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Database: UniProt
Entry: P14921
LinkDB: P14921
Original site: P14921 
ID   ETS1_HUMAN              Reviewed;         441 AA.
AC   P14921; A9UL17; F5GYX9; Q14278; Q16080; Q6N087; Q96AC5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   17-JUN-2020, entry version 219.
DE   RecName: Full=Protein C-ets-1;
DE   AltName: Full=p54;
GN   Name=ETS1; Synonyms=EWSR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3060801;
RA   Reddy E.S.P., Rao V.N.;
RT   "Structure, expression and alternative splicing of the human c-ets-1 proto-
RT   oncogene.";
RL   Oncogene Res. 3:239-246(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2847145; DOI=10.1073/pnas.85.21.7862;
RA   Watson D.K., McWilliams M.J., Lapis P., Lautenberger J.A.,
RA   Schweinfest C.W., Papas T.S.;
RT   "Mammalian ets-1 and ets-2 genes encode highly conserved proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7862-7866(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ETS-1 P27), ALTERNATIVE SPLICING,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19377509; DOI=10.1038/onc.2009.72;
RA   Laitem C., Leprivier G., Choul-Li S., Begue A., Monte D., Larsimont D.,
RA   Dumont P., Duterque-Coquillaud M., Aumercier M.;
RT   "Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on the
RT   transcriptional properties and the subcellular localization of Ets-1 p51.";
RL   Oncogene 28:2087-2099(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C-ETS-1A).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Endometrium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Lung;
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   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX   PubMed=1614856; DOI=10.1093/nar/20.11.2699;
RA   Majerus M.-A., Bibollet-Ruche F., Telliez J.-B., Wasylyk B., Bailleul B.;
RT   "Serum, AP-1 and Ets-1 stimulate the human ets-1 promoter.";
RL   Nucleic Acids Res. 20:2699-2703(1992).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 146-174.
RX   PubMed=8231246;
RA   Collyn d'Hooghe M., Galiegue-Zouitina S., Szymiczek D., Lantoine D.,
RA   Quief S., Loucheux-Lefebvre M.H., Kerckaert J.P.;
RT   "Quantitative and qualitative variation of ETS-1 transcripts in hematologic
RT   malignancies.";
RL   Leukemia 7:1777-1785(1993).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-337.
RX   PubMed=2997781; DOI=10.1073/pnas.82.21.7294;
RA   Watson D.K., McWilliams-Smith M.J., Nunn M.F., Duesberg P.H., O'Brien S.J.,
RA   Papas T.S.;
RT   "The ets sequence from the transforming gene of avian erythroblastosis
RT   virus, E26, has unique domains on human chromosomes 11 and 21: both loci
RT   are transcriptionally active.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7294-7298(1985).
RN   [12]
RP   INTERACTION WITH UBE2I.
RX   PubMed=9333025; DOI=10.1038/sj.onc.1201301;
RA   Hahn S.L., Criqui-Filipe P., Wasylyk B.;
RT   "Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-
RT   conjugating enzyme.";
RL   Oncogene 15:1489-1495(1997).
RN   [13]
RP   FUNCTION.
RX   PubMed=10698492; DOI=10.1038/sj.onc.1203385;
RA   Li R., Pei H., Watson D.K., Papas T.S.;
RT   "EAP1/Daxx interacts with ETS1 and represses transcriptional activation of
RT   ETS1 target genes.";
RL   Oncogene 19:745-753(2000).
RN   [14]
RP   FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, INTERACTION WITH SP100,
RP   SUBCELLULAR LOCATION, AND ACTIVATION DOMAIN.
RX   PubMed=11909962; DOI=10.1128/mcb.22.8.2687-2702.2002;
RA   Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.;
RT   "Sp100 interacts with ETS-1 and stimulates its transcriptional activity.";
RL   Mol. Cell. Biol. 22:2687-2702(2002).
RN   [15]
RP   FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, AND INTERACTION WITH SP100.
RX   PubMed=15247905; DOI=10.1038/sj.onc.1207891;
RA   Yordy J.S., Li R., Sementchenko V.I., Pei H., Muise-Helmericks R.C.,
RA   Watson D.K.;
RT   "SP100 expression modulates ETS1 transcriptional activity and inhibits cell
RT   invasion.";
RL   Oncogene 23:6654-6665(2004).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [17]
RP   FUNCTION IN ENDOTHELIAL CELL MIGRATION, AND INDUCTION.
RX   PubMed=15592518; DOI=10.1038/sj.onc.1208245;
RA   Yordy J.S., Moussa O., Pei H., Chaussabel D., Li R., Watson D.K.;
RT   "SP100 inhibits ETS1 activity in primary endothelial cells.";
RL   Oncogene 24:916-931(2005).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-285, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-15 AND LYS-305, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [20]
RP   REVIEW ON FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=20378371; DOI=10.1016/j.cyto.2010.03.006;
RA   Russell L., Garrett-Sinha L.A.;
RT   "Transcription factor Ets-1 in cytokine and chemokine gene regulation.";
RL   Cytokine 51:217-226(2010).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; THR-265 AND SER-267, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [22]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [23]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-15 AND LYS-138, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [24]
RP   STRUCTURE BY NMR OF 320-415.
RX   PubMed=8521493; DOI=10.1016/0092-8674(95)90189-2;
RA   Werner M.H., Clore G.M., Fisher C.L., Fisher R.J., Trinh L., Shiloach J.,
RA   Gronenborn A.M.;
RT   "The solution structure of the human ETS1-DNA complex reveals a novel mode
RT   of binding and true side chain intercalation.";
RL   Cell 83:761-771(1995).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 280-441 IN COMPLEX WITH DNA, AND
RP   SUBUNIT.
RX   PubMed=18566588; DOI=10.1038/emboj.2008.117;
RA   Lamber E.P., Vanhille L., Textor L.C., Kachalova G.S., Sieweke M.H.,
RA   Wilmanns M.;
RT   "Regulation of the transcription factor Ets-1 by DNA-mediated homo-
RT   dimerization.";
RL   EMBO J. 27:2006-2017(2008).
CC   -!- FUNCTION: Transcription factor. Directly controls the expression of
CC       cytokine and chemokine genes in a wide variety of different cellular
CC       contexts. May control the differentiation, survival and proliferation
CC       of lymphoid cells. May also regulate angiogenesis through regulation of
CC       expression of genes controlling endothelial cell migration and
CC       invasion. {ECO:0000269|PubMed:10698492, ECO:0000269|PubMed:11909962,
CC       ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518}.
CC   -!- SUBUNIT: Binds DNA as a homodimer; homodimerization is required for
CC       transcription activation. Interacts with MAF and MAFB. Interacts with
CC       PAX5; the interaction alters DNA-binding properties (By similarity).
CC       Interacts with DAXX. Interacts with UBE2I. Interacts with SP100; the
CC       interaction is direct and modulates ETS1 transcriptional activity.
CC       {ECO:0000250, ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:15247905,
CC       ECO:0000269|PubMed:18566588, ECO:0000269|PubMed:9333025}.
CC   -!- INTERACTION:
CC       P14921; Q06481: APLP2; NbExp=2; IntAct=EBI-913209, EBI-79306;
CC       P14921; Q4LE39: ARID4B; NbExp=2; IntAct=EBI-913209, EBI-2680990;
CC       P14921; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-913209, EBI-2680384;
CC       P14921; O60841: EIF5B; NbExp=2; IntAct=EBI-913209, EBI-928530;
CC       P14921; P14921: ETS1; NbExp=2; IntAct=EBI-913209, EBI-913209;
CC       P14921; P05412: JUN; NbExp=3; IntAct=EBI-913209, EBI-852823;
CC       P14921; P28482: MAPK1; NbExp=3; IntAct=EBI-913209, EBI-959949;
CC       P14921; O00470: MEIS1; NbExp=2; IntAct=EBI-913209, EBI-1210694;
CC       P14921; P78527: PRKDC; NbExp=2; IntAct=EBI-913209, EBI-352053;
CC       P14921; P23497: SP100; NbExp=4; IntAct=EBI-913209, EBI-751145;
CC       P14921; Q05519: SRSF11; NbExp=2; IntAct=EBI-913209, EBI-1051785;
CC       P14921; P17542: TAL1; NbExp=2; IntAct=EBI-913209, EBI-1753878;
CC       P14921; P70338: Gfi1; Xeno; NbExp=2; IntAct=EBI-913209, EBI-3954754;
CC       P14921-1; Q8NHY2: COP1; NbExp=3; IntAct=EBI-913224, EBI-1176214;
CC       P14921-1; Q9UER7-1: DAXX; NbExp=3; IntAct=EBI-913224, EBI-287635;
CC       P14921-1; P12931: SRC; NbExp=2; IntAct=EBI-913224, EBI-621482;
CC       P14921-2; Q9UER7-1: DAXX; NbExp=2; IntAct=EBI-913228, EBI-287635;
CC       P14921-3; Q12778: FOXO1; NbExp=2; IntAct=EBI-21403286, EBI-1108782;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19377509}. Nucleus
CC       {ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:19377509}.
CC       Note=Delocalizes from nucleus to cytoplasm when coexpressed with
CC       isoform Ets-1 p27. {ECO:0000269|PubMed:19377509}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=c-ETS-1A; Synonyms=Ets-1 p51;
CC         IsoId=P14921-1; Sequence=Displayed;
CC       Name=c-ETS-1B; Synonyms=Ets-1 p42;
CC         IsoId=P14921-2; Sequence=VSP_001464;
CC       Name=3;
CC         IsoId=P14921-3; Sequence=VSP_043152;
CC       Name=Ets-1 p27; Synonyms=Ets-1Delta(III-VI);
CC         IsoId=P14921-4; Sequence=VSP_046056;
CC       Name=5;
CC         IsoId=P14921-5; Sequence=VSP_055485, VSP_055486;
CC   -!- TISSUE SPECIFICITY: Highly expressed within lymphoid cells. Isoforms c-
CC       ETS-1A and Ets-1 p27 are both detected in all fetal tissues tested, but
CC       vary with tissue type in adult tissues. None is detected in brain or
CC       kidney. {ECO:0000269|PubMed:19377509, ECO:0000269|PubMed:20378371}.
CC   -!- INDUCTION: Up-regulated by retinoic acid, VEGF, TNF-alpha/TNFA,
CC       lipopolysaccharide and in response to hypoxia (at protein level).
CC       {ECO:0000269|PubMed:15592518}.
CC   -!- PTM: Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which
CC       inhibits transcriptional activity. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated; which induces proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Ets-1 p27]: Acts as a dominant-negative for
CC       isoform c-ETS-1A. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ETS1ID40502ch11q24.html";
DR   EMBL; X14798; CAA32904.1; -; mRNA.
DR   EMBL; X14798; CAA32903.1; -; mRNA.
DR   EMBL; J04101; AAA52410.1; -; mRNA.
DR   EMBL; X65469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S67063; AAB28747.1; -; mRNA.
DR   EMBL; AY943926; AAY19514.1; -; mRNA.
DR   EMBL; BT019452; AAV38259.1; -; mRNA.
DR   EMBL; BX640634; CAE45783.1; -; mRNA.
DR   EMBL; AP001995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP003397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67709.1; -; Genomic_DNA.
DR   EMBL; BC017314; AAH17314.1; -; mRNA.
DR   EMBL; M11921; AAA52409.1; -; Genomic_DNA.
DR   CCDS; CCDS44767.1; -. [P14921-3]
DR   CCDS; CCDS53724.1; -. [P14921-4]
DR   CCDS; CCDS81648.1; -. [P14921-2]
DR   CCDS; CCDS8475.1; -. [P14921-1]
DR   PIR; A32066; TVHUET.
DR   RefSeq; NP_001137292.1; NM_001143820.1. [P14921-3]
DR   RefSeq; NP_001155894.1; NM_001162422.1. [P14921-4]
DR   RefSeq; NP_001317380.1; NM_001330451.1. [P14921-2]
DR   RefSeq; NP_005229.1; NM_005238.3. [P14921-1]
DR   RefSeq; XP_016872803.1; XM_017017314.1. [P14921-3]
DR   PDB; 1GVJ; X-ray; 1.53 A; A/B=297-441.
DR   PDB; 2NNY; X-ray; 2.58 A; A/B=280-441.
DR   PDB; 2STT; NMR; -; A=320-415.
DR   PDB; 2STW; NMR; -; A=320-415.
DR   PDB; 3MFK; X-ray; 3.00 A; A/B=280-441.
DR   PDB; 3RI4; X-ray; 3.00 A; A/D=280-441.
DR   PDB; 3WTS; X-ray; 2.35 A; C/H=276-441.
DR   PDB; 3WTT; X-ray; 2.35 A; C/H=276-441.
DR   PDB; 3WTU; X-ray; 2.70 A; C/H=276-441.
DR   PDB; 3WTV; X-ray; 2.70 A; C/H=276-441.
DR   PDB; 3WTW; X-ray; 2.90 A; C/H=276-441.
DR   PDB; 3WTX; X-ray; 2.80 A; C/H=276-441.
DR   PDB; 3WTY; X-ray; 2.70 A; C/H=276-441.
DR   PDB; 3WTZ; X-ray; 2.61 A; A/B=276-441.
DR   PDB; 3WU0; X-ray; 2.60 A; A/B=276-441.
DR   PDB; 3WU1; X-ray; 2.40 A; B=333-441.
DR   PDB; 4L0Y; X-ray; 2.50 A; B=296-441.
DR   PDB; 4L0Z; X-ray; 2.70 A; B=296-441.
DR   PDB; 4L18; X-ray; 2.30 A; B/F=296-441.
DR   PDB; 4LG0; X-ray; 2.19 A; B=331-440.
DR   PDB; 5ZMC; X-ray; 2.99 A; B=331-441.
DR   PDBsum; 1GVJ; -.
DR   PDBsum; 2NNY; -.
DR   PDBsum; 2STT; -.
DR   PDBsum; 2STW; -.
DR   PDBsum; 3MFK; -.
DR   PDBsum; 3RI4; -.
DR   PDBsum; 3WTS; -.
DR   PDBsum; 3WTT; -.
DR   PDBsum; 3WTU; -.
DR   PDBsum; 3WTV; -.
DR   PDBsum; 3WTW; -.
DR   PDBsum; 3WTX; -.
DR   PDBsum; 3WTY; -.
DR   PDBsum; 3WTZ; -.
DR   PDBsum; 3WU0; -.
DR   PDBsum; 3WU1; -.
DR   PDBsum; 4L0Y; -.
DR   PDBsum; 4L0Z; -.
DR   PDBsum; 4L18; -.
DR   PDBsum; 4LG0; -.
DR   PDBsum; 5ZMC; -.
DR   SMR; P14921; -.
DR   BioGRID; 108414; 55.
DR   CORUM; P14921; -.
DR   DIP; DIP-35183N; -.
DR   IntAct; P14921; 74.
DR   MINT; P14921; -.
DR   STRING; 9606.ENSP00000376436; -.
DR   MoonDB; P14921; Predicted.
DR   iPTMnet; P14921; -.
DR   PhosphoSitePlus; P14921; -.
DR   BioMuta; ETS1; -.
DR   DMDM; 119641; -.
DR   CPTAC; CPTAC-1206; -.
DR   EPD; P14921; -.
DR   MassIVE; P14921; -.
DR   MaxQB; P14921; -.
DR   PaxDb; P14921; -.
DR   PeptideAtlas; P14921; -.
DR   PRIDE; P14921; -.
DR   ProteomicsDB; 24875; -.
DR   ProteomicsDB; 53095; -. [P14921-1]
DR   ProteomicsDB; 53096; -. [P14921-2]
DR   ProteomicsDB; 53097; -. [P14921-3]
DR   ProteomicsDB; 75952; -.
DR   Antibodypedia; 3750; 716 antibodies.
DR   DNASU; 2113; -.
DR   Ensembl; ENST00000319397; ENSP00000324578; ENSG00000134954. [P14921-1]
DR   Ensembl; ENST00000392668; ENSP00000376436; ENSG00000134954. [P14921-3]
DR   Ensembl; ENST00000526145; ENSP00000433500; ENSG00000134954. [P14921-2]
DR   Ensembl; ENST00000531611; ENSP00000435666; ENSG00000134954. [P14921-5]
DR   Ensembl; ENST00000535549; ENSP00000441430; ENSG00000134954. [P14921-4]
DR   GeneID; 2113; -.
DR   KEGG; hsa:2113; -.
DR   UCSC; uc001qej.3; human. [P14921-1]
DR   CTD; 2113; -.
DR   DisGeNET; 2113; -.
DR   EuPathDB; HostDB:ENSG00000134954.14; -.
DR   GeneCards; ETS1; -.
DR   HGNC; HGNC:3488; ETS1.
DR   HPA; ENSG00000134954; Tissue enhanced (lymphoid).
DR   MalaCards; ETS1; -.
DR   MIM; 164720; gene.
DR   neXtProt; NX_P14921; -.
DR   OpenTargets; ENSG00000134954; -.
DR   Orphanet; 536; Systemic lupus erythematosus.
DR   PharmGKB; PA27902; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   eggNOG; ENOG410Z0ZF; LUCA.
DR   GeneTree; ENSGT00940000159519; -.
DR   HOGENOM; CLU_1229532_0_0_1; -.
DR   InParanoid; P14921; -.
DR   KO; K02678; -.
DR   OMA; SFESCER; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; P14921; -.
DR   TreeFam; TF316214; -.
DR   Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR   SignaLink; P14921; -.
DR   SIGNOR; P14921; -.
DR   BioGRID-ORCS; 2113; 3 hits in 817 CRISPR screens.
DR   ChiTaRS; ETS1; human.
DR   EvolutionaryTrace; P14921; -.
DR   GeneWiki; ETS1; -.
DR   GenomeRNAi; 2113; -.
DR   Pharos; P14921; Tbio.
DR   PRO; PR:P14921; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P14921; protein.
DR   Bgee; ENSG00000134954; Expressed in blood and 207 other tissues.
DR   ExpressionAtlas; P14921; baseline and differential.
DR   Genevisible; P14921; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0008134; F:transcription factor binding; NAS:UniProtKB.
DR   GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; IMP:BHF-UCL.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR   GO; GO:0030578; P:PML body organization; IDA:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0051272; P:positive regulation of cellular component movement; IMP:BHF-UCL.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:BHF-UCL.
DR   GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR   GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0010715; P:regulation of extracellular matrix disassembly; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   CDD; cd08542; SAM_PNT-ETS-1; 1.
DR   DisProt; DP01441; -.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   IDEAL; IID00025; -.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041886; SAM_PNT-ETS-1.
DR   InterPro; IPR016311; Transform_prot_C-ets.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PIRSF; PIRSF001698; Transforming_factor_C-ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
KW   Immunity; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..441
FT                   /note="Protein C-ets-1"
FT                   /id="PRO_0000204069"
FT   DOMAIN          51..136
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        335..415
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          130..243
FT                   /note="Activation domain; required for transcription
FT                   activation"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         38
FT                   /note="Phosphothreonine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:P27577"
FT   MOD_RES         223
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:15592455"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P27577"
FT   MOD_RES         265
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P27577"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         305
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   CROSSLNK        8
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        15
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000244|PubMed:25755297,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        138
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        227
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..27
FT                   /note="MKAAVDLKPTLTIIKTEKVDLELFPSP -> MSYFVDSAGSSPVPYSAPRPA
FT                   VVRQGPSNTYEDPRMNCGFQSNYHQQRPCYPFWDEMATQEVPTGLEHCVS (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_043152"
FT   VAR_SEQ         28..243
FT                   /note="Missing (in isoform Ets-1 p27)"
FT                   /evidence="ECO:0000303|PubMed:19377509"
FT                   /id="VSP_046056"
FT   VAR_SEQ         244..330
FT                   /note="Missing (in isoform c-ETS-1B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001464"
FT   VAR_SEQ         262..272
FT                   /note="DRLTQSWSSQS -> GQEMGKEEKQT (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055485"
FT   VAR_SEQ         273..441
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055486"
FT   CONFLICT        162
FT                   /note="Y -> C (in Ref. 10; AAB28747)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236..243
FT                   /note="MCMGRTSR -> FLPPPLPP (in Ref. 11; AAA52409)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="I -> V (in Ref. 3; AAY19514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332..337
FT                   /note="SGPIQL -> RRPPAA (in Ref. 11; AAA52409)"
FT                   /evidence="ECO:0000305"
FT   HELIX           304..313
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   HELIX           323..330
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   STRAND          331..334
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   HELIX           337..345
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   HELIX           348..350
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   TURN            351..353
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   STRAND          354..356
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   STRAND          358..361
FT                   /evidence="ECO:0000244|PDB:2STT"
FT   STRAND          362..364
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   HELIX           368..379
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   HELIX           386..395
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   TURN            396..400
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   STRAND          401..404
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   STRAND          408..414
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   HELIX           418..422
FT                   /evidence="ECO:0000244|PDB:1GVJ"
FT   HELIX           426..432
FT                   /evidence="ECO:0000244|PDB:1GVJ"
SQ   SEQUENCE   441 AA;  50408 MW;  3B66BCC464B393FB CRC64;
     MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ
     QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM NGAALCALGK DCFLELAPDF
     VGDILWEHLE ILQKEDVKPY QVNGVNPAYP ESRYTSDYFI SYGIEHAQCV PPSEFSEPSF
     ITESYQTLHP ISSEELLSLK YENDYPSVIL RDPLQTDTLQ NDYFAIKQEV VTPDNMCMGR
     TSRGKLGGQD SFESIESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDSED YPAALPNHKP
     KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG
     WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS
     LLGYTPEELH AMLDVKPDAD E
//
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