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Protein

Serine/threonine-protein kinase RIM15

Gene

RIM15

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein kinase that positively regulates proper entry into stationary phase of cells under nutrient starvation conditions. Involved in glycogen and trehalose accumulation, derepression of stress-induced genes, induction of thermotolerance and starvation resistance, and proper G1 cell cycle arrest. Also involved in the activation of a meiotic genes activation pathway. Phosphorylates IGO1 and IGO2, both involved in the TORC1 control of gene expression and chronological life span.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Kinase activity is inhibited by phosphorylation by cAMP-dependent protein kinase (PKA).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei823 – 8231ATPPROSITE-ProRule annotation
Active sitei918 – 9181Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi800 – 8089ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • age-dependent response to oxidative stress involved in chronological cell aging Source: SGD
  • cellular response to heat Source: SGD
  • cellular response to nitrogen starvation Source: SGD
  • cellular response to starvation Source: SGD
  • meiotic cell cycle Source: UniProtKB-KW
  • phosphorelay signal transduction system Source: InterPro
  • positive regulation of autophagy Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of meiotic nuclear division Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Meiosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30429-MONOMER.
BRENDAi2.7.11.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RIM15 (EC:2.7.11.1)
Gene namesi
Name:RIM15
Synonyms:TAK1
Ordered Locus Names:YFL033C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL033C.
SGDiS000001861. RIM15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi823 – 8231K → Y: Loss of kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17701770Serine/threonine-protein kinase RIM15PRO_0000086605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei380 – 3801PhosphoserineCombined sources
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei704 – 7041PhosphothreonineCombined sources
Modified residuei709 – 7091PhosphoserineCombined sources
Modified residuei733 – 7331PhosphoserineCombined sources
Modified residuei736 – 7361PhosphoserineCombined sources
Modified residuei737 – 7371PhosphoserineCombined sources
Modified residuei747 – 7471PhosphothreonineCombined sources
Modified residuei1044 – 10441PhosphoserineCombined sources
Modified residuei1048 – 10481PhosphoserineCombined sources
Modified residuei1064 – 10641PhosphoserineCombined sources
Modified residuei1075 – 10751Phosphothreonine; by PHO851 Publication
Modified residuei1421 – 14211PhosphoserineCombined sources
Modified residuei1531 – 15311PhosphoserineCombined sources
Modified residuei1538 – 15381PhosphoserineCombined sources
Modified residuei1542 – 15421PhosphoserineCombined sources
Modified residuei1565 – 15651PhosphoserineCombined sources
Modified residuei1764 – 17641PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylated. Phosphorylation by PKA strongly inhibits kinase activity. Phosphorylation by cyclin-CDK PHO80-PHO85 under favorable growth condition causes inactivation of RIM15 by promoting its export to the cytoplasm.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43565.

PTM databases

iPTMnetiP43565.

Interactioni

Subunit structurei

Interacts with the cyclin-dependent kinase (CDK) PHO85 and IGO1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KIN2P131862EBI-15150,EBI-9723

Protein-protein interaction databases

BioGridi31114. 163 interactions.
DIPiDIP-2510N.
IntActiP43565. 6 interactions.
MINTiMINT-674598.

Structurei

3D structure databases

ProteinModelPortaliP43565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini794 – 1254461Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1255 – 132066AGC-kinase C-terminalAdd
BLAST
Domaini1636 – 1750115Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi343 – 35816Poly-AsnAdd
BLAST
Compositional biasi620 – 6245Poly-Ser
Compositional biasi975 – 9806Poly-Asn
Compositional biasi1213 – 12186Poly-Glu
Compositional biasi1386 – 13916Poly-Thr

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00830000128396.
HOGENOMiHOG000248031.
InParanoidiP43565.
KOiK12767.
OMAiKHERIPS.
OrthoDBiEOG7Z95VF.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011006. CheY-like_superfamily.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
PF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNRSNTAGG SQAMKEGLGI NKLSPISSNS NPSSLTSSNY EKYLQLATEK
60 70 80 90 100
NPCMILELEL DGKVRYGSPQ WNTITGVADD SGSSPTYIAD LILGSDQDKG
110 120 130 140 150
VFQKATDMLL MNDDTSCTIT FKIKAADYEG SAGCDDESTI TTLEARGILI
160 170 180 190 200
RDGHTQLPSH TMWIVKPRTN DWSDFYANED AQDDMVIQLS DNCDDIDIQL
210 220 230 240 250
PEEFAKTLGF GAKIFVQYLK RIRLEMIIDE FNLPLPKMEL CRVCENFVPV
260 270 280 290 300
WWLETHSQSC VCEHRTESLI QLLHDNLLEQ QAILANFTKD SEYKGSQIQV
310 320 330 340 350
RSNNFLNQVL DSLRELCQDA IDINPSEMVP DLYHSLSTFP QDNGNNNNNN
360 370 380 390 400
NNNNNNNNAL LDQFPIQKDT VSLNSYFQFS PRTNHNIQNV TSWQSRFFLN
410 420 430 440 450
DDQDPGLALL IHDTLDLARK KVDAVLRLDN AMTYSLKIKN EVNNYVVQLI
460 470 480 490 500
REQIEINKHA ILTHPMNLRS SSIFHSPLPQ IHSQQPEAEN LIYSSSTPLQ
510 520 530 540 550
VQHDQCASFE APSKSHLEPI PFPVSSIEET PTANDIRHPS PLPRSCSNTV
560 570 580 590 600
MKLPTPRRKL DSNGLFSDAY LNADIIPNPS IESTISIDRD NNTNSRGSSM
610 620 630 640 650
KQYGIGEATD SRTSNSERPS SSSSRLGIRS RSITPRQKIE YSHVDNDDRT
660 670 680 690 700
NEMLSRDKDS LQPQPSVDTT ITSSTQATTT GTKTNSNNST NSVLPKLMTS
710 720 730 740 750
ISLTPRRGSP SFGNLASHSM QQTNSFKLIH DKSPISSPFT FSKDFLTPEQ
760 770 780 790 800
HPSNIARTDS INNAMLTSPN MPLSPLLLAT NQTVKSPTPS IKDYDILKPI
810 820 830 840 850
SKGAYGSVYL ARKKLTGDYF AIKVLRKSDM IAKNQVTNVK SERAIMMVQS
860 870 880 890 900
DKPYVARLFA SFQNKDNLFL VMEYLPGGDL ATLIKMMGYL PDQWAKQYLT
910 920 930 940 950
EIVVGVNDMH QNGIIHHDLK PENLLIDNAG HVKLTDFGLS RAGLIRRHKF
960 970 980 990 1000
VPHKSSLSIS STLPIDNPAN NFTMNNNNSN HSQLSTPDSF TSDHKQYNRS
1010 1020 1030 1040 1050
KKSSLGQQYE HSEYSSTSNS HSMTPTPSTN TVVYPSYYRG KDRSHGSSNI
1060 1070 1080 1090 1100
DLPASLRRSE SQLSFSLLDI SRSSTPPLAN PTNSNANNIM RRKSLTENKS
1110 1120 1130 1140 1150
FSNDLLSSDA IAATNTNINS NNNISLSPAP SDLALFYPDD SKQNKKFFGT
1160 1170 1180 1190 1200
PDYLAPETIE GKGEDNKQCD WWSVGCIFFE LLLGYPPFHA ETPDAVFKKI
1210 1220 1230 1240 1250
LSGVIQWPEF KNEEEEREFL TPEAKDLIEK LLVVDPAKRL GAKGIQEIKD
1260 1270 1280 1290 1300
HPYFKNVDWD HVYDEEASFV PTIDNPEDTD YFDLRGAELQ DFGDDIENDN
1310 1320 1330 1340 1350
ANILFGKHGI NTDVSELSAA NLSPPLNHKN ILSRKLSMSN TTNRSSNNSN
1360 1370 1380 1390 1400
SSVHDFGAHT PVNKLSIASV LESVPQETGY ITPNGTGTTT TSAKNSPNLK
1410 1420 1430 1440 1450
NLSLAIPPHM RDRRSSKLND SQTEFGSFNF RNLSALDKAN KDAINRLKSE
1460 1470 1480 1490 1500
HFSEQPGVHR RTSSASLMGS SSDGSVSTPG SNASNTTSGG KLKIHKPTIS
1510 1520 1530 1540 1550
GSPSTFGTFP KTFLRSDSFS TRSYSPERSI SIDSSTLSRK GSIIGDNQQT
1560 1570 1580 1590 1600
TANSSDSPTM TKFKSPLSPA NTTTVSSYFS RQRVLSKSFS QRTNSSDLSA
1610 1620 1630 1640 1650
EESDRLQAIS RVNSLRNRRR SGRKSSSTSE IGYHMDVLVC EPIPIHRYRV
1660 1670 1680 1690 1700
TKDLENLGCT VVSVGAGDEL VSRATSGVSF DLIMTALKLP KLGAIDIVQL
1710 1720 1730 1740 1750
LKQTNGANST TPIVAITNYF QEAATSRVFD DVLEKPVKLD ELKKLVAKYA
1760 1770
LKKSQEDEEH TILSDSDETH
Length:1,770
Mass (Da):196,531
Last modified:November 1, 1995 - v1
Checksum:iDC1064825000FAFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09206.1.
U83459 Genomic DNA. Translation: AAB64088.1.
AJ001030 Genomic DNA. Translation: CAA04486.1.
BK006940 Genomic DNA. Translation: DAA12408.1.
PIRiS56221.
RefSeqiNP_116620.1. NM_001179933.1.

Genome annotation databases

EnsemblFungiiBAA09206; BAA09206; BAA09206.
YFL033C; YFL033C; YFL033C.
GeneIDi850511.
KEGGisce:YFL033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09206.1.
U83459 Genomic DNA. Translation: AAB64088.1.
AJ001030 Genomic DNA. Translation: CAA04486.1.
BK006940 Genomic DNA. Translation: DAA12408.1.
PIRiS56221.
RefSeqiNP_116620.1. NM_001179933.1.

3D structure databases

ProteinModelPortaliP43565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31114. 163 interactions.
DIPiDIP-2510N.
IntActiP43565. 6 interactions.
MINTiMINT-674598.

PTM databases

iPTMnetiP43565.

Proteomic databases

MaxQBiP43565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09206; BAA09206; BAA09206.
YFL033C; YFL033C; YFL033C.
GeneIDi850511.
KEGGisce:YFL033C.

Organism-specific databases

EuPathDBiFungiDB:YFL033C.
SGDiS000001861. RIM15.

Phylogenomic databases

GeneTreeiENSGT00830000128396.
HOGENOMiHOG000248031.
InParanoidiP43565.
KOiK12767.
OMAiKHERIPS.
OrthoDBiEOG7Z95VF.

Enzyme and pathway databases

BioCyciYEAST:G3O-30429-MONOMER.
BRENDAi2.7.11.1. 984.

Miscellaneous databases

NextBioi966227.
PROiP43565.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011006. CheY-like_superfamily.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
PF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Stimulation of yeast meiotic gene expression by the glucose-repressible protein kinase Rim15p."
    Vidan S., Mitchell A.P.
    Mol. Cell. Biol. 17:2688-2697(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  4. "Saccharomyces cerevisiae cAMP-dependent protein kinase controls entry into stationary phase through the Rim15p protein kinase."
    Reinders A., Buerckert N., Boller T., Wiemken A., De Virgilio C.
    Genes Dev. 12:2943-2955(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LYS-823.
  5. "Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex."
    Wanke V., Pedruzzi I., Cameroni E., Dubouloz F., De Virgilio C.
    EMBO J. 24:4271-4278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-1075, SUBCELLULAR LOCATION.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733 AND SER-1764, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-476; THR-704 AND THR-747, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704; SER-709; SER-733; SER-736; SER-737; SER-1044; SER-1048; SER-1064; SER-1421; SER-1531; SER-1538; SER-1542 AND SER-1565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Initiation of the TORC1-regulated G0 program requires Igo1/2, which license specific mRNAs to evade degradation via the 5'-3' mRNA decay pathway."
    Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S., Devgan G., Snyder M., Broach J.R., De Virgilio C.
    Mol. Cell 38:345-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IGO1.

Entry informationi

Entry nameiRIM15_YEAST
AccessioniPrimary (citable) accession number: P43565
Secondary accession number(s): D6VTJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.