MRK1_YEAST
ID MRK1_YEAST Reviewed; 501 AA.
AC P50873; D6VRS0; Q07470;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Serine/threonine-protein kinase MRK1;
DE EC=2.7.11.1;
GN Name=MRK1; OrderedLocusNames=YDL079C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-501.
RX PubMed=7695629; DOI=10.1006/bbrc.1995.1398;
RA Hardy T.A., Wu D., Roach P.J.;
RT "Novel Saccharomyces cerevisiae gene, MRK1, encoding a putative protein
RT kinase with similarity to mammalian glycogen synthase kinase-3 and
RT Drosophila Zeste-White3/Shaggy.";
RL Biochem. Biophys. Res. Commun. 208:728-734(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP 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 -!- 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. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z74127; CAA98645.1; -; Genomic_DNA.
DR EMBL; U22348; AAA74429.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006938; DAA11780.1; -; Genomic_DNA.
DR PIR; S67615; S67615.
DR RefSeq; NP_010204.1; NM_001180138.1.
DR AlphaFoldDB; P50873; -.
DR SMR; P50873; -.
DR BioGRID; 31982; 93.
DR IntAct; P50873; 6.
DR MINT; P50873; -.
DR STRING; 4932.YDL079C; -.
DR iPTMnet; P50873; -.
DR MaxQB; P50873; -.
DR PaxDb; P50873; -.
DR PRIDE; P50873; -.
DR EnsemblFungi; YDL079C_mRNA; YDL079C; YDL079C.
DR GeneID; 851480; -.
DR KEGG; sce:YDL079C; -.
DR SGD; S000002237; MRK1.
DR VEuPathDB; FungiDB:YDL079C; -.
DR eggNOG; KOG0658; Eukaryota.
DR GeneTree; ENSGT00520000055635; -.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; P50873; -.
DR OMA; ANKHENI; -.
DR BioCyc; YEAST:G3O-29489-MON; -.
DR BRENDA; 2.7.11.26; 984.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:P50873; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P50873; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:SGD.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IGI:SGD.
DR GO; GO:0042176; P:regulation of protein catabolic process; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Transferase.
FT CHAIN 1..501
FT /note="Serine/threonine-protein kinase MRK1"
FT /id="PRO_0000086399"
FT DOMAIN 164..447
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 170..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 501 AA; 57819 MW; B0C938AF8E63E5AA CRC64;
MTDVLRSLVR KISFNNSDNL QLKHKTSIQS NTALEKKKRK PDTIKKVSDV QVHHTVPNFN
NSSEYINDIE NLIISKLIDG GKEGIAVDHI EHANISDSKT DGKVANKHEN ISSKLSKEKV
EKMINFDYRY IKTKERTIHK RVYKHDRKTD VDRKNHGGTI DISYPTTEVV GHGSFGVVVT
TVIIETNQKV AIKKVLQDRR YKNRELETMK MLCHPNTVGL QYYFYEKDEE DEVYLNLVLD
YMPQSLYQRL RHFVNLKMQM PRVEIKFYAY QLFKALNYLH NVPRICHRDI KPQNLLVDPT
TFSFKICDFG SAKCLKPDQP NVSYICSRYY RAPELMFGAT NYSNQVDVWS SACVIAELLL
GKPLFSGESG IDQLVEIIKI MGIPTKDEIS GMNPNYEDHV FPNIKPITLA EIFKAEDPDT
LDLLTKTLKY HPCERLVPLQ CLLSSYFDET KRCDTDTYVK AQNLRIFDFD VETELGHVPL
VERPAIEERL KHFVSAPSSS L
