BCK2_YEAST
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 03-AUG-2022, entry version 150.
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; 248.
DR DIP; DIP-6406N; -.
DR IntAct; P33306; 14.
DR MINT; P33306; -.
DR STRING; 4932.YER167W; -.
DR iPTMnet; P33306; -.
DR MaxQB; P33306; -.
DR PaxDb; P33306; -.
DR PRIDE; P33306; -.
DR EnsemblFungi; YER167W_mRNA; YER167W; YER167W.
DR GeneID; 856914; -.
DR KEGG; sce:YER167W; -.
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 BioCyc; YEAST:G3O-30328-MON; -.
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
