RIM15_YEAST
ID RIM15_YEAST Reviewed; 1770 AA.
AC P43565; D6VTJ8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Serine/threonine-protein kinase RIM15;
DE EC=2.7.11.1;
GN Name=RIM15; Synonyms=TAK1; OrderedLocusNames=YFL033C;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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], AND CHARACTERIZATION.
RX PubMed=9111339; DOI=10.1128/mcb.17.5.2688;
RA Vidan S., Mitchell A.P.;
RT "Stimulation of yeast meiotic gene expression by the glucose-repressible
RT protein kinase Rim15p.";
RL Mol. Cell. Biol. 17:2688-2697(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF LYS-823.
RX PubMed=9744870; DOI=10.1101/gad.12.18.2943;
RA Reinders A., Buerckert N., Boller T., Wiemken A., De Virgilio C.;
RT "Saccharomyces cerevisiae cAMP-dependent protein kinase controls entry into
RT stationary phase through the Rim15p protein kinase.";
RL Genes Dev. 12:2943-2955(1998).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT THR-1075, AND SUBCELLULAR LOCATION.
RX PubMed=16308562; DOI=10.1038/sj.emboj.7600889;
RA Wanke V., Pedruzzi I., Cameroni E., Dubouloz F., De Virgilio C.;
RT "Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex.";
RL EMBO J. 24:4271-4278(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733 AND SER-1764, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-476; THR-704 AND
RP THR-747, AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704; SER-709; SER-733;
RP SER-736; SER-737; SER-1044; SER-1048; SER-1064; SER-1421; SER-1531;
RP SER-1538; SER-1542 AND SER-1565, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP FUNCTION, AND INTERACTION WITH IGO1.
RX PubMed=20471941; DOI=10.1016/j.molcel.2010.02.039;
RA Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S.,
RA Devgan G., Snyder M., Broach J.R., De Virgilio C.;
RT "Initiation of the TORC1-regulated G0 program requires Igo1/2, which
RT license specific mRNAs to evade degradation via the 5'-3' mRNA decay
RT pathway.";
RL Mol. Cell 38:345-355(2010).
CC -!- FUNCTION: Protein kinase that positively regulates proper entry into
CC stationary phase of cells under nutrient starvation conditions.
CC Involved in glycogen and trehalose accumulation, derepression of
CC stress-induced genes, induction of thermotolerance and starvation
CC resistance, and proper G1 cell cycle arrest. Also involved in the
CC activation of a meiotic genes activation pathway. Phosphorylates IGO1
CC and IGO2, both involved in the TORC1 control of gene expression and
CC chronological life span. {ECO:0000269|PubMed:16308562,
CC ECO:0000269|PubMed:20471941, ECO:0000269|PubMed:9744870}.
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 -!- ACTIVITY REGULATION: Kinase activity is inhibited by phosphorylation by
CC cAMP-dependent protein kinase (PKA). {ECO:0000269|PubMed:9744870}.
CC -!- SUBUNIT: Interacts with the cyclin-dependent kinase (CDK) PHO85 and
CC IGO1. {ECO:0000269|PubMed:20471941}.
CC -!- INTERACTION:
CC P43565; P13186: KIN2; NbExp=2; IntAct=EBI-15150, EBI-9723;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16308562}. Nucleus
CC {ECO:0000269|PubMed:16308562}.
CC -!- PTM: Autophosphorylated. Phosphorylation by PKA strongly inhibits
CC kinase activity. Phosphorylation by cyclin-CDK PHO80-PHO85 under
CC favorable growth condition causes inactivation of RIM15 by promoting
CC its export to the cytoplasm. {ECO:0000269|PubMed:16308562}.
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; D50617; BAA09206.1; -; Genomic_DNA.
DR EMBL; U83459; AAB64088.1; -; Genomic_DNA.
DR EMBL; AJ001030; CAA04486.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12408.1; -; Genomic_DNA.
DR PIR; S56221; S56221.
DR RefSeq; NP_116620.1; NM_001179933.1.
DR AlphaFoldDB; P43565; -.
DR SMR; P43565; -.
DR BioGRID; 31114; 385.
DR DIP; DIP-2510N; -.
DR ELM; P43565; -.
DR IntAct; P43565; 16.
DR MINT; P43565; -.
DR STRING; 4932.YFL033C; -.
DR CarbonylDB; P43565; -.
DR iPTMnet; P43565; -.
DR MaxQB; P43565; -.
DR PaxDb; P43565; -.
DR PRIDE; P43565; -.
DR EnsemblFungi; YFL033C_mRNA; YFL033C; YFL033C.
DR GeneID; 850511; -.
DR KEGG; sce:YFL033C; -.
DR SGD; S000001861; RIM15.
DR VEuPathDB; FungiDB:YFL033C; -.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000157002; -.
DR HOGENOM; CLU_000709_4_0_1; -.
DR InParanoid; P43565; -.
DR OMA; QFDIIMT; -.
DR BioCyc; YEAST:G3O-30429-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P43565; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43565; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR GO; GO:1903452; P:positive regulation of G1 to G0 transition; IMP:SGD.
DR GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IMP:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0051039; P:positive regulation of transcription involved in meiotic cell cycle; IMP:SGD.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00448; REC; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Meiosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1770
FT /note="Serine/threonine-protein kinase RIM15"
FT /id="PRO_0000086605"
FT DOMAIN 794..1254
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1255..1320
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1636..1750
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 334..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 918
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 800..808
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 823
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 704
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 747
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1075
FT /note="Phosphothreonine; by PHO85"
FT /evidence="ECO:0000269|PubMed:16308562"
FT MOD_RES 1421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MUTAGEN 823
FT /note="K->Y: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:9744870"
SQ SEQUENCE 1770 AA; 196531 MW; DC1064825000FAFF CRC64;
MFNRSNTAGG SQAMKEGLGI NKLSPISSNS NPSSLTSSNY EKYLQLATEK NPCMILELEL
DGKVRYGSPQ WNTITGVADD SGSSPTYIAD LILGSDQDKG VFQKATDMLL MNDDTSCTIT
FKIKAADYEG SAGCDDESTI TTLEARGILI RDGHTQLPSH TMWIVKPRTN DWSDFYANED
AQDDMVIQLS DNCDDIDIQL PEEFAKTLGF GAKIFVQYLK RIRLEMIIDE FNLPLPKMEL
CRVCENFVPV WWLETHSQSC VCEHRTESLI QLLHDNLLEQ QAILANFTKD SEYKGSQIQV
RSNNFLNQVL DSLRELCQDA IDINPSEMVP DLYHSLSTFP QDNGNNNNNN NNNNNNNNAL
LDQFPIQKDT VSLNSYFQFS PRTNHNIQNV TSWQSRFFLN DDQDPGLALL IHDTLDLARK
KVDAVLRLDN AMTYSLKIKN EVNNYVVQLI REQIEINKHA ILTHPMNLRS SSIFHSPLPQ
IHSQQPEAEN LIYSSSTPLQ VQHDQCASFE APSKSHLEPI PFPVSSIEET PTANDIRHPS
PLPRSCSNTV MKLPTPRRKL DSNGLFSDAY LNADIIPNPS IESTISIDRD NNTNSRGSSM
KQYGIGEATD SRTSNSERPS SSSSRLGIRS RSITPRQKIE YSHVDNDDRT NEMLSRDKDS
LQPQPSVDTT ITSSTQATTT GTKTNSNNST NSVLPKLMTS ISLTPRRGSP SFGNLASHSM
QQTNSFKLIH DKSPISSPFT FSKDFLTPEQ HPSNIARTDS INNAMLTSPN MPLSPLLLAT
NQTVKSPTPS IKDYDILKPI SKGAYGSVYL ARKKLTGDYF AIKVLRKSDM IAKNQVTNVK
SERAIMMVQS DKPYVARLFA SFQNKDNLFL VMEYLPGGDL ATLIKMMGYL PDQWAKQYLT
EIVVGVNDMH QNGIIHHDLK PENLLIDNAG HVKLTDFGLS RAGLIRRHKF VPHKSSLSIS
STLPIDNPAN NFTMNNNNSN HSQLSTPDSF TSDHKQYNRS KKSSLGQQYE HSEYSSTSNS
HSMTPTPSTN TVVYPSYYRG KDRSHGSSNI DLPASLRRSE SQLSFSLLDI SRSSTPPLAN
PTNSNANNIM RRKSLTENKS FSNDLLSSDA IAATNTNINS NNNISLSPAP SDLALFYPDD
SKQNKKFFGT PDYLAPETIE GKGEDNKQCD WWSVGCIFFE LLLGYPPFHA ETPDAVFKKI
LSGVIQWPEF KNEEEEREFL TPEAKDLIEK LLVVDPAKRL GAKGIQEIKD HPYFKNVDWD
HVYDEEASFV PTIDNPEDTD YFDLRGAELQ DFGDDIENDN ANILFGKHGI NTDVSELSAA
NLSPPLNHKN ILSRKLSMSN TTNRSSNNSN SSVHDFGAHT PVNKLSIASV LESVPQETGY
ITPNGTGTTT TSAKNSPNLK NLSLAIPPHM RDRRSSKLND SQTEFGSFNF RNLSALDKAN
KDAINRLKSE HFSEQPGVHR RTSSASLMGS SSDGSVSTPG SNASNTTSGG KLKIHKPTIS
GSPSTFGTFP KTFLRSDSFS TRSYSPERSI SIDSSTLSRK GSIIGDNQQT TANSSDSPTM
TKFKSPLSPA NTTTVSSYFS RQRVLSKSFS QRTNSSDLSA EESDRLQAIS RVNSLRNRRR
SGRKSSSTSE IGYHMDVLVC EPIPIHRYRV TKDLENLGCT VVSVGAGDEL VSRATSGVSF
DLIMTALKLP KLGAIDIVQL LKQTNGANST TPIVAITNYF QEAATSRVFD DVLEKPVKLD
ELKKLVAKYA LKKSQEDEEH TILSDSDETH
