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Protein

Serine/threonine-protein kinase STE7

Gene

STE7

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

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.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Phosphorylated at multiple sites in response to pheromone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei220 – 2201ATPPROSITE-ProRule annotation
Active sitei331 – 3311Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi197 – 2059ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase activity Source: SGD
  3. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of MAPK activity involved in conjugation with cellular fusion Source: SGD
  2. invasive growth in response to glucose limitation Source: SGD
  3. MAPK cascade involved in cell wall organization or biogenesis Source: SGD
  4. MAPK cascade involved in conjugation with cellular fusion Source: SGD
  5. protein phosphorylation Source: SGD
  6. pseudohyphal growth Source: SGD
  7. regulation of transposition, RNA-mediated Source: SGD
  8. signal transduction involved in filamentous growth Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Pheromone response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29553-MONOMER.
BRENDAi2.7.12.2. 984.
ReactomeiREACT_191508. Signaling by FGFR.
REACT_207653. Signal transduction by L1.
REACT_235121. ERK1 activation.
REACT_248688. Signalling to ERK5.
REACT_253962. ERK2 activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase STE7 (EC:2.7.12.2)
Gene namesi
Name:STE7
Ordered Locus Names:YDL159W
ORF Names:D1525
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL159w.
SGDiS000002318. STE7.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. mating projection tip Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi353 – 3531S → A: No loss of activity. 1 Publication
Mutagenesisi359 – 3591S → A: Inactivation. 1 Publication
Mutagenesisi363 – 3631T → A: Inactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Serine/threonine-protein kinase STE7PRO_0000086688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591Phosphoserine1 Publication
Modified residuei363 – 3631Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06784.
PaxDbiP06784.
PeptideAtlasiP06784.

Expressioni

Gene expression databases

GenevestigatoriP06784.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC14Q006842EBI-18389,EBI-4192
FUS3P1689215EBI-18389,EBI-7193
HOG1P324852EBI-18389,EBI-8437
KSS1P1468114EBI-18389,EBI-9945
STE5P329178EBI-18389,EBI-18373

Protein-protein interaction databases

BioGridi31905. 46 interactions.
DIPiDIP-9N.
IntActiP06784. 27 interactions.
MINTiMINT-411435.
STRINGi4932.YDL159W.

Structurei

3D structure databases

ProteinModelPortaliP06784.
SMRiP06784. Positions 190-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini191 – 466276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00690000102311.
HOGENOMiHOG000234206.
InParanoidiP06784.
KOiK11226.
OMAiGGHNDTP.
OrthoDBiEOG7380F1.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06784-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFQRKTLQRR NLKGLNLNLH PDVGNNGQLQ EKTETHQGQS RIEGHVMSNI
60 70 80 90 100
NAIQNNSNLF LRRGIKKKLT LDAFGDDQAI SKPNTVVIQQ PQNEPVLVLS
110 120 130 140 150
SLSQSPCVSS SSSLSTPCII DAYSNNFGLS PSSTNSTPST IQGLSNIATP
160 170 180 190 200
VENEHSISLP PLEESLSPAA ADLKDTLSGT SNGNYIQLQD LVQLGKIGAG
210 220 230 240 250
NSGTVVKALH VPDSKIVAKK TIPVEQNNST IINQLVRELS IVKNVKPHEN
260 270 280 290 300
IITFYGAYYN QHINNEIIIL MEYSDCGSLD KILSVYKRFV QRGTVSSKKT
310 320 330 340 350
WFNELTISKI AYGVLNGLDH LYRQYKIIHR DIKPSNVLIN SKGQIKLCDF
360 370 380 390 400
GVSKKLINSI ADTFVGTSTY MSPERIQGNV YSIKGDVWSL GLMIIELVTG
410 420 430 440 450
EFPLGGHNDT PDGILDLLQR IVNEPSPRLP KDRIYSKEMT DFVNRCCIKN
460 470 480 490 500
ERERSSIHEL LHHDLIMKYV SPSKDDKFRH WCRKIKSKIK EDKRIKREAL
510
DRAKLEKKQS ERSTH
Length:515
Mass (Da):57,709
Last modified:January 1, 1988 - v1
Checksum:iC8A75899CFBE8BDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA25048.
RefSeqiNP_010122.1. NM_001180219.1.

Genome annotation databases

EnsemblFungiiYDL159W; YDL159W; YDL159W.
GeneIDi851396.
KEGGisce:YDL159W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA25048.
RefSeqiNP_010122.1. NM_001180219.1.

3D structure databases

ProteinModelPortaliP06784.
SMRiP06784. Positions 190-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31905. 46 interactions.
DIPiDIP-9N.
IntActiP06784. 27 interactions.
MINTiMINT-411435.
STRINGi4932.YDL159W.

Proteomic databases

MaxQBiP06784.
PaxDbiP06784.
PeptideAtlasiP06784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL159W; YDL159W; YDL159W.
GeneIDi851396.
KEGGisce:YDL159W.

Organism-specific databases

CYGDiYDL159w.
SGDiS000002318. STE7.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00690000102311.
HOGENOMiHOG000234206.
InParanoidiP06784.
KOiK11226.
OMAiGGHNDTP.
OrthoDBiEOG7380F1.

Enzyme and pathway databases

BioCyciYEAST:G3O-29553-MONOMER.
BRENDAi2.7.12.2. 984.
ReactomeiREACT_191508. Signaling by FGFR.
REACT_207653. Signal transduction by L1.
REACT_235121. ERK1 activation.
REACT_248688. Signalling to ERK5.
REACT_253962. ERK2 activation.

Miscellaneous databases

NextBioi968558.
PROiP06784.

Gene expression databases

GenevestigatoriP06784.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
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. "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.
    , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTE7_YEAST
AccessioniPrimary (citable) accession number: P06784
Secondary accession number(s): D6VRJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 4, 2015
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

Miscellaneous

Present with 672 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3

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 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.