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P21965 (MCK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase MCK1

EC=2.7.12.1
Alternative name(s):
Meiosis and centromere regulatory kinase
Gene names
Name:MCK1
Synonyms:YPK1
Ordered Locus Names:YNL307C
ORF Names:N0392
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be an autophosphorylating tyrosine kinase, a bifunctional (serine/tyrosine-specific) protein kinase, or a serine kinase that is a substrate for an associated tyrosine kinase. MCK1 is a transcriptional activator of IME1, it stimulates spore maturation, and play a positive regulatory role in both mitotic centromere function and activation of early meiotic gene expression.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Post-translational modification

Phosphorylated at tyrosine and serine.

Miscellaneous

Present with 396 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processascospore formation

Inferred from mutant phenotype Ref.2. Source: SGD

cellular response to heat

Inferred from mutant phenotype PubMed 12529445. Source: SGD

cellular response to salt stress

Inferred from mutant phenotype PubMed 12529445. Source: SGD

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 12399380. Source: SGD

meiotic nuclear division

Inferred from mutant phenotype Ref.2. Source: SGD

mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.3. Source: SGD

negative regulation of catalytic activity

Inferred from mutant phenotype PubMed 22918234. Source: GOC

protein phosphorylation

Inferred from direct assay PubMed 8407952. Source: SGD

protein phosphorylation involved in cellular protein catabolic process

Inferred from mutant phenotype PubMed 17954914PubMed 23236290. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin binding

Inferred from physical interaction PubMed 22918234. Source: SGD

enzyme inhibitor activity

Inferred from mutant phenotype PubMed 22918234. Source: SGD

protein binding

Inferred from physical interaction PubMed 20489023. Source: IntAct

protein serine/threonine kinase activity

Inferred from sequence or structural similarity PubMed 12529445. Source: SGD

protein serine/threonine/tyrosine kinase activity

Inferred from direct assay PubMed 8407952. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC14Q006842EBI-10517,EBI-4192

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 375374Protein kinase MCK1
PRO_0000086317

Regions

Domain35 – 327293Protein kinase
Nucleotide binding41 – 499ATP By similarity

Sites

Active site1641Proton acceptor By similarity
Binding site681ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue1981Phosphoserine Ref.10 Ref.11
Modified residue1991Phosphotyrosine Ref.9 Ref.11
Modified residue2021Phosphoserine Ref.11

Sequences

Sequence LengthMass (Da)Tools
P21965 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: BCF0C776B6E3841B

FASTA37543,136
        10         20         30         40         50         60 
MSTEEQNGVP LQRGSEFIAD DVTSNKSNNT RRMLVKEYRK IGRGAFGTVV QAYLTQDKKN 

        70         80         90        100        110        120 
WLGPFAIKKV PAHTEYKSRE LQILRIADHP NIVKLQYFFT HLSPQDNKVY QHLAMECLPE 

       130        140        150        160        170        180 
TLQIEINRYV TNKLEMPLKH IRLYTYQIAR GMLYLHGLGV CHRDIKPSNV LVDPETGVLK 

       190        200        210        220        230        240 
ICDFGSAKKL EHNQPSISYI CSRFYRAPEL IIGCTQYTTQ IDIWGLGCVM GEMLIGKAIF 

       250        260        270        280        290        300 
QGQEPLLQLR EIAKLLGPPD KRFIFFSNPA YDGPLFSKPL FSGSSQQRFE KYFGHSGPDG 

       310        320        330        340        350        360 
IDLLMKILVY EPQQRLSPRR ILAHQFFNEL RNDDTFLPRG FTEPIKLPNL FDFNDFELQI 

       370 
LGEFADKIKP TKVAE 

« Hide

References

« Hide 'large scale' references
[1]"Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity."
Dailey D., Schieven G.L., Lim M.-Y., Marquardt H., Gilmore T., Thorner J., Martin G.S.
Mol. Cell. Biol. 10:6244-6256(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"The yeast MCK1 gene encodes a protein kinase homolog that activates early meiotic gene expression."
Neigeborn L., Mitchell A.P.
Genes Dev. 5:533-548(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A suppressor of a centromere DNA mutation encodes a putative protein kinase (MCK1)."
Shero J.H., Hieter P.
Genes Dev. 5:549-560(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV identifies six known genes, a new member of the hexose transporter family and ten new open reading frames."
Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.
Yeast 11:1077-1085(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / FY1676.
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV carrying a ribosomal protein gene cluster, the genes encoding a plasma membrane protein and a subunit of replication factor C, and a novel putative serine/threonine protein kinase gene."
Maurer K.C.T., Urbanus J.H.M., Planta R.J.
Yeast 11:1303-1310(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
Strain: ATCC 96604 / S288c / FY1679.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"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.
[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 SER-198, 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-198; TYR-199 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55054 Genomic DNA. Translation: CAA38895.1.
M55984 Genomic DNA. Translation: AAA34764.1.
Z46259 Genomic DNA. Translation: CAA86388.1.
Z71583 Genomic DNA. Translation: CAA96236.1.
Z71582 Genomic DNA. Translation: CAA96235.1.
BK006947 Genomic DNA. Translation: DAA10254.1.
PIRA39622.
RefSeqNP_014092.1. NM_001183145.1.

3D structure databases

ProteinModelPortalP21965.
SMRP21965. Positions 41-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35532. 426 interactions.
DIPDIP-5860N.
IntActP21965. 43 interactions.
MINTMINT-681308.
STRING4932.YNL307C.

Proteomic databases

MaxQBP21965.
PaxDbP21965.
PeptideAtlasP21965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL307C; YNL307C; YNL307C.
GeneID855409.
KEGGsce:YNL307C.

Organism-specific databases

CYGDYNL307c.
SGDS000005251. MCK1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000116084.
HOGENOMHOG000233017.
KOK00924.
OMAYKSRELE.
OrthoDBEOG7CZKGN.

Enzyme and pathway databases

BioCycYEAST:G3O-33294-MONOMER.
BRENDA2.7.11.26. 984.

Gene expression databases

GenevestigatorP21965.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979250.
PROP21965.

Entry information

Entry nameMCK1_YEAST
AccessionPrimary (citable) accession number: P21965
Secondary accession number(s): D6W0N8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families