UniProtKB - P43565 (RIM15_YEAST)
Serine/threonine-protein kinase RIM15
RIM15
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 PublicationsCatalytic activityi
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 823 | ATPPROSITE-ProRule annotation | 1 | |
Active sitei | 918 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 800 – 808 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- protein kinase activity Source: SGD
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: SGD
- protein serine kinase activity Source: RHEA
GO - Biological processi
- 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 by RNA polymerase II Source: SGD
- positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation Source: SGD
- positive regulation of transcription from RNA polymerase II promoter in response to heat stress Source: SGD
- positive regulation of transcription involved in meiotic cell cycle Source: SGD
- protein autophosphorylation Source: SGD
- protein phosphorylation Source: SGD
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Meiosis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 984 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:RIM15 Synonyms:TAK1 Ordered Locus Names:YFL033C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000001861, RIM15 |
VEuPathDBi | FungiDB:YFL033C |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 823 | K → Y: Loss of kinase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000086605 | 1 – 1770 | Serine/threonine-protein kinase RIM15Add BLAST | 1770 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 380 | PhosphoserineCombined sources | 1 | |
Modified residuei | 476 | PhosphoserineCombined sources | 1 | |
Modified residuei | 704 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 709 | PhosphoserineCombined sources | 1 | |
Modified residuei | 733 | PhosphoserineCombined sources | 1 | |
Modified residuei | 736 | PhosphoserineCombined sources | 1 | |
Modified residuei | 737 | PhosphoserineCombined sources | 1 | |
Modified residuei | 747 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1044 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1048 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1064 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1075 | Phosphothreonine; by PHO851 Publication | 1 | |
Modified residuei | 1421 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1531 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1538 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1542 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1565 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1764 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | P43565 |
PaxDbi | P43565 |
PRIDEi | P43565 |
PTM databases
CarbonylDBi | P43565 |
iPTMneti | P43565 |
Interactioni
Subunit structurei
Interacts with the cyclin-dependent kinase (CDK) PHO85 and IGO1.
1 PublicationBinary interactionsi
P43565
With | #Exp. | IntAct |
---|---|---|
KIN2 [P13186] | 2 | EBI-15150,EBI-9723 |
Protein-protein interaction databases
BioGRIDi | 31114, 385 interactors |
DIPi | DIP-2510N |
ELMi | P43565 |
IntActi | P43565, 16 interactors |
MINTi | P43565 |
STRINGi | 4932.YFL033C |
Miscellaneous databases
RNActi | P43565, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 794 – 1254 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 461 | |
Domaini | 1255 – 1320 | AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST | 66 | |
Domaini | 1636 – 1750 | Response regulatoryPROSITE-ProRule annotationAdd BLAST | 115 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 334 – 358 | DisorderedSequence analysisAdd BLAST | 25 | |
Regioni | 530 – 563 | DisorderedSequence analysisAdd BLAST | 34 | |
Regioni | 583 – 694 | DisorderedSequence analysisAdd BLAST | 112 | |
Regioni | 970 – 1032 | DisorderedSequence analysisAdd BLAST | 63 | |
Regioni | 1378 – 1403 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 1448 – 1507 | DisorderedSequence analysisAdd BLAST | 60 | |
Regioni | 1519 – 1572 | DisorderedSequence analysisAdd BLAST | 54 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 336 – 358 | Polar residuesSequence analysisAdd BLAST | 23 | |
Compositional biasi | 583 – 635 | Polar residuesSequence analysisAdd BLAST | 53 | |
Compositional biasi | 636 – 656 | Basic and acidic residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 657 – 694 | Polar residuesSequence analysisAdd BLAST | 38 | |
Compositional biasi | 970 – 993 | Polar residuesSequence analysisAdd BLAST | 24 | |
Compositional biasi | 1001 – 1032 | Polar residuesSequence analysisAdd BLAST | 32 | |
Compositional biasi | 1378 – 1402 | Polar residuesSequence analysisAdd BLAST | 25 | |
Compositional biasi | 1458 – 1507 | Polar residuesSequence analysisAdd BLAST | 50 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0605, Eukaryota |
GeneTreei | ENSGT00940000157002 |
HOGENOMi | CLU_000709_4_0_1 |
InParanoidi | P43565 |
OMAi | ISQVLQW |
Family and domain databases
InterProi | View 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 |
Pfami | View protein in Pfam PF00069, Pkinase, 2 hits |
SMARTi | View protein in SMART SM00448, REC, 1 hit SM00133, S_TK_X, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF52172, SSF52172, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View 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 |
i Sequence
Sequence statusi: Complete.
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
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 |
PIRi | S56221 |
RefSeqi | NP_116620.1, NM_001179933.1 |
Genome annotation databases
EnsemblFungii | YFL033C_mRNA; YFL033C; YFL033C |
GeneIDi | 850511 |
KEGGi | sce:YFL033C |
Similar proteinsi
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 |
PIRi | S56221 |
RefSeqi | NP_116620.1, NM_001179933.1 |
3D structure databases
SMRi | P43565 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 31114, 385 interactors |
DIPi | DIP-2510N |
ELMi | P43565 |
IntActi | P43565, 16 interactors |
MINTi | P43565 |
STRINGi | 4932.YFL033C |
PTM databases
CarbonylDBi | P43565 |
iPTMneti | P43565 |
Proteomic databases
MaxQBi | P43565 |
PaxDbi | P43565 |
PRIDEi | P43565 |
Genome annotation databases
EnsemblFungii | YFL033C_mRNA; YFL033C; YFL033C |
GeneIDi | 850511 |
KEGGi | sce:YFL033C |
Organism-specific databases
SGDi | S000001861, RIM15 |
VEuPathDBi | FungiDB:YFL033C |
Phylogenomic databases
eggNOGi | KOG0605, Eukaryota |
GeneTreei | ENSGT00940000157002 |
HOGENOMi | CLU_000709_4_0_1 |
InParanoidi | P43565 |
OMAi | ISQVLQW |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 984 |
Miscellaneous databases
PROi | PR:P43565 |
RNActi | P43565, protein |
Family and domain databases
InterProi | View 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 |
Pfami | View protein in Pfam PF00069, Pkinase, 2 hits |
SMARTi | View protein in SMART SM00448, REC, 1 hit SM00133, S_TK_X, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF52172, SSF52172, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | RIM15_YEAST | |
Accessioni | P43565Primary (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: | February 23, 2022 | |
This is version 211 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome VI
Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names - SIMILARITY comments
Index of protein domains and families