ID ELF4_HUMAN Reviewed; 663 AA. AC Q99607; D3DTG1; O60435; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 24-JAN-2024, entry version 187. DE RecName: Full=ETS-related transcription factor Elf-4; DE AltName: Full=E74-like factor 4; DE AltName: Full=Myeloid Elf-1-like factor; GN Name=ELF4 {ECO:0000312|EMBL:CAI42882.1}; GN Synonyms=ELFR {ECO:0000312|EMBL:AAC17452.1}, MEF GN {ECO:0000312|EMBL:AAB53693.1}; 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:AAB53693.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Promyelocytic leukemia {ECO:0000269|PubMed:8895518}; RX PubMed=8895518; RA Miyazaki Y., Sun X., Uchida H., Zhang J., Nimer S.; RT "MEF, a novel transcription factor with an Elf-1 like DNA binding domain RT but distinct transcriptional activating properties."; RL Oncogene 13:1721-1729(1996). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC17452.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Ewing sarcoma {ECO:0000269|PubMed:9524226}; 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 [3] {ECO:0000305, ECO:0000312|EMBL:CAI42882.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000312|EMBL:AAH17194.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta {ECO:0000312|EMBL:AAH17194.1}; 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 [6] {ECO:0000305} RP FUNCTION, AND 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 [7] {ECO:0000305} RP FUNCTION, AND INDUCTION. RX PubMed=14625302; DOI=10.1074/jbc.m307524200; RA Hedvat C.V., Yao J., Sokolic R.A., Nimer S.D.; RT "Myeloid ELF1-like factor is a potent activator of interleukin-8 expression RT in hematopoietic cells."; RL J. Biol. Chem. 279:6395-6400(2004). RN [8] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML. RX PubMed=14976184; DOI=10.1074/jbc.m312439200; RA Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T., RA Matsuzaki K., Nakao M., Li J.-D., Kai H.; RT "Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates RT lysozyme transcription in epithelial cells through interaction with RT promyelocytic leukemia protein."; RL J. Biol. Chem. 279:19091-19098(2004). RN [9] RP CHROMOSOMAL TRANSLOCATION WITH ERG. RX PubMed=16303180; DOI=10.1016/j.leukres.2005.10.014; RA Moore S.D., Offor O., Ferry J.A., Amrein P.C., Morton C.C., Dal Cin P.; RT "ELF4 is fused to ERG in a case of acute myeloid leukemia with a RT t(X;21)(q25-26;q22)."; RL Leuk. Res. 30:1037-1042(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-648, 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 [11] RP FUNCTION. RX PubMed=19380490; DOI=10.1128/mcb.01551-08; RA Sashida G., Liu Y., Elf S., Miyata Y., Ohyashiki K., Izumi M., Menendez S., RA Nimer S.D.; RT "ELF4/MEF activates MDM2 expression and blocks oncogene-induced p16 RT activation to promote transformation."; RL Mol. Cell. Biol. 29:3687-3699(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-188 AND SER-641, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [15] RP VARIANT AIFBL2 SER-251, INVOLVEMENT IN AIFBL2, CHARACTERIZATION OF VARIANT RP AIFBL2 SER-251, CHARACTERIZATION OF VARIANTS THR-95; VAL-147; LYS-177; RP ASN-187; THR-345; LEU-368; ILE-382; MET-408; MET-411; VAL-500; LEU-512 AND RP CYS-604, AND FUNCTION. RX PubMed=34326534; DOI=10.1038/s41590-021-00984-4; RA Tyler P.M., Bucklin M.L., Zhao M., Maher T.J., Rice A.J., Ji W., Warner N., RA Pan J., Morotti R., McCarthy P., Griffiths A., van Rossum A.M.C., RA Hollink I.H.I.M., Dalm V.A.S.H., Catanzaro J., Lakhani S.A., Muise A.M., RA Lucas C.L.; RT "Human autoinflammatory disease reveals ELF4 as a transcriptional regulator RT of inflammation."; RL Nat. Immunol. 22:1118-1126(2021). RN [16] RP VARIANT AIFBL2 ARG-231, INVOLVEMENT IN AIFBL2, CHARACTERIZATION OF VARIANT RP AIFBL2 ARG-231, MUTAGENESIS OF LEU-211; TRP-212; LEU-219; PHE-239; TRP-251; RP GLY-252; LYS-255 AND MET-260, AND FUNCTION. RX PubMed=35266071; DOI=10.1007/s10875-022-01243-3; RA Sun G., Qiu L., Yu L., An Y., Ding Y., Zhou L., Wu J., Yang X., Zhang Z., RA Tang X., Xia H., Cao L., You F., Zhao X., Du H.; RT "Loss of Function Mutation in ELF4 Causes Autoinflammatory and RT Immunodeficiency Disease in Human."; RL J. Clin. Immunol. 42:798-810(2022). CC -!- FUNCTION: Transcriptional activator that binds to DNA sequences CC containing the consensus 5'-WGGA-3'. Transactivates promoters of the CC hematopoietic growth factor genes CSF2, IL3, IL8, and of the bovine CC lysozyme gene. Acts synergistically with RUNX1 to transactivate the IL3 CC promoter (By similarity). Transactivates the PRF1 promoter in natural CC killer (NK) cells and CD8+ T cells (PubMed:34326534). Plays a role in CC the development and function of NK and NK T-cells and in innate CC immunity. Controls the proliferation and homing of CD8+ T-cells via the CC Kruppel-like factors KLF4 and KLF2 (By similarity). Controls cell CC senescence in a p53-dependent manner. Can also promote cellular CC transformation through inhibition of the p16 pathway. Is a CC transcriptional regulator of inflammation, controlling T-helper 17 CC (Th17) cells and macrophage inflammatory responses. Required for CC sustained transcription of anti-inflammatory genes, including IL1RN CC (PubMed:34326534, PubMed:35266071). Is a negative regulator of pro- CC inflammatory cytokines expression including IL17A, IL1B, IL6, TNFA and CC CXCL1 (PubMed:34326534, PubMed:35266071). Down-regulates expression of CC TREM1, a cell surface receptor involved in the amplification of CC inflammatory responses (By similarity) (PubMed:34326534, CC PubMed:35266071). {ECO:0000250, ECO:0000269|PubMed:10207087, CC ECO:0000269|PubMed:14625302, ECO:0000269|PubMed:14976184, CC ECO:0000269|PubMed:19380490, ECO:0000269|PubMed:34326534, CC ECO:0000269|PubMed:35266071, ECO:0000269|PubMed:8895518, CC ECO:0000269|PubMed:9524226}. CC -!- SUBUNIT: Interacts with RUNX1 (via the Runt domain); the interaction CC transactivates the IL3 promoter. Interacts (via its C-terminus) with CC PML; the interaction translocates ELF4 to PML nuclear bodies and CC enhances transactivation of LYZ. {ECO:0000269|PubMed:10207087, CC ECO:0000269|PubMed:14976184}. CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:14976184}. CC Note=Accumulation into PML nuclear bodies is mediated by PML. CC -!- TISSUE SPECIFICITY: Abundantly expressed in the placenta and in a CC variety of myeloid leukemia cell lines. Moderate levels of expression CC in heart, lung, spleen, thymus, peripheral blood lymphocytes, ovary and CC colon. Lower levels of expression in Jurkat T-cells and other T-cell CC lines and no expression in brain. {ECO:0000269|PubMed:8895518, CC ECO:0000269|PubMed:9524226}. CC -!- INDUCTION: By ponisterone A in erythroleukemia cells. CC {ECO:0000269|PubMed:14625302}. CC -!- DISEASE: Note=A chromosomal aberration involving ELF4 has been found in CC a case of acute myeloid leukemia (AML). Translocation CC t(X;21)(q25-26;q22) with ERG. {ECO:0000269|PubMed:16303180}. CC -!- DISEASE: Autoinflammatory syndrome, familial, X-linked, Behcet-like 2 CC (AIFBL2) [MIM:301074]: An X-linked recessive, autoinflammatory disorder CC characterized by ulceration of the oral mucosa and skin inflammation. CC Additional variable features may include gastrointestinal ulceration, CC arthritis, recurrent fevers, and iron deficiency anemia. Disease onset CC is in early childhood. {ECO:0000269|PubMed:34326534, CC ECO:0000269|PubMed:35266071}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC17452.1; Type=Frameshift; Evidence={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; U32645; AAB53693.1; -; mRNA. DR EMBL; AF000670; AAC17452.1; ALT_FRAME; mRNA. DR EMBL; AL136450; CAI42882.1; -; Genomic_DNA. DR EMBL; Z81363; CAI42882.1; JOINED; Genomic_DNA. DR EMBL; Z81363; CAI42371.1; -; Genomic_DNA. DR EMBL; AL136450; CAI42371.1; JOINED; Genomic_DNA. DR EMBL; CH471107; EAX11813.1; -; Genomic_DNA. DR EMBL; CH471107; EAX11814.1; -; Genomic_DNA. DR EMBL; BC017194; AAH17194.1; -; mRNA. DR CCDS; CCDS14617.1; -. DR RefSeq; NP_001120669.1; NM_001127197.1. DR RefSeq; NP_001412.1; NM_001421.3. DR RefSeq; XP_005262446.1; XM_005262389.3. DR AlphaFoldDB; Q99607; -. DR SMR; Q99607; -. DR BioGRID; 108315; 112. DR IntAct; Q99607; 106. DR MINT; Q99607; -. DR STRING; 9606.ENSP00000311280; -. DR GlyGen; Q99607; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q99607; -. DR PhosphoSitePlus; Q99607; -. DR BioMuta; ELF4; -. DR DMDM; 68052244; -. DR EPD; Q99607; -. DR jPOST; Q99607; -. DR MassIVE; Q99607; -. DR MaxQB; Q99607; -. DR PaxDb; 9606-ENSP00000311280; -. DR PeptideAtlas; Q99607; -. DR ProteomicsDB; 78352; -. DR Pumba; Q99607; -. DR Antibodypedia; 16200; 476 antibodies from 30 providers. DR DNASU; 2000; -. DR Ensembl; ENST00000308167.10; ENSP00000311280.6; ENSG00000102034.18. DR Ensembl; ENST00000335997.11; ENSP00000338608.7; ENSG00000102034.18. DR GeneID; 2000; -. DR KEGG; hsa:2000; -. DR MANE-Select; ENST00000308167.10; ENSP00000311280.6; NM_001421.4; NP_001412.1. DR UCSC; uc004evd.5; human. DR AGR; HGNC:3319; -. DR CTD; 2000; -. DR DisGeNET; 2000; -. DR GeneCards; ELF4; -. DR HGNC; HGNC:3319; ELF4. DR HPA; ENSG00000102034; Tissue enhanced (bone). DR MalaCards; ELF4; -. DR MIM; 300775; gene. DR MIM; 301074; phenotype. DR neXtProt; NX_Q99607; -. DR OpenTargets; ENSG00000102034; -. DR Orphanet; 476102; Hereditary pediatric Behcet-like disease. DR Orphanet; 632; Short stature due to isolated growth hormone deficiency with X-linked hypogammaglobulinemia. DR PharmGKB; PA27747; -. DR VEuPathDB; HostDB:ENSG00000102034; -. DR eggNOG; KOG3804; Eukaryota. DR GeneTree; ENSGT00940000161870; -. DR HOGENOM; CLU_027279_1_0_1; -. DR InParanoid; Q99607; -. DR OMA; DDQEGHC; -. DR OrthoDB; 4245771at2759; -. DR PhylomeDB; Q99607; -. DR TreeFam; TF318679; -. DR PathwayCommons; Q99607; -. DR SignaLink; Q99607; -. DR SIGNOR; Q99607; -. DR BioGRID-ORCS; 2000; 17 hits in 813 CRISPR screens. DR ChiTaRS; ELF4; human. DR GeneWiki; ELF4; -. DR GenomeRNAi; 2000; -. DR Pharos; Q99607; Tbio. DR PRO; PR:Q99607; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q99607; Protein. DR Bgee; ENSG00000102034; Expressed in endometrium epithelium and 165 other cell types or tissues. DR ExpressionAtlas; Q99607; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. 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:0001787; P:natural killer cell proliferation; ISS:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB. DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:UniProtKB. DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:UniProtKB. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB. DR GO; GO:0001866; P:NK T cell proliferation; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; ETS; 1. DR PANTHER; PTHR11849:SF170; ETS-RELATED TRANSCRIPTION FACTOR ELF-4; 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; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. DR Genevisible; Q99607; HS. PE 1: Evidence at protein level; KW Activator; Chromosomal rearrangement; Disease variant; DNA-binding; KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..663 FT /note="ETS-related transcription factor Elf-4" FT /id="PRO_0000204089" FT DNA_BIND 209..291 FT /note="ETS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237" FT REGION 87..206 FT /note="RUNX1-binding" FT /evidence="ECO:0000269|PubMed:10207087" FT REGION 140..203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 302..353 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 493..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 582..605 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 635..663 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 147..172 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..348 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 25..26 FT /note="Breakpoint for translocation to form ELF4-ERG FT oncogene" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT VARIANT 95 FT /note="A -> T (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs147410657)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087047" FT VARIANT 147 FT /note="A -> V (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs150084985)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087048" FT VARIANT 177 FT /note="R -> K (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs747352505)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087049" FT VARIANT 187 FT /note="T -> N (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs137884184)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087050" FT VARIANT 231 FT /note="W -> R (in AIFBL2; loss of transcriptional activity FT shown in IFNB1 promoter-driven luciferase assay; decreased FT IFNB1 promoter binding; impaired binding to GPR35, GPR162 FT and PLCB2 promoters)" FT /evidence="ECO:0000269|PubMed:35266071" FT /id="VAR_087051" FT VARIANT 251 FT /note="W -> S (in AIFBL2; elevated IL17A expression in FT patient colon biopsies; patient CD8+ T cells have reduced FT PRF1 expression when activated with IL-2 compared to CD8+ T FT cells from a healthy donor; severely decreased FT transcriptional activity shown in IFNB1 promoter-driven FT luciferase assay)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087052" FT VARIANT 345 FT /note="S -> T (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs141440727)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087053" FT VARIANT 368 FT /note="P -> L (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs576980542)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087054" FT VARIANT 382 FT /note="V -> I (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs148953158)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087055" FT VARIANT 408 FT /note="V -> M (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs199975202)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087056" FT VARIANT 411 FT /note="V -> M (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs145786527)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087057" FT VARIANT 500 FT /note="A -> V (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs145281864)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087058" FT VARIANT 512 FT /note="P -> L (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs370055472)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087059" FT VARIANT 604 FT /note="R -> C (no effect on transcriptional activity shown FT in IFNB1 promoter-driven luciferase assay; FT dbSNP:rs141284451)" FT /evidence="ECO:0000269|PubMed:34326534" FT /id="VAR_087060" FT MUTAGEN 211 FT /note="L->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 212 FT /note="W->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 219 FT /note="L->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 239 FT /note="F->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 251 FT /note="W->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay. Loss of INFB1 FT promoter binding. Does not bind GPR35, GPR162 and PLCB2 FT promoters." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 252 FT /note="G->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 255 FT /note="K->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT MUTAGEN 260 FT /note="M->A: Loss of transcriptional activity shown in FT IFNB1 promoter-driven luciferase assay." FT /evidence="ECO:0000269|PubMed:35266071" FT CONFLICT 293..294 FT /note="MP -> IA (in Ref. 2; AAC17452)" FT /evidence="ECO:0000305" FT CONFLICT 499 FT /note="P -> L (in Ref. 2; AAC17452)" FT /evidence="ECO:0000305" SQ SEQUENCE 663 AA; 70730 MW; 1696085D31B09BC5 CRC64; MAITLQPSDL IFEFASNGMD DDIHQLEDPS VFPAVIVEQV PYPDLLHLYS GLELDDVHNG IITDGTLCMT QDQILEGSFL LTDDNEATSH TMSTAEVLLN MESPSDILDE KQIFSTSEML PDSDPAPAVT LPNYLFPASE PDALNRAGDT SDQEGHSLEE KASREESAKK TGKSKKRIRK TKGNRSTSPV TDPSIPIRKK SKDGKGSTIY LWEFLLALLQ DRNTCPKYIK WTQREKGIFK LVDSKAVSKL WGKQKNKPDM NYETMGRALR YYYQRGILAK VEGQRLVYQF KEMPKDLVVI EDEDESSEAT AAPPQASTAS VASASTTRRT SSRVSSRSAP QGKGSSSWEK PKIQHVGLQP SASLELGPSL DEEIPTTSTM LVSPAEGQVK LTKAVSASSV PSNIHLGVAP VGSGSALTLQ TIPLTTVLTN GPPASTTAPT QLVLQSVPAA STFKDTFTLQ ASFPLNASFQ DSQVAAPGAP LILSGLPQLL AGANRPTNPA PPTVTGAGPA GPSSQPPGTV IAAFIRTSGT TAAPRVKEGP LRSSSYVQGM VTGAPMEGLL VPEETLRELL RDQAHLQPLP TQVVSRGSHN PSLLGNQTLS PPSRPTVGLT PVAELELSSG SGSLLMAEPS VTTSGSLLTR SPTPAPFSPF NPTSLIKMEP HDI //