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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)DescriptionActionsGraphical viewLength
Binding sitei823ATPPROSITE-ProRule annotation1
Active sitei918Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi800 – 808ATPPROSITE-ProRule annotation9

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
  • intracellular signal transduction Source: GO_Central
  • peptidyl-serine phosphorylation Source: SGD
  • phosphorelay signal transduction system Source: InterPro
  • positive regulation of autophagy Source: SGD
  • positive regulation of G1 to G0 transition Source: SGD
  • positive regulation of mitotic cell cycle phase transition Source: SGD
  • positive regulation of transcription involved in meiotic cell cycle Source: SGD
  • protein autophosphorylation Source: SGD
  • protein phosphorylation Source: SGD

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processMeiosis
LigandATP-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi823K → Y: Loss of kinase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866051 – 1770Serine/threonine-protein kinase RIM15Add BLAST1770

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei380PhosphoserineCombined sources1
Modified residuei476PhosphoserineCombined sources1
Modified residuei704PhosphothreonineCombined sources1
Modified residuei709PhosphoserineCombined sources1
Modified residuei733PhosphoserineCombined sources1
Modified residuei736PhosphoserineCombined sources1
Modified residuei737PhosphoserineCombined sources1
Modified residuei747PhosphothreonineCombined sources1
Modified residuei1044PhosphoserineCombined sources1
Modified residuei1048PhosphoserineCombined sources1
Modified residuei1064PhosphoserineCombined sources1
Modified residuei1075Phosphothreonine; by PHO851 Publication1
Modified residuei1421PhosphoserineCombined sources1
Modified residuei1531PhosphoserineCombined sources1
Modified residuei1538PhosphoserineCombined sources1
Modified residuei1542PhosphoserineCombined sources1
Modified residuei1565PhosphoserineCombined sources1
Modified residuei1764PhosphoserineCombined sources1

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.
PRIDEiP43565.

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. 372 interactors.
DIPiDIP-2510N.
ELMiP43565.
IntActiP43565. 16 interactors.
MINTiMINT-674598.
STRINGi4932.YFL033C.

Structurei

3D structure databases

ProteinModelPortaliP43565.
SMRiP43565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini794 – 1254Protein kinasePROSITE-ProRule annotationAdd BLAST461
Domaini1255 – 1320AGC-kinase C-terminalAdd BLAST66
Domaini1636 – 1750Response regulatoryPROSITE-ProRule annotationAdd BLAST115

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi343 – 358Poly-AsnAdd BLAST16
Compositional biasi620 – 624Poly-Ser5
Compositional biasi975 – 980Poly-Asn6
Compositional biasi1213 – 1218Poly-Glu6
Compositional biasi1386 – 1391Poly-Thr6

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063286.
HOGENOMiHOG000248031.
InParanoidiP43565.
KOiK12767.
OMAiICEDHPV.
OrthoDBiEOG092C0HH3.

Family and domain databases

CDDicd00156. REC. 1 hit.
InterProiView protein in InterPro
IPR000961. AGC-kinase_C.
IPR011006. CheY-like_superfamily.
IPR011009. Kinase-like_dom_sf.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001789. Sig_transdc_resp-reg_receiver.
PfamiView protein in Pfam
PF00069. Pkinase. 2 hits.
PF00072. Response_reg. 1 hit.
SMARTiView protein in SMART
SM00448. REC. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiView protein in PROSITE
PS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiRIM15_YEAST
AccessioniPrimary (citable) accession number: P43565
Secondary accession number(s): D6VTJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 22, 2017
This is version 185 of the entry and version 1 of the sequence. See 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