ICE1_HUMAN
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 03-AUG-2022, entry version 136.
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};
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; 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; 44.
DR IntAct; Q9Y2F5; 24.
DR MINT; Q9Y2F5; -.
DR STRING; 9606.ENSP00000296564; -.
DR GlyGen; Q9Y2F5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2F5; -.
DR PhosphoSitePlus; Q9Y2F5; -.
DR BioMuta; ICE1; -.
DR DMDM; 296439500; -.
DR EPD; Q9Y2F5; -.
DR jPOST; Q9Y2F5; -.
DR MassIVE; Q9Y2F5; -.
DR MaxQB; Q9Y2F5; -.
DR PaxDb; Q9Y2F5; -.
DR PeptideAtlas; Q9Y2F5; -.
DR PRIDE; Q9Y2F5; -.
DR ProteomicsDB; 85753; -.
DR Antibodypedia; 64954; 46 antibodies from 10 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 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; DHWTIIN; -.
DR OrthoDB; 265329at2759; -.
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; 554 hits in 1031 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 210 other tissues.
DR ExpressionAtlas; Q9Y2F5; baseline and differential.
DR Genevisible; Q9Y2F5; HS.
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.
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
