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Protein

Serine/threonine-protein kinase RCK2

Gene

RCK2

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 involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ser-520 phosphorylation by HOG1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei201 – 2011ATPPROSITE-ProRule annotation
Active sitei313 – 3131Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1779ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to oxidative stress Source: SGD
  • osmosensory signaling pathway Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of meiotic nuclear division Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32353-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-171007. p38MAPK events.
R-SCE-2559580. Oxidative Stress Induced Senescence.
R-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-4420097. VEGFA-VEGFR2 Pathway.
R-SCE-450302. activated TAK1 mediates p38 MAPK activation.
R-SCE-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-SCE-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RCK2 (EC:2.7.11.1)
Alternative name(s):
CAM kinase-like protein kinase CLK1
Gene namesi
Name:RCK2
Synonyms:CLK1, CMK3
Ordered Locus Names:YLR248W
ORF Names:L9672.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR248W.
SGDiS000004238. RCK2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 610610Serine/threonine-protein kinase RCK2PRO_0000086604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei187 – 1871PhosphoserineCombined sources
Modified residuei350 – 3501PhosphothreonineCombined sources
Modified residuei520 – 5201Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated. Phosphorylated by HOG1 at Ser-520 after osmotic stress.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38623.

PTM databases

iPTMnetiP38623.

Interactioni

Protein-protein interaction databases

BioGridi31516. 79 interactions.
DIPiDIP-5079N.
IntActiP38623. 6 interactions.
MINTiMINT-508548.

Structurei

3D structure databases

ProteinModelPortaliP38623.
SMRiP38623. Positions 163-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 478316Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni493 – 50614Calmodulin-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00830000128274.
HOGENOMiHOG000183591.
InParanoidiP38623.
KOiK08286.
OMAiWWDEISP.
OrthoDBiEOG7S4XG2.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 3 hits.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKIKALFSK KKPDQADLSQ ESKKPFKGKT RSSGTNNKDV SQITSSPKKS
60 70 80 90 100
FQDKNIVQYP SVVADDHHMK SLTDELVTTI DSDSSPSDNI TTENVETVTS
110 120 130 140 150
VPAIDVHESS EGQLSSDPLI SDESLSEQSE IISDIQDDST DDDNMEDEIP
160 170 180 190 200
EKSFLEQKEL IGYKLINKIG EGAFSKVFRA IPAKNSSNEF LTKNYKAVAI
210 220 230 240 250
KVIKKADLSS INGDHRKKDK GKDSTKTSSR DQVLKEVALH KTVSAGCSQI
260 270 280 290 300
VAFIDFQETD SYYYIIQELL TGGEIFGEIV RLTYFSEDLS RHVIKQLALA
310 320 330 340 350
VKHMHSLGVV HRDIKPENLL FEPIEFTRSI KPKLRKSDDP QTKADEGIFT
360 370 380 390 400
PGVGGGGIGI VKLADFGLSK QIFSKNTKTP CGTVGYTAPE VVKDEHYSMK
410 420 430 440 450
VDMWGIGCVL YTMLCGFPPF YDEKIDTLTE KISRGEYTFL KPWWDEISAG
460 470 480 490 500
AKNAVAKLLE LEPSKRYDID QFLDDPWLNT FDCLPKEGES SQKKAGTSER
510 520 530 540 550
RHPHKKQFQL FQRDSSLLFS PAAVAMRDAF DIGNAVKRTE EDRMGTRGGL
560 570 580 590 600
GSLAEDEELE DSYSGAQGDE QLEQNMFQLT LDTSTILQRR KKVQENDVGP
610
TIPISATIRE
Length:610
Mass (Da):68,062
Last modified:October 5, 2010 - v3
Checksum:i00DDC674F6723E6A
GO

Sequence cautioni

The sequence CAA50389.1 differs from that shown. Reason: Frameshift at position 569. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091S → N in CAA50389 (PubMed:8112585).Curated
Sequence conflicti109 – 1091S → N in AAA64421 (PubMed:8939941).Curated
Sequence conflicti188 – 1881N → H in CAA50389 (PubMed:8112585).Curated
Sequence conflicti188 – 1881N → H in AAA64421 (PubMed:8939941).Curated
Sequence conflicti233 – 2331V → A in CAA50389 (PubMed:8112585).Curated
Sequence conflicti233 – 2331V → A in AAA64421 (PubMed:8939941).Curated
Sequence conflicti328 – 3281R → P in CAA50389 (PubMed:8112585).Curated
Sequence conflicti328 – 3281R → P in AAA64421 (PubMed:8939941).Curated
Sequence conflicti456 – 4561A → S in CAA50389 (PubMed:8112585).Curated
Sequence conflicti456 – 4561A → S in AAA64421 (PubMed:8939941).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71065 Genomic DNA. Translation: CAA50389.1. Frameshift.
U23464 Genomic DNA. Translation: AAA64421.1.
U20865 Genomic DNA. Translation: AAB67392.1.
BK006945 Genomic DNA. Translation: DAA09562.1.
PIRiS59394.
RefSeqiNP_013349.1. NM_001182135.1.

Genome annotation databases

EnsemblFungiiYLR248W; YLR248W; YLR248W.
GeneIDi850950.
KEGGisce:YLR248W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71065 Genomic DNA. Translation: CAA50389.1. Frameshift.
U23464 Genomic DNA. Translation: AAA64421.1.
U20865 Genomic DNA. Translation: AAB67392.1.
BK006945 Genomic DNA. Translation: DAA09562.1.
PIRiS59394.
RefSeqiNP_013349.1. NM_001182135.1.

3D structure databases

ProteinModelPortaliP38623.
SMRiP38623. Positions 163-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31516. 79 interactions.
DIPiDIP-5079N.
IntActiP38623. 6 interactions.
MINTiMINT-508548.

PTM databases

iPTMnetiP38623.

Proteomic databases

MaxQBiP38623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR248W; YLR248W; YLR248W.
GeneIDi850950.
KEGGisce:YLR248W.

Organism-specific databases

EuPathDBiFungiDB:YLR248W.
SGDiS000004238. RCK2.

Phylogenomic databases

GeneTreeiENSGT00830000128274.
HOGENOMiHOG000183591.
InParanoidiP38623.
KOiK08286.
OMAiWWDEISP.
OrthoDBiEOG7S4XG2.

Enzyme and pathway databases

BioCyciYEAST:G3O-32353-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-171007. p38MAPK events.
R-SCE-2559580. Oxidative Stress Induced Senescence.
R-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-4420097. VEGFA-VEGFR2 Pathway.
R-SCE-450302. activated TAK1 mediates p38 MAPK activation.
R-SCE-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-SCE-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

PROiP38623.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 3 hits.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
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. "Two novel deduced serine/threonine protein kinases from Saccharomyces cerevisiae."
    Dahlkvist A., Sunnerhagen P.
    Gene 139:27-33(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204510 / AB320.
  2. "Identification and characterization of the CLK1 gene product, a novel CaM kinase-like protein kinase from the yeast Saccharomyces cerevisiae."
    Melcher M.L., Thorner J.
    J. Biol. Chem. 271:29958-29968(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: YNN 214.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Rck2 kinase is a substrate for the osmotic stress-activated mitogen-activated protein kinase Hog1."
    Bilsland-Marchesan E., Arino J., Saito H., Sunnerhagen P., Posas F.
    Mol. Cell. Biol. 20:3887-3895(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-520, ENZYME REGULATION, INTERACTION WITH HOG1.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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 SER-46; SER-50 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRCK2_YEAST
AccessioniPrimary (citable) accession number: P38623
Secondary accession number(s): D6VYP6, Q02532, Q06557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 5, 2010
Last modified: July 6, 2016
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1790 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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 one 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.