Serine/threonine-protein kinase RIM15 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Sequence or UniProt identifier

>sp|P43565|RIM15_YEAST Serine/threonine-protein kinase RIM15 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RIM15 PE=1 SV=1 MFNRSNTAGGSQAMKEGLGINKLSPISSNSNPSSLTSSNYEKYLQLATEKNPCMILELEL DGKVRYGSPQWNTITGVADDSGSSPTYIADLILGSDQDKGVFQKATDMLLMNDDTSCTIT FKIKAADYEGSAGCDDESTITTLEARGILIRDGHTQLPSHTMWIVKPRTNDWSDFYANED AQDDMVIQLSDNCDDIDIQLPEEFAKTLGFGAKIFVQYLKRIRLEMIIDEFNLPLPKMEL CRVCENFVPVWWLETHSQSCVCEHRTESLIQLLHDNLLEQQAILANFTKDSEYKGSQIQV RSNNFLNQVLDSLRELCQDAIDINPSEMVPDLYHSLSTFPQDNGNNNNNNNNNNNNNNAL LDQFPIQKDTVSLNSYFQFSPRTNHNIQNVTSWQSRFFLNDDQDPGLALLIHDTLDLARK KVDAVLRLDNAMTYSLKIKNEVNNYVVQLIREQIEINKHAILTHPMNLRSSSIFHSPLPQ IHSQQPEAENLIYSSSTPLQVQHDQCASFEAPSKSHLEPIPFPVSSIEETPTANDIRHPS PLPRSCSNTVMKLPTPRRKLDSNGLFSDAYLNADIIPNPSIESTISIDRDNNTNSRGSSM KQYGIGEATDSRTSNSERPSSSSSRLGIRSRSITPRQKIEYSHVDNDDRTNEMLSRDKDS LQPQPSVDTTITSSTQATTTGTKTNSNNSTNSVLPKLMTSISLTPRRGSPSFGNLASHSM QQTNSFKLIHDKSPISSPFTFSKDFLTPEQHPSNIARTDSINNAMLTSPNMPLSPLLLAT NQTVKSPTPSIKDYDILKPISKGAYGSVYLARKKLTGDYFAIKVLRKSDMIAKNQVTNVK SERAIMMVQSDKPYVARLFASFQNKDNLFLVMEYLPGGDLATLIKMMGYLPDQWAKQYLT EIVVGVNDMHQNGIIHHDLKPENLLIDNAGHVKLTDFGLSRAGLIRRHKFVPHKSSLSIS STLPIDNPANNFTMNNNNSNHSQLSTPDSFTSDHKQYNRSKKSSLGQQYEHSEYSSTSNS HSMTPTPSTNTVVYPSYYRGKDRSHGSSNIDLPASLRRSESQLSFSLLDISRSSTPPLAN PTNSNANNIMRRKSLTENKSFSNDLLSSDAIAATNTNINSNNNISLSPAPSDLALFYPDD SKQNKKFFGTPDYLAPETIEGKGEDNKQCDWWSVGCIFFELLLGYPPFHAETPDAVFKKI LSGVIQWPEFKNEEEEREFLTPEAKDLIEKLLVVDPAKRLGAKGIQEIKDHPYFKNVDWD HVYDEEASFVPTIDNPEDTDYFDLRGAELQDFGDDIENDNANILFGKHGINTDVSELSAA NLSPPLNHKNILSRKLSMSNTTNRSSNNSNSSVHDFGAHTPVNKLSIASVLESVPQETGY ITPNGTGTTTTSAKNSPNLKNLSLAIPPHMRDRRSSKLNDSQTEFGSFNFRNLSALDKAN KDAINRLKSEHFSEQPGVHRRTSSASLMGSSSDGSVSTPGSNASNTTSGGKLKIHKPTIS GSPSTFGTFPKTFLRSDSFSTRSYSPERSISIDSSTLSRKGSIIGDNQQTTANSSDSPTM TKFKSPLSPANTTTVSSYFSRQRVLSKSFSQRTNSSDLSAEESDRLQAISRVNSLRNRRR SGRKSSSTSEIGYHMDVLVCEPIPIHRYRVTKDLENLGCTVVSVGAGDELVSRATSGVSF DLIMTALKLPKLGAIDIVQLLKQTNGANSTTPIVAITNYFQEAATSRVFDDVLEKPVKLD ELKKLVAKYALKKSQEDEEHTILSDSDETH

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P43565 (RIM15_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1770 AA.
Sequence status	Complete.
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.4 Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Kinase activity is inhibited by phosphorylation by cAMP-dependent protein kinase (PKA). Ref.4
Subunit structure	Interacts with the cyclin-dependent kinase (CDK) PHO85.
Subcellular location	Cytoplasm. Nucleus Ref.5.
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.5 Ref.6 Ref.7 Ref.8
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 Reference proteome
Gene Ontology (GO)
Biological process	age-dependent response to oxidative stress involved in chronological cell aging Inferred from mutant phenotype. Source: SGD meiosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of meiosis Inferred from mutant phenotype Ref.3. Source: SGD regulation of transcription, DNA-dependent 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
KIN2	P13186	2	EBI-15150,EBI-9723

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

AGC-kinase C-terminal

Domain

1636 – 1750

115

Response regulatory

Nucleotide binding

800 – 808

ATP By similarity

Compositional bias

343 – 358

Poly-Asn

Compositional bias

620 – 624

Poly-Ser

Compositional bias

975 – 980

Poly-Asn

Compositional bias

1213 – 1218

Poly-Glu

Compositional bias

1386 – 1391

Poly-Thr

Sites

Active site

918

Proton acceptor By similarity

Binding site

823

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

380

Phosphoserine Ref.8

Modified residue

476

Phosphoserine Ref.8

Modified residue

547

Phosphoserine Ref.8

Modified residue

704

Phosphothreonine Ref.8

Modified residue

709

Phosphoserine Ref.8

Modified residue

711

Phosphoserine Ref.8

Modified residue

733

Phosphoserine Ref.6 Ref.8

Modified residue

747

Phosphothreonine Ref.8

Modified residue

1047

Phosphoserine Ref.7 Ref.8

Modified residue

1048

Phosphoserine Ref.7 Ref.8

Modified residue

1074

Phosphoserine Ref.8

Modified residue

1075

Phosphothreonine; by PHO85 Ref.5 Ref.8

Modified residue

1568

Phosphoserine Ref.8

Modified residue

1595

Phosphoserine Ref.8

Modified residue

1761

Phosphothreonine Ref.8

Modified residue

1764

Phosphoserine Ref.6 Ref.7 Ref.8

Experimental info

Mutagenesis

823

K → Y: Loss of kinase activity. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P43565 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DC1064825000FAFF
Show »

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

« Hide

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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 9111339] [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: 9744870] [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: 16308562] [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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733 AND SER-1764, MASS SPECTROMETRY. Strain: ADR376.
[7]	"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.
[8]	"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
EMBL GenBank DDBJ	D50617 Genomic DNA. Translation: BAA09206.1. U83459 Genomic DNA. Translation: AAB64088.1. AJ001030 Genomic DNA. Translation: CAA04486.1. BK006940 Genomic DNA. Translation: DAA12408.1.
PIR	S56221.
RefSeq	NP_116620.1. NM_001179933.1.
3D structure databases
ProteinModelPortal	P43565.
SMR	P43565. Positions 787-1284, 1637-1750.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2510N.
IntAct	P43565. 5 interactions.
MINT	MINT-674598.
STRING	P43565.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YFL033C; YFL033C; YFL033C.
GeneID	850511.
KEGG	sce:YFL033C.
NMPDR	fig\|4932.3.peg.2246.
Organism-specific databases
CYGD	YFL033c.
SGD	S000001861. RIM15.
Phylogenomic databases
eggNOG	fuNOG05196.
GeneTree	EFGT00070000008712.
HOGENOM	HBG203588.
OMA	RICERQI.
OrthoDB	EOG4BGD43.
Enzyme and pathway databases
BRENDA	2.7.11.1. 984.
Gene expression databases
ArrayExpress	P43565.
Genevestigator	P43565.
GermOnline	YFL033C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011006. CheY-like_superfamily. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
KO	K12767.
Pfam	PF00069. Pkinase. 2 hits. 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]
SUPFAM	SSF52172. CheY_like. 1 hit. SSF56112. Kinase_like. 1 hit.
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
NextBio	966227.

Entry information

Entry name

RIM15_YEAST

Accession

Primary (citable) accession number: P43565
Secondary accession number(s): D6VTJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	December 14, 2011
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents