YGK3_YEAST
ID YGK3_YEAST Reviewed; 375 AA.
AC Q12222; D6W1U0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Glycogen synthase kinase-3 homolog YGK3;
DE EC=2.7.11.1;
GN Name=YGK3; OrderedLocusNames=YOL128C;
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 96604 / S288c / FY1679;
RX PubMed=8896265;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1013::aid-yea980%3e3.0.co;2-5;
RA Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E.,
RA Arino J.;
RT "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome
RT XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase,
RT the ribosomal L25 gene and four new open reading frames.";
RL Yeast 12:1013-1020(1996).
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=10958669; DOI=10.1128/mcb.20.18.6712-6720.2000;
RA Andoh T., Hirata Y., Kikuchi A.;
RT "Yeast glycogen synthase kinase 3 is involved in protein degradation in
RT cooperation with Bul1, Bul2, and Rsp5.";
RL Mol. Cell. Biol. 20:6712-6720(2000).
RN [5]
RP FUNCTION.
RX PubMed=12704202; DOI=10.1074/jbc.m210691200;
RA Griffioen G., Swinnen S., Thevelein J.M.;
RT "Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3
RT phosphorylation of a cAMP-dependent protein kinase regulatory subunit.";
RL J. Biol. Chem. 278:23460-23471(2003).
RN [6]
RP FUNCTION.
RX PubMed=12529445; DOI=10.1091/mbc.e02-05-0247;
RA Hirata Y., Andoh T., Asahara T., Kikuchi A.;
RT "Yeast glycogen synthase kinase-3 activates Msn2p-dependent transcription
RT of stress responsive genes.";
RL Mol. Biol. Cell 14:302-312(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, 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).
CC -!- FUNCTION: Required for heat stress-instigated phosphorylation of BCY1
CC which is involved in cell wall integrity signaling. Regulates activity
CC of MSN2, a transcription factor that binds to the stress-response
CC element (STRE). Probably promotes formation of a complex between MSN2
CC and DNA. Regulates the stability of ROG1. {ECO:0000269|PubMed:10958669,
CC ECO:0000269|PubMed:12529445, ECO:0000269|PubMed:12704202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U41293; AAC49464.1; -; Genomic_DNA.
DR EMBL; Z74870; CAA99147.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10656.1; -; Genomic_DNA.
DR PIR; S63442; S63442.
DR RefSeq; NP_014513.1; NM_001183382.1.
DR AlphaFoldDB; Q12222; -.
DR SMR; Q12222; -.
DR BioGRID; 34247; 69.
DR DIP; DIP-4548N; -.
DR IntAct; Q12222; 15.
DR MINT; Q12222; -.
DR STRING; 4932.YOL128C; -.
DR iPTMnet; Q12222; -.
DR MaxQB; Q12222; -.
DR PaxDb; Q12222; -.
DR PRIDE; Q12222; -.
DR EnsemblFungi; YOL128C_mRNA; YOL128C; YOL128C.
DR GeneID; 853992; -.
DR KEGG; sce:YOL128C; -.
DR SGD; S000005488; YGK3.
DR VEuPathDB; FungiDB:YOL128C; -.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q12222; -.
DR OMA; SSEIHEY; -.
DR BioCyc; YEAST:G3O-33523-MON; -.
DR PRO; PR:Q12222; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12222; protein.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:SGD.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR CDD; cd14137; STKc_GSK3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR039192; STKc_GSK3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..375
FT /note="Glycogen synthase kinase-3 homolog YGK3"
FT /id="PRO_0000086159"
FT DOMAIN 41..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 375 AA; 43206 MW; 966C17A6F981C45E CRC64;
MLKVNNVFGS NPNRMTKLED EHYFIDDIVS IKNRQKSKMY VREGKRIGHG SFGTVTQSIL
SSNSIEWLGP YAIKRVVKSP KVQSLELEIL QNIRHPNLVT LEFFFESHCT TKDGGHLYQK
NFVMEYIPQT LSSEIHEYFD NGSKMPTKHI KLYTFQILRA LLTLHSMSIC HGDLKPSNIL
IIPSSGIAKV CDFGSAQRLD DNTELKTYFC SRFYRAPELL LNSKDYTTQI DIWSLGCIIG
EMIKGQPLFK GDSANSQLEE IAKLLGRFPK SSIKNSQELQ DSLNDQKFKK FMHWFPSIEF
FDVEFLLKVL TYDATERCDA RQLMAHEFFD ALRNETYFLP RGSSMPVHLP DLFNFSASEK
RALGEYYNLI VPSLD
