GenomeNet

Database: UniProt
Entry: P78545
LinkDB: P78545
Original site: P78545 
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   07-OCT-2020, entry version 187.
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; 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}.
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   SMR; P78545; -.
DR   BioGRID; 108314; 31.
DR   IntAct; P78545; 6.
DR   STRING; 9606.ENSP00000352673; -.
DR   iPTMnet; P78545; -.
DR   PhosphoSitePlus; P78545; -.
DR   BioMuta; ELF3; -.
DR   DMDM; 74739735; -.
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; 420 antibodies.
DR   DNASU; 1999; -.
DR   Ensembl; ENST00000359651; ENSP00000352673; ENSG00000163435. [P78545-1]
DR   Ensembl; ENST00000367283; ENSP00000356252; ENSG00000163435. [P78545-1]
DR   Ensembl; ENST00000367284; ENSP00000356253; ENSG00000163435. [P78545-1]
DR   GeneID; 1999; -.
DR   KEGG; hsa:1999; -.
DR   UCSC; uc001gxg.5; human. [P78545-1]
DR   CTD; 1999; -.
DR   DisGeNET; 1999; -.
DR   EuPathDB; HostDB:ENSG00000163435.15; -.
DR   GeneCards; ELF3; -.
DR   HGNC; HGNC:3318; ELF3.
DR   HPA; ENSG00000163435; Tissue enhanced (intestine).
DR   MIM; 602191; gene.
DR   neXtProt; NX_P78545; -.
DR   OpenTargets; ENSG00000163435; -.
DR   PharmGKB; PA27746; -.
DR   eggNOG; KOG3804; Eukaryota.
DR   GeneTree; ENSGT00940000158955; -.
DR   HOGENOM; CLU_048172_0_0_1; -.
DR   InParanoid; P78545; -.
DR   KO; K09429; -.
DR   OMA; ASWSGKQ; -.
DR   PhylomeDB; P78545; -.
DR   TreeFam; TF318679; -.
DR   PathwayCommons; P78545; -.
DR   Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR   SIGNOR; P78545; -.
DR   BioGRID-ORCS; 1999; 13 hits in 894 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 ectocervix and 152 other tissues.
DR   ExpressionAtlas; P78545; baseline and differential.
DR   Genevisible; P78545; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
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:0045747; P:positive regulation of Notch signaling pathway; TAS:Reactome.
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; 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: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; Polymorphism; 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   MOTIF           137..145
FT                   /note="9aaTAD"
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:0000244|PDB:2E8P"
FT   HELIX           64..66
FT                   /evidence="ECO:0000244|PDB:2E8P"
FT   HELIX           69..82
FT                   /evidence="ECO:0000244|PDB:2E8P"
FT   TURN            92..94
FT                   /evidence="ECO:0000244|PDB:2E8P"
FT   HELIX           100..104
FT                   /evidence="ECO:0000244|PDB:2E8P"
FT   HELIX           107..113
FT                   /evidence="ECO:0000244|PDB:2E8P"
FT   HELIX           115..117
FT                   /evidence="ECO:0000244|PDB:2E8P"
FT   HELIX           118..130
FT                   /evidence="ECO:0000244|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
//
DBGET integrated database retrieval system