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 27-MAR-2024, entry version 205. 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; 123. DR DIP; DIP-185N; -. DR ELM; P32519; -. DR IntAct; P32519; 110. DR MINT; P32519; -. DR STRING; 9606.ENSP00000239882; -. DR GlyCosmos; P32519; 19 sites, 2 glycans. DR GlyGen; P32519; 22 sites, 2 O-linked glycans (22 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; 9606-ENSP00000239882; -. DR PeptideAtlas; P32519; -. DR ProteomicsDB; 19727; -. DR ProteomicsDB; 54879; -. [P32519-1] DR Pumba; P32519; -. DR ABCD; P32519; 54 sequenced antibodies. DR Antibodypedia; 906; 438 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 AGR; HGNC:3316; -. 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; DEKRMTT; -. DR OrthoDB; 4245771at2759; -. 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; 27 hits in 1184 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 203 other cell types or tissues. DR ExpressionAtlas; P32519; baseline and differential. 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:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl. 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: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; 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:SF156; ETS-RELATED TRANSCRIPTION FACTOR ELF-1; 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; P32519; HS. 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 //