SIN3_YEAST
ID SIN3_YEAST Reviewed; 1536 AA.
AC P22579; D6W263; Q08049;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Transcriptional regulatory protein SIN3;
GN Name=SIN3; Synonyms=CPE1, GAM2, RPD1, SDI1, SDS16, UME4;
GN OrderedLocusNames=YOL004W;
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], AND FUNCTION.
RC STRAIN=S288c / GRF88;
RX PubMed=2233725; DOI=10.1128/mcb.10.11.5927-5936.1990;
RA Wang H., Clark I., Nicholson P.R., Herskowitz I., Stillman D.J.;
RT "The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO,
RT contains four paired amphipathic helix motifs.";
RL Mol. Cell. Biol. 10:5927-5936(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=1944290; DOI=10.1128/mcb.11.12.6306-6316.1991;
RA Vidal M., Strich R., Easton Esposito R., Gaber R.F.;
RT "RPD1 (SIN3/UME4) is required for maximal activation and repression of
RT diverse yeast genes.";
RL Mol. Cell. Biol. 11:6306-6316(1991).
RN [5]
RP FUNCTION.
RX PubMed=1603074; DOI=10.1007/bf00587597;
RA Yoshimoto H., Ohmae M., Yamashita I.;
RT "The Saccharomyces cerevisiae GAM2/SIN3 protein plays a role in both
RT activation and repression of transcription.";
RL Mol. Gen. Genet. 233:327-330(1992).
RN [6]
RP FUNCTION.
RX PubMed=8441414; DOI=10.1128/mcb.13.3.1805-1814.1993;
RA Wang H., Stillman D.J.;
RT "Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA
RT fusion protein.";
RL Mol. Cell. Biol. 13:1805-1814(1993).
RN [7]
RP FUNCTION.
RX PubMed=8978024; DOI=10.1093/genetics/144.4.1343;
RA Vannier D., Balderes D., Shore D.;
RT "Evidence that the transcriptional regulators SIN3 and RPD3, and a novel
RT gene (SDS3) with similar functions, are involved in transcriptional
RT silencing in S. cerevisiae.";
RL Genetics 144:1343-1353(1996).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE RPD3 COMPLEX.
RX PubMed=9234741; DOI=10.1128/mcb.17.8.4852;
RA Kasten M.M., Dorland S., Stillman D.J.;
RT "A large protein complex containing the yeast Sin3p and Rpd3p
RT transcriptional regulators.";
RL Mol. Cell. Biol. 17:4852-4858(1997).
RN [9]
RP INTERACTION WITH STB1.
RX PubMed=9393435; DOI=10.1007/s004380050581;
RA Kasten M.M., Stillman D.J.;
RT "Identification of the Saccharomyces cerevisiae genes STB1-STB5 encoding
RT Sin3p binding proteins.";
RL Mol. Gen. Genet. 256:376-386(1997).
RN [10]
RP FUNCTION OF THE RPD3 COMPLEX.
RX PubMed=9710596; DOI=10.1128/mcb.18.9.5121;
RA Kadosh D., Struhl K.;
RT "Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex
RT generates a highly localized domain of repressed chromatin in vivo.";
RL Mol. Cell. Biol. 18:5121-5127(1998).
RN [11]
RP FUNCTION.
RX PubMed=9572144; DOI=10.1038/33952;
RA Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M.;
RT "Transcriptional repression by UME6 involves deacetylation of lysine 5 of
RT histone H4 by RPD3.";
RL Nature 392:831-835(1998).
RN [12]
RP FUNCTION OF THE RPD3 COMPLEX.
RX PubMed=10388812; DOI=10.1093/genetics/152.3.921;
RA Sun Z.-W., Hampsey M.;
RT "A general requirement for the Sin3-Rpd3 histone deacetylase complex in
RT regulating silencing in Saccharomyces cerevisiae.";
RL Genetics 152:921-932(1999).
RN [13]
RP INTERACTION WITH ESS1.
RX PubMed=10899127; DOI=10.1093/emboj/19.14.3739;
RA Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.;
RT "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-
RT Rpd3 histone deacetylase.";
RL EMBO J. 19:3739-3749(2000).
RN [14]
RP FUNCTION.
RX PubMed=10931932; DOI=10.1093/nar/28.16.3160;
RA Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr.,
RA Lopes J.M.;
RT "Combinatorial regulation of phospholipid biosynthetic gene expression by
RT the UME6, SIN3 and RPD3 genes.";
RL Nucleic Acids Res. 28:3160-3167(2000).
RN [15]
RP FUNCTION, AND INTERACTION WITH UME6.
RX PubMed=11238941; DOI=10.1128/mcb.21.6.2057-2069.2001;
RA Washburn B.K., Easton Esposito R.;
RT "Identification of the Sin3-binding site in Ume6 defines a two-step process
RT for conversion of Ume6 from a transcriptional repressor to an activator in
RT yeast.";
RL Mol. Cell. Biol. 21:2057-2069(2001).
RN [16]
RP IDENTIFICATION IN THE RPD3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12672825; DOI=10.1074/jbc.c300036200;
RA Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A., Cote J.;
RT "Opposite role of yeast ING family members in p53-dependent transcriptional
RT activation.";
RL J. Biol. Chem. 278:19171-19175(2003).
RN [17]
RP FUNCTION OF THE RPD3 COMPLEX.
RX PubMed=12808094; DOI=10.1128/mcb.23.13.4522-4531.2003;
RA Scott K.L., Plon S.E.;
RT "Loss of Sin3/Rpd3 histone deacetylase restores the DNA damage response in
RT checkpoint-deficient strains of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:4522-4531(2003).
RN [18]
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 [19]
RP FUNCTION OF THE RPD3 COMPLEX.
RX PubMed=15141165; DOI=10.1038/sj.emboj.7600233;
RA Schroeder M., Clark R., Liu C.Y., Kaufman R.J.;
RT "The unfolded protein response represses differentiation through the RPD3-
RT SIN3 histone deacetylase.";
RL EMBO J. 23:2281-2292(2004).
RN [20]
RP FUNCTION.
RX PubMed=15143171; DOI=10.1128/mcb.24.11.4769-4780.2004;
RA Aparicio J.G., Viggiani C.J., Gibson D.G., Aparicio O.M.;
RT "The Rpd3-Sin3 histone deacetylase regulates replication timing and enables
RT intra-S origin control in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:4769-4780(2004).
RN [21]
RP FUNCTION OF THE RPD3 COMPLEX.
RX PubMed=14737171; DOI=10.1038/nature02258;
RA De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F.;
RT "The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive
RT genes.";
RL Nature 427:370-374(2004).
RN [22]
RP FUNCTION OF THE RPD3 COMPLEX.
RX PubMed=14711989; DOI=10.1073/pnas.0304797101;
RA Jazayeri A., McAinsh A.D., Jackson S.P.;
RT "Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break
RT repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1644-1649(2004).
RN [23]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA Washburn M.P., Workman J.L.;
RT "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT the Rpd3L complex.";
RL Biochim. Biophys. Acta 1731:77-87(2005).
RN [24]
RP IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND FUNCTION OF THE RPD3C(S) COMPLEX.
RX PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
RA Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
RA Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C.,
RA Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M.,
RA Greenblatt J.F., Buratowski S., Krogan N.J.;
RT "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
RT repressive Rpd3 complex.";
RL Cell 123:593-605(2005).
RN [25]
RP FUNCTION.
RX PubMed=15722108; DOI=10.1016/j.mad.2004.10.007;
RA Kaeberlein M., Kirkland K.T., Fields S., Kennedy B.K.;
RT "Genes determining yeast replicative life span in a long-lived genetic
RT background.";
RL Mech. Ageing Dev. 126:491-504(2005).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-304, AND IDENTIFICATION BY
RP 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303; THR-304; SER-316 AND
RP SER-1046, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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: Catalytic component of the RPD3 histone deacetylase complexes
CC RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine
CC residues on the N-terminal part of the core histones (H2A, H2B, H3 and
CC H4). Histone deacetylation gives a tag for epigenetic repression and
CC plays an important role in transcriptional regulation, cell cycle
CC progression and developmental events. SIN3 has also a RPD3 independent
CC function required for normal longevity. {ECO:0000269|PubMed:10388812,
CC ECO:0000269|PubMed:10931932, ECO:0000269|PubMed:11238941,
CC ECO:0000269|PubMed:12808094, ECO:0000269|PubMed:14711989,
CC ECO:0000269|PubMed:14737171, ECO:0000269|PubMed:15141165,
CC ECO:0000269|PubMed:15143171, ECO:0000269|PubMed:15722108,
CC ECO:0000269|PubMed:1603074, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:1944290, ECO:0000269|PubMed:2233725,
CC ECO:0000269|PubMed:8441414, ECO:0000269|PubMed:8978024,
CC ECO:0000269|PubMed:9234741, ECO:0000269|PubMed:9572144,
CC ECO:0000269|PubMed:9710596}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC Component of the RPD3C(S) complex composed of at least EAF3, RCO1,
CC RPD3, SIN3, and UME1. Interacts with ESS1 and STB1.
CC {ECO:0000269|PubMed:10899127, ECO:0000269|PubMed:11238941,
CC ECO:0000269|PubMed:12672825, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:16314178, ECO:0000269|PubMed:9234741,
CC ECO:0000269|PubMed:9393435}.
CC -!- INTERACTION:
CC P22579; Q12432: EAF3; NbExp=8; IntAct=EBI-17160, EBI-6281;
CC P22579; P21957: OPI1; NbExp=6; IntAct=EBI-17160, EBI-12555;
CC P22579; P32561: RPD3; NbExp=10; IntAct=EBI-17160, EBI-15864;
CC P22579; P22579: SIN3; NbExp=2; IntAct=EBI-17160, EBI-17160;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; M36822; AAA34839.1; -; Genomic_DNA.
DR EMBL; Z74746; CAA99003.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10779.1; -; Genomic_DNA.
DR PIR; S66686; RGBYS3.
DR RefSeq; NP_014639.1; NM_001183258.1.
DR PDB; 6XAW; X-ray; 1.84 A; A=402-473.
DR PDB; 6XDJ; X-ray; 2.20 A; A/B/C/D=402-473.
DR PDBsum; 6XAW; -.
DR PDBsum; 6XDJ; -.
DR AlphaFoldDB; P22579; -.
DR SMR; P22579; -.
DR BioGRID; 34400; 1170.
DR ComplexPortal; CPX-1851; RPD3S histone deacetylase complex.
DR ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR DIP; DIP-597N; -.
DR IntAct; P22579; 87.
DR MINT; P22579; -.
DR STRING; 4932.YOL004W; -.
DR CarbonylDB; P22579; -.
DR iPTMnet; P22579; -.
DR MaxQB; P22579; -.
DR PaxDb; P22579; -.
DR PRIDE; P22579; -.
DR TopDownProteomics; P22579; -.
DR EnsemblFungi; YOL004W_mRNA; YOL004W; YOL004W.
DR GeneID; 854158; -.
DR KEGG; sce:YOL004W; -.
DR SGD; S000005364; SIN3.
DR VEuPathDB; FungiDB:YOL004W; -.
DR eggNOG; KOG4204; Eukaryota.
DR GeneTree; ENSGT00940000171042; -.
DR HOGENOM; CLU_001360_2_1_1; -.
DR InParanoid; P22579; -.
DR OMA; MCEEVIK; -.
DR BioCyc; YEAST:G3O-33421-MON; -.
DR PRO; PR:P22579; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22579; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:SGD.
DR GO; GO:0070822; C:Sin3-type complex; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:SGD.
DR GO; GO:0044804; P:autophagy of nucleus; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0016575; P:histone deacetylation; IMP:SGD.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0051038; P:negative regulation of transcription involved in meiotic cell cycle; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000117; P:regulation of transcription involved in G2/M transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR Gene3D; 1.20.1160.11; -; 3.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cell cycle; Cell division; Chromatin regulator;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1536
FT /note="Transcriptional regulatory protein SIN3"
FT /id="PRO_0000121544"
FT DOMAIN 217..287
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 404..474
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 656..727
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 510
FT /note="Q -> QAQ (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 406..421
FT /evidence="ECO:0007829|PDB:6XAW"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:6XAW"
FT HELIX 426..441
FT /evidence="ECO:0007829|PDB:6XAW"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:6XAW"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6XAW"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:6XAW"
SQ SEQUENCE 1536 AA; 174839 MW; 0834726312B13878 CRC64;
MSQVWHNSNS QSNDVATSND ATGSNERNEK EPSLQGNKPG FVQQQQRITL PSLSALSTKE
EDRRDSNGQQ ALTSHAAHIL GYPPPHSNAM PSIATDSALK QPHEYHPRPK SSSSSPSINA
SLMNAGPAPL PTVGAASFSL SRFDNPLPIK APVHTEEPKS YNGLQEEEKA TQRPQDCKEV
PAGVQPADAP DPSSNHADAN DDNNNNENSH DEDADYRPLN VKDALSYLEQ VKFQFSSRPD
IYNLFLDIMK DFKSQAIDTP GVIERVSTLF RGYPILIQGF NTFLPQGYRI ECSSNPDDPI
RVTTPMGTTT VNNNISPSGR GTTDAQELGS FPESDGNGVQ QPSNVPMVPS SVYQSEQNQD
QQQSLPLLAT SSGLPSIQQP EMPAHRQIPQ SQSLVPQEDA KKNVDVEFSQ AISYVNKIKT
RFADQPDIYK HFLEILQTYQ REQKPINEVY AQVTHLFQNA PDLLEDFKKF LPDSSASANQ
QVQHAQQHAQ QQHEAQMHAQ AQAQAQAQAQ VEQQKQQQQF LYPASGYYGH PSNRGIPQQN
LPPIGSFSPP TNGSTVHEAY QDQQHMQPPH FMPLPSIVQH GPNMVHQGIA NENPPLSDLR
TSLTEQYAPS SIQHQQQHPQ SISPIANTQY GDIPVRPEID LDPSIVPVVP EPTEPIENNI
SLNEEVTFFE KAKRYIGNKH LYTEFLKILN LYSQDILDLD DLVEKVDFYL GSNKELFTWF
KNFVGYQEKT KCIENIVHEK HRLDLDLCEA FGPSYKRLPK SDTFMPCSGR DDMCWEVLND
EWVGHPVWAS EDSGFIAHRK NQYEETLFKI EEERHEYDFY IESNLRTIQC LETIVNKIEN
MTENEKANFK LPPGLGHTSM TIYKKVIRKV YDKERGFEII DALHEHPAVT APVVLKRLKQ
KDEEWRRAQR EWNKVWRELE QKVFFKSLDH LGLTFKQADK KLLTTKQLIS EISSIKVDQT
NKKIHWLTPK PKSQLDFDFP DKNIFYDILC LADTFITHTT AYSNPDKERL KDLLKYFISL
FFSISFEKIE ESLYSHKQNV SESSGSDDGS SIASRKRPYQ QEMSLLDILH RSRYQKLKRS
NDEDGKVPQL SEPPEEEPNT IEEEELIDEE AKNPWLTGNL VEEANSQGII QNRSIFNLFA
NTNIYIFFRH WTTIYERLLE IKQMNERVTK EINTRSTVTF AKDLDLLSSQ LSEMGLDFVG
EDAYKQVLRL SRRLINGDLE HQWFEESLRQ AYNNKAFKLY TIDKVTQSLV KHAHTLMTDA
KTAEIMALFV KDRNASTTSA KDQIIYRLQV RSHMSNTENM FRIEFDKRTL HVSIQYIALD
DLTLKEPKAD EDKWKYYVTS YALPHPTEGI PHEKLKIPFL ERLIEFGQDI DGTEVDEEFS
PEGISVSTLK IKIQPITYQL HIENGSYDVF TRKATNKYPT IANDNTQKGM VSQKKELISK
FLDCAVGLRN NLDEAQKLSM QKKWENLKDS IAKTSAGNQG IESETEKGKI TKQEQSDNLD
SSTASVLPAS ITTVPQDDNI ETTGNTESSD KGAKIQ
