Serine/threonine-protein kinase STE11 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P23561 (STE11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 140. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase STE11
EC=2.7.11.1

Gene names

Name:	STE11
Ordered Locus Names:	YLR362W
ORF Names:	L8039.10

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	717 AA.
Sequence status	Complete.
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 phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases. Ref.4 Ref.11
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.9 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 process	Pheromone response
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade involved in cell wall biogenesis Inferred from genetic interaction PubMed 10880465. Source: SGD MAPK cascade involved in osmosensory signaling pathway Inferred from mutant phenotype PubMed 9180081. 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 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_component	cytoplasm Inferred from direct assay PubMed 9755161. Source: SGD
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
itself		3	EBI-18259,EBI-18259
FUS3	P16892	5	EBI-18259,EBI-7193
KSS1	P14681	6	EBI-18259,EBI-9945
STE5	P32917	7	EBI-18259,EBI-18373
STE50	P25344	6	EBI-18259,EBI-18305

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 717

717

Serine/threonine-protein kinase STE11

PRO_0000086684

Regions

Domain

20 – 84

SAM

Domain

415 – 712

298

Protein kinase

Nucleotide binding

421 – 429

ATP By similarity

Sites

Active site

579

Proton acceptor By similarity

Binding site

444

ATP By similarity

Amino acid modifications

Modified residue

241

Phosphoserine Ref.8

Modified residue

323

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

326

Phosphoserine Ref.8

Modified residue

387

Phosphoserine Ref.8

Experimental info

Mutagenesis

I → R: Disrupts interaction with STE50 and abolishes signal transduction. Ref.9

Secondary structure

717

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23561 [UniParc].

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

FASTA

717

80,721

        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' referencesShow '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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY.
[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-241; SER-323; SER-326 AND SER-387, MASS SPECTROMETRY.
[9]	"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.
[10]	"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.
[11]	"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.
+	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.

PIR

S51380.

RefSeq

NP_013466.1. NM_001182251.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OW5	NMR	-	A	15-92	[»]
1X9X	NMR	-	A/B	16-83	[»]

ProteinModelPortal

P23561.

SMR

P23561. Positions 22-83, 385-712.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-861N.

IntAct

P23561. 18 interactions.

MINT

MINT-408610.

STRING

4932.YLR362W.

Proteomic databases

PaxDb

P23561.

PeptideAtlas

P23561.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR362W; YLR362W; YLR362W.

GeneID

851076.

KEGG

sce:YLR362W.

Organism-specific databases

SGD

S000004354. STE11.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00700000104370.

HOGENOM

HOG000172453.

K11228.

OMA

VELVTIC.

OrthoDB

EOG4QG0P3.

Enzyme and pathway databases

BRENDA

2.7.11.25. 984.

Gene expression databases

Genevestigator

P23561.

GermOnline

YLR362W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23561.

NextBio

967729.

Entry information

Entry name

STE11_YEAST

Accession

Primary (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:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents