Serine/threonine-protein kinase RIM15 - Saccharomyces cerevisiae (Baker's yeast)

Sequence

>sp|P43565|RIM15_YEAST Serine/threonine-protein kinase RIM15 OS=Saccharomyces cerevisiae 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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Reviewed, UniProtKB/Swiss-Prot P43565 (RIM15_YEAST)

Last modified September 2, 2008. Version 90. History...

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

Documents (3) |

Third-party data |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

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

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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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Kinase activity is inhibited by phosphorylation by cAMP-dependent protein kinase (PKA).
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.
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.

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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 protein amino acid phosphorylation Ref.3 Inferred from direct assay. Source: SGD regulation of meiosis Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein kinase activity Ref.3 Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

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

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 1770

1770

Serine/threonine-protein kinase RIM15

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

Modified residue

380

Phosphoserine

Modified residue

476

Phosphoserine

Modified residue

547

Phosphoserine

Modified residue

704

Phosphothreonine

Modified residue

709

Phosphoserine

Modified residue

711

Phosphoserine

Modified residue

733

Phosphoserine

Modified residue

747

Phosphothreonine

Modified residue

1047

Phosphoserine

Modified residue

1048

Phosphoserine

Modified residue

1074

Phosphoserine

Modified residue

1075

Phosphothreonine; by PHO85

Modified residue

1568

Phosphoserine

Modified residue

1595

Phosphoserine

Modified residue

1761

Phosphothreonine

Modified residue

1764

Phosphoserine

Experimental info

Mutagenesis

823

K → Y: Loss of kinase activity

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Sequences

Sequence

Length

Mass (Da)

Tools

P43565-1 [UniParc].

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

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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.

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Cross-references

Sequence databases
	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
HSSP	HSSP built from PDB template 1FOT based on UniProtKB P06244.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2510N.
IntAct	P43565.
Genome annotation databases
Ensembl	YFL033C. Saccharomyces cerevisiae. [Contig view]
GeneID	850511.
GenomeReviews	Gene locus YFL033C in contig D50617_GR.
KEGG	sce:YFL033C.
NMPDR	fig\|4932.3.peg.2246.
Organism-specific databases
CYGD	YFL033c.
SGD	S000001861. RIM15.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P43565.
Gene expression databases
ArrayExpress	P43565.
GermOnline	YFL033C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000961. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 2 hits. PD000039. Response_reg. 1 hit. [Graphical view] [Entries sharing at least one domain]
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]
BLOCKS	Search...
Other Resources
LinkHub	P43565.
ProtoNet	Search...

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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:	September 2, 2008
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents