ETS1_HUMAN
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 03-AUG-2022, entry version 229.
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; 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";
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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 AlphaFoldDB; P14921; -.
DR BMRB; P14921; -.
DR SMR; P14921; -.
DR BioGRID; 108414; 100.
DR CORUM; P14921; -.
DR DIP; DIP-35183N; -.
DR IntAct; P14921; 114.
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 jPOST; 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; 791 antibodies from 42 providers.
DR DNASU; 2113; -.
DR Ensembl; ENST00000319397.6; ENSP00000324578.5; ENSG00000134954.14. [P14921-1]
DR Ensembl; ENST00000392668.8; ENSP00000376436.3; ENSG00000134954.14. [P14921-3]
DR Ensembl; ENST00000526145.6; ENSP00000433500.1; ENSG00000134954.14. [P14921-2]
DR Ensembl; ENST00000531611.5; ENSP00000435666.1; ENSG00000134954.14. [P14921-5]
DR Ensembl; ENST00000535549.5; ENSP00000441430.1; ENSG00000134954.14. [P14921-4]
DR GeneID; 2113; -.
DR KEGG; hsa:2113; -.
DR MANE-Select; ENST00000392668.8; ENSP00000376436.3; NM_001143820.2; NP_001137292.1. [P14921-3]
DR UCSC; uc001qej.3; human. [P14921-1]
DR CTD; 2113; -.
DR DisGeNET; 2113; -.
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 VEuPathDB; HostDB:ENSG00000134954; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000159519; -.
DR HOGENOM; CLU_1229532_0_0_1; -.
DR InParanoid; P14921; -.
DR OMA; ADMECAD; -.
DR OrthoDB; 526256at2759; -.
DR PhylomeDB; P14921; -.
DR TreeFam; TF316214; -.
DR PathwayCommons; P14921; -.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR SignaLink; P14921; -.
DR SIGNOR; P14921; -.
DR BioGRID-ORCS; 2113; 25 hits in 1113 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 visceral pleura and 180 other tissues.
DR ExpressionAtlas; P14921; baseline and differential.
DR Genevisible; P14921; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
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:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ARUK-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IMP:BHF-UCL.
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: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: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 miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
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: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; IPR045688; Ets1_N_flank.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
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 PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF19525; Ets1_N_flank; 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:0007744|PubMed:19608861"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|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:0007744|PubMed:15592455"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007744|PubMed:19690332"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|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:0007829|PDB:1GVJ"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:1GVJ"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3WTS"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:1GVJ"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1GVJ"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:1GVJ"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1GVJ"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:2STT"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1GVJ"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:1GVJ"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:1GVJ"
FT TURN 396..400
FT /evidence="ECO:0007829|PDB:1GVJ"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:1GVJ"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:1GVJ"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:1GVJ"
FT HELIX 426..432
FT /evidence="ECO:0007829|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
