ID CYC8_YEAST Reviewed; 966 AA. AC P14922; D6VQB2; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 04-NOV-2026, entry version 243. DE RecName: Full=General transcriptional corepressor CYC8; DE AltName: Full=Glucose repression mediator protein CYC8; GN Name=CYC8; Synonyms=CRT8, SSN6; OrderedLocusNames=YBR112C; GN ORFNames=YBR0908; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2854095; DOI=10.1016/0378-1119(88)90316-2; RA Trumbly R.J.; RT "Cloning and characterization of the CYC8 gene mediating glucose repression RT in yeast."; RL Gene 73:97-111(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3316983; DOI=10.1128/mcb.7.10.3637-3645.1987; RA Schultz J., Carlson M.; RT "Molecular analysis of SSN6, a gene functionally related to the SNF1 RT protein kinase of Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 7:3637-3645(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1626431; DOI=10.1002/yea.320080507; RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.; RT "Molecular analysis of yeast chromosome II between CMD1 and LYS2: the RT excision repair gene RAD16 located in this region belongs to a novel group RT of double-finger proteins."; RL Yeast 8:397-408(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP DOMAINS TPR REPEATS. RX PubMed=2404612; DOI=10.1016/0092-8674(90)90745-z; RA Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.; RT "A repeating amino acid motif in CDC23 defines a family of proteins and a RT new relationship among genes required for mitosis and RNA synthesis."; RL Cell 60:307-317(1990). RN [7] RP INTERACTION WITH MATALPHA2. RX PubMed=7498787; DOI=10.1101/gad.9.23.2903; RA Smith R.L., Redd M.J., Johnson A.D.; RT "The tetratricopeptide repeats of Ssn6 interact with the homeo domain of RT alpha 2."; RL Genes Dev. 9:2903-2910(1995). RN [8] RP INTERACTION WITH MIG1. RX PubMed=7724528; DOI=10.1073/pnas.92.8.3132; RA Treitel M.A., Carlson M.; RT "Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3132-3136(1995). RN [9] RP SUBUNIT. RX PubMed=8943325; DOI=10.1128/mcb.16.12.6707; RA Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.; RT "The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four RT Tup1 subunits."; RL Mol. Cell. Biol. 16:6707-6714(1996). RN [10] RP INTERACTION WITH RFX1. RX PubMed=9741624; DOI=10.1016/s0092-8674(00)81601-3; RA Huang M., Zhou Z., Elledge S.J.; RT "The DNA replication and damage checkpoint pathways induce transcription by RT inhibition of the Crt1 repressor."; RL Cell 94:595-605(1998). RN [11] RP INTERACTION WITH TUP1; HOS2 AND RPD3, AND FUNCTION OF THE CYC8-TUP1 RP COMPLEX. RX PubMed=11069890; DOI=10.1101/gad.829100; RA Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., RA Stillman D.J., Roth S.Y.; RT "Ssn6-Tup1 interacts with class I histone deacetylases required for RT repression."; RL Genes Dev. 14:2737-2744(2000). RN [12] RP INTERACTION WITH PGD1, AND FUNCTION OF THE CYC8-TUP1 COMPLEX. RX PubMed=10722672; DOI=10.1074/jbc.275.12.8397; RA Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.; RT "Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II RT holoenzyme."; RL J. Biol. Chem. 275:8397-8403(2000). RN [13] RP INTERACTION WITH MATALPHA2. RX PubMed=10759558; DOI=10.1073/pnas.070506797; RA Smith R.L., Johnson A.D.; RT "A sequence resembling a peroxisomal targeting sequence directs the RT interaction between the tetratricopeptide repeats of Ssn6 and the RT homeodomain of alpha 2."; RL Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000). RN [14] RP FUNCTION OF THE CYC8-TUP1 COMPLEX. RX PubMed=11230135; DOI=10.1093/emboj/20.5.1123; RA Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.; RT "Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in RT response to osmotic stress."; RL EMBO J. 20:1123-1133(2001). RN [15] RP INTERACTION WITH SUT1. RX PubMed=11401714; DOI=10.1046/j.1365-2958.2001.02450.x; RA Regnacq M., Alimardani P., El Moudni B., Berges T.; RT "SUT1p interaction with Cyc8p(Ssn6p) relieves hypoxic genes from Cyc8p- RT Tup1p repression in Saccharomyces cerevisiae."; RL Mol. Microbiol. 40:1085-1096(2001). RN [16] RP INTERACTION WITH CTI6. RX PubMed=12086626; DOI=10.1016/s1097-2765(02)00545-2; RA Papamichos-Chronakis M., Petrakis T., Ktistaki E., Topalidou I., RA Tzamarias D.; RT "Cti6, a PHD domain protein, bridges the Cyc8-Tup1 corepressor and the SAGA RT coactivator to overcome repression at GAL1."; RL Mol. Cell 9:1297-1305(2002). RN [17] RP INTERACTION WITH HOS1; HOS2 AND RPD3. RX PubMed=14525981; DOI=10.1074/jbc.m309753200; RA Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.; RT "Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo."; RL J. Biol. Chem. 278:50158-50162(2003). RN [18] RP FUNCTION OF THE CYC8-TUP1 COREPRESSOR COMPLEX. RX PubMed=11784848; DOI=10.1128/mcb.22.3.693-703.2002; RA Davie J.K., Trumbly R.J., Dent S.Y.; RT "Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo."; RL Mol. Cell. Biol. 22:693-703(2002). RN [19] RP FUNCTION OF THE CYC8-TUP1 COMPLEX. RX PubMed=14665463; DOI=10.1128/ec.2.6.1288-1303.2003; RA Mennella T.A., Klinkenberg L.G., Zitomer R.S.; RT "Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent RT exclusion of TATA binding protein."; RL Eukaryot. Cell 2:1288-1303(2003). RN [20] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; SER-817 AND SER-943, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-475; SER-768; RP SER-866 AND SER-943, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [24] RP PRION FORMATION. RX PubMed=19219034; DOI=10.1038/ncb1843; RA Patel B.K., Gavin-Smyth J., Liebman S.W.; RT "The yeast global transcriptional co-repressor protein Cyc8 can propagate RT as a prion."; RL Nat. Cell Biol. 11:344-349(2009). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-741; SER-815; RP SER-817 AND SER-943, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Acts as a component of the CYC8-TUP1 corepressor complex CC which is involved in the repression of many genes in a wide variety of CC physiological processes including heme-regulated and catabolite CC repressed genes. May also be involved in the derepression of at least CC some target genes. The complex is recruited to target genes by CC interaction with DNA-bound transcriptional repressors, like MATALPHA2, CC MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to CC produce a repressive chromatin structure, interacts with hypoacetylated CC N-terminal tails of histones H3 and H4 that have been programmed for CC repression by the action of histone deacetylases and interferes CC directly with the transcriptional machinery by associating with the RNA CC polymerase II mediator complex. {ECO:0000269|PubMed:10722672, CC ECO:0000269|PubMed:11069890, ECO:0000269|PubMed:11230135, CC ECO:0000269|PubMed:11784848, ECO:0000269|PubMed:14665463}. CC -!- SUBUNIT: Associates with TUP1 to form the CYC8-TUP1 (or TUP1-SSN6) CC corepressor complex that is composed of 4 copies of TUP1 and one copy CC of CYC8. Interacts with MATALPHA2, CTI6, MIG1, TUP1, SUT1, RFX1, PGD1, CC HOS1, HOS2 and RPD3. {ECO:0000269|PubMed:10722672, CC ECO:0000269|PubMed:10759558, ECO:0000269|PubMed:11069890, CC ECO:0000269|PubMed:11401714, ECO:0000269|PubMed:12086626, CC ECO:0000269|PubMed:14525981, ECO:0000269|PubMed:7498787, CC ECO:0000269|PubMed:7724528, ECO:0000269|PubMed:8943325, CC ECO:0000269|PubMed:9741624}. CC -!- INTERACTION: CC P14922; P53096: HOS2; NbExp=4; IntAct=EBI-18215, EBI-8475; CC P14922; P40356: PGD1; NbExp=3; IntAct=EBI-18215, EBI-13268; CC P14922; P48743: RFX1; NbExp=2; IntAct=EBI-18215, EBI-15036; CC P14922; P32561: RPD3; NbExp=6; IntAct=EBI-18215, EBI-15864; CC P14922; P16649: TUP1; NbExp=7; IntAct=EBI-18215, EBI-19654; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is CC unstructured in its native, soluble form, and which forms a parallel CC in-register beta-sheet in its amyloid form. {ECO:0000250}. CC -!- MISCELLANEOUS: [OCT+] is the prion form of CYC8. [OCT+] is the result CC of a conformational change of the cellular CYC8 protein that becomes CC self-propagating and infectious. [OCT+]-aggregates sequester soluble CC CYC8, resulting in increased levels of iso-2-cytochrome c, defects in CC sporulation and mating, higher levels of invertase derepression and CC increased flocculation, reminiscent of a partial loss of function of CC the CYC8-TUP1 corepressor complex. [OCT+] can be cured by GdnHCl and by CC inactivation of the molecular chaperone HSP104, which is required for CC [OCT+] propagation. It is speculated that prion properties of CC transcription factors may generate an optimized phenotypic CC heterogeneity that buffers yeast populations against diverse CC environmental insults. {ECO:0000305|PubMed:19219034}. CC -!- MISCELLANEOUS: Present with 3890 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the CYC8/SSN6 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; M23440; AAA34545.1; -; Genomic_DNA. DR EMBL; M17826; AAA35103.1; -; Genomic_DNA. DR EMBL; X66247; CAA46973.1; -; Genomic_DNA. DR EMBL; X78993; CAA55615.1; -; Genomic_DNA. DR EMBL; Z35981; CAA85069.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07232.1; -; Genomic_DNA. DR PIR; S25365; S25365. DR RefSeq; NP_009670.3; NM_001178460.3. DR AlphaFoldDB; P14922; -. DR SMR; P14922; -. DR BioGRID; 32816; 203. DR ComplexPortal; CPX-1663; CYC8-TUP1 corepressor complex. DR DIP; DIP-696N; -. DR FunCoup; P14922; 561. DR IntAct; P14922; 13. DR STRING; 4932.YBR112C; -. DR GlyCosmos; P14922; 2 sites, 1 glycan. DR GlyGen; P14922; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P14922; -. DR PaxDb; 4932-YBR112C; -. DR PeptideAtlas; P14922; -. DR EnsemblFungi; YBR112C_mRNA; YBR112C; YBR112C. DR GeneID; 852410; -. DR KEGG; sce:YBR112C; -. DR AGR; SGD:S000000316; -. DR SGD; S000000316; CYC8. DR VEuPathDB; FungiDB:YBR112C; -. DR eggNOG; KOG1124; Eukaryota. DR HOGENOM; CLU_006762_3_0_1; -. DR InParanoid; P14922; -. DR OMA; AEHAWRM; -. DR OrthoDB; 418911at2759; -. DR BioCyc; YEAST:G3O-29073-MONOMER; -. DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence. DR BioGRID-ORCS; 852410; 7 hits in 10 CRISPR screens. DR PRO; PR:P14922; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P14922; protein. DR GO; GO:0160051; C:Cyc8(Ssn6)-Tup1 general repressor complex; IPI:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0017053; C:transcription repressor complex; IPI:SGD. DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central. DR GO; GO:0042826; F:histone deacetylase binding; IDA:SGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD. DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD. DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD. DR GO; GO:0006972; P:hyperosmotic response; IDA:ComplexPortal. DR GO; GO:0000278; P:mitotic cell cycle; IMP:SGD. DR GO; GO:2000879; P:negative regulation of dipeptide transport; IMP:SGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD. DR FunFam; 1.25.40.10:FF:001929; Cyc8p; 1. DR FunFam; 1.25.40.10:FF:000078; Transcriptional corepressor Cyc8; 1. DR FunFam; 1.25.40.10:FF:000163; Transcriptional corepressor Cyc8; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR14017:SF1; LD02225P; 1. DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1. DR Pfam; PF00515; TPR_1; 1. DR Pfam; PF13432; TPR_16; 1. DR Pfam; PF13176; TPR_7; 1. DR SMART; SM00028; TPR; 10. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50005; TPR; 9. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Amyloid; Nucleus; Phosphoprotein; Prion; Reference proteome; Repeat; KW Repressor; TPR repeat; Transcription; Transcription regulation. FT CHAIN 1..966 FT /note="General transcriptional corepressor CYC8" FT /id="PRO_0000106327" FT REPEAT 46..79 FT /note="TPR 1" FT REPEAT 80..113 FT /note="TPR 2" FT REPEAT 114..147 FT /note="TPR 3" FT REPEAT 150..183 FT /note="TPR 4" FT REPEAT 187..220 FT /note="TPR 5" FT REPEAT 224..257 FT /note="TPR 6" FT REPEAT 262..295 FT /note="TPR 7" FT REPEAT 296..329 FT /note="TPR 8" FT REPEAT 330..363 FT /note="TPR 9" FT REPEAT 364..398 FT /note="TPR 10" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 412..489 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 467..682 FT /note="Prion domain (PrD)" FT REGION 631..666 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 699..723 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 759..966 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..36 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 412..429 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 439..489 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 637..666 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 699..713 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 759..780 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 797..808 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 814..823 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 826..843 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..860 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 870..880 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 882..896 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 897..906 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 924..936 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 940..950 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 429 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 475 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 710 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 741 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 768 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 815 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 817 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 866 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 943 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CONFLICT 547 FT /note="Q -> K (in Ref. 1; AAA34545 and 2; AAA35103)" FT /evidence="ECO:0000305" SQ SEQUENCE 966 AA; 107202 MW; FC2D0D0C1B181207 CRC64; MNPGGEQTIM EQPAQQQQQQ QQQQQQQQQQ AAVPQQPLDP LTQSTAETWL SIASLAETLG DGDRAAMAYD ATLQFNPSSA KALTSLAHLY RSRDMFQRAA ELYERALLVN PELSDVWATL GHCYLMLDDL QRAYNAYQQA LYHLSNPNVP KLWHGIGILY DRYGSLDYAE EAFAKVLELD PHFEKANEIY FRLGIIYKHQ GKWSQALECF RYILPQPPAP LQEWDIWFQL GSVLESMGEW QGAKEAYEHV LAQNQHHAKV LQQLGCLYGM SNVQFYDPQK ALDYLLKSLE ADPSDATTWY HLGRVHMIRT DYTAAYDAFQ QAVNRDSRNP IFWCSIGVLY YQISQYRDAL DAYTRAIRLN PYISEVWYDL GTLYETCNNQ LSDALDAYKQ AARLDVNNVH IRERLEALTK QLENPGNINK SNGAPTNASP APPPVILQPT LQPNDQGNPL NTRISAQSAN ATASMVQQQH PAQQTPINSS ATMYSNGASP QLQAQAQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAHAQA QAQAQAQAQA QAQAQAQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLQP LPRQQLQQKG VSVQMLNPQQ GQPYITQPTV IQAHQLQPFS TQAMEHPQSS QLPPQQQQLQ SVQHPQQLQG QPQAQAPQPL IQHNVEQNVL PQKRYMEGAI HTLVDAAVSS STHTENNTKS PRQPTHAIPT QAPATGITNA EPQVKKQKLN SPNSNINKLV NTATSIEENA KSEVSNQSPA VVESNTNNTS QEEKPVKANS IPSVIGAQEP PQEASPAEEA TKAASVSPST KPLNTEPESS SVQPTVSSES STTKANDQST AETIELSTAT VPAEASPVED EVRQHSKEEN GTTEASAPST EEAEPAASRD AEKQQDETAA TTITVIKPTL ETMETVKEEA KMREEEQTSQ EKSPQENTLP RENVVRQVEE DENYDD //