RIM11_YEAST
ID RIM11_YEAST Reviewed; 370 AA.
AC P38615; D6VZW2; Q6Q5K4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Serine/threonine-protein kinase RIM11/MSD1;
DE EC=2.7.11.1;
DE AltName: Full=Regulator of IME2 protein 11;
GN Name=RIM11; Synonyms=GSK3, MDS1; OrderedLocusNames=YMR139W;
GN ORFNames=YM9375.08;
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.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8264650; DOI=10.1128/mcb.14.1.831-839.1994;
RA Puziss J.W., Hardy T.A., Johnson R.B., Roach P.J., Hieter P.;
RT "MDS1, a dosage suppressor of an mck1 mutant, encodes a putative yeast
RT homolog of glycogen synthase kinase 3.";
RL Mol. Cell. Biol. 14:831-839(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7969131; DOI=10.1128/mcb.14.12.7909-7919.1994;
RA Bowdish K.S., Yuan H.E., Mitchell A.P.;
RT "Analysis of RIM11, a yeast protein kinase that phosphorylates the meiotic
RT activator IME1.";
RL Mol. Cell. Biol. 14:7909-7919(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8244030; DOI=10.1016/0378-1119(93)90173-z;
RA Bianchi M.W., Plyte S.E., Kreis M., Woodgett J.R.;
RT "A Saccharomyces cerevisiae protein-serine kinase related to mammalian
RT glycogen synthase kinase-3 and the Drosophila melanogaster gene shaggy
RT product.";
RL Gene 134:51-56(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP PHOSPHORYLATION AT TYR-199.
RX PubMed=10679022; DOI=10.1091/mbc.11.2.663;
RA Zhan X.L., Hong Y., Zhu T., Mitchell A.P., Deschenes R.J., Guan K.L.;
RT "Essential functions of protein tyrosine phosphatases PTP2 and PTP3 and
RT RIM11 tyrosine phosphorylation in Saccharomyces cerevisiae meiosis and
RT sporulation.";
RL Mol. Biol. Cell 11:663-676(2000).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, AND IDENTIFICATION BY
RP 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 [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, 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).
RN [13]
RP INTERACTION WITH TDA1.
RX PubMed=21460040; DOI=10.1101/gad.1998811;
RA Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M.,
RA Gerstein M., Snyder M.;
RT "Diverse protein kinase interactions identified by protein microarrays
RT reveal novel connections between cellular processes.";
RL Genes Dev. 25:767-778(2011).
CC -!- FUNCTION: Serine/threonine protein kinase that is thought to function
CC in regulating kinetochore activity and entry into meiosis. Could
CC phosphorylate IME1.
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 -!- SUBUNIT: Interacts with TDA1. {ECO:0000269|PubMed:21460040}.
CC -!- INTERACTION:
CC P38615; P21190: IME1; NbExp=4; IntAct=EBI-10642, EBI-9199;
CC P38615; P25293: NAP1; NbExp=8; IntAct=EBI-10642, EBI-11850;
CC -!- MISCELLANEOUS: Present with 6990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U03280; AAC48917.1; -; Unassigned_DNA.
DR EMBL; L29284; AAB04166.1; -; Genomic_DNA.
DR EMBL; L12761; AAA16206.1; -; Unassigned_DNA.
DR EMBL; Z47071; CAA87353.1; -; Genomic_DNA.
DR EMBL; AY557994; AAS56320.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10036.1; -; Genomic_DNA.
DR PIR; A56347; A56347.
DR RefSeq; NP_013859.1; NM_001182641.1.
DR AlphaFoldDB; P38615; -.
DR SMR; P38615; -.
DR BioGRID; 35316; 195.
DR DIP; DIP-1566N; -.
DR IntAct; P38615; 41.
DR MINT; P38615; -.
DR STRING; 4932.YMR139W; -.
DR iPTMnet; P38615; -.
DR MaxQB; P38615; -.
DR PaxDb; P38615; -.
DR PRIDE; P38615; -.
DR EnsemblFungi; YMR139W_mRNA; YMR139W; YMR139W.
DR GeneID; 855170; -.
DR KEGG; sce:YMR139W; -.
DR SGD; S000004747; RIM11.
DR VEuPathDB; FungiDB:YMR139W; -.
DR eggNOG; KOG0658; Eukaryota.
DR GeneTree; ENSGT00520000055635; -.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; P38615; -.
DR OMA; EMQYTQC; -.
DR BioCyc; YEAST:G3O-32832-MON; -.
DR BRENDA; 2.7.11.26; 984.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:P38615; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38615; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IDA:SGD.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; 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..370
FT /note="Serine/threonine-protein kinase RIM11/MSD1"
FT /id="PRO_0000086319"
FT DOMAIN 39..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 199
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10679022,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT CONFLICT 57
FT /note="V -> I (in Ref. 3; AAA16206)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="K -> R (in Ref. 6; AAS56320)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="E -> G (in Ref. 3; AAA16206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 43005 MW; 59D92C9D42408E97 CRC64;
MNIQSNNSPN LSNNIVSKQV YYAHPPPTID PNDPVQISFP TTEVVGHGSF GVVFATVIQE
TNEKVAIKKV LQDKRFKNRE LEIMKMLSHI NIIDLKYFFY ERDSQDEIYL NLILEYMPQS
LYQRLRHFVH QRTPMSRLEI KYYMFQLFKS LNYLHHFANV CHRDIKPQNL LVDPETWSLK
LCDFGSAKQL KPTEPNVSYI CSRYYRAPEL IFGATNYTNQ IDIWSSGCVM AELLLGQPMF
PGESGIDQLV EIIKILGTPS KQEICSMNPN YMEHKFPQIK PIPLSRVFKK EDDQTVEFLA
DVLKYDPLER FNALQCLCSP YFDELKLDDG KINQITTDLK LLEFDENVEL GHLSPDELSS
VKKKLYPKSK
