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 27-MAR-2024, entry version 238. 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), FUNCTION (ISOFORM ETS-1 RP P27), ALTERNATIVE SPLICING, 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, AND INTERACTION WITH DAXX. 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 (PubMed:10698492, PubMed:11909962). CC Directly controls the expression of cytokine and chemokine genes in a CC wide variety of different cellular contexts (PubMed:20378371). May CC control the differentiation, survival and proliferation of lymphoid CC cells (PubMed:20378371). May also regulate angiogenesis through CC regulation of expression of genes controlling endothelial cell CC migration and invasion (PubMed:15247905, PubMed:15592518). CC {ECO:0000269|PubMed:10698492, ECO:0000269|PubMed:11909962, CC ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518, CC ECO:0000303|PubMed:20378371}. CC -!- FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform CC c-ETS-1A. {ECO:0000269|PubMed:19377509}. CC -!- ACTIVITY REGULATION: Autoinhibited by a module composed of four alpha CC helices (HI-1, HI-2, H4, and H5) that flank the DNA-binding ETS domain, CC reducing the affinity for DNA. Phosphorylation by CaMK2/CaMKII in CC response to calcium signaling decreases affinity for DNA. CC {ECO:0000250|UniProtKB:P27577}. CC -!- SUBUNIT: Binds DNA as a homodimer; homodimerization is required for CC transcription activation (PubMed:18566588). Interacts with MAF and MAFB CC (By similarity). Interacts with PAX5; the interaction alters DNA- CC binding properties (By similarity). Interacts with DAXX CC (PubMed:10698492). Interacts with UBE2I (PubMed:9333025). Interacts CC with SP100; the interaction is direct and modulates ETS1 CC transcriptional activity (PubMed:11909962, PubMed:15247905). CC {ECO:0000250|UniProtKB:P27577, ECO:0000269|PubMed:10698492, CC 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: Nucleus {ECO:0000269|PubMed:11909962, CC ECO:0000269|PubMed:19377509}. Cytoplasm {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|UniProtKB:P27577}. CC -!- PTM: Ubiquitinated; which induces proteasomal degradation. CC {ECO:0000250|UniProtKB:P27577}. CC -!- PTM: Phosphorylation at Ser-251, Ser-282 and Ser-285 by CaMK2/CaMKII in CC response to calcium signaling decreases affinity for DNA: an increasing CC number of phosphoserines causes DNA-binding to become progressively CC weaker. {ECO:0000250|UniProtKB:P27577}. 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="https://atlasgeneticsoncology.org/gene/40502/ETS1"; 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; 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; 102. DR CORUM; P14921; -. DR DIP; DIP-35183N; -. DR IntAct; P14921; 116. DR MINT; P14921; -. DR STRING; 9606.ENSP00000376436; -. DR MoonDB; P14921; Predicted. DR GlyGen; P14921; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000376436; -. DR PeptideAtlas; P14921; -. DR ProteomicsDB; 24875; -. DR ProteomicsDB; 53095; -. [P14921-1] DR ProteomicsDB; 53096; -. [P14921-2] DR ProteomicsDB; 53097; -. [P14921-3] DR ProteomicsDB; 75952; -. DR Pumba; P14921; -. DR Antibodypedia; 3750; 923 antibodies from 42 providers. DR DNASU; 2113; -. DR Ensembl; ENST00000319397.7; 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 AGR; HGNC:3488; -. 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; DPWMTCG; -. DR OrthoDB; 3915960at2759; -. 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; 27 hits in 1191 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 182 other cell types or tissues. DR ExpressionAtlas; P14921; baseline and differential. 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:0003676; F:nucleic acid binding; EXP:DisProt. 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: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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. 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: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; 1.10.150.50; Transcription Factor, Ets-1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; ETS; 1. DR PANTHER; PTHR11849:SF209; PROTEIN C-ETS-1; 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; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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. DR Genevisible; P14921; HS. 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 /evidence="ECO:0000269|PubMed:11909962" FT REGION 304..312 FT /note="Helix HI-1" FT /evidence="ECO:0000250|UniProtKB:P27577" FT REGION 323..330 FT /note="Helix HI-2" FT /evidence="ECO:0000250|UniProtKB:P27577" FT REGION 418..422 FT /note="Helix H4" FT /evidence="ECO:0000250|UniProtKB:P27577" FT REGION 426..432 FT /note="Helix H5" FT /evidence="ECO:0000250|UniProtKB:P27577" 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 //