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Protein

Dual specificity protein kinase YAK1

Gene

YAK1

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

Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability. Phosphorylates POP2.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei398 – 3981ATPPROSITE-ProRule annotation
Active sitei496 – 4961Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi375 – 3839ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • peptidyl-tyrosine phosphorylation Source: GOC
  • positive regulation of cell-substrate adhesion Source: CACAO
  • positive regulation of transcription, DNA-templated Source: CACAO
  • protein phosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31586-MONOMER.
BRENDAi2.7.12.1. 984.
ReactomeiR-SCE-6804756. Regulation of TP53 Activity through Phosphorylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein kinase YAK1 (EC:2.7.12.1)
Gene namesi
Name:YAK1
Ordered Locus Names:YJL141C
ORF Names:J0652
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL141C.
SGDiS000003677. YAK1.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Shuttles between both compartments in response to glucose.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 807807Dual specificity protein kinase YAK1PRO_0000086828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineCombined sources
Modified residuei115 – 1151PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei240 – 2401PhosphoserineCombined sources
Modified residuei245 – 2451PhosphoserineCombined sources
Modified residuei247 – 2471PhosphoserineCombined sources
Modified residuei288 – 2881PhosphothreonineCombined sources
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei530 – 5301PhosphotyrosineCombined sources1 Publication

Post-translational modificationi

Phosphorylated; highly.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14680.
PeptideAtlasiP14680.

PTM databases

iPTMnetiP14680.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HRT1Q082733EBI-20777,EBI-31686

Protein-protein interaction databases

BioGridi33616. 137 interactions.
DIPiDIP-1374N.
IntActiP14680. 26 interactions.
MINTiMINT-401556.

Structurei

3D structure databases

ProteinModelPortaliP14680.
SMRiP14680. Positions 282-738.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 704336Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 8530Gln-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119032.
HOGENOMiHOG000170931.
InParanoidiP14680.
KOiK18670.
OMAiRECLIHF.
OrthoDBiEOG7WDNBB.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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.

P14680-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSSNNNDSS SSNSNMNNSL SPTLVTHSDA SMGSGRASPD NSHMGRGIWN
60 70 80 90 100
PSYVNQGSQR SPQQQHQNHH QQQQQQQQQQ QQNSQFCFVN PWNEEKVTNS
110 120 130 140 150
QQNLVYPPQY DDLNSNESLD AYRRRKSSLV VPPARAPAPN PFQYDSYPAY
160 170 180 190 200
TSSNTSLAGN SSGQYPSGYQ QQQQQVYQQG AIHPSQFGSR FVPSLYDRQD
210 220 230 240 250
FQRRQSLAAT NYSSNFSSLN SNTNQGTNSI PVMSPYRRLS AYPPSTSPPL
260 270 280 290 300
QPPFKQLRRD EVQGQKLSIP QMQLCNSKND LQPVLNATPK FRRASLNSKT
310 320 330 340 350
ISPLVSVTKS LITTYSLCSP EFTYQTSKNP KRVLTKPSEG KCNNGFDNIN
360 370 380 390 400
SDYILYVNDV LGVEQNRKYL VLDILGQGTF GQVVKCQNLL TKEILAVKVV
410 420 430 440 450
KSRTEYLTQS ITEAKILELL NQKIDPTNKH HFLRMYDSFV HKNHLCLVFE
460 470 480 490 500
LLSNNLYELL KQNKFHGLSI QLIRTFTTQI LDSLCVLKES KLIHCDLKPE
510 520 530 540 550
NILLCAPDKP ELKIIDFGSS CEEARTVYTY IQSRFYRAPE IILGIPYSTS
560 570 580 590 600
IDMWSLGCIV AELFLGIPIF PGASEYNQLT RIIDTLGYPP SWMIDMGKNS
610 620 630 640 650
GKFMKKLAPE ESSSSTQKHR MKTIEEFCRE YNIVEKPSKQ YFKWRKLPDI
660 670 680 690 700
IRNYRYPKSI QNSQELIDQE MQNRECLIHF LGGVLNLNPL ERWTPQQAML
710 720 730 740 750
HPFITKQEFT GEWFPPGSSL PGPSEKHDDA KGQQSEYGSA NDSSNNAGHN
760 770 780 790 800
YVYNPSSATG GADSVDIGAI SKRKENTSGD ISNNFAVTHS VQEGPTSAFN

KLHIVEE
Length:807
Mass (Da):91,245
Last modified:April 1, 1990 - v1
Checksum:iE0B7C56FAA35E056
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16056 Genomic DNA. Translation: CAA34192.1.
X87371 Genomic DNA. Translation: CAA60814.1.
Z49417 Genomic DNA. Translation: CAA89437.1.
BK006943 Genomic DNA. Translation: DAA08659.1.
PIRiA32582.
RefSeqiNP_012394.1. NM_001181574.1.

Genome annotation databases

EnsemblFungiiYJL141C; YJL141C; YJL141C.
GeneIDi853300.
KEGGisce:YJL141C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16056 Genomic DNA. Translation: CAA34192.1.
X87371 Genomic DNA. Translation: CAA60814.1.
Z49417 Genomic DNA. Translation: CAA89437.1.
BK006943 Genomic DNA. Translation: DAA08659.1.
PIRiA32582.
RefSeqiNP_012394.1. NM_001181574.1.

3D structure databases

ProteinModelPortaliP14680.
SMRiP14680. Positions 282-738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33616. 137 interactions.
DIPiDIP-1374N.
IntActiP14680. 26 interactions.
MINTiMINT-401556.

PTM databases

iPTMnetiP14680.

Proteomic databases

MaxQBiP14680.
PeptideAtlasiP14680.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL141C; YJL141C; YJL141C.
GeneIDi853300.
KEGGisce:YJL141C.

Organism-specific databases

EuPathDBiFungiDB:YJL141C.
SGDiS000003677. YAK1.

Phylogenomic databases

GeneTreeiENSGT00760000119032.
HOGENOMiHOG000170931.
InParanoidiP14680.
KOiK18670.
OMAiRECLIHF.
OrthoDBiEOG7WDNBB.

Enzyme and pathway databases

BioCyciYEAST:G3O-31586-MONOMER.
BRENDAi2.7.12.1. 984.
ReactomeiR-SCE-6804756. Regulation of TP53 Activity through Phosphorylation.

Miscellaneous databases

PROiP14680.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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. "Loss of Ras activity in Saccharomyces cerevisiae is suppressed by disruptions of a new kinase gene, YAKI, whose product may act downstream of the cAMP-dependent protein kinase."
    Garrett S., Broach J.
    Genes Dev. 3:1336-1348(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI."
    Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.
    Yeast 12:787-797(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [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. "Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal."
    Moriya H., Shimizu-Yoshida Y., Omori A., Iwashita S., Katoh M., Sakai A.
    Genes Dev. 15:1217-1228(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Saccharomyces cerevisiae Yak1p protein kinase autophosphorylates on tyrosine residues and phosphorylates myelin basic protein on a C-terminal serine residue."
    Kassis S., Melhuish T., Annan R.S., Chen S.L., Lee J.C., Livi G.P., Creasy C.L.
    Biochem. J. 348:263-272(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-530.
  7. "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.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND TYR-530, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, 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 SER-38 AND THR-288, 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-115; SER-118; SER-127; SER-206; SER-240; SER-245; SER-247; THR-288 AND TYR-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYAK1_YEAST
AccessioniPrimary (citable) accession number: P14680
Secondary accession number(s): D6VW43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.