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 04-NOV-2026, entry version 214. 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}, ESX GN {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] RP INTERACTION WITH ZNF768. RX PubMed=30476274; DOI=10.1093/nar/gky1148; RA Rohrmoser M., Kluge M., Yahia Y., Gruber-Eber A., Maqbool M.A., Forne I., RA Krebs S., Blum H., Greifenberg A.K., Geyer M., Descostes N., Imhof A., RA Andrau J.C., Friedel C.C., Eick D.; RT "MIR sequences recruit zinc finger protein ZNF768 to expressed genes."; RL Nucleic Acids Res. 47:700-715(2019). RN [34] {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. Interacts with ZNF768 CC (PubMed:30476274). {ECO:0000269|PubMed:10391676, CC ECO:0000269|PubMed:12624109, ECO:0000269|PubMed:15075319, CC ECO:0000269|PubMed:17060315, ECO:0000269|PubMed:30476274}. 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}. 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; 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_001114309.2. [P78545-1] DR RefSeq; NP_004424.3; NM_004433.5. [P78545-1] DR PDB; 2E8P; NMR; -; A=48-132. DR AlphaFoldDB; P78545; -. DR SMR; P78545; -. DR BioGRID; 108314; 53. DR FunCoup; P78545; 1729. DR IntAct; P78545; 32. DR NDEx; IQUERY-CP-ELF3; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000352673; -. DR GlyGen; P78545; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P78545; -. DR PhosphoSitePlus; P78545; -. DR BioMuta; ELF3; -. DR DMDM; 74739735; -. DR jPOST; P78545; -. DR MassIVE; P78545; -. DR PaxDb; 9606-ENSP00000352673; -. DR PeptideAtlas; P78545; -. DR ProteomicsDB; 57646; -. [P78545-1] DR ProteomicsDB; 57647; -. [P78545-2] DR Pumba; P78545; -. DR Antibodypedia; 924; 533 antibodies from 41 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 AGR; HGNC:3318; -. DR ClinPGx; PA27746; -. 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 OpenTargets; ENSG00000163435; -. DR VEuPathDB; HostDB:ENSG00000163435; -. DR eggNOG; KOG3804; Eukaryota. DR GeneTree; ENSGT00940000158955; -. DR HOGENOM; CLU_048172_0_0_1; -. DR InParanoid; P78545; -. DR OMA; ADFGYYN; -. DR OrthoDB; 5961210at2759; -. DR PAN-GO; P78545; 4 GO annotations based on evolutionary models. DR PhylomeDB; P78545; -. DR PathwayCommons; P78545; -. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR SignaLink; P78545; -. DR SIGNOR; P78545; -. DR Agora; ENSG00000163435; -. DR BioGRID-ORCS; 1999; 34 hits in 1175 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 134 other cell types or tissues. DR ExpressionAtlas; P78545; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. 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:0030154; P:cell differentiation; IBA:GO_Central. 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 DNA-templated transcription; 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 CDD; cd08537; SAM_PNT-ESE-1-like; 1. DR FunFam; 1.10.10.10:FF:000136; ETS homologous factor isoform X1; 1. DR FunFam; 1.10.150.50:FF:000063; ETS-related transcription factor Elf-3 isoform X1; 1. 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 InterPro; IPR042693; Elf-3_PNT. 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; ETS; 1. DR PANTHER; PTHR11849:SF13; ETS-RELATED TRANSCRIPTION FACTOR ELF-3; 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; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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; Proteomics identification; Reference proteome; Repressor; KW Transcription; 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 181..216 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 231..241 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..251 FT /note="Basic 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 //