Reviewed, UniProtKB/Swiss-Prot P06784 (STE7_YEAST)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase STE7
    EC=2.7.12.2

Gene names

Name:	STE7
Ordered Locus Names:	YDL159W
ORF Names:	D1525

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases. Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Phosphorylated at multiple sites in response to pheromone.
Miscellaneous	Present with 672 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Pheromone response
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	invasive growth in response to glucose limitation Inferred from mutant phenotype. Source: SGD pheromone-dependent signal transduction involved in conjugation with cellular fusion Traceable author statement. Source: SGD protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro pseudohyphal growth Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Traceable author statement. Source: SGD protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FUS3	P16892	5	EBI-18389,EBI-7193
KSS1	P14681	8	EBI-18389,EBI-9945
STE5	P32917	4	EBI-18389,EBI-18373

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 515	515	Serine/threonine-protein kinase STE7		PRO_0000086688
Regions
	Domain	191 – 466	276	Protein kinase
	Nucleotide binding	197 – 205	9	ATP By similarity
Sites
	Active site	331	1	Proton acceptor By similarity
	Binding site	220	1	ATP By similarity
Amino acid modifications
	Modified residue	149	1	Phosphothreonine Ref.7
	Modified residue	359	1	Phosphoserine Ref.5
	Modified residue	363	1	Phosphothreonine Ref.5
Experimental info
	Mutagenesis	353	1	S → A: No loss of activity.
	Mutagenesis	359	1	S → A: Inactivation.
	Mutagenesis	363	1	T → A: Inactivation.

Sequences

	Sequence		Length	Mass (Da)
	P06784-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: C8A75899CFBE8BDE	FASTA	515	57,709
	10 20 30 40 50 60 MFQRKTLQRR NLKGLNLNLH PDVGNNGQLQ EKTETHQGQS RIEGHVMSNI NAIQNNSNLF 70 80 90 100 110 120 LRRGIKKKLT LDAFGDDQAI SKPNTVVIQQ PQNEPVLVLS SLSQSPCVSS SSSLSTPCII 130 140 150 160 170 180 DAYSNNFGLS PSSTNSTPST IQGLSNIATP VENEHSISLP PLEESLSPAA ADLKDTLSGT 190 200 210 220 230 240 SNGNYIQLQD LVQLGKIGAG NSGTVVKALH VPDSKIVAKK TIPVEQNNST IINQLVRELS 250 260 270 280 290 300 IVKNVKPHEN IITFYGAYYN QHINNEIIIL MEYSDCGSLD KILSVYKRFV QRGTVSSKKT 310 320 330 340 350 360 WFNELTISKI AYGVLNGLDH LYRQYKIIHR DIKPSNVLIN SKGQIKLCDF GVSKKLINSI 370 380 390 400 410 420 ADTFVGTSTY MSPERIQGNV YSIKGDVWSL GLMIIELVTG EFPLGGHNDT PDGILDLLQR 430 440 450 460 470 480 IVNEPSPRLP KDRIYSKEMT DFVNRCCIKN ERERSSIHEL LHHDLIMKYV SPSKDDKFRH 490 500 510 WCRKIKSKIK EDKRIKREAL DRAKLEKKQS ERSTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the yeast regulatory gene STE7 predicts a protein homologous to protein kinases." Teague M.A., Chaleff D.T., Errede B. Proc. Natl. Acad. Sci. U.S.A. 83:7371-7375(1986) [PubMed: 3532111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Analysis of a 23 kb region on the left arm of yeast chromosome IV." Delaveau T.T.D., Blugeon C., Jacq C., Perea J. Yeast 12:1587-1592(1996) [PubMed: 8972581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-515. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase." Cairns B.R., Ramer S.W., Kornberg K.D. Genes Dev. 6:1305-1318(1992) [PubMed: 1628833] [Abstract] Cited for: POSSIBLE FUNCTION.
[5]	"Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues." Zheng C.-F., Guan K.-L. EMBO J. 13:1123-1131(1994) [PubMed: 8131746] [Abstract] Cited for: PHOSPHORYLATION AT SER-359 AND THR-363, MUTAGENESIS.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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 THR-149, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M14097 Genomic DNA. Translation: AAA35118.1. Z67750 Genomic DNA. Translation: CAA91587.1. Z74207 Genomic DNA. Translation: CAA98732.1. X97751 Genomic DNA. Translation: CAA66332.1.
PIR	A25048.
RefSeq	NP_010122.1.
3D structure databases
HSSP	HSSP built from PDB template 1F3M based on UniProtKB Q13153.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9N.
IntAct	P06784. 4 interactions.
STRING	P06784.
Proteomic databases
PeptideAtlas	P06784.
PRIDE	P06784.
Genome annotation databases
Ensembl	YDL159W; YDL159W; YDL159W; Saccharomyces cerevisiae. [Genome view]
GeneID	851396.
GenomeReviews	Gene locus YDL159W in contig Z71256_GR.
KEGG	sce:YDL159W.
NMPDR	fig|4932.3.peg.858.
Organism-specific databases
CYGD	YDL159w.
SGD	S000002318. STE7.
Phylogenomic databases
OMA	YKIIHRD.
Enzyme and pathway databases
BRENDA	2.7.12.2. 250.
Gene expression databases
ArrayExpress	P06784.
Genevestigator	P06784.
GermOnline	YDL159W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968558.

Entry information

Entry name

STE7_YEAST

Accession

Primary (citable) accession number: P06784

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	November 3, 2009
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)