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UniProtKB/Swiss-Prot entry O15350


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name P73_HUMAN
Primary accession number O15350
Secondary accession numbers O15351 Q17RN8 Q5TBV5 Q5TBV6 Q8NHW9 Q8TDY5 Q8TDY6 Q9NTK8
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 108)
Name and origin of the protein
Protein name Tumor protein p73
Synonyms p53-like transcription factor
p53-related protein
Gene name
Name: TP73
Synonyms: P73
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=Colon;
DOI=10.1016/S0092-8674(00)80540-1; PubMed=9288759 [NCBI, ExPASy, EBI, Israel, Japan]
Kaghad M., Bonnet H., Yang A., Creancier L., Biscan J.-C., Valent A., Minty A., Chalon P., Lelias J.-M., Dumont X., Ferrara P., McKeon F., Caput D.;
"Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers.";
Cell 90:809-819(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
DOI=10.1006/geno.1998.5387; PubMed=9721206 [NCBI, ExPASy, EBI, Israel, Japan]
Mai M., Huang H., Reed C., Qian C., Smith J.S., Alderete B., Jenkins R., Smith D.I., Liu W.;
"Genomic organization and mutation analysis of p73 in oligodendrogliomas with chromosome 1 p-arm deletions.";
Genomics 51:359-363(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA AND DELTA).
TISSUE=Neuroblastoma;
DOI=10.1084/jem.188.9.1763; PubMed=9802988 [NCBI, ExPASy, EBI, Israel, Japan]
De Laurenzi V., Costanzo A., Barcaroli D., Terrinoni A., Falco M., Annicchiarico-Petruzzelli M., Levrero M., Melino G.;
"Two new p73 splice variants, gamma and delta, with different transcriptional activity.";
J. Exp. Med. 188:1763-1768(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EPSILON AND ZETA).
TISSUE=Hepatoma, Lymphocyte, Mammary cancer, and Skin;
DOI=10.1038/sj.cdd.4400521; PubMed=10381648 [NCBI, ExPASy, EBI, Israel, Japan]
De Laurenzi V., Catani M.V., Terrinoni A., Corazzari M., Melino G., Costanzo A., Levrero M., Knight R.A.;
"Additional complexity in p73: induction by mitogens in lymphoid cells and identification of two new splicing variants epsilon and zeta.";
Cell Death Differ. 6:389-390(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
DOI=10.1038/sj.onc.1202677; PubMed=10362363 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshikawa H., Nagashima M., Khan M.A., McMenamin M.G., Hagiwara K., Harris C.C.;
"Mutational analysis of p73 and p53 in human cancer cell lines.";
Oncogene 18:3415-3421(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DN-ALPHA; DN-BETA AND DN-GAMMA), FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1038/sj.cdd.4400962; PubMed=11753569 [NCBI, ExPASy, EBI, Israel, Japan]
Grob T.J., Novak U., Maisse C., Barcaroli D., Luthi A.U., Pirnia F., Hugli B., Graber H.U., De Laurenzi V., Fey M.F., Melino G., Tobler A.;
"Human DeltaNp73 regulates a dominant negative feedback loop for TAp73 and p53.";
Cell Death Differ. 8:1213-1223(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DN-ALPHA AND DN-BETA).
Nakagawa T., Takahashi M., Ozaki T., Watanabe K., Nakagawara A.;
"Identification of the p73-specific target sequence present in the deltaNp73 proper promoter.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PHOSPHORYLATION (ISOFORMS ALPHA AND BETA).
DOI=10.1038/21704; PubMed=10391251 [NCBI, ExPASy, EBI, Israel, Japan]
Yuan Z.-M., Shioya H., Ishiko T., Sun X., Gu J., Huang Y., Lu H., Kharbanda S., Weichselbaum R., Kufe D.;
"p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage.";
Nature 399:814-817(1999).
[11]
ERRATUM.
Yuan Z.-M., Shioya H., Ishiko T., Sun X., Gu J., Huang Y., Lu H., Kharbanda S., Weichselbaum R., Kufe D.;
Nature 400:792-792(1999).
[12]
FUNCTION.
DOI=10.1093/jnci/91.7.594; PubMed=10203277 [NCBI, ExPASy, EBI, Israel, Japan]
Kaelin W.G. Jr.;
"The emerging p53 gene family.";
J. Natl. Cancer Inst. 91:594-598(1999).
[13]
SUMOYLATION AT LYS-627, AND MUTAGENESIS OF LYS-627.
DOI=10.1074/jbc.M004293200; PubMed=10961991 [NCBI, ExPASy, EBI, Israel, Japan]
Minty A., Dumont X., Kaghad M., Caput D.;
"Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif.";
J. Biol. Chem. 275:36316-36323(2000).
[14]
INTERACTION WITH HIPK2.
DOI=10.1074/jbc.M200153200; PubMed=11925430 [NCBI, ExPASy, EBI, Israel, Japan]
Kim E.-J., Park J.-S., Um S.-J.;
"Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo.";
J. Biol. Chem. 277:32020-32028(2002).
[15]
INTERACTION WITH HECW2.
DOI=10.1016/S0006-291X(03)01347-0; PubMed=12890487 [NCBI, ExPASy, EBI, Israel, Japan]
Miyazaki K., Ozaki T., Kato C., Hanamoto T., Fujita T., Irino S., Watanabe K., Nakagawa T., Nakagawara A.;
"A novel HECT-type E3 ubiquitin ligase, NEDL2, stabilizes p73 and enhances its transcriptional activity.";
Biochem. Biophys. Res. Commun. 308:106-113(2003).
[16]
INTERACTION WITH WWOX, DOMAIN, AND MUTAGENESIS OF TYR-487.
DOI=10.1073/pnas.0400805101; PubMed=15070730 [NCBI, ExPASy, EBI, Israel, Japan]
Aqeilan R.I., Pekarsky Y., Herrero J.J., Palamarchuk A., Letofsky J., Druck T., Trapasso F., Han S.-Y., Melino G., Huebner K., Croce C.M.;
"Functional association between Wwox tumor suppressor protein and p73, a p53 homolog.";
Proc. Natl. Acad. Sci. U.S.A. 101:4401-4406(2004).
[17]
INTERACTION WITH RANBP9, AND SUBCELLULAR LOCATION.
DOI=10.1038/sj.onc.1208257; PubMed=15558019 [NCBI, ExPASy, EBI, Israel, Japan]
Kramer S., Ozaki T., Miyazaki K., Kato C., Hanamoto T., Nakagawara A.;
"Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells.";
Oncogene 24:938-944(2005).
[18]
IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP53.
DOI=10.1074/jbc.M108535200; PubMed=11706030 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuji K., Mizumoto K., Yamochi T., Nishimoto I., Matsuoka M.;
"Differential effect of ik3-1/cables on p53- and p73-induced cell death.";
J. Biol. Chem. 277:2951-2957(2002).
[19]
STRUCTURE BY NMR OF 487-554.
DOI=10.1093/emboj/18.16.4438; PubMed=10449409 [NCBI, ExPASy, EBI, Israel, Japan]
Chi S.W., Ayed A., Arrowsmith C.H.;
"Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain.";
EMBO J. 18:4438-4445(1999).
Comments
  • FUNCTION: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein.
  • COFACTOR: Binds 1 zinc ion per subunit (By similarity).
  • SUBUNIT: Found in a complex with p53/TP53 and CABLES1. The C-terminal oligomerization domain binds to the ABL tyrosine kinase SH3 domain. Interacts with HECW2. Isoform Beta interacts homotypically and with p53/TP53, whereas isoform Alpha does not. Isoform Gamma interacts homotypically and with all p73 isoforms. Isoform Delta interacts with isoform Gamma, isoform Alpha, and homotypically. Isoforms Alpha and Beta interact with HIPK2. Isoform Alpha interacts with RANBP9. Isoform Beta interacts with WWOX.
  • INTERACTION:
    Q9ESJ1:Cables1 (xeno); NbExp=1; IntAct=EBI-389606, EBI-604411;
    P03126:E6 (xeno); NbExp=1; IntAct=EBI-389619, EBI-1177242;
    P03126:E6 (xeno); NbExp=1; IntAct=EBI-389623, EBI-1177242;
    P09429:HMGB1; NbExp=1; IntAct=EBI-389606, EBI-389432;
  • SUBCELLULAR LOCATION: Nucleus. Note=Accumulates in the nucleus in response to DNA damage.
  • ALTERNATIVE PRODUCTS: 9 named isoforms [FASTA] produced by alternative promoter usage and alternative splicing.
    NameAlpha
    Isoform IDO15350-1
    This is the isoform sequence displayed in this entry.
    NameBeta
    Isoform IDO15350-2
    Note: Produced by alternative splicing of isoform Alpha.
    Features which should be applied to build the isoform sequence: VSP_006539.
    NameGamma
    Isoform IDO15350-3
    Note: Produced by alternative splicing of isoform Alpha. The splicing of exon 11 results in a frameshift from the original reading frame.
    Features which should be applied to build the isoform sequence: VSP_006540, VSP_006541.
    NameDelta
    Isoform IDO15350-4
    Note: Produced by alternative splicing of isoform Alpha.
    Features which should be applied to build the isoform sequence: VSP_006542, VSP_006543.
    NameEpsilon
    Isoform IDO15350-5
    Note: Produced by alternative splicing of isoform Alpha. The splicing of exon 11 results in a frameshift from the original reading frame. The splicing of exon 13 reverts the reading frame to the sequence of isoform Alpha.
    Features which should be applied to build the isoform sequence: VSP_006544, VSP_006545.
    NameZeta
    Isoform IDO15350-6
    Note: Produced by alternative splicing of isoform Alpha.
    Features which should be applied to build the isoform sequence: VSP_006546.
    NamedN-Alpha
    Isoform IDO15350-8
    Note: Produced by alternative promoter usage.
    Features which should be applied to build the isoform sequence: VSP_014368.
    NamedN-Beta
    Isoform IDO15350-9
    Note: Produced by alternative splicing of isoform dN-Alpha.
    Features which should be applied to build the isoform sequence: VSP_014368, VSP_006539.
    NamedN-Gamma
    Isoform IDO15350-10
    Note: Produced by alternative splicing of isoform dN-Alpha.
    Features which should be applied to build the isoform sequence: VSP_014368, VSP_006540, VSP_006541.
  • TISSUE SPECIFICITY: Brain, kidney, placenta, colon, heart, liver, spleen, skeletal muscle, prostate, thymus and pancreas. Highly expressed in fetal tissue.
  • INDUCTION: Not induced by DNA damage. Isoforms lacking the transactivation domain block gene induction.
  • DOMAIN: Possesses an acidic transactivation domain, a central DNA binding domain and a C-terminal oligomerization domain that binds to the ABL tyrosine kinase SH3 domain.
  • DOMAIN: The WW-binding motif mediates interaction with WWOX.
  • PTM: Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity.
  • DISEASE: Maps to a chromosome region frequently mutated in diverse cell lines of human cancer. Appears not to be frequently mutated in human cancers, in contrast to p53. Hemizygosity is observed in neuroblastoma and oligodendroglioma.
  • MISCELLANEOUS: Activated and stabilized by interaction with RANBP9.
  • SIMILARITY: Belongs to the p53 family.
  • SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y11416; CAA72220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11416; CAA72221.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11416; CAA72219.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079094; AAD39696.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079082; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079083; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079084; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079085; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079086; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079087; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079088; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079089; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079090; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079091; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079092; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079093; AAD39696.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077628; AAC61887.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077616; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077617; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077618; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077619; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077620; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077621; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077624; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077625; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077626; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF077627; AAC61887.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY040827; AAK81884.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY040828; AAK81885.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY040829; AAK81886.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB055065; BAB87244.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB055066; BAB87245.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136528; CAI19123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136528; CAI19124.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136528; CAI19125.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136528; CAI19126.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136528; CAI19127.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117251; AAI17252.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117253; AAI17254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00006160; -.
IPI00215708; -.
IPI00215709; -.
IPI00215710; -.
IPI00215711; -.
IPI00215712; -.
IPI00607588; -.
IPI00607833; -.
IPI00607886; -.
RefSeq NP_001119712.1; -.
NP_001119713.1; -.
NP_001119714.1; -.
NP_005418.1; -.
UniGene Hs.697294
3D structure databases
PDB
1COK; NMR; -; A=487-554.[ExPASy / RCSB / EBI]
1DXS; X-ray; 2.54 A; A=487-564.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1COK; -.
1DXS; -.
DisProt DP00319; -.
ModBase O15350.
Protein-protein interaction databases
DIP DIP:24202N; -.
IntAct O15350; 6.
PTM databases
PhosphoSite O15350; -.
Organism-specific databases
GeneCards GC01P003592; -.
H-InvDB HIX0028501; -.
HGNC HGNC:12003; TP73.
GenAtlas TP73.
HPA CAB002514; -.
CAB003022; -.
MIM 601990; gene. [NCBI / EBI]
PharmGKB PA36684; -.
Gene expression databases
ArrayExpress O15350; -.
Bgee O15350; -.
GermOnline ENSG00000078900; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from MGI).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006915; Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0008630; Biological process: DNA damage response, signal transduction resulting in induction of apoptosis (traceable author statement from ProtInc).
GO:0006298; Biological process: mismatch repair (traceable author statement from ProtInc).
GO:0045786; Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0030308; Biological process: negative regulation of cell growth (inferred from electronic annotation from InterPro).
GO:0045893; Biological process: positive regulation of transcription, DNA-dependent (inferred from direct assay from MGI).
GO:0002347; Biological process: response to tumor cell (inferred from electronic annotation from InterPro).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011615; p53_DNA_bd.
IPR012346; p53_RUNT_DNA_bd.
IPR010991; p53_tetrameristn.
IPR002117; p53_tumour_Ag.
IPR001660; SAM.
IPR011510; SAM_2.
IPR013761; SAM_type.
IPR015551; Trp53.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.720; p53_RUNT_DNA_bd; 1.
G3DSA:1.10.150.50; SAM_type; 1.
PANTHER PTHR11447; Trp53; 1.
Pfam PF00870; P53; 1.
PF07710; P53_tetramer; 1.
PF07647; SAM_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00386; P53SUPPRESSR.
ProDom PD002681; P53; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00454; SAM; 1.
SMART graphical view of domain structure.
PROSITE PS00348; P53; 1.
PS50105; SAM_DOMAIN; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O15350; -.
Genome annotation databases
Ensembl ENSG00000078900; Homo sapiens. [Contig view]
GeneID 7161; -.
KEGG hsa:7161; -.
Phylogenomic databases
HOVERGEN O15350; -.
OMA O15350; VGQPPPH.
Other
NextBio 28022; -.
PMAP-CutDB O15350; -.
SOURCE TP73; Homo sapiens.
ProtoNet O15350.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Alternative promoter usage; Alternative splicing; Anti-oncogene; Apoptosis; Cell cycle; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Transcription; Transcription regulation; Ubl conjugation; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   636  636     Tumor protein p73. PRO_0000185728
DOMAIN   485   551  67     SAM. 
REGION   1    46  46     Transactivation (By similarity). 
REGION   131   310  180     DNA-binding (Potential). 
REGION   345   386  42     Oligomerization (Potential). 
REGION   345   380  36     Interaction with HIPK2. 
MOTIF   483   487  5     WW-binding. 
COMPBIAS   1    55  55     Asp/Glu-rich (acidic). 
COMPBIAS   168   171  4     Poly-Pro. 
COMPBIAS   391   394  4     Poly-Gln. 
COMPBIAS   483   486  4     Poly-Pro. 
METAL   194   194        Zinc (By similarity). 
METAL   197   197        Zinc (By similarity). 
METAL   258   258        Zinc (By similarity). 
METAL   262   262        Zinc (By similarity). 
MOD_RES   99    99        Phosphotyrosine; by ABL; in isoform Beta. 
CROSSLNK   627   627        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform Alpha. 
VAR_SEQ   1    62        MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNE VVGGTDSSMDVFHLEGMTTSVM -> MLYVGDPARHLAT (in isoform dN-Alpha, isoform dN-Beta and isoform dN-Gamma). VSP_014368
VAR_SEQ   400   495        Missing (in isoform Zeta). VSP_006546
VAR_SEQ   400   476        SHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSS AATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMV -> PRDAQQPWPRSASQQRRDEQQPQRPVHGLGVPLHSATPLP RRPQPRQFFNRIGVSKLHRVFHLPRVTEHLPPAEPDH (in isoform Gamma and isoform dN-Gamma). VSP_006540
VAR_SEQ   400   445        SHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSS AATPNL -> PRDAQQPWPRSASQQRRDEQQPQRPVHGLGVPLHSATPLP RRPQPR (in isoform Epsilon). VSP_006544
VAR_SEQ   400   403        SHLQ -> TWGP (in isoform Delta). VSP_006542
VAR_SEQ   404   636        Missing (in isoform Delta). VSP_006543
VAR_SEQ   446   526        Missing (in isoform Epsilon). VSP_006545
VAR_SEQ   477   636        Missing (in isoform Gamma and isoform dN-Gamma). VSP_006541
VAR_SEQ   495   636        SFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIP EQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGS GELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGF DLPDCKARKQPIKEEFTEAEIH -> RTWGP (in isoform Beta and isoform dN-Beta). VSP_006539
MUTAGEN   487   487        Y->A: Loss of interaction with WWOX. 
MUTAGEN   627   627        K->R: Strongly diminishes sumoylation but does not affect transcriptional activity. 
HELIX   493   499  7      
HELIX   506   510  5      
TURN   511   513  3      
HELIX   517   521  5      
HELIX   525   530  6      
TURN   535   537  3      
HELIX   538   547  10      
Sequence information
Length: 636 AA [This is the length of the unprocessed precursor] Molecular weight: 69623 Da [This is the MW of the unprocessed precursor] CRC64: A467493C5D93EEE0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQSTATSPD GGTTFEHLWS SLEPDSTYFD LPQSSRGNNE VVGGTDSSMD VFHLEGMTTS 

        70         80         90        100        110        120 
VMAQFNLLSS TMDQMSSRAA SASPYTPEHA ASVPTHSPYA QPSSTFDTMS PAPVIPSNTD 

       130        140        150        160        170        180 
YPGPHHFEVT FQQSSTAKSA TWTYSPLLKK LYCQIAKTCP IQIKVSTPPP PGTAIRAMPV 

       190        200        210        220        230        240 
YKKAEHVTDV VKRCPNHELG RDFNEGQSAP ASHLIRVEGN NLSQYVDDPV TGRQSVVVPY 

       250        260        270        280        290        300 
EPPQVGTEFT TILYNFMCNS SCVGGMNRRP ILIIITLEMR DGQVLGRRSF EGRICACPGR 

       310        320        330        340        350        360 
DRKADEDHYR EQQALNESSA KNGAASKRAF KQSPPAVPAL GAGVKKRRHG DEDTYYLQVR 

       370        380        390        400        410        420 
GRENFEILMK LKESLELMEL VPQPLVDSYR QQQQLLQRPS HLQPPSYGPV LSPMNKVHGG 

       430        440        450        460        470        480 
MNKLPSVNQL VGQPPPHSSA ATPNLGPVGP GMLNNHGHAV PANGEMSSSH SAQSMVSGSH 

       490        500        510        520        530        540 
CTPPPPYHAD PSLVSFLTGL GCPNCIEYFT SQGLQSIYHL QNLTIEDLGA LKIPEQYRMT 

       550        560        570        580        590        600 
IWRGLQDLKQ GHDYSTAQQL LRSSNAATIS IGGSGELQRQ RVMEAVHFRV RHTITIPNRG 

       610        620        630 
GPGGGPDEWA DFGFDLPDCK ARKQPIKEEF TEAEIH 

O15350 in FASTA format

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