ELF3_HUMAN
ID ELF3_HUMAN Reviewed; 371 AA.
AC P78545; B2R5Q6; Q6IAP8; Q7RU03; Q7Z3X2; Q8NFG2; Q99718;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=ETS-related transcription factor Elf-3;
DE AltName: Full=E74-like factor 3;
DE AltName: Full=Epithelial-restricted with serine box;
DE AltName: Full=Epithelium-restricted Ets protein ESX;
DE AltName: Full=Epithelium-specific Ets transcription factor 1;
DE Short=ESE-1;
GN Name=ELF3 {ECO:0000312|HGNC:HGNC:3318};
GN Synonyms=ERT {ECO:0000312|EMBL:AAB67238.1},
GN ESX {ECO:0000312|EMBL:AAB58075.1}, JEN;
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] {ECO:0000305, ECO:0000312|EMBL:AAB65823.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=9234700; DOI=10.1128/mcb.17.8.4419;
RA Oettgen P., Alani R.M., Barcinski M.A., Brown L., Akbarali Y., Boltax J.,
RA Kunsch C., Munger K., Libermann T.A.;
RT "Isolation and characterization of a novel epithelium-specific
RT transcription factor, ESE-1, a member of the ets family.";
RL Mol. Cell. Biol. 17:4419-4433(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC51884.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9336459; DOI=10.1093/nar/25.21.4287;
RA Andreoli J.M., Jang S.-I., Chung E., Coticchia C.M., Steinert P.M.,
RA Markova N.G.;
RT "The expression of a novel, epithelium-specific ets transcription factor is
RT restricted to the most differentiated layers in the epidermis.";
RL Nucleic Acids Res. 25:4287-4295(1997).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAB58075.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta {ECO:0000312|EMBL:AAB58075.1};
RX PubMed=9129154; DOI=10.1038/sj.onc.1200978;
RA Chang C.-H., Scott G.K., Kuo W.-L., Xiong X., Suzdaltseva Y., Park J.W.,
RA Sayre P., Erny K., Collins C., Gray J.W., Benz C.C.;
RT "ESX: a structurally unique Ets overexpressed early during human breast
RT tumorigenesis.";
RL Oncogene 14:1617-1622(1997).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAB96586.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal lung {ECO:0000312|EMBL:AAB96586.1};
RX PubMed=9395241; DOI=10.1038/sj.onc.1201427;
RA Tymms M.J., Ng A.Y.N., Thomas R.S., Schutte B.C., Zhou J., Eyre H.J.,
RA Sutherland G.R., Seth A., Rosenberg M., Papas T., Debouck C., Kola I.;
RT "A novel epithelial-expressed ETS gene, ELF3: human and murine cDNA
RT sequences, murine genomic organization, human mapping to 1q32.2 and
RT expression in tissues and cancer.";
RL Oncogene 15:2449-2462(1997).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAB67238.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Placenta {ECO:0000312|EMBL:AAB67238.1};
RX PubMed=9417054; DOI=10.1074/jbc.273.1.110;
RA Choi S.-G., Yi Y., Kim Y.-S., Kato M., Chang J., Chung H.-W., Hahm K.-B.,
RA Yang H.-K., Rhee H.H., Bang Y.-J., Kim S.-J.;
RT "A novel ets-related transcription factor, ERT/ESX/ESE-1, regulates
RT expression of the transforming growth factor-beta type II receptor.";
RL J. Biol. Chem. 273:110-117(1998).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAD45237.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP TBP, AND SUBCELLULAR LOCATION.
RX PubMed=10391676; DOI=10.1038/sj.onc.1202674;
RA Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C.;
RT "Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX,
RT confers potent transactivating capacity and binds to TATA-binding protein
RT (TBP).";
RL Oncogene 18:3682-3695(1999).
RN [7] {ECO:0000305, ECO:0000312|EMBL:CAD29859.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=12119107; DOI=10.1016/s0378-1119(02)00650-9;
RA Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S., Cohen P.,
RA Foulon T.;
RT "Human aminopeptidase B (rnpep) on chromosome 1q32.2: complementary DNA,
RT genomic structure and expression.";
RL Gene 292:129-140(2002).
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAM70481.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC TISSUE=Mammary cancer {ECO:0000269|PubMed:14997048};
RX PubMed=14997048; DOI=10.1023/b:brea.0000010710.51614.2d;
RA Kaplan M.H., Wang X.P., Xu H.P., Dosik M.H.;
RT "Partially unspliced and fully spliced ELF3 mRNA, including a new Alu
RT element in human breast cancer.";
RL Breast Cancer Res. Treat. 83:171-187(2004).
RN [9] {ECO:0000305, ECO:0000312|EMBL:CAD97611.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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 [12] {ECO:0000312|EMBL:AL691482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [13] {ECO:0000305, ECO:0000312|EMBL:CAD97611.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [14] {ECO:0000305, ECO:0000312|EMBL:AAH03569.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung {ECO:0000312|EMBL:AAH03569.1};
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 [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=10644990; DOI=10.1038/sj.onc.1203252;
RA Chang J., Lee C., Hahm K.-B., Yi Y., Choi S.-G., Kim S.-J.;
RT "Over-expression of ERT(ESX/ESE-1/ELF3), an ets-related transcription
RT factor, induces endogenous TGF-beta type II receptor expression and
RT restores the TGF-beta signaling pathway in Hs578t human breast cancer
RT cells.";
RL Oncogene 19:151-154(2000).
RN [16] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 247-ARG--PRO-250; TRP-315; LYS-319 AND
RP 334-ARG--TYR-337.
RX PubMed=10773884; DOI=10.1038/sj.onc.1203441;
RA Brembeck F.H., Opitz O.G., Libermann T.A., Rustgi A.K.;
RT "Dual function of the epithelial specific ets transcription factor, ELF3,
RT in modulating differentiation.";
RL Oncogene 19:1941-1949(2000).
RN [17] {ECO:0000305}
RP FUNCTION.
RX PubMed=11036073; DOI=10.1074/jbc.m006507200;
RA Rudders S., Gaspar J., Madore R., Voland C., Grall F., Patel A.,
RA Pellacani A., Perrella M.A., Libermann T.A., Oettgen P.;
RT "ESE-1 is a novel transcriptional mediator of inflammation that interacts
RT with NF-kappa B to regulate the inducible nitric-oxide synthase gene.";
RL J. Biol. Chem. 276:3302-3309(2001).
RN [18] {ECO:0000305}
RP FUNCTION.
RX PubMed=11313868; DOI=10.1038/sj.onc.1204227;
RA Park S.H., Kim Y.S., Park B.-K., Hougaard S., Kim S.-J.;
RT "Sequence-specific enhancer binding protein is responsible for the
RT differential expression of ERT/ESX/ELF-3/ESE-1/jen gene in human gastric
RT cancer cell lines: implication for the loss of TGF-beta type II receptor
RT expression.";
RL Oncogene 20:1235-1245(2001).
RN [19] {ECO:0000305}
RP INDUCTION.
RX PubMed=12032832; DOI=10.1038/sj.onc.1205503;
RA Neve R.M., Ylstra B., Chang C.-H., Albertson D.G., Benz C.C.;
RT "ErbB2 activation of ESX gene expression.";
RL Oncogene 21:3934-3938(2002).
RN [20] {ECO:0000305}
RP FUNCTION.
RX PubMed=12713734; DOI=10.1089/104454903321515896;
RA Eckel K.L., Tentler J.J., Cappetta G.J., Diamond S.E.,
RA Gutierrez-Hartmann A.;
RT "The epithelial-specific ETS transcription factor ESX/ESE-1/Elf-3 modulates
RT breast cancer-associated gene expression.";
RL DNA Cell Biol. 22:79-94(2003).
RN [21] {ECO:0000305}
RP FUNCTION.
RX PubMed=12414801; DOI=10.1074/jbc.m208241200;
RA Kwon J.H., Keates S., Simeonidis S., Grall F., Libermann T.A., Keates A.C.;
RT "ESE-1, an enterocyte-specific Ets transcription factor, regulates MIP-
RT 3alpha gene expression in Caco-2 human colonic epithelial cells.";
RL J. Biol. Chem. 278:875-884(2003).
RN [22] {ECO:0000305}
RP FUNCTION, AND SUBUNIT.
RX PubMed=12624109; DOI=10.1074/jbc.m300508200;
RA Cabral A., Fischer D.F., Vermeij W.P., Backendorf C.;
RT "Distinct functional interactions of human Skn-1 isoforms with Ese-1 during
RT keratinocyte terminal differentiation.";
RL J. Biol. Chem. 278:17792-17799(2003).
RN [23] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=12682075; DOI=10.1074/jbc.m212258200;
RA Reddy S.P.M., Vuong H., Adiseshaiah P.;
RT "Interplay between proximal and distal promoter elements is required for
RT squamous differentiation marker induction in the bronchial epithelium: role
RT for ESE-1, Sp1, and AP-1 proteins.";
RL J. Biol. Chem. 278:21378-21387(2003).
RN [24] {ECO:0000305}
RP FUNCTION.
RX PubMed=14715662; DOI=10.1074/jbc.m308593200;
RA Brown C., Gaspar J., Pettit A., Lee R., Gu X., Wang H., Manning C.,
RA Voland C., Goldring S.R., Goldring M.B., Libermann T.A., Gravallese E.M.,
RA Oettgen P.;
RT "ESE-1 is a novel transcriptional mediator of angiopoietin-1 expression in
RT the setting of inflammation.";
RL J. Biol. Chem. 279:12794-12803(2004).
RN [25] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CREBBP; EP300; XRCC5 AND XRCC6.
RX PubMed=15075319; DOI=10.1074/jbc.m401356200;
RA Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.;
RT "Positive and negative modulation of the transcriptional activity of the
RT ETS factor ESE-1 through interaction with p300, CREB-binding protein, and
RT Ku 70/86.";
RL J. Biol. Chem. 279:25241-25250(2004).
RN [26] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15169914; DOI=10.1128/mcb.24.12.5548-5564.2004;
RA Prescott J.D., Koto K.S.N., Singh M., Gutierrez-Hartmann A.;
RT "The ETS transcription factor ESE-1 transforms MCF-12A human mammary
RT epithelial cells via a novel cytoplasmic mechanism.";
RL Mol. Cell. Biol. 24:5548-5564(2004).
RN [27] {ECO:0000305}
RP FUNCTION.
RX PubMed=14767472; DOI=10.1038/sj.onc.1207391;
RA Schedin P.J., Eckel-Mahan K.L., McDaniel S.M., Prescott J.D., Brodsky K.S.,
RA Tentler J.J., Gutierrez-Hartmann A.;
RT "ESX induces transformation and functional epithelial to mesenchymal
RT transition in MCF-12A mammary epithelial cells.";
RL Oncogene 23:1766-1779(2004).
RN [28] {ECO:0000305}
RP FUNCTION.
RX PubMed=15794755; DOI=10.1111/j.1742-4658.2005.04592.x;
RA Grall F.T., Prall W.C., Wei W., Gu X., Cho J.-Y., Choy B.K., Zerbini L.F.,
RA Inan M.S., Goldring S.R., Gravallese E.M., Goldring M.B., Oettgen P.,
RA Libermann T.A.;
RT "The Ets transcription factor ESE-1 mediates induction of the COX-2 gene by
RT LPS in monocytes.";
RL FEBS J. 272:1676-1687(2005).
RN [29] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=16307850; DOI=10.1016/j.gene.2005.10.001;
RA Neve R.M., Parmar H., Amend C., Chen C., Rizzino A., Benz C.C.;
RT "Identification of an epithelial-specific enhancer regulating ESX
RT expression.";
RL Gene 367:118-125(2006).
RN [30] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17060315; DOI=10.1074/jbc.m608389200;
RA Kohno Y., Okamoto T., Ishibe T., Nagayama S., Shima Y., Nishijo K.,
RA Shibata K.R., Fukiage K., Otsuka S., Uejima D., Araki N., Naka N.,
RA Nakashima Y., Aoyama T., Nakayama T., Nakamura T., Toguchida J.;
RT "Expression of claudin7 is tightly associated with epithelial structures in
RT synovial sarcomas and regulated by an Ets family transcription factor,
RT ELF3.";
RL J. Biol. Chem. 281:38941-38950(2006).
RN [31]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [33] {ECO:0000305, ECO:0000312|EMBL:CAD97611.1}
RP STRUCTURE BY NMR OF 45-132.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal SAM-domain of E74-like factor 3.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: Transcriptional activator that binds and transactivates ETS
CC sequences containing the consensus nucleotide core sequence GGA[AT].
CC Acts synergistically with POU2F3 to transactivate the SPRR2A promoter
CC and with RUNX1 to transactivate the ANGPT1 promoter. Also
CC transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2,
CC SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity.
CC Involved in mediating vascular inflammation. May play an important role
CC in epithelial cell differentiation and tumorigenesis. May be a critical
CC downstream effector of the ERBB2 signaling pathway. May be associated
CC with mammary gland development and involution. Plays an important role
CC in the regulation of transcription with TATA-less promoters in
CC preimplantation embryos, which is essential in preimplantation
CC development (By similarity). {ECO:0000250, ECO:0000269|PubMed:10391676,
CC ECO:0000269|PubMed:10644990, ECO:0000269|PubMed:10773884,
CC ECO:0000269|PubMed:11036073, ECO:0000269|PubMed:11313868,
CC ECO:0000269|PubMed:12414801, ECO:0000269|PubMed:12624109,
CC ECO:0000269|PubMed:12682075, ECO:0000269|PubMed:12713734,
CC ECO:0000269|PubMed:14715662, ECO:0000269|PubMed:14767472,
CC ECO:0000269|PubMed:15075319, ECO:0000269|PubMed:15169914,
CC ECO:0000269|PubMed:15794755, ECO:0000269|PubMed:16307850,
CC ECO:0000269|PubMed:17060315, ECO:0000269|PubMed:9129154,
CC ECO:0000269|PubMed:9234700, ECO:0000269|PubMed:9336459,
CC ECO:0000269|PubMed:9395241, ECO:0000269|PubMed:9417054}.
CC -!- SUBUNIT: Interacts with TBP. Interacts with CREBBP and EP300; these act
CC as transcriptional coactivators of ELF3 and positively modulate its
CC function. Interacts with XRCC5/KU86 and XRCC6/KU70; these inhibit the
CC ability of ELF3 to bind DNA and negatively modulate its transcriptional
CC activity. Associated with CLND7 and POU2F3.
CC {ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:12624109,
CC ECO:0000269|PubMed:15075319, ECO:0000269|PubMed:17060315}.
CC -!- INTERACTION:
CC P78545; Q16236: NFE2L2; NbExp=5; IntAct=EBI-1057285, EBI-2007911;
CC P78545; P41743: PRKCI; NbExp=2; IntAct=EBI-1057285, EBI-286199;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10391676,
CC ECO:0000269|PubMed:15169914, ECO:0000269|PubMed:17060315}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:10391676,
CC ECO:0000269|PubMed:15169914, ECO:0000269|PubMed:17060315}.
CC Note=Localizes to the cytoplasm where it has been shown to transform
CC MCF-12A mammary epithelial cells via a novel cytoplasmic mechanism.
CC Also transiently expressed and localized to the nucleus where it
CC induces apoptosis in non-transformed breast epithelial cells MCF-10A
CC and MCF-12A via a transcription-dependent mechanism.
CC {ECO:0000269|PubMed:10391676, ECO:0000269|PubMed:15169914,
CC ECO:0000269|PubMed:17060315}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms may exist. {ECO:0000269|PubMed:9234700};
CC Name=1 {ECO:0000269|PubMed:9234700}; Synonyms=ESE-1b
CC {ECO:0000269|PubMed:9234700};
CC IsoId=P78545-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9234700}; Synonyms=ESE-1a
CC {ECO:0000269|PubMed:9234700};
CC IsoId=P78545-2; Sequence=VSP_052433;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in tissues containing a high
CC content of terminally differentiated epithelial cells including mammary
CC gland, colon, trachea, kidney, prostate, uterus, stomach and skin.
CC {ECO:0000269|PubMed:9129154, ECO:0000269|PubMed:9234700,
CC ECO:0000269|PubMed:9336459, ECO:0000269|PubMed:9395241}.
CC -!- INDUCTION: Transcriptionally regulated by ERBB2 receptor signaling in
CC breast cancer epithelial cells. Up-regulated by phorbol 12-myristate
CC 13-acetate (PMA) in bronchial epithelial cells. By retinoic acid in
CC MCF-7 mammary epithelial cells (at protein level).
CC {ECO:0000269|PubMed:12032832, ECO:0000269|PubMed:12682075,
CC ECO:0000269|PubMed:16307850}.
CC -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:17467953}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
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DR EMBL; U73843; AAB65823.1; -; mRNA.
DR EMBL; U73844; AAB65824.1; -; mRNA.
DR EMBL; U97156; AAC51884.1; -; mRNA.
DR EMBL; U66894; AAB58075.1; -; mRNA.
DR EMBL; AF016295; AAB96586.1; -; mRNA.
DR EMBL; AF017307; AAB67238.1; -; mRNA.
DR EMBL; AF110184; AAD45237.1; -; Genomic_DNA.
DR EMBL; BN000001; CAD29859.1; -; Genomic_DNA.
DR EMBL; AF517841; AAM70481.1; -; mRNA.
DR EMBL; CR457106; CAG33387.1; -; mRNA.
DR EMBL; AK312273; BAG35203.1; -; mRNA.
DR EMBL; BX537368; CAD97611.1; -; mRNA.
DR EMBL; AL691482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91389.1; -; Genomic_DNA.
DR EMBL; BC003569; AAH03569.1; -; mRNA.
DR CCDS; CCDS1419.1; -. [P78545-1]
DR RefSeq; NP_001107781.1; NM_001114309.1. [P78545-1]
DR RefSeq; NP_004424.3; NM_004433.4. [P78545-1]
DR PDB; 2E8P; NMR; -; A=48-132.
DR PDBsum; 2E8P; -.
DR AlphaFoldDB; P78545; -.
DR SMR; P78545; -.
DR BioGRID; 108314; 53.
DR IntAct; P78545; 26.
DR STRING; 9606.ENSP00000352673; -.
DR iPTMnet; P78545; -.
DR PhosphoSitePlus; P78545; -.
DR BioMuta; ELF3; -.
DR DMDM; 74739735; -.
DR EPD; P78545; -.
DR jPOST; P78545; -.
DR MassIVE; P78545; -.
DR MaxQB; P78545; -.
DR PaxDb; P78545; -.
DR PeptideAtlas; P78545; -.
DR PRIDE; P78545; -.
DR ProteomicsDB; 57646; -. [P78545-1]
DR ProteomicsDB; 57647; -. [P78545-2]
DR Antibodypedia; 924; 457 antibodies from 38 providers.
DR DNASU; 1999; -.
DR Ensembl; ENST00000359651.7; ENSP00000352673.3; ENSG00000163435.16. [P78545-1]
DR Ensembl; ENST00000367283.7; ENSP00000356252.3; ENSG00000163435.16. [P78545-1]
DR Ensembl; ENST00000367284.10; ENSP00000356253.5; ENSG00000163435.16. [P78545-1]
DR GeneID; 1999; -.
DR KEGG; hsa:1999; -.
DR MANE-Select; ENST00000367284.10; ENSP00000356253.5; NM_004433.5; NP_004424.3.
DR UCSC; uc001gxg.5; human. [P78545-1]
DR CTD; 1999; -.
DR DisGeNET; 1999; -.
DR GeneCards; ELF3; -.
DR HGNC; HGNC:3318; ELF3.
DR HPA; ENSG00000163435; Tissue enhanced (esophagus).
DR MIM; 602191; gene.
DR neXtProt; NX_P78545; -.
DR OpenTargets; ENSG00000163435; -.
DR PharmGKB; PA27746; -.
DR VEuPathDB; HostDB:ENSG00000163435; -.
DR eggNOG; KOG3804; Eukaryota.
DR GeneTree; ENSGT00940000158955; -.
DR HOGENOM; CLU_048172_0_0_1; -.
DR InParanoid; P78545; -.
DR OMA; ASWSGKQ; -.
DR PhylomeDB; P78545; -.
DR TreeFam; TF318679; -.
DR PathwayCommons; P78545; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR SignaLink; P78545; -.
DR SIGNOR; P78545; -.
DR BioGRID-ORCS; 1999; 28 hits in 1093 CRISPR screens.
DR ChiTaRS; ELF3; human.
DR EvolutionaryTrace; P78545; -.
DR GenomeRNAi; 1999; -.
DR Pharos; P78545; Tbio.
DR PRO; PR:P78545; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P78545; protein.
DR Bgee; ENSG00000163435; Expressed in lower esophagus mucosa and 132 other tissues.
DR ExpressionAtlas; P78545; baseline and differential.
DR Genevisible; P78545; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
DR GO; GO:0060056; P:mammary gland involution; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd08537; SAM_PNT-ESE-1-like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR042693; Elf-3_PNT.
DR InterPro; IPR033074; Elf3.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF13; PTHR11849:SF13; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF02198; SAM_PNT; 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; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; DNA-binding; Inflammatory response;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..371
FT /note="ETS-related transcription factor Elf-3"
FT /id="PRO_0000287681"
FT DOMAIN 46..132
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 273..355
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 173..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..145
FT /note="9aaTAD"
FT COMPBIAS 190..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 173..195
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9234700"
FT /id="VSP_052433"
FT VARIANT 317
FT /note="Q -> K (in dbSNP:rs1135542)"
FT /id="VAR_048945"
FT MUTAGEN 247..250
FT /note="RGRP->AAAA: No effect on transcriptional repression
FT on KRT4 promoter."
FT /evidence="ECO:0000269|PubMed:10773884"
FT MUTAGEN 315
FT /note="W->A: Partially abrogates repressive effect on the
FT KRT4 promoter; when associated with A-319."
FT /evidence="ECO:0000269|PubMed:10773884"
FT MUTAGEN 319
FT /note="K->A: Partially abrogates repressive effect on the
FT KRT4 promoter; when associated with A-315."
FT /evidence="ECO:0000269|PubMed:10773884"
FT MUTAGEN 334..337
FT /note="RYYY->AAAA: Partially abrogates repressive effect on
FT the KRT4 promoter."
FT /evidence="ECO:0000269|PubMed:10773884"
FT CONFLICT 3
FT /note="A -> T (in Ref. 8; AAM70481)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..56
FT /note="EK -> GE (in Ref. 7; CAD29859)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="S -> L (in Ref. 8; AAM70481)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..130
FT /note="TS -> SA (in Ref. 7; CAD29859)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="D -> Y (in Ref. 8; AAM70481)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..161
FT /note="DQ -> GE (in Ref. 7; CAD29859)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="T -> A (in Ref. 7; CAD29859)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="H -> L (in Ref. 9; CAG33387)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="K -> E (in Ref. 11; CAD97611)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="Y -> C (in Ref. 8; AAM70481)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="A -> G (in Ref. 7; CAD29859)"
FT /evidence="ECO:0000305"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2E8P"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2E8P"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:2E8P"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2E8P"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:2E8P"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2E8P"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2E8P"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:2E8P"
SQ SEQUENCE 371 AA; 41454 MW; 81A23A7DECBE2EF9 CRC64;
MAATCEISNI FSNYFSAMYS SEDSTLASVP PAATFGADDL VLTLSNPQMS LEGTEKASWL
GEQPQFWSKT QVLDWISYQV EKNKYDASAI DFSRCDMDGA TLCNCALEEL RLVFGPLGDQ
LHAQLRDLTS SSSDELSWII ELLEKDGMAF QEALDPGPFD QGSPFAQELL DDGQQASPYH
PGSCGAGAPS PGSSDVSTAG TGASRSSHSS DSGGSDVDLD PTDGKLFPSD GFRDCKKGDP
KHGKRKRGRP RKLSKEYWDC LEGKKSKHAP RGTHLWEFIR DILIHPELNE GLMKWENRHE
GVFKFLRSEA VAQLWGQKKK NSNMTYEKLS RAMRYYYKRE ILERVDGRRL VYKFGKNSSG
WKEEEVLQSR N
