|UniProtKB:O15350};
DE AltName: Full=p53-like transcription factor {ECO:0000250|UniProtKB:O15350};
DE AltName: Full=p53-related protein {ECO:0000250|UniProtKB:O15350};
GN Name=Tp73;
GN Synonyms=P73 {ECO:0000312|EMBL:CAB81953.1},
GN Trp73 {ECO:0000312|MGI:MGI:1336991};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB81953.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10716451; DOI=10.1038/35003607;
RA Yang A., Walker N., Bronson R., Kaghad M., Oosterwegel M., Bonnin J.,
RA Vagner C., Bonnet H., Dikkes P., Sharpe A., McKeon F., Caput D.;
RT "p73-deficient mice have neurological, pheromonal and inflammatory defects
RT but lack spontaneous tumours.";
RL Nature 404:99-103(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB30732.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 118-631 (ISOFORM 1/2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB30732.1};
RC TISSUE=Egg {ECO:0000312|EMBL:BAE24089.1}, and
RC Head {ECO:0000312|EMBL:BAB30732.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:CAM18775.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH66045.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH66045.1};
RC TISSUE=Fetal brain {ECO:0000312|EMBL:AAH66045.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAD32213.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-631 (ISOFORMS 1/2), AND FUNCTION.
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAD32213.1};
RX PubMed=10232589;
RA Herranz M., Santos J., Salido E., Fernandez-Piqueras J., Serrano M.;
RT "Mouse p73 gene maps to the distal part of chromosome 4 and might be
RT involved in the progression of gamma-radiation-induced T-cell lymphomas.";
RL Cancer Res. 59:2068-2071(1999).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=11932750; DOI=10.1038/416560a;
RA Flores E.R., Tsai K.Y., Crowley D., Sengupta S., Yang A., McKeon F.,
RA Jacks T.;
RT "p63 and p73 are required for p53-dependent apoptosis in response to DNA
RT damage.";
RL Nature 416:560-564(2002).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=15113856; DOI=10.1136/jcp.2003.012559;
RA Oniscu A., Sphyris N., Morris R.G., Bader S., Harrison D.J.;
RT "p73alpha is a candidate effector in the p53 independent apoptosis pathway
RT of cisplatin damaged primary murine colonocytes.";
RL J. Clin. Pathol. 57:492-498(2004).
RN [9]
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=16461361; DOI=10.1083/jcb.200509132;
RA Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y.,
RA Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M.,
RA Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.;
RT "Transcriptional repression induces a slowly progressive atypical neuronal
RT death associated with changes of YAP isoforms and p73.";
RL J. Cell Biol. 172:589-604(2006).
RN [10]
RP FUNCTION.
RX PubMed=26947080; DOI=10.1016/j.celrep.2016.02.035;
RA Marshall C.B., Mays D.J., Beeler J.S., Rosenbluth J.M., Boyd K.L.,
RA Santos Guasch G.L., Shaver T.M., Tang L.J., Liu Q., Shyr Y., Venters B.J.,
RA Magnuson M.A., Pietenpol J.A.;
RT "p73 Is Required for Multiciliogenesis and Regulates the Foxj1-Associated
RT Gene Network.";
RL Cell Rep. 14:2289-2300(2016).
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. Is an activator of FOXJ1 expression, essential for the
CC positive regulation of lung ciliated cell differentiation
CC (PubMed:26947080). {ECO:0000250|UniProtKB:O15350,
CC ECO:0000269|PubMed:10232589, ECO:0000269|PubMed:11932750,
CC ECO:0000269|PubMed:26947080}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O15350};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O15350};
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, HIPK2, RANBP9 and WWOX (By similarity). Interacts
CC (via SAM domain) with FBXO45 (via B30.2/SPRY domain) (By similarity).
CC Interacts with YAP1 (phosphorylated form) (By similarity). Interacts
CC with HCK (via SH3 domain); this inhibits TP73 activity and degradation
CC (By similarity). Interacts (via SAM domain) with NQO1; this interaction
CC is NADH-dependent, stabilizes TP73 in response to oxidative stress and
CC protects it from ubiquitin-independent degradation by the 20S
CC proteasome. {ECO:0000250|UniProtKB:O15350}.
CC -!- INTERACTION:
CC Q9JJP2; P46938: Yap1; NbExp=2; IntAct=EBI-1770138, EBI-1211949;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15113856}. Cytoplasm
CC {ECO:0000250}. Note=Accumulates in the nucleus in response to DNA
CC damage. {ECO:0000269|PubMed:15113856}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:10716451}; Synonyms=Alpha
CC {ECO:0000250|UniProtKB:O15350};
CC IsoId=Q9JJP2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10716451, ECO:0000269|PubMed:15489334};
CC Synonyms=dN-Alpha {ECO:0000250|UniProtKB:O15350};
CC IsoId=Q9JJP2-2; Sequence=VSP_053081;
CC Name=3;
CC IsoId=Q9JJP2-3; Sequence=VSP_053081, VSP_053083, VSP_053084;
CC Name=4 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9JJP2-4; Sequence=VSP_053081, VSP_053082;
CC -!- TISSUE SPECIFICITY: Found in striatal neurons of mutant huntingtin
CC (htt) transgenic mice (at protein level). Isoform 1 is expressed in the
CC nasal epithelium, the vomeronasal organ, the hippocampus and the
CC hypothalamus. {ECO:0000269|PubMed:10716451,
CC ECO:0000269|PubMed:16461361}.
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. {ECO:0000250}.
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX.
CC {ECO:0000250|UniProtKB:O15350}.
CC -!- PTM: Sumoylated on Lys-622, which potentiates proteasomal degradation
CC but does not affect transcriptional activity. {ECO:0000250}.
CC -!- PTM: Phosphorylation by PLK1 and PLK3 inhibits the transcription
CC regulator activity and pro-apoptotic function (By similarity). Higher
CC levels of phosphorylation seen in striatal neurons of. mutant
CC huntingtin (htt) transgenic mice. {ECO:0000250,
CC ECO:0000269|PubMed:16461361}.
CC -!- PTM: Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by
CC the proteasome. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Tp73 display a runting phenotype and
CC high rates of mortality due to massive gastrointestinal hemorrhages or
CC intracranial bleeding. The gastrointestinal tract suffers loss of
CC enterocytes and excessive mucosecretions in the duodenum, ileum and
CC cecum. Survivors exhibit hippocampal dysgenesis, hydrocephalus, chronic
CC infections and inflammation, as well as abnormalities in pheromone
CC sensory pathways. {ECO:0000269|PubMed:10716451}.
CC -!- MISCELLANEOUS: Activated and stabilized by interaction with RANBP9.
CC {ECO:0000250|UniProtKB:O15350}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:10716451, ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 2. {ECO:0000269|PubMed:10716451, ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 2. {ECO:0000269|PubMed:10716451, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000250|UniProtKB:O15350}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM18775.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y19234; CAB81953.1; -; mRNA.
DR EMBL; Y19235; CAB81954.1; -; mRNA.
DR EMBL; AK017412; BAB30732.1; -; mRNA.
DR EMBL; AK139633; BAE24089.1; -; mRNA.
DR EMBL; AL806525; CAM18773.1; -; Genomic_DNA.
DR EMBL; AL806525; CAM18774.1; -; Genomic_DNA.
DR EMBL; AL806525; CAM18775.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH466594; EDL14957.1; -; Genomic_DNA.
DR EMBL; BC066045; AAH66045.1; -; mRNA.
DR EMBL; AF138873; AAD32213.1; -; Genomic_DNA.
DR CCDS; CCDS19009.2; -. [Q9JJP2-1]
DR CCDS; CCDS51396.1; -. [Q9JJP2-4]
DR CCDS; CCDS51397.1; -. [Q9JJP2-2]
DR RefSeq; NP_001119802.1; NM_001126330.1. [Q9JJP2-2]
DR RefSeq; NP_001119803.1; NM_001126331.1. [Q9JJP2-4]
DR RefSeq; NP_035772.2; NM_011642.3. [Q9JJP2-1]
DR AlphaFoldDB; Q9JJP2; -.
DR SMR; Q9JJP2; -.
DR BioGRID; 204326; 5.
DR DIP; DIP-41942N; -.
DR IntAct; Q9JJP2; 5.
DR MINT; Q9JJP2; -.
DR STRING; 10090.ENSMUSP00000101269; -.
DR iPTMnet; Q9JJP2; -.
DR PhosphoSitePlus; Q9JJP2; -.
DR PaxDb; Q9JJP2; -.
DR PRIDE; Q9JJP2; -.
DR Antibodypedia; 3467; 1168 antibodies from 43 providers.
DR DNASU; 22062; -.
DR Ensembl; ENSMUST00000097762; ENSMUSP00000095368; ENSMUSG00000029026. [Q9JJP2-4]
DR Ensembl; ENSMUST00000105643; ENSMUSP00000101268; ENSMUSG00000029026. [Q9JJP2-3]
DR Ensembl; ENSMUST00000105644; ENSMUSP00000101269; ENSMUSG00000029026. [Q9JJP2-1]
DR Ensembl; ENSMUST00000133533; ENSMUSP00000114418; ENSMUSG00000029026. [Q9JJP2-2]
DR GeneID; 22062; -.
DR KEGG; mmu:22062; -.
DR UCSC; uc008wbg.2; mouse. [Q9JJP2-2]
DR UCSC; uc012dqi.1; mouse. [Q9JJP2-4]
DR CTD; 22062; -.
DR MGI; MGI:1336991; Trp73.
DR VEuPathDB; HostDB:ENSMUSG00000029026; -.
DR eggNOG; ENOG502QQ48; Eukaryota.
DR GeneTree; ENSGT00950000183153; -.
DR HOGENOM; CLU_019621_1_1_1; -.
DR InParanoid; Q9JJP2; -.
DR OMA; MKDWRWI; -.
DR OrthoDB; 257530at2759; -.
DR PhylomeDB; Q9JJP2; -.
DR TreeFam; TF106101; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR BioGRID-ORCS; 22062; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Trp73; mouse.
DR PRO; PR:Q9JJP2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JJP2; protein.
DR Bgee; ENSMUSG00000029026; Expressed in telencephalon lateral wall and 63 other tissues.
DR ExpressionAtlas; Q9JJP2; baseline and differential.
DR Genevisible; Q9JJP2; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0033326; P:cerebrospinal fluid secretion; IMP:MGI.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IGI:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0048666; P:neuron development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:MGI.
DR GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IGI:MGI.
DR GO; GO:1901248; P:positive regulation of lung ciliated cell differentiation; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Activator; Alternative promoter usage; Alternative splicing; Apoptosis;
KW Cell cycle; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
FT CHAIN 1..631
FT /note="Tumor protein p73"
FT /id="PRO_0000370211"
FT DOMAIN 479..545
FT /note="SAM"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT REGION 23..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..302
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT REGION 306..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Oligomerization"
FT /evidence="ECO:0000255"
FT REGION 337..372
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT MOTIF 477..481
FT /note="PPxY motif"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT COMPBIAS 88..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT MOD_RES 24
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT MOD_RES 25
FT /note="Phosphotyrosine; by SRC and HCK"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT MOD_RES 91
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15350"
FT VAR_SEQ 1..54
FT /note="MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQ
FT GM -> MLYVGDPMRHLAT (in isoform 2, isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:10716451,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_053081"
FT VAR_SEQ 394..489
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053082"
FT VAR_SEQ 489..493
FT /note="SFLTG -> RTLGL (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053083"
FT VAR_SEQ 494..631
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053084"
FT CONFLICT 118
FT /note="H -> D (in Ref. 2; BAB30732)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="S -> G (in Ref. 2; BAE24089)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="C -> S (in Ref. 5; AAD32213)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..353
FT /note="RG -> SAS (in Ref. 5; AAD32213)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="P -> H (in Ref. 5; AAD32213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 69096 MW; E364D566A90CBF1D CRC64;
MAQTSSSSSS TFEHLWSSLE PDSTYFDLPQ PSQGTSEASG SEESNMDVFH LQGMAQFNLL
SSAMDQMGSR AAPASPYTPE HAASAPTHSP YAQPSSTFDT MSPAPVIPSN TDYPGPHHFE
VTFQQSSTAK SATWTYSPLL KKLYCQIAKT CPIQIKVSTP PPPGTAIRAM PVYKKAEHVT
DIVKRCPNHE LGRDFNEGQS APASHLIRVE GNNLAQYVDD PVTGRQSVVV PYEPPQVGTE
FTTILYNFMC NSSCVGGMNR RPILVIITLE TRDGQVLGRR SFEGRICACP GRDRKADEDH
YREQQALNES TTKNGAASKR AFKQSPPAIP ALGTNVKKRR HGDEDMFYMH VRGRENFEIL
MKVKESLELM ELVPQPLVDS YRQQQQQQLL QRPSHLQPPS YGPVLSPMNK VHGGVNKLPS
VNQLVGQPPP HSSAAGPNLG PMGSGMLNSH GHSMPANGEM NGGHSSQTMV SGSHCTPPPP
YHADPSLVSF LTGLGCPNCI ECFTSQGLQS IYHLQNLTIE DLGALKVPDQ YRMTIWRGLQ
DLKQSHDCGQ QLLRSSSNAA TISIGGSGEL QRQRVMEAVH FRVRHTITIP NRGGAGAVTG
PDEWADFGFD LPDCKSRKQP IKEEFTETES H
