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Database: UniProt
Entry: ETS1_HUMAN
LinkDB: ETS1_HUMAN
Original site: 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   16-OCT-2019, entry version 214.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   proto-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.,
RA   Larsimont D., Dumont P., Duterque-Coquillaud M., Aumercier M.;
RT   "Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on
RT   the transcriptional properties and the subcellular localization of
RT   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
RT   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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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.,
RA   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
RT   hematologic 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.,
RA   O'Brien S.J., 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
RT   loci 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
RT   activation of 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
RT   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
RT   cell invasion.";
RL   Oncogene 23:6654-6665(2004).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND IDENTIFICATION
RP   BY 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
RT   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.,
RA   Walther T.C., 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
RT   regulation.";
RL   Cytokine 51:217-226(2010).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; THR-265 AND
RP   SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RP   MASS 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and 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-
RT   modification 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.,
RA   Shiloach J., Gronenborn A.M.;
RT   "The solution structure of the human ETS1-DNA complex reveals a novel
RT   mode 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,
RP   AND 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
CC       of cytokine and chemokine genes in a wide variety of different
CC       cellular contexts. May control the differentiation, survival and
CC       proliferation of lymphoid cells. May also regulate angiogenesis
CC       through regulation of expression of genes controlling endothelial
CC       cell migration and invasion. {ECO:0000269|PubMed:10698492,
CC       ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:15247905,
CC       ECO:0000269|PubMed:15592518}.
CC   -!- SUBUNIT: Binds DNA as a homodimer; homodimerization is required
CC       for transcription activation. Interacts with MAF and MAFB.
CC       Interacts with PAX5; the interaction alters DNA-binding properties
CC       (By similarity). Interacts with DAXX. Interacts with UBE2I.
CC       Interacts with SP100; the interaction is direct and modulates ETS1
CC       transcriptional activity. {ECO:0000250,
CC       ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:15247905,
CC       ECO:0000269|PubMed:18566588, ECO:0000269|PubMed:9333025}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-913209, EBI-913209;
CC       Q06481:APLP2; NbExp=2; IntAct=EBI-913209, EBI-79306;
CC       Q4LE39:ARID4B; NbExp=2; IntAct=EBI-913209, EBI-2680990;
CC       Q8NHY2:COP1; NbExp=3; IntAct=EBI-913224, EBI-1176214;
CC       Q9BQA9:CYBC1; NbExp=3; IntAct=EBI-913209, EBI-2680384;
CC       Q9UER7-1:DAXX; NbExp=3; IntAct=EBI-913224, EBI-287635;
CC       O60841:EIF5B; NbExp=2; IntAct=EBI-913209, EBI-928530;
CC       P70338:Gfi1 (xeno); NbExp=2; IntAct=EBI-913209, EBI-3954754;
CC       P05412:JUN; NbExp=3; IntAct=EBI-913209, EBI-852823;
CC       P28482:MAPK1; NbExp=3; IntAct=EBI-913209, EBI-959949;
CC       O00470:MEIS1; NbExp=2; IntAct=EBI-913209, EBI-1210694;
CC       P78527:PRKDC; NbExp=2; IntAct=EBI-913209, EBI-352053;
CC       P23497:SP100; NbExp=4; IntAct=EBI-913209, EBI-751145;
CC       P12931:SRC; NbExp=2; IntAct=EBI-913224, EBI-621482;
CC       Q05519:SRSF11; NbExp=2; IntAct=EBI-913209, EBI-1051785;
CC       P17542:TAL1; NbExp=2; IntAct=EBI-913209, EBI-1753878;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19377509}.
CC       Nucleus {ECO:0000269|PubMed:11909962,
CC       ECO:0000269|PubMed:19377509}. Note=Delocalizes from nucleus to
CC       cytoplasm when coexpressed with isoform Ets-1 p27.
CC       {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         Note=No experimental confirmation available.;
CC       Name=Ets-1 p27; Synonyms=Ets-1Delta(III-VI);
CC         IsoId=P14921-4; Sequence=VSP_046056;
CC         Note=Acts as a dominant-negative for isoform c-ETS-1A.;
CC       Name=5;
CC         IsoId=P14921-5; Sequence=VSP_055485, VSP_055486;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed within lymphoid cells.
CC       Isoforms c-ETS-1A and Ets-1 p27 are both detected in all fetal
CC       tissues tested, but vary with tissue type in adult tissues. None
CC       is detected in brain or kidney. {ECO:0000269|PubMed:19377509,
CC       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;
CC       which inhibits transcriptional activity. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated; which induces proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and 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; 53.
DR   CORUM; P14921; -.
DR   DIP; DIP-35183N; -.
DR   IntAct; P14921; 73.
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   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   GeneCards; ETS1; -.
DR   HGNC; HGNC:3488; ETS1.
DR   HPA; CAB002575; -.
DR   HPA; HPA063230; -.
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; HOG000285953; -.
DR   InParanoid; P14921; -.
DR   KO; K02678; -.
DR   OMA; TDMECAD; -.
DR   OrthoDB; 570797at2759; -.
DR   PhylomeDB; P14921; -.
DR   TreeFam; TF316214; -.
DR   Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR   SignaLink; P14921; -.
DR   SIGNOR; P14921; -.
DR   ChiTaRS; ETS1; human.
DR   EvolutionaryTrace; P14921; -.
DR   GeneWiki; ETS1; -.
DR   GenomeRNAi; 2113; -.
DR   Pharos; P14921; -.
DR   PRO; PR:P14921; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000134954; Expressed in 208 organ(s), highest expression level in blood.
DR   ExpressionAtlas; P14921; baseline and differential.
DR   Genevisible; P14921; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IC: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 proximal promoter 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: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:0061614; P:pri-miRNA 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: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   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
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; Complete proteome;
KW   Cytoplasm; DNA-binding; Immunity; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    441       Protein C-ets-1.
FT                                /FTId=PRO_0000204069.
FT   DOMAIN       51    136       PNT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00762}.
FT   DNA_BIND    335    415       ETS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00237}.
FT   REGION      130    243       Activation domain; required for
FT                                transcription activation.
FT   MOD_RES       8      8       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES      15     15       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES      38     38       Phosphothreonine; by MAPK.
FT                                {ECO:0000250|UniProtKB:P27577}.
FT   MOD_RES     223    223       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:15592455}.
FT   MOD_RES     251    251       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     254    254       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P27577}.
FT   MOD_RES     265    265       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     267    267       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     270    270       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     282    282       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P27577}.
FT   MOD_RES     285    285       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     305    305       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   CROSSLNK      8      8       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK     15     15       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    138    138       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    227    227       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ       1     27       MKAAVDLKPTLTIIKTEKVDLELFPSP -> MSYFVDSAGS
FT                                SPVPYSAPRPAVVRQGPSNTYEDPRMNCGFQSNYHQQRPCY
FT                                PFWDEMATQEVPTGLEHCVS (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_043152.
FT   VAR_SEQ      28    243       Missing (in isoform Ets-1 p27).
FT                                {ECO:0000303|PubMed:19377509}.
FT                                /FTId=VSP_046056.
FT   VAR_SEQ     244    330       Missing (in isoform c-ETS-1B).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_001464.
FT   VAR_SEQ     262    272       DRLTQSWSSQS -> GQEMGKEEKQT (in isoform
FT                                5). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_055485.
FT   VAR_SEQ     273    441       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_055486.
FT   CONFLICT    162    162       Y -> C (in Ref. 10; AAB28747).
FT                                {ECO:0000305}.
FT   CONFLICT    236    243       MCMGRTSR -> FLPPPLPP (in Ref. 11;
FT                                AAA52409). {ECO:0000305}.
FT   CONFLICT    255    255       I -> V (in Ref. 3; AAY19514).
FT                                {ECO:0000305}.
FT   CONFLICT    332    337       SGPIQL -> RRPPAA (in Ref. 11; AAA52409).
FT                                {ECO:0000305}.
FT   HELIX       304    313       {ECO:0000244|PDB:1GVJ}.
FT   HELIX       323    330       {ECO:0000244|PDB:1GVJ}.
FT   STRAND      331    334       {ECO:0000244|PDB:3WTS}.
FT   HELIX       337    345       {ECO:0000244|PDB:1GVJ}.
FT   HELIX       348    350       {ECO:0000244|PDB:1GVJ}.
FT   TURN        351    353       {ECO:0000244|PDB:1GVJ}.
FT   STRAND      354    356       {ECO:0000244|PDB:1GVJ}.
FT   STRAND      358    361       {ECO:0000244|PDB:2STT}.
FT   STRAND      362    364       {ECO:0000244|PDB:1GVJ}.
FT   HELIX       368    379       {ECO:0000244|PDB:1GVJ}.
FT   HELIX       386    395       {ECO:0000244|PDB:1GVJ}.
FT   TURN        396    400       {ECO:0000244|PDB:1GVJ}.
FT   STRAND      401    404       {ECO:0000244|PDB:1GVJ}.
FT   STRAND      408    414       {ECO:0000244|PDB:1GVJ}.
FT   HELIX       418    422       {ECO:0000244|PDB:1GVJ}.
FT   HELIX       426    432       {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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