ID   ICE1_HUMAN              Reviewed;        2266 AA.
AC   Q9Y2F5; Q68DE1; Q6ZT40; Q7L587; Q7Z3A9; Q9NTH9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 5.
DT   24-JUL-2024, entry version 147.
DE   RecName: Full=Little elongation complex subunit 1;
DE   AltName: Full=Interactor of little elongator complex ELL subunit 1;
GN   Name=ICE1; Synonyms=KIAA0947;
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 [LARGE SCALE MRNA], AND VARIANTS SER-391 AND ILE-901.
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1090, AND VARIANTS SER-391 AND
RP   ILE-901.
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-2266, AND VARIANT ILE-901.
RC   TISSUE=Amygdala, and 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1746-2266.
RC   TISSUE=Uterus;
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-1692; SER-1697;
RP   SER-1699; SER-1701 AND SER-1903, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-958; THR-1642;
RP   SER-1854 AND SER-1903, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1218, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588 AND SER-1854, AND
RP   IDENTIFICATION BY 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   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, AND
RP   INTERACTION WITH ELL.
RX   PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA   Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA   Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA   Eissenberg J.C., Shilatifard A.;
RT   "The little elongation complex regulates small nuclear RNA transcription.";
RL   Mol. Cell 44:954-965(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1854, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-533; SER-558;
RP   SER-589; SER-925; SER-1692; SER-1697; SER-1699; SER-1712; SER-1838;
RP   SER-1854 AND SER-1903, 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   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, AND
RP   INTERACTION WITH ELL; ICE2 AND ZC3H8.
RX   PubMed=23932780; DOI=10.1016/j.molcel.2013.07.003;
RA   Hu D., Smith E.R., Garruss A.S., Mohaghegh N., Varberg J.M., Lin C.,
RA   Jackson J., Gao X., Saraf A., Florens L., Washburn M.P., Eissenberg J.C.,
RA   Shilatifard A.;
RT   "The little elongation complex functions at initiation and elongation
RT   phases of snRNA gene transcription.";
RL   Mol. Cell 51:493-505(2013).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-832 AND SER-1903, AND
RP   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: Component of the little elongation complex (LEC), a complex
CC       required to regulate small nuclear RNA (snRNA) gene transcription by
CC       RNA polymerase II and III (PubMed:22195968, PubMed:23932780).
CC       Specifically acts as a scaffold protein that promotes the LEC complex
CC       formation and recruitment and RNA polymerase II occupancy at snRNA
CC       genes in subnuclear bodies (PubMed:23932780).
CC       {ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780}.
CC   -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC       composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts
CC       (via N-terminus domain) with ELL. Interacts (via C-terminus domain)
CC       with ICE2 and ZC3H8. {ECO:0000269|PubMed:22195968,
CC       ECO:0000269|PubMed:23932780}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22195968,
CC       ECO:0000269|PubMed:23932780}. Nucleus, Cajal body
CC       {ECO:0000269|PubMed:23932780}. Note=Colocalizes with COIL in subnuclear
CC       Cajal and histone locus bodies. Associates to transcriptionally active
CC       chromatin at snRNA genes. {ECO:0000269|PubMed:23932780}.
CC   -!- DOMAIN: The N-termimus domain is necessary and sufficient for its
CC       targeting to subnuclear cajal and histone locus bodies.
CC       {ECO:0000269|PubMed:22195968}.
CC   -!- SIMILARITY: Belongs to the ICE1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76791.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC86755.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=CAB70661.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB70661.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB023164; BAA76791.3; ALT_INIT; mRNA.
DR   EMBL; AC010253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK126937; BAC86755.1; ALT_SEQ; mRNA.
DR   EMBL; AL137260; CAB70661.1; ALT_SEQ; mRNA.
DR   EMBL; BX538020; CAD97966.1; -; mRNA.
DR   EMBL; CR749441; CAH18279.1; -; mRNA.
DR   EMBL; BC004902; AAH04902.2; -; mRNA.
DR   CCDS; CCDS47187.1; -.
DR   PIR; T46331; T46331.
DR   RefSeq; NP_056140.1; NM_015325.2.
DR   AlphaFoldDB; Q9Y2F5; -.
DR   SMR; Q9Y2F5; -.
DR   BioGRID; 116955; 53.
DR   ComplexPortal; CPX-2712; Little elongation complex, ELL variant.
DR   ComplexPortal; CPX-2713; Little elongation complex, ELL2 variant.
DR   ComplexPortal; CPX-2714; Little elongation complex, ELL3 variant.
DR   IntAct; Q9Y2F5; 23.
DR   STRING; 9606.ENSP00000296564; -.
DR   GlyGen; Q9Y2F5; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9Y2F5; -.
DR   PhosphoSitePlus; Q9Y2F5; -.
DR   BioMuta; ICE1; -.
DR   DMDM; 296439500; -.
DR   jPOST; Q9Y2F5; -.
DR   MassIVE; Q9Y2F5; -.
DR   PaxDb; 9606-ENSP00000296564; -.
DR   PeptideAtlas; Q9Y2F5; -.
DR   ProteomicsDB; 85753; -.
DR   Pumba; Q9Y2F5; -.
DR   Antibodypedia; 64954; 42 antibodies from 9 providers.
DR   Ensembl; ENST00000296564.9; ENSP00000296564.7; ENSG00000164151.12.
DR   GeneID; 23379; -.
DR   KEGG; hsa:23379; -.
DR   MANE-Select; ENST00000296564.9; ENSP00000296564.7; NM_015325.3; NP_056140.1.
DR   UCSC; uc003jdm.6; human.
DR   AGR; HGNC:29154; -.
DR   CTD; 23379; -.
DR   DisGeNET; 23379; -.
DR   GeneCards; ICE1; -.
DR   HGNC; HGNC:29154; ICE1.
DR   HPA; ENSG00000164151; Low tissue specificity.
DR   MIM; 617958; gene.
DR   neXtProt; NX_Q9Y2F5; -.
DR   OpenTargets; ENSG00000164151; -.
DR   PharmGKB; PA162411094; -.
DR   VEuPathDB; HostDB:ENSG00000164151; -.
DR   eggNOG; ENOG502QX8H; Eukaryota.
DR   GeneTree; ENSGT00950000183199; -.
DR   HOGENOM; CLU_001630_0_0_1; -.
DR   InParanoid; Q9Y2F5; -.
DR   OMA; YCYTGIR; -.
DR   OrthoDB; 5309998at2759; -.
DR   PhylomeDB; Q9Y2F5; -.
DR   TreeFam; TF330760; -.
DR   PathwayCommons; Q9Y2F5; -.
DR   Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR   SignaLink; Q9Y2F5; -.
DR   SIGNOR; Q9Y2F5; -.
DR   BioGRID-ORCS; 23379; 561 hits in 1092 CRISPR screens.
DR   ChiTaRS; ICE1; human.
DR   GenomeRNAi; 23379; -.
DR   Pharos; Q9Y2F5; Tbio.
DR   PRO; PR:Q9Y2F5; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y2F5; Protein.
DR   Bgee; ENSG00000164151; Expressed in sural nerve and 212 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2F5; baseline and differential.
DR   GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR   GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR   GO; GO:0035363; C:histone locus body; IDA:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IMP:UniProtKB.
DR   PANTHER; PTHR11852:SF4; LITTLE ELONGATION COMPLEX SUBUNIT 1; 1.
DR   PANTHER; PTHR11852; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..2266
FT                   /note="Little elongation complex subunit 1"
FT                   /id="PRO_0000295724"
FT   REGION          223..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          925..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1295..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1467..1510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1543..1707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1809..1902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          23..186
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        936..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1295..1349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1481..1508
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1563..1621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1644..1668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1676..1700
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1809..1847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1881..1902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         707
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q286"
FT   MOD_RES         832
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         925
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         958
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1218
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q286"
FT   MOD_RES         1642
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1692
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1697
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1699
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1701
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1854
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1903
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   VARIANT         391
FT                   /note="C -> S (in dbSNP:rs2619844)"
FT                   /evidence="ECO:0000269|PubMed:10231032,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_033341"
FT   VARIANT         596
FT                   /note="K -> E (in dbSNP:rs10475299)"
FT                   /id="VAR_033342"
FT   VARIANT         901
FT                   /note="V -> I (in dbSNP:rs2578500)"
FT                   /evidence="ECO:0000269|PubMed:10231032,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_033343"
FT   VARIANT         1054
FT                   /note="T -> A (in dbSNP:rs3806873)"
FT                   /id="VAR_033344"
FT   VARIANT         1058
FT                   /note="G -> D (in dbSNP:rs3806874)"
FT                   /id="VAR_033345"
FT   VARIANT         1597
FT                   /note="Q -> P (in dbSNP:rs10065646)"
FT                   /id="VAR_033346"
FT   VARIANT         1618
FT                   /note="P -> L (in dbSNP:rs3747731)"
FT                   /id="VAR_055943"
FT   CONFLICT        465
FT                   /note="T -> S (in Ref. 4; BAC86755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        757
FT                   /note="P -> G (in Ref. 5; CAD97966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        821
FT                   /note="K -> R (in Ref. 5; CAH18279)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1112
FT                   /note="E -> V (in Ref. 5; CAH18279)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1186
FT                   /note="D -> G (in Ref. 5; CAD97966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1756
FT                   /note="Y -> F (in Ref. 5; CAD97966)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2266 AA;  247891 MW;  69EC121F4543B92D CRC64;
     MMPGETHSAA PGTAADLSRC QGCASLQQNL NEYVEALITL KQKIINTDNL LTEYQKKCDE
     LQFARRENSN LHHQVEEMLQ KISPLQKCQE ELGSLKAELE EKKSSLKLYQ DTHQEYARVK
     EECLKSDAQK KKLEAKVKKL QEAAVKQTQD FKQLRNEKKI LEKEFKKTQE RLDEFSKQKN
     EKELRHIGTQ ISSDSYGSID KRKVKLLLKE LWLCVNTTHR LPGEGSRCVP EKPAKAITSS
     RVPGEDGTLP PTQGSPLRTS NVQTCLTKLS MEIKEDFLCQ NVEKQSSSGT NCSSDHVFNE
     NGNLEVLVQS HRDGGSTEFV DHDHFFDEDL QAAIDFFKLP PPLLSPVPSP PPMSSPHPGS
     LPSSFAPETY FGEYTDSSDN DSVQLRNSAE CVSEDDTTES QNYFGSLRKN KGSGTWEEKP
     KSHEAIQALN TWEVNKVTTS GLETFTATLR ESSATHSLVG EKHWTTASRS MSDRKRDILH
     ETKTQMEVRE MDKSVQTEKT IHKLTRGLCI ERLSASPAQE KEAAPGKSEL CSSPLGKRPL
     NELMESEGKT VLSKMMGSPK SEFTKWTRIN EITSEPDRIT VSGHFHRLSR ELEKEKEDTQ
     GFTLGESPES EDDDSGDGMD VAGLDIETSF SSSSTLVALS VGSNPQSSSG LDCGNDTDIT
     TKVFSTEPHH SEHKLQTKTL NTLHLQSEPP ECSIGGNNLE NSLCALSPEL GASNFNDQKS
     SGIEYTKVVK GLTKIHSLPR SVFMKATKDG QCESQDPRIE LTLNKPDFTS LIGSQAALIK
     SGLGFVKSTS WHHSDLLRKG GEESLRAKSE HEQKTSHQLQ KAMPFLQNRG PTPKPDLLRE
     NNNPVEFKTT ASVLPNQVSV ITKQTRPEKV QSAKLEHLRP HRVEPTLVTE NSGNKTGMST
     VAKCDGERDD TTQNITEVAA VKSISPEVSA SRRKLDFNSP GGSSPVENSD CSTNSRLSFS
     PENILIQNQD IVREAAVQGD GQKQRQPQAT DLDSSGTHGS EMLPATEVTV SGGFSVEETS
     CGDTGRSGGE ALAVANDSTS TPQNANGLWK LKSTTPGGAL PECFGTTDTT FSSAFCRKHG
     ETQDTSQSSL PGTLHCYTGI REGGDDTEVE SEAFSCSEGS EQQDAPDDSQ KNLGDTDAAV
     AEVRPSLEVG YLTSALQDFN ISTFSELDRL STSEVVMFLE SCQLGDYSSG DSVSECSSKG
     TLSKEMNKEL KASEIGEKYR KQPCEEETLG TCEEWIESEE DDYSLKNTSQ LTQCSLETLS
     EVLTKIRQEL QTNSEDCNGK DTGSLLLLNV NNNMTTENLK EKSPFRETTG SSSHASEPTP
     QAAALDTEGS SPISGMPQNE NPQSRPEARS DAGRQTDGGE EDLPEPVEPS ALCSDSVMEP
     SIEQSSNCEA ETTFQCQIAT VTSEVINVLI NKDQNLVIEK GDNWTIISGV AVLPHVDQVT
     LCDIPGDIPI SQDQGELEAG CIPVTSAEKS PEASHTGPAF QEAPCGNNLS CPQEDVSSSG
     QSTNFDKSRL RNRPVKPSIW ISSQIYDQNF ETQIVASDHT YYNSKLEPSG KNKNRSKISN
     KDQSNKPVKT SASSRVETHQ SEVAQSFSGE KANTKTQRSQ TQTILANADT STPTDCSPDT
     LSKIRQEVGP PLPPLLAPLI ATPPRTSQPL SPLISSSSPS SPASPVGQVS PFRETPVPPA
     MSPWPEDPRR ASPPDPSPSP SAASASERVV PSPLQFCAAT PKHALPVPGR LPPCASGHAA
     VGGPQENSVK ILDTMYPELS ARARTLNILK GNIQLTRGPP ADCKNLPGPA SAMIGFKTIT
     SAATAFVKTG SSSGGDCNQD KSRDLGTQQD SSGKRTLSTS TLRSAKRLRL DTGSPEPETR
     GVTAEGIHKN LPGNLPPAEV ATTNEERSCS SPAVSAVSQL PLSPKETVES HDKAIANALK
     KIAEFSFDLL PVIRSHVYVG NISKKPVMRD QEKEVVYEFS TTKKHLAECL LHSILSELKI
     QKISMDHNYI HALCRVYVGI CRQLGDLERA RLFCYSLLKE DFPESEKLTL FIANMWHDIF
     LSQSVINKAM QLVARQRAKG EVLNCLRAFL NWEKNAPVDV GFMVSKLLLT IQLCPKTEFQ
     PSEKFGEDLS DNTWEYIFAI DLLCCHQKWI WTHDNIISKE LWPVMDKWIK YRKGHANIAY
     TPDIIIASIL RLIGRLGQLG LKEGFPSAVK NISSVIGMFI QHAHDEDIPW GIQLAAVYAL
     CDLSPSNPAE ISKILEAWRR EASKSVPSAI VSCLEEVSAL STEELG
//