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Protein

Serine/threonine-protein kinase RIM11/MSD1

Gene

RIM11

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

Serine/threonine protein kinase that is thought to function in regulating kinetochore activity and entry into meiosis. Could phosphorylates IME1.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei68 – 681ATPPROSITE-ProRule annotation
Active sitei164 – 1641Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 539ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • cellular response to heat Source: SGD
  • cellular response to salt stress Source: SGD
  • protein phosphorylation Source: SGD
  • proteolysis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32832-MONOMER.
BRENDAi2.7.11.26. 984.
ReactomeiREACT_333905. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RIM11/MSD1 (EC:2.7.11.1)
Alternative name(s):
Regulator of IME2 protein 11
Gene namesi
Name:RIM11
Synonyms:GSK3, MDS1
Ordered Locus Names:YMR139W
ORF Names:YM9375.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR139w.
EuPathDBiFungiDB:YMR139W.
SGDiS000004747. RIM11.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Serine/threonine-protein kinase RIM11/MSD1PRO_0000086319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991Phosphotyrosine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38615.
PaxDbiP38615.
PeptideAtlasiP38615.

Interactioni

Subunit structurei

Interacts with TDA1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NAP1P252938EBI-10642,EBI-11850

Protein-protein interaction databases

BioGridi35316. 106 interactions.
DIPiDIP-1566N.
IntActiP38615. 19 interactions.
MINTiMINT-397554.

Structurei

3D structure databases

ProteinModelPortaliP38615.
SMRiP38615. Positions 36-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 322284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
InParanoidiP38615.
KOiK12766.
OMAiPTERQSA.
OrthoDBiEOG7CZKGN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIQSNNSPN LSNNIVSKQV YYAHPPPTID PNDPVQISFP TTEVVGHGSF
60 70 80 90 100
GVVFATVIQE TNEKVAIKKV LQDKRFKNRE LEIMKMLSHI NIIDLKYFFY
110 120 130 140 150
ERDSQDEIYL NLILEYMPQS LYQRLRHFVH QRTPMSRLEI KYYMFQLFKS
160 170 180 190 200
LNYLHHFANV CHRDIKPQNL LVDPETWSLK LCDFGSAKQL KPTEPNVSYI
210 220 230 240 250
CSRYYRAPEL IFGATNYTNQ IDIWSSGCVM AELLLGQPMF PGESGIDQLV
260 270 280 290 300
EIIKILGTPS KQEICSMNPN YMEHKFPQIK PIPLSRVFKK EDDQTVEFLA
310 320 330 340 350
DVLKYDPLER FNALQCLCSP YFDELKLDDG KINQITTDLK LLEFDENVEL
360 370
GHLSPDELSS VKKKLYPKSK
Length:370
Mass (Da):43,005
Last modified:October 1, 1994 - v1
Checksum:i59D92C9D42408E97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571V → I in AAA16206 (PubMed:8244030).Curated
Sequence conflicti331 – 3311K → R in AAS56320 (PubMed:17322287).Curated
Sequence conflicti343 – 3431E → G in AAA16206 (PubMed:8244030).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03280 Unassigned DNA. Translation: AAC48917.1.
L29284 Genomic DNA. Translation: AAB04166.1.
L12761 Unassigned DNA. Translation: AAA16206.1.
Z47071 Genomic DNA. Translation: CAA87353.1.
AY557994 Genomic DNA. Translation: AAS56320.1.
BK006946 Genomic DNA. Translation: DAA10036.1.
PIRiA56347.
RefSeqiNP_013859.1. NM_001182641.1.

Genome annotation databases

EnsemblFungiiYMR139W; YMR139W; YMR139W.
GeneIDi855170.
KEGGisce:YMR139W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03280 Unassigned DNA. Translation: AAC48917.1.
L29284 Genomic DNA. Translation: AAB04166.1.
L12761 Unassigned DNA. Translation: AAA16206.1.
Z47071 Genomic DNA. Translation: CAA87353.1.
AY557994 Genomic DNA. Translation: AAS56320.1.
BK006946 Genomic DNA. Translation: DAA10036.1.
PIRiA56347.
RefSeqiNP_013859.1. NM_001182641.1.

3D structure databases

ProteinModelPortaliP38615.
SMRiP38615. Positions 36-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35316. 106 interactions.
DIPiDIP-1566N.
IntActiP38615. 19 interactions.
MINTiMINT-397554.

Proteomic databases

MaxQBiP38615.
PaxDbiP38615.
PeptideAtlasiP38615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR139W; YMR139W; YMR139W.
GeneIDi855170.
KEGGisce:YMR139W.

Organism-specific databases

CYGDiYMR139w.
EuPathDBiFungiDB:YMR139W.
SGDiS000004747. RIM11.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
InParanoidiP38615.
KOiK12766.
OMAiPTERQSA.
OrthoDBiEOG7CZKGN.

Enzyme and pathway databases

BioCyciYEAST:G3O-32832-MONOMER.
BRENDAi2.7.11.26. 984.
ReactomeiREACT_333905. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

NextBioi978608.
PROiP38615.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MDS1, a dosage suppressor of an mck1 mutant, encodes a putative yeast homolog of glycogen synthase kinase 3."
    Puziss J.W., Hardy T.A., Johnson R.B., Roach P.J., Hieter P.
    Mol. Cell. Biol. 14:831-839(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 204508 / S288c.
  2. "Analysis of RIM11, a yeast protein kinase that phosphorylates the meiotic activator IME1."
    Bowdish K.S., Yuan H.E., Mitchell A.P.
    Mol. Cell. Biol. 14:7909-7919(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A Saccharomyces cerevisiae protein-serine kinase related to mammalian glycogen synthase kinase-3 and the Drosophila melanogaster gene shaggy product."
    Bianchi M.W., Plyte S.E., Kreis M., Woodgett J.R.
    Gene 134:51-56(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. "Essential functions of protein tyrosine phosphatases PTP2 and PTP3 and RIM11 tyrosine phosphorylation in Saccharomyces cerevisiae meiosis and sporulation."
    Zhan X.L., Hong Y., Zhu T., Mitchell A.P., Deschenes R.J., Guan K.L.
    Mol. Biol. Cell 11:663-676(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-199.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes."
    Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M., Gerstein M., Snyder M.
    Genes Dev. 25:767-778(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDA1.

Entry informationi

Entry nameiRIM11_YEAST
AccessioniPrimary (citable) accession number: P38615
Secondary accession number(s): D6VZW2, Q6Q5K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 22, 2015
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6990 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.