Reviewed, UniProtKB/Swiss-Prot P43565 (RIM15_YEAST)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase RIM15
    EC=2.7.11.1

Gene names

Name:	RIM15
Synonyms:	TAK1
Ordered Locus Names:	YFL033C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1770 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 propoer G1 cell cycle arrest. Also involved in the activation of a meiotic genes activation pathway. Ref.3 Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Kinase activity is inhibited by phosphorylation by cAMP-dependent protein kinase (PKA). Ref.3
Subunit structure	Interacts with the cyclin-dependent kinase (CDK) PHO85.
Subcellular location	Cytoplasm. Nucleus.
Post-translational modification	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. Ref.4 Ref.5 Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain. Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Meiosis
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	age-dependent response to oxidative stress during chronological cell aging Inferred from mutant phenotype. Source: SGD meiosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.3 Inferred from direct assay. Source: SGD regulation of meiosis Ref.2 Inferred from mutant phenotype. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PHO85	P17157	1	EBI-15150,EBI-13327

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1770	1770	Serine/threonine-protein kinase RIM15		PRO_0000086605
Regions
	Domain	794 – 1254	461	Protein kinase
	Domain	1255 – 1320	66	AGC-kinase C-terminal
	Domain	1636 – 1750	115	Response regulatory
	Nucleotide binding	800 – 808	9	ATP By similarity
	Compositional bias	343 – 358	16	Poly-Asn
	Compositional bias	620 – 624	5	Poly-Ser
	Compositional bias	975 – 980	6	Poly-Asn
	Compositional bias	1213 – 1218	6	Poly-Glu
	Compositional bias	1386 – 1391	6	Poly-Thr
Sites
	Active site	918	1	Proton acceptor By similarity
	Binding site	823	1	ATP By similarity
Amino acid modifications
	Modified residue	24	1	Phosphoserine Ref.7
	Modified residue	380	1	Phosphoserine Ref.7
	Modified residue	476	1	Phosphoserine Ref.7
	Modified residue	547	1	Phosphoserine Ref.7
	Modified residue	704	1	Phosphothreonine Ref.7
	Modified residue	709	1	Phosphoserine Ref.7
	Modified residue	711	1	Phosphoserine Ref.7
	Modified residue	733	1	Phosphoserine Ref.5 Ref.7
	Modified residue	747	1	Phosphothreonine Ref.7
	Modified residue	1047	1	Phosphoserine Ref.6 Ref.7
	Modified residue	1048	1	Phosphoserine Ref.6 Ref.7
	Modified residue	1074	1	Phosphoserine Ref.7
	Modified residue	1075	1	Phosphothreonine; by PHO85 Ref.4 Ref.7
	Modified residue	1568	1	Phosphoserine Ref.7
	Modified residue	1595	1	Phosphoserine Ref.7
	Modified residue	1761	1	Phosphothreonine Ref.7
	Modified residue	1764	1	Phosphoserine Ref.5 Ref.6 Ref.7
Experimental info
	Mutagenesis	823	1	K → Y: Loss of kinase activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P43565-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DC1064825000FAFF	FASTA	1,770	196,531
	10 20 30 40 50 60 MFNRSNTAGG SQAMKEGLGI NKLSPISSNS NPSSLTSSNY EKYLQLATEK NPCMILELEL 70 80 90 100 110 120 DGKVRYGSPQ WNTITGVADD SGSSPTYIAD LILGSDQDKG VFQKATDMLL MNDDTSCTIT 130 140 150 160 170 180 FKIKAADYEG SAGCDDESTI TTLEARGILI RDGHTQLPSH TMWIVKPRTN DWSDFYANED 190 200 210 220 230 240 AQDDMVIQLS DNCDDIDIQL PEEFAKTLGF GAKIFVQYLK RIRLEMIIDE FNLPLPKMEL 250 260 270 280 290 300 CRVCENFVPV WWLETHSQSC VCEHRTESLI QLLHDNLLEQ QAILANFTKD SEYKGSQIQV 310 320 330 340 350 360 RSNNFLNQVL DSLRELCQDA IDINPSEMVP DLYHSLSTFP QDNGNNNNNN NNNNNNNNAL 370 380 390 400 410 420 LDQFPIQKDT VSLNSYFQFS PRTNHNIQNV TSWQSRFFLN DDQDPGLALL IHDTLDLARK 430 440 450 460 470 480 KVDAVLRLDN AMTYSLKIKN EVNNYVVQLI REQIEINKHA ILTHPMNLRS SSIFHSPLPQ 490 500 510 520 530 540 IHSQQPEAEN LIYSSSTPLQ VQHDQCASFE APSKSHLEPI PFPVSSIEET PTANDIRHPS 550 560 570 580 590 600 PLPRSCSNTV MKLPTPRRKL DSNGLFSDAY LNADIIPNPS IESTISIDRD NNTNSRGSSM 610 620 630 640 650 660 KQYGIGEATD SRTSNSERPS SSSSRLGIRS RSITPRQKIE YSHVDNDDRT NEMLSRDKDS 670 680 690 700 710 720 LQPQPSVDTT ITSSTQATTT GTKTNSNNST NSVLPKLMTS ISLTPRRGSP SFGNLASHSM 730 740 750 760 770 780 QQTNSFKLIH DKSPISSPFT FSKDFLTPEQ HPSNIARTDS INNAMLTSPN MPLSPLLLAT 790 800 810 820 830 840 NQTVKSPTPS IKDYDILKPI SKGAYGSVYL ARKKLTGDYF AIKVLRKSDM IAKNQVTNVK 850 860 870 880 890 900 SERAIMMVQS DKPYVARLFA SFQNKDNLFL VMEYLPGGDL ATLIKMMGYL PDQWAKQYLT 910 920 930 940 950 960 EIVVGVNDMH QNGIIHHDLK PENLLIDNAG HVKLTDFGLS RAGLIRRHKF VPHKSSLSIS 970 980 990 1000 1010 1020 STLPIDNPAN NFTMNNNNSN HSQLSTPDSF TSDHKQYNRS KKSSLGQQYE HSEYSSTSNS 1030 1040 1050 1060 1070 1080 HSMTPTPSTN TVVYPSYYRG KDRSHGSSNI DLPASLRRSE SQLSFSLLDI SRSSTPPLAN 1090 1100 1110 1120 1130 1140 PTNSNANNIM RRKSLTENKS FSNDLLSSDA IAATNTNINS NNNISLSPAP SDLALFYPDD 1150 1160 1170 1180 1190 1200 SKQNKKFFGT PDYLAPETIE GKGEDNKQCD WWSVGCIFFE LLLGYPPFHA ETPDAVFKKI 1210 1220 1230 1240 1250 1260 LSGVIQWPEF KNEEEEREFL TPEAKDLIEK LLVVDPAKRL GAKGIQEIKD HPYFKNVDWD 1270 1280 1290 1300 1310 1320 HVYDEEASFV PTIDNPEDTD YFDLRGAELQ DFGDDIENDN ANILFGKHGI NTDVSELSAA 1330 1340 1350 1360 1370 1380 NLSPPLNHKN ILSRKLSMSN TTNRSSNNSN SSVHDFGAHT PVNKLSIASV LESVPQETGY 1390 1400 1410 1420 1430 1440 ITPNGTGTTT TSAKNSPNLK NLSLAIPPHM RDRRSSKLND SQTEFGSFNF RNLSALDKAN 1450 1460 1470 1480 1490 1500 KDAINRLKSE HFSEQPGVHR RTSSASLMGS SSDGSVSTPG SNASNTTSGG KLKIHKPTIS 1510 1520 1530 1540 1550 1560 GSPSTFGTFP KTFLRSDSFS TRSYSPERSI SIDSSTLSRK GSIIGDNQQT TANSSDSPTM 1570 1580 1590 1600 1610 1620 TKFKSPLSPA NTTTVSSYFS RQRVLSKSFS QRTNSSDLSA EESDRLQAIS RVNSLRNRRR 1630 1640 1650 1660 1670 1680 SGRKSSSTSE IGYHMDVLVC EPIPIHRYRV TKDLENLGCT VVSVGAGDEL VSRATSGVSF 1690 1700 1710 1720 1730 1740 DLIMTALKLP KLGAIDIVQL LKQTNGANST TPIVAITNYF QEAATSRVFD DVLEKPVKLD 1750 1760 1770 ELKKLVAKYA LKKSQEDEEH TILSDSDETH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed: 7670463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"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: 9111339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[3]	"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: 9744870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LYS-823.
[4]	"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: 16308562] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-1075, SUBCELLULAR LOCATION.
[5]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733 AND SER-1764, MASS SPECTROMETRY.
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1047; SER-1048 AND SER-1764, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-380; SER-476; SER-547; THR-704; SER-709; SER-711; SER-733; THR-747; SER-1047; SER-1048; SER-1074; THR-1075; SER-1568; SER-1595; THR-1761 AND SER-1764, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D50617 Genomic DNA. Translation: BAA09206.1. U83459 Genomic DNA. Translation: AAB64088.1. AJ001030 Genomic DNA. Translation: CAA04486.1.
PIR	S56221.
RefSeq	NP_116620.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2510N.
IntAct	P43565. 4 interactions.
STRING	P43565.
Proteomic databases
PRIDE	P43565.
Genome annotation databases
Ensembl	YFL033C; YFL033C; YFL033C; Saccharomyces cerevisiae. [Genome view]
GeneID	850511.
KEGG	sce:YFL033C.
NMPDR	fig|4932.3.peg.2246.
Organism-specific databases
CYGD	YFL033c.
SGD	S000001861. RIM15.
Phylogenomic databases
HOGENOM	P43565.
OMA	RICERQI
OrthoDB	EOG9FTXGS
Enzyme and pathway databases
BRENDA	2.7.11.1. 250.
Gene expression databases
ArrayExpress	P43565.
Genevestigator	P43565.
GermOnline	YFL033C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011006. CheY-like. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
SMART	SM00448. REC. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	966227.

Entry information

Entry name

RIM15_YEAST

Accession

Primary (citable) accession number: P43565

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)