ELF1_HUMAN
ID ELF1_HUMAN Reviewed; 619 AA.
AC P32519; B4E2I5; E9PDQ9; Q8N6F6; Q9UDE1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=ETS-related transcription factor Elf-1;
DE AltName: Full=E74-like factor 1;
GN Name=ELF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1527846; DOI=10.1128/jvi.66.10.5890-5897.1992;
RA Leiden J.M., Wang C.Y., Petryniak B., Markovitz D.M., Nabel G.J.,
RA Thompson C.B.;
RT "A novel Ets-related transcription factor, Elf-1, binds to human
RT immunodeficiency virus type 2 regulatory elements that are required for
RT inducible trans activation in T cells.";
RL J. Virol. 66:5890-5897(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-58 AND
RP SER-343.
RC TISSUE=Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 204-289 (ISOFORM 1).
RX PubMed=1545787; DOI=10.1128/mcb.12.3.1043-1053.1992;
RA Thompson C.B., Wang C.Y., Ho I.C., Bohjanen P.R., Petryniak B., June C.H.,
RA Miesfeldt S., Zhang L., Nabel G.J., Karpinski B.;
RT "Cis-acting sequences required for inducible interleukin-2 enhancer
RT function bind a novel Ets-related protein, Elf-1.";
RL Mol. Cell. Biol. 12:1043-1053(1992).
RN [7]
RP INTERACTION WITH RB.
RX PubMed=8493578; DOI=10.1126/science.8493578;
RA Wang C.Y., Petryniak B., Thompson C.B., Kaelin W.G. Jr., Leiden J.M.;
RT "Regulation of the Ets-related transcription factor Elf-1 by binding to the
RT retinoblastoma protein.";
RL Science 260:1330-1335(1993).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8756667; DOI=10.1128/mcb.16.9.5091;
RA Oettgen P., Akbarali Y., Boltax J., Best J., Kunsch C., Libermann T.A.;
RT "Characterization of NERF, a novel transcription factor related to the Ets
RT factor ELF-1.";
RL Mol. Cell. Biol. 16:5091-5106(1996).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=9524226; DOI=10.1016/s0378-1119(98)00022-5;
RA Aryee D.N.T., Petermann R., Kos K., Henn T., Haas O.A., Kovar H.;
RT "Cloning of a novel human ELF-1-related ETS transcription factor, ELFR, its
RT characterization and chromosomal assignment relative to ELF-1.";
RL Gene 210:71-78(1998).
RN [10]
RP INTERACTION WITH RUNX1.
RX PubMed=10207087; DOI=10.1128/mcb.19.5.3635;
RA Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.;
RT "Functional and physical interactions between AML1 proteins and an ETS
RT protein, MEF: implications for the pathogenesis of t(8;21)-positive
RT leukemias.";
RL Mol. Cell. Biol. 19:3635-3644(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-432, AND
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167 AND SER-432, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-168; SER-187;
RP THR-190 AND SER-432, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-163; SER-187 AND
RP THR-190, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Transcription factor that activates the LYN and BLK
CC promoters. Appears to be required for the T-cell-receptor-mediated
CC trans activation of HIV-2 gene expression. Binds specifically to two
CC purine-rich motifs in the HIV-2 enhancer. {ECO:0000269|PubMed:8756667}.
CC -!- SUBUNIT: Binds to the underphosphorylated form of RB. May interact with
CC other transcription factors in order to regulate specific genes.
CC Interacts with RUNX1. {ECO:0000269|PubMed:10207087,
CC ECO:0000269|PubMed:8493578}.
CC -!- INTERACTION:
CC P32519; P31276: HOXC13; NbExp=3; IntAct=EBI-765526, EBI-2293590;
CC P32519; Q13952-2: NFYC; NbExp=3; IntAct=EBI-765526, EBI-11956831;
CC P32519; P08047: SP1; NbExp=2; IntAct=EBI-765526, EBI-298336;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P32519-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P32519-2; Sequence=VSP_045682;
CC -!- TISSUE SPECIFICITY: In fetal tissues, it is highly expressed in heart,
CC lung liver and kidney, and weakly expressed in brain. In adult, it is
CC highly expressed in pancreas, spleen, thymus and peripheral blood
CC leukocytes, expressed at moderate levels in heart, placenta, lung,
CC liver, skeletal muscle, kidney, prostate, ovary, small intestine and
CC colon, and weakly expressed in brain and testis.
CC {ECO:0000269|PubMed:8756667, ECO:0000269|PubMed:9524226}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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; M82882; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK304289; BAG65147.1; -; mRNA.
DR EMBL; AL157877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08640.1; -; Genomic_DNA.
DR EMBL; BC030507; AAH30507.1; -; mRNA.
DR CCDS; CCDS45043.1; -. [P32519-2]
DR CCDS; CCDS9374.1; -. [P32519-1]
DR PIR; A43361; A43361.
DR RefSeq; NP_001138825.1; NM_001145353.1. [P32519-2]
DR RefSeq; NP_758961.1; NM_172373.3. [P32519-1]
DR RefSeq; XP_005266333.1; XM_005266276.1.
DR RefSeq; XP_005266334.1; XM_005266277.3.
DR RefSeq; XP_011533252.1; XM_011534950.1.
DR RefSeq; XP_016875898.1; XM_017020409.1.
DR RefSeq; XP_016875899.1; XM_017020410.1.
DR RefSeq; XP_016875900.1; XM_017020411.1.
DR RefSeq; XP_016875901.1; XM_017020412.1.
DR RefSeq; XP_016875902.1; XM_017020413.1.
DR AlphaFoldDB; P32519; -.
DR SMR; P32519; -.
DR BioGRID; 108312; 116.
DR DIP; DIP-185N; -.
DR ELM; P32519; -.
DR IntAct; P32519; 109.
DR MINT; P32519; -.
DR STRING; 9606.ENSP00000239882; -.
DR GlyGen; P32519; 19 sites, 2 O-linked glycans (19 sites).
DR iPTMnet; P32519; -.
DR MetOSite; P32519; -.
DR PhosphoSitePlus; P32519; -.
DR BioMuta; ELF1; -.
DR DMDM; 212288097; -.
DR EPD; P32519; -.
DR jPOST; P32519; -.
DR MassIVE; P32519; -.
DR MaxQB; P32519; -.
DR PaxDb; P32519; -.
DR PeptideAtlas; P32519; -.
DR PRIDE; P32519; -.
DR ProteomicsDB; 19727; -.
DR ProteomicsDB; 54879; -. [P32519-1]
DR ABCD; P32519; 55 sequenced antibodies.
DR Antibodypedia; 906; 395 antibodies from 39 providers.
DR DNASU; 1997; -.
DR Ensembl; ENST00000239882.7; ENSP00000239882.3; ENSG00000120690.16. [P32519-1]
DR Ensembl; ENST00000625359.1; ENSP00000486912.1; ENSG00000120690.16. [P32519-2]
DR GeneID; 1997; -.
DR KEGG; hsa:1997; -.
DR MANE-Select; ENST00000239882.7; ENSP00000239882.3; NM_172373.4; NP_758961.1.
DR UCSC; uc001uxs.4; human. [P32519-1]
DR CTD; 1997; -.
DR DisGeNET; 1997; -.
DR GeneCards; ELF1; -.
DR HGNC; HGNC:3316; ELF1.
DR HPA; ENSG00000120690; Tissue enhanced (bone).
DR MIM; 189973; gene.
DR neXtProt; NX_P32519; -.
DR OpenTargets; ENSG00000120690; -.
DR PharmGKB; PA27744; -.
DR VEuPathDB; HostDB:ENSG00000120690; -.
DR eggNOG; KOG3804; Eukaryota.
DR GeneTree; ENSGT00940000157039; -.
DR InParanoid; P32519; -.
DR OMA; HNYSGLT; -.
DR PhylomeDB; P32519; -.
DR TreeFam; TF318679; -.
DR PathwayCommons; P32519; -.
DR Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR Reactome; R-HSA-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR SignaLink; P32519; -.
DR SIGNOR; P32519; -.
DR BioGRID-ORCS; 1997; 25 hits in 1103 CRISPR screens.
DR ChiTaRS; ELF1; human.
DR GenomeRNAi; 1997; -.
DR Pharos; P32519; Tbio.
DR PRO; PR:P32519; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P32519; protein.
DR Bgee; ENSG00000120690; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; P32519; baseline and differential.
DR Genevisible; P32519; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
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:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR022084; TF_Elf_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF12310; Elf-1_N; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..619
FT /note="ETS-related transcription factor Elf-1"
FT /id="PRO_0000204085"
FT DNA_BIND 208..290
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 158..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 122..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045682"
FT VARIANT 58
FT /note="N -> S (in dbSNP:rs7799)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048942"
FT VARIANT 343
FT /note="T -> S (in dbSNP:rs1056820)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048943"
FT VARIANT 403
FT /note="T -> I (in dbSNP:rs7323148)"
FT /id="VAR_048944"
SQ SEQUENCE 619 AA; 67498 MW; FA0A51B3965616F3 CRC64;
MAAVVQQNDL VFEFASNVME DERQLGDPAI FPAVIVEHVP GADILNSYAG LACVEEPNDM
ITESSLDVAE EEIIDDDDDD ITLTVEASCH DGDETIETIE AAEALLNMDS PGPMLDEKRI
NNNIFSSPED DMVVAPVTHV SVTLDGIPEV METQQVQEKY ADSPGASSPE QPKRKKGRKT
KPPRPDSPAT TPNISVKKKN KDGKGNTIYL WEFLLALLQD KATCPKYIKW TQREKGIFKL
VDSKAVSRLW GKHKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK EMPKDLIYIN
DEDPSSSIES SDPSLSSSAT SNRNQTSRSR VSSSPGVKGG ATTVLKPGNS KAAKPKDPVE
VAQPSEVLRT VQPTQSPYPT QLFRTVHVVQ PVQAVPEGEA ARTSTMQDET LNSSVQSIRT
IQAPTQVPVV VSPRNQQLHT VTLQTVPLTT VIASTDPSAG TGSQKFILQA IPSSQPMTVL
KENVMLQSQK AGSPPSIVLG PAQVQQVLTS NVQTICNGTV SVASSPSFSA TAPVVTFSPR
SSQLVAHPPG TVITSVIKTQ ETKTLTQEVE KKESEDHLKE NTEKTEQQPQ PYVMVVSSSN
GFTSQVAMKQ NELLEPNSF
