ID   BCK2_YEAST              Reviewed;         851 AA.
AC   P33306; D3DM75;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Protein BCK2;
DE   AltName: Full=Bypass of kinase C protein;
GN   Name=BCK2; Synonyms=CTR7; OrderedLocusNames=YER167W;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8395014; DOI=10.1128/mcb.13.9.5843-5853.1993;
RA   Lee K.S., Hines L.K., Levin D.E.;
RT   "A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type
RT   1-related protein phosphatases function within the PKC1-mediated pathway.";
RL   Mol. Cell. Biol. 13:5843-5853(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND SER-761, AND
RP   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: Dosage dependent suppressor of PKC1 deletion and MPK1
CC       deletion. Involved in cell lysis.
CC   -!- INTERACTION:
CC       P33306; P16892: FUS3; NbExp=2; IntAct=EBI-3480, EBI-7193;
CC       P33306; P38853: KEL1; NbExp=2; IntAct=EBI-3480, EBI-9619;
CC       P33306; P13186: KIN2; NbExp=4; IntAct=EBI-3480, EBI-9723;
CC       P33306; P14681: KSS1; NbExp=5; IntAct=EBI-3480, EBI-9945;
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DR   EMBL; L10242; AAA34452.1; -; Genomic_DNA.
DR   EMBL; U18922; AAB64694.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07829.1; -; Genomic_DNA.
DR   PIR; S50670; S50670.
DR   RefSeq; NP_011094.3; NM_001179057.3.
DR   AlphaFoldDB; P33306; -.
DR   BioGRID; 36920; 255.
DR   DIP; DIP-6406N; -.
DR   IntAct; P33306; 14.
DR   MINT; P33306; -.
DR   STRING; 4932.YER167W; -.
DR   GlyGen; P33306; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P33306; -.
DR   MaxQB; P33306; -.
DR   PaxDb; 4932-YER167W; -.
DR   PeptideAtlas; P33306; -.
DR   EnsemblFungi; YER167W_mRNA; YER167W; YER167W.
DR   GeneID; 856914; -.
DR   KEGG; sce:YER167W; -.
DR   AGR; SGD:S000000969; -.
DR   SGD; S000000969; BCK2.
DR   VEuPathDB; FungiDB:YER167W; -.
DR   eggNOG; ENOG502RH5A; Eukaryota.
DR   HOGENOM; CLU_016939_0_0_1; -.
DR   InParanoid; P33306; -.
DR   OMA; GHRKKQE; -.
DR   OrthoDB; 2015217at2759; -.
DR   BioCyc; YEAST:G3O-30328-MONOMER; -.
DR   BioGRID-ORCS; 856914; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P33306; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P33306; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:SGD.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..851
FT                   /note="Protein BCK2"
FT                   /id="PRO_0000064883"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         757
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         761
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        4..5
FT                   /note="NS -> HC (in Ref. 1; AAA34452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="T -> A (in Ref. 1; AAA34452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="L -> F (in Ref. 1; AAA34452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        812
FT                   /note="F -> C (in Ref. 1; AAA34452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        827
FT                   /note="N -> K (in Ref. 1; AAA34452)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   851 AA;  93738 MW;  9F824F2701FC452D CRC64;
     MPKNSHHHRS SSVNSTKSRS TESTNKWKIP HYYRRSASGS TQASPDRNSS TGSCSTPVLP
     TMNVMSSPKK VLLEDPRDNH TKAKKSSRKK SGEMVFVNYT VQDTANENDT DLQTQPVSVP
     APKAKLKKKS SKRRMLKIFG SSKNEHIEDI VEEQPMVLQM DSESKPLSGT PISESGIDAS
     SLTTKRSYNS FLKHNRLNGK TPFSGNLSFP SLNMMGNTTD LPIDNNDFCS EKEVVPKSTH
     DPSLAKPPSR FTESETNSTP NLSSIPLMNT KNTRLKYNKV APQSSDRQKS QESGLYHSTE
     SFNFKDQNYS NNKSSLSLNS DLSTPHFAKH SPDSPRTSRS FNCGDSQSKV KLPEENDASI
     AFSKMFTRKR ANTGGSTCSL ASPTIAQTIQ QSNIKVNKLP TQRTTSVGSL SSMSNRYSPI
     RVASPGRARS ATRGSSLYRL SRDLNSLPSV TDLPEMDSTT PVNEIFLDGQ PQHKSGSVKG
     GHRKKQESIS DAQRIQHSNS YITTPSSSLV TPPYYMTGYT LPSSASASST PNVLETHNMN
     FVPSTSTVTS YRPSSNFSSF DKEYSNENDA SGEFSAFNTP MENIPALKGI PRSTLEENEE
     EDVLVQDIPN TAHFQRRDIM GMDTHRKDDS LDFNSLMPHG STTSSSIVDS VMTNSISTTT
     SNATGNYFQD QDKYTLVNTG LGLSDANLDH FIRSQWKHAS RSESNNNTGN RVSYSGSTPN
     NVDTTKTNLQ VYTEFDFENP ESFFHEQSKL LGEMGHSNNN SNSAINMNEP KSADTYIGNI
     SPDTSATVSL GDLMGSNVSN NSERNFYDGH TFVPQYQANS SVENSNNQNA APIANNDIDN
     NLQSFYFDNS N
//