ELF4_HUMAN
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 03-AUG-2022, entry version 179.
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},
GN MEF {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).
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). Also transactivates the PRF1 promoter in
CC natural killer (NK) cells. Plays a role in the development and function
CC of NK and NK T-cells and in innate immunity. Controls the proliferation
CC and homing of CD8+ T-cells via the Kruppel-like factors KLF4 and KLF2
CC (By similarity). Controls cell senescence in a p53-dependent manner.
CC Can also promote cellular transformation through inhibition of the p16
CC pathway. {ECO:0000250, ECO:0000269|PubMed:10207087,
CC ECO:0000269|PubMed:14625302, ECO:0000269|PubMed:14976184,
CC ECO:0000269|PubMed:19380490, 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 t(X;21)(q25-
CC 26;q22) with ERG. {ECO:0000269|PubMed:16303180}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17452.1; Type=Frameshift; Evidence={ECO:0000305};
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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; 109.
DR IntAct; Q99607; 104.
DR STRING; 9606.ENSP00000311280; -.
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; Q99607; -.
DR PeptideAtlas; Q99607; -.
DR PRIDE; Q99607; -.
DR ProteomicsDB; 78352; -.
DR Antibodypedia; 16200; 392 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 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 neXtProt; NX_Q99607; -.
DR OpenTargets; ENSG00000102034; -.
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; IVEQLPC; -.
DR OrthoDB; 837296at2759; -.
DR PhylomeDB; Q99607; -.
DR TreeFam; TF318679; -.
DR PathwayCommons; Q99607; -.
DR SignaLink; Q99607; -.
DR SIGNOR; Q99607; -.
DR BioGRID-ORCS; 2000; 16 hits in 730 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 163 other tissues.
DR ExpressionAtlas; Q99607; baseline and differential.
DR Genevisible; Q99607; HS.
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:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR GO; GO:0001787; P:natural killer cell proliferation; ISS:UniProtKB.
DR GO; GO:0001866; P:NK T cell proliferation; ISS:UniProtKB.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR033070; Elf4.
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 PANTHER; PTHR11849:SF170; PTHR11849:SF170; 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; Chromosomal rearrangement; DNA-binding; Nucleus; Phosphoprotein;
KW 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 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
