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P23561 (STE11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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 STE11

EC=2.7.11.25
Gene names
Name:STE11
Ordered Locus Names:YLR362W
ORF Names:L8039.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length717 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 phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases. Ref.4 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Homodimer Probable. Interacts (via SAM domain) with STE50 (via SAM domain). Interacts with PBS2 and SHO1. Ref.6 Ref.10 Ref.11

Miscellaneous

Present with 736 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence caution

The sequence AAB67571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processPheromone response
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade involved in cell wall organization or biogenesis

Inferred from genetic interaction PubMed 10880465. Source: SGD

MAPK cascade involved in osmosensory signaling pathway

Inferred from mutant phenotype PubMed 9180081. Source: SGD

activation of MAPKK activity

Inferred from direct assay PubMed 8159759. Source: SGD

cellular response to heat

Inferred from mutant phenotype PubMed 12455951. Source: SGD

invasive growth in response to glucose limitation

Inferred from mutant phenotype PubMed 8001818. Source: SGD

osmosensory signaling pathway via Sho1 osmosensor

Inferred from genetic interaction PubMed 9180081. Source: SGD

pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 8455599. Source: SGD

protein phosphorylation

Inferred from direct assay Ref.1. Source: SGD

pseudohyphal growth

Inferred from mutant phenotype PubMed 8259520. 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 8259520. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 9755161. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from direct assay PubMed 8159759. Source: SGD

SAM domain binding

Inferred from direct assay PubMed 16337230. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 7851759PubMed 8062390PubMed 8670882. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10688190PubMed 11283351PubMed 15020407PubMed 16429126PubMed 16778768PubMed 20489023PubMed 7851759PubMed 8062390. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Serine/threonine-protein kinase STE11
PRO_0000086684

Regions

Domain20 – 8465SAM
Domain415 – 712298Protein kinase
Nucleotide binding421 – 4299ATP By similarity

Sites

Active site5791Proton acceptor By similarity
Binding site4441ATP By similarity

Amino acid modifications

Modified residue3231Phosphoserine Ref.7 Ref.8
Modified residue4651Phosphoserine Ref.9

Experimental info

Mutagenesis591I → R: Disrupts interaction with STE50 and abolishes signal transduction. Ref.10

Secondary structure

........... 717
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23561 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: E9E0DF27114EEEEF

FASTA71780,721
        10         20         30         40         50         60 
MEQTQTAEGT DLLIGDEKTN DLPFVQLFLE EIGCTQYLDS FIQCNLVTEE EIKYLDKDIL 

        70         80         90        100        110        120 
IALGVNKIGD RLKILRKSKS FQRDKRIEQV NRLKNLMEKV SSLSTATLSM NSELIPEKHC 

       130        140        150        160        170        180 
VIFILNDGSA KKVNVNGCFN ADSIKKRLIR RLPHELLATN SNGEVTKMVQ DYDVFVLDYT 

       190        200        210        220        230        240 
KNVLHLLYDV ELVTICHAND RVEKNRLIFV SKDQTPSDKA ISTSKKLYLR TLSALSQVGP 

       250        260        270        280        290        300 
SSSNLLAQNK GISHNNAEGK LRIDNTEKDR IRQIFNQRPP SEFISTNLAG YFPHTDMKRL 

       310        320        330        340        350        360 
QKTMRESFRH SARLSIAQRR PLSAESNNIG DILLKHSNAV DMALLQGLDQ TRLSSKLDTT 

       370        380        390        400        410        420 
KIPKLAHKRP EDNDAISNQL ELLSVESGEE EDHDFFGEDS DIVSLPTKIA TPKNWLKGAC 

       430        440        450        460        470        480 
IGSGSFGSVY LGMNAHTGEL MAVKQVEIKN NNIGVPTDNN KQANSDENNE QEEQQEKIED 

       490        500        510        520        530        540 
VGAVSHPKTN QNIHRKMVDA LQHEMNLLKE LHHENIVTYY GASQEGGNLN IFLEYVPGGS 

       550        560        570        580        590        600 
VSSMLNNYGP FEESLITNFT RQILIGVAYL HKKNIIHRDI KGANILIDIK GCVKITDFGI 

       610        620        630        640        650        660 
SKKLSPLNKK QNKRASLQGS VFWMSPEVVK QTATTAKADI WSTGCVVIEM FTGKHPFPDF 

       670        680        690        700        710 
SQMQAIFKIG TNTTPEIPSW ATSEGKNFLR KAFELDYQYR PSALELLQHP WLDAHII 

« Hide

References

« Hide 'large scale' references
[1]"STE11 is a protein kinase required for cell-type-specific transcription and signal transduction in yeast."
Rhodes N., Connell L., Errede B.
Genes Dev. 4:1862-1874(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF INITIATION SITE.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[5]"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].
[6]"Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway."
Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A.
Mol. Cell 14:825-832(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PBS2 AND SHO1.
[7]"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-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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 SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50."
Kwan J.J., Warner N., Pawson T., Donaldson L.W.
J. Mol. Biol. 342:681-693(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 15-92, INTERACTION WITH STE50, MUTAGENESIS OF ILE-59.
[11]"Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex."
Bhattacharjya S., Xu P., Gingras R., Shaykhutdinov R., Wu C., Whiteway M., Ni F.
J. Mol. Biol. 344:1071-1087(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 16-83, SUBUNIT, INTERACTION WITH STE50.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53431 Genomic DNA. Translation: CAA37522.1.
U19103 Genomic DNA. Translation: AAB67571.1. Different initiation.
BK006945 Genomic DNA. Translation: DAA09666.1.
PIRS51380.
RefSeqNP_013466.1. NM_001182251.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OW5NMR-A15-92[»]
1X9XNMR-A/B16-83[»]
ProteinModelPortalP23561.
SMRP23561. Positions 22-83, 394-712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31623. 107 interactions.
DIPDIP-861N.
IntActP23561. 19 interactions.
MINTMINT-408610.
STRING4932.YLR362W.

Proteomic databases

MaxQBP23561.
PaxDbP23561.
PeptideAtlasP23561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR362W; YLR362W; YLR362W.
GeneID851076.
KEGGsce:YLR362W.

Organism-specific databases

SGDS000004354. STE11.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117243.
HOGENOMHOG000172453.
KOK11228.
OMAVELVTIC.
OrthoDBEOG71K6B8.

Enzyme and pathway databases

BioCycYEAST:G3O-32433-MONOMER.
BRENDA2.7.11.25. 984.

Gene expression databases

GenevestigatorP23561.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR029458. Ras-bd_By2.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF14847. Ras_bdg_2. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23561.
NextBio967729.

Entry information

Entry nameSTE11_YEAST
AccessionPrimary (citable) accession number: P23561
Secondary accession number(s): D6VZ00
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references