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P06784 (STE7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:
Serine/threonine-protein kinase STE7
EC=2.7.12.2
Gene names
Name:STE7
Ordered Locus Names:YDL159W
ORF Names:D1525
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Protein existenceEvidence 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.5

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.

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 processPheromone response
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade involved in cell wall biogenesis

Inferred from genetic interaction PubMed 10880465. Source: SGD

MAPK cascade involved in conjugation with cellular fusion

Inferred from direct assay PubMed 8455599. Source: SGD

activation of MAPK activity involved in conjugation with cellular fusion

Inferred from direct assay PubMed 8384702. Source: SGD

invasive growth in response to glucose limitation

Inferred from mutant phenotype PubMed 8001818. Source: SGD

pseudohyphal growth

Inferred from mutant phenotype PubMed 8643578. Source: SGD

regulation of transposition, RNA-mediated

Inferred from mutant phenotype PubMed 9566871. Source: SGD

signal transduction involved in filamentous growth

Inferred from mutant phenotype PubMed 15456892. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11781566. Source: SGD

mating projection tip

Inferred from direct assay PubMed 11781566PubMed 17952059. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from direct assay PubMed 8384702. Source: SGD

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Serine/threonine-protein kinase STE7
PRO_0000086688

Regions

Domain191 – 466276Protein kinase
Nucleotide binding197 – 2059ATP By similarity

Sites

Active site3311Proton acceptor By similarity
Binding site2201ATP By similarity

Amino acid modifications

Modified residue1491Phosphothreonine Ref.8
Modified residue3591Phosphoserine Ref.6
Modified residue3631Phosphothreonine Ref.6

Experimental info

Mutagenesis3531S → A: No loss of activity.
Mutagenesis3591S → A: Inactivation.
Mutagenesis3631T → A: Inactivation.

Sequences

Sequence LengthMass (Da)Tools
P06784 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: C8A75899CFBE8BDE

FASTA51557,709
        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

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-515.
Strain: ATCC 96604 / S288c / FY1679.
[5]"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] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-359 AND THR-363, MUTAGENESIS.
[7]"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].
[8]"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-149, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14097 Genomic DNA. Translation: AAA35118.1.
Z67750 Genomic DNA. Translation: CAA91587.1.
Z74207 Genomic DNA. Translation: CAA98732.1.
X97751 Genomic DNA. Translation: CAA66332.1.
BK006938 Genomic DNA. Translation: DAA11702.1.
PIRA25048.
RefSeqNP_010122.1. NM_001180219.1.

3D structure databases

ProteinModelPortalP06784.
SMRP06784. Positions 190-491.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9N.
IntActP06784. 13 interactions.
MINTMINT-411435.
STRING4932.YDL159W.

Proteomic databases

PaxDbP06784.
PeptideAtlasP06784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL159W; YDL159W; YDL159W.
GeneID851396.
KEGGsce:YDL159W.

Organism-specific databases

CYGDYDL159w.
SGDS000002318. STE7.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00690000102311.
HOGENOMHOG000234206.
KOK11226.
OMAGLMIIEL.
OrthoDBEOG43V342.

Enzyme and pathway databases

BRENDA2.7.12.2. 984.

Gene expression databases

GenevestigatorP06784.
GermOnlineYDL159W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968558.

Entry information

Entry nameSTE7_YEAST
AccessionPrimary (citable) accession number: P06784
Secondary accession number(s): D6VRJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 1, 2013
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome IV

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents