P14680 (YAK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein kinase YAK1
EC=2.7.12.1

Gene names

Name:	YAK1
Ordered Locus Names:	YJL141C
ORF Names:	J0652

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles between both compartments in response to glucose.
Post-translational modification	Phosphorylated; highly. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay Ref.5. Source: SGD nucleus Inferred from direct assay Ref.5. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from mutant phenotype. Source: SGD protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HRT1	Q08273	3	EBI-20777,EBI-31686

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 807	807	Dual specificity protein kinase YAK1		PRO_0000086828
Regions
	Domain	369 – 704	336	Protein kinase
	Nucleotide binding	375 – 383	9	ATP By similarity
	Compositional bias	56 – 85	30	Gln-rich
Sites
	Active site	496	1	Proton acceptor By similarity
	Binding site	398	1	ATP By similarity
Amino acid modifications
	Modified residue	38	1	Phosphoserine Ref.11
	Modified residue	127	1	Phosphoserine Ref.7 Ref.9 Ref.11
	Modified residue	128	1	Phosphoserine Ref.7 Ref.9 Ref.11
	Modified residue	206	1	Phosphoserine Probable
	Modified residue	240	1	Phosphoserine Probable
	Modified residue	247	1	Phosphoserine Ref.11
	Modified residue	288	1	Phosphothreonine Ref.11
	Modified residue	295	1	Phosphoserine Ref.7 Ref.10
	Modified residue	298	1	Phosphoserine Ref.10
	Modified residue	529	1	Phosphothreonine Ref.11
	Modified residue	530	1	Phosphotyrosine Ref.6 Ref.8 Ref.9 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P14680 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: E0B7C56FAA35E056	FASTA	807	91,245
	10 20 30 40 50 60 MNSSNNNDSS SSNSNMNNSL SPTLVTHSDA SMGSGRASPD NSHMGRGIWN PSYVNQGSQR 70 80 90 100 110 120 SPQQQHQNHH QQQQQQQQQQ QQNSQFCFVN PWNEEKVTNS QQNLVYPPQY DDLNSNESLD 130 140 150 160 170 180 AYRRRKSSLV VPPARAPAPN PFQYDSYPAY TSSNTSLAGN SSGQYPSGYQ QQQQQVYQQG 190 200 210 220 230 240 AIHPSQFGSR FVPSLYDRQD FQRRQSLAAT NYSSNFSSLN SNTNQGTNSI PVMSPYRRLS 250 260 270 280 290 300 AYPPSTSPPL QPPFKQLRRD EVQGQKLSIP QMQLCNSKND LQPVLNATPK FRRASLNSKT 310 320 330 340 350 360 ISPLVSVTKS LITTYSLCSP EFTYQTSKNP KRVLTKPSEG KCNNGFDNIN SDYILYVNDV 370 380 390 400 410 420 LGVEQNRKYL VLDILGQGTF GQVVKCQNLL TKEILAVKVV KSRTEYLTQS ITEAKILELL 430 440 450 460 470 480 NQKIDPTNKH HFLRMYDSFV HKNHLCLVFE LLSNNLYELL KQNKFHGLSI QLIRTFTTQI 490 500 510 520 530 540 LDSLCVLKES KLIHCDLKPE NILLCAPDKP ELKIIDFGSS CEEARTVYTY IQSRFYRAPE 550 560 570 580 590 600 IILGIPYSTS IDMWSLGCIV AELFLGIPIF PGASEYNQLT RIIDTLGYPP SWMIDMGKNS 610 620 630 640 650 660 GKFMKKLAPE ESSSSTQKHR MKTIEEFCRE YNIVEKPSKQ YFKWRKLPDI IRNYRYPKSI 670 680 690 700 710 720 QNSQELIDQE MQNRECLIHF LGGVLNLNPL ERWTPQQAML HPFITKQEFT GEWFPPGSSL 730 740 750 760 770 780 PGPSEKHDDA KGQQSEYGSA NDSSNNAGHN YVYNPSSATG GADSVDIGAI SKRKENTSGD 790 800 ISNNFAVTHS VQEGPTSAFN KLHIVEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2558053] [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: 8813765] [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: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 11358866] [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: 10816418] [Abstract] Cited for: PHOSPHORYLATION AT TYR-530.
[7]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-128 AND SER-295, MASS SPECTROMETRY. Strain: 2124.
[8]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-530, MASS SPECTROMETRY. Strain: YAL6B.
[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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-128 AND TYR-530, MASS SPECTROMETRY. Strain: ADR376.
[10]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-298, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-127; SER-128; SER-247; THR-288; THR-529 AND TYR-530, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16056 Genomic DNA. Translation: CAA34192.1. X87371 Genomic DNA. Translation: CAA60814.1. Z49417 Genomic DNA. Translation: CAA89437.1. BK006943 Genomic DNA. Translation: DAA08659.1.
PIR	A32582.
RefSeq	NP_012394.1. NM_001181574.1.
3D structure databases
ProteinModelPortal	P14680.
SMR	P14680. Positions 338-716.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1374N.
IntAct	P14680. 36 interactions.
MINT	MINT-401556.
STRING	P14680.
Proteomic databases
PeptideAtlas	P14680.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL141C; YJL141C; YJL141C.
GeneID	853300.
KEGG	sce:YJL141C.
NMPDR	fig|4932.3.peg.3359.
Organism-specific databases
CYGD	YJL141c.
SGD	S000003677. YAK1.
Phylogenomic databases
eggNOG	fuNOG04561.
GeneTree	EFGT00070000008724.
HOGENOM	HBG396244.
OMA	SIQLIRT.
OrthoDB	EOG4XH377.
Enzyme and pathway databases
BRENDA	2.7.12.1. 984.
Gene expression databases
ArrayExpress	P14680.
Genevestigator	P14680.
GermOnline	YJL141C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K00924.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973618.

Entry information

Entry name

YAK1_YEAST

Accession

Primary (citable) accession number: P14680
Secondary accession number(s): D6VW43

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program