CYC8_YEAST
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 03-AUG-2022, entry version 224.
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 component of the CYC8-TUP1 corepressor complex which
CC 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=6; 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}.
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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; 176.
DR ComplexPortal; CPX-1663; CYP8-TUP1 corepressor complex.
DR DIP; DIP-696N; -.
DR IntAct; P14922; 10.
DR MINT; P14922; -.
DR STRING; 4932.YBR112C; -.
DR iPTMnet; P14922; -.
DR MaxQB; P14922; -.
DR PaxDb; P14922; -.
DR PRIDE; P14922; -.
DR EnsemblFungi; YBR112C_mRNA; YBR112C; YBR112C.
DR GeneID; 852410; -.
DR KEGG; sce:YBR112C; -.
DR SGD; S000000316; CYC8.
DR VEuPathDB; FungiDB:YBR112C; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000168210; -.
DR HOGENOM; CLU_006762_3_0_1; -.
DR InParanoid; P14922; -.
DR OMA; YLGRVEM; -.
DR BioCyc; YEAST:G3O-29073-MON; -.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-3214842; HDMs demethylate histones.
DR PRO; PR:P14922; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P14922; protein.
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; IGI:SGD.
DR GO; GO:0006972; P:hyperosmotic response; IDA:ComplexPortal.
DR GO; GO:1900191; P:negative regulation of single-species biofilm formation; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48452; SSF48452; 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 412..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..941
FT /note="Basic and acidic 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
