Mitogen-activated protein kinase KSS1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P14681 (KSS1_YEAST)

Last modified November 3, 2009. Version 114. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase KSS1
      Short name=MAP kinase KSS1
    EC=2.7.11.24
Alternative name(s):
    Kinase suppressor of SST2

Gene names

Name:	KSS1
Ordered Locus Names:	YGR040W

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Together with closely related FUS3, KSS1 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated KSS1 activates both pathways, whereas activated FUS3 activates the mating but suppresses the filamentation pathway. KSS1 activity is down-regulated by FUS3 during pheromone induction to prevent inappropriate activation of the filamentation pathway. During induction of filamentation, KSS1 activates the transcription factor STE12 resulting in its binding to and activation of filamentation specific genes. Non-activated KSS1 has a kinase-independent repressive effect on STE12 transcriptional activity, that is mediated by direct binding to STE12 and depends on the presence of DIG1 and DIG2, and that is required for the suppression of filamenation under normal growth conditions. SSN3/SRB10 contributes further to the suppression of filamentation under these conditions by reducing STE12 stability independent of KSS1. FUS3 can partially compensate for the lack of KSS1 but filamentation becomes constitutively induced at a low level in the absence of any signal. KSS1 phosphorylates STE7, STE5, FAR1, DIG1, DIG2, STE12, and SST2. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by tyrosine and threonine phosphorylation after pheromone treatment or carbon/nitrogen limitation.
Subunit structure	In the nucleus, KSS1 forms a complex with DIG1, DIG2 and STE12; in contrast to FUS3 the interaction of KSS1 with STE12 does not depend on DIG1 and DIG2. Phosphorylated KSS1 shows reduced interaction with STE12. During pheromone activation and phosphorylation, KSS1 forms a membrane-associated complex with the scaffold protein STE5, the MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4; interacting directly with STE7 and STE5 proteins.
Subcellular location	Nucleus. Cytoplasm. Periplasm. Note: KSS1 shuttles rapidly between the cytoplasm and the nucleus independent of its activation state. Ref.12
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-183 and Tyr-185 by STE7 in response to pheromone or carbon/nitrogen limitation, which activates the enzyme. Activated FUS3 down-regulates KSS1 phosphorylation. Ref.6 Ref.16
Miscellaneous	Present with 5480 molecules/cell in log phase SD medium. Ref.15
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Nucleus Periplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW invasive growth in response to glucose limitation Inferred from mutant phenotype. Source: SGD negative regulation of transcription factor activity Ref.9 Inferred from mutant phenotype. Source: SGD pheromone-dependent signal transduction involved in conjugation with cellular fusion Ref.11 Inferred from expression pattern. Source: SGD protein amino acid phosphorylation Ref.7 Inferred from direct assay. Source: SGD signal transduction during filamentous growth Ref.8 Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: SGD periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Ref.7 Inferred from direct assay. Source: SGD transcription factor binding Ref.9 Inferred from physical interaction. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
STE11	P23561	2	EBI-9945,EBI-18259
STE12	P13574	2	EBI-9945,EBI-18264
STE7	P06784	8	EBI-9945,EBI-18389
TCA17	P32613	1	EBI-9945,EBI-22370

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 368

368

Mitogen-activated protein kinase KSS1

PRO_0000186333

Regions

Domain

13 – 313

301

Protein kinase

Nucleotide binding

19 – 27

ATP By similarity

Motif

183 – 185

TXY

Compositional bias

345 – 349

Poly-Glu

Sites

Active site

143

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

183

Phosphothreonine Ref.16

Modified residue

185

Phosphotyrosine Ref.16

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Sequences

Sequence

Length

Mass (Da)

Tools

P14681-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5FA42161B5FD51B5
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FASTA

368

42,692

        10         20         30         40         50         60 
MARTITFDIP SQYKLVDLIG EGAYGTVCSA IHKPSGIKVA IKKIQPFSKK LFVTRTIREI 

        70         80         90        100        110        120 
KLLRYFHEHE NIISILDKVR PVSIDKLNAV YLVEELMETD LQKVINNQNS GFSTLSDDHV 

       130        140        150        160        170        180 
QYFTYQILRA LKSIHSAQVI HRDIKPSNLL LNSNCDLKVC DFGLARCLAS SSDSRETLVG 

       190        200        210        220        230        240 
FMTEYVATRW YRAPEIMLTF QEYTTAMDIW SCGCILAEMV SGKPLFPGRD YHHQLWLILE 

       250        260        270        280        290        300 
VLGTPSFEDF NQIKSKRAKE YIANLPMRPP LPWETVWSKT DLNPDMIDLL DKMLQFNPDK 

       310        320        330        340        350        360 
RISAAEALRH PYLAMYHDPS DEPEYPPLNL DDEFWKLDNK IMRPEEEEEV PIEMLKDMLY 


DELMKTME

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A putative protein kinase overcomes pheromone-induced arrest of cell cycling in S. cerevisiae." Courchesne W.E., Kunisawa R., Thorner J. Cell 58:1107-1119(1989) [PubMed: 2673544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Quantitative trait loci mapped to single-nucleotide resolution in yeast." Deutschbauer A.M., Davis R.W. Nat. Genet. 37:1333-1340(2005) [PubMed: 16273108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SK1.
[3]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed: 9290212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Signal transduction in Saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of FUS3 and KSS1." Gartner A., Nasmyth K., Ammerer G. Genes Dev. 6:1280-1292(1992) [PubMed: 1628831] [Abstract] Cited for: PHOSPHORYLATION.
[7]	"Two novel targets of the MAP kinase Kss1 are negative regulators of invasive growth in the yeast Saccharomyces cerevisiae." Cook J.G., Bardwell L., Kron S.J., Thorner J. Genes Dev. 10:2831-2848(1996) [PubMed: 8918885] [Abstract] Cited for: FUNCTION, COMPLEX WITH DIG1; DIG2 AND STE12.
[8]	"MAP kinases with distinct inhibitory functions impart signaling specificity during yeast differentiation." Madhani H.D., Styles C.A., Fink G.R. Cell 91:673-684(1997) [PubMed: 9393860] [Abstract] Cited for: FUNCTION, INHIBITION OF FILAMENTATION.
[9]	"Repression of yeast Ste12 transcription factor by direct binding of unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK." Bardwell L., Cook J.G., Voora D., Baggott D.M., Martinez A.R., Thorner J. Genes Dev. 12:2887-2898(1998) [PubMed: 9744865] [Abstract] Cited for: FUNCTION, INTERACTION WITH STE12.
[10]	"Differential regulation of transcription: repression by unactivated mitogen-activated protein kinase Kss1 requires the Dig1 and Dig2 proteins." Bardwell L., Cook J.G., Zhu-Shimoni J.X., Voora D., Thorner J. Proc. Natl. Acad. Sci. U.S.A. 95:15400-15405(1998) [PubMed: 9860980] [Abstract] Cited for: FUNCTION, FUNCTIONAL DEPENDANCE ON DIG1/DIG2.
[11]	"Specificity of MAP kinase signaling in yeast differentiation involves transient versus sustained MAPK activation." Sabbagh W. Jr., Flatauer L.J., Bardwell A.J., Bardwell L. Mol. Cell 8:683-691(2001) [PubMed: 11583629] [Abstract] Cited for: FUNCTION, REGULATION OF ACTIVITY BY FUS3.
[12]	"MAP kinase dynamics in response to pheromones in budding yeast." van Drogen F., Stucke V.M., Jorritsma G., Peter M. Nat. Cell Biol. 3:1051-1059(2001) [PubMed: 11781566] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"Program-specific distribution of a transcription factor dependent on partner transcription factor and MAPK signaling." Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L., Fink G.R., Young R.A. Cell 113:395-404(2003) [PubMed: 12732146] [Abstract] Cited for: FUNCTION, REGULATION OF STE12 PROMOTER SELECTIVITY.
[14]	"Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the transcription factor Ste12." Nelson C., Goto S., Lund K., Hung W., Sadowski I. Nature 421:187-190(2003) [PubMed: 12520306] [Abstract] Cited for: FUNCTION, STE12 STABILITY.
[15]	"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].
[16]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M26398 Genomic DNA. Translation: AAA34882.1. DQ115391 Genomic DNA. Translation: AAZ22456.1. Z72825 Genomic DNA. Translation: CAA97038.1. AY557773 Genomic DNA. Translation: AAS56099.1.
PIR	A33297.
RefSeq	NP_011554.1.
3D structure databases
HSSP	HSSP built from PDB template 1KV1 based on UniProtKB Q16539.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:60N.
IntAct	P14681. 41 interactions.
STRING	P14681.
Proteomic databases
PeptideAtlas	P14681.
PRIDE	P14681.
Genome annotation databases
Ensembl	YGR040W; YGR040W; YGR040W; Saccharomyces cerevisiae. [Genome view]
GeneID	852931.
GenomeReviews	Gene locus YGR040W in contig Y13135_GR.
KEGG	sce:YGR040W.
NMPDR	fig\|4932.3.peg.2670.
Organism-specific databases
CYGD	YGR040w.
SGD	S000003272. KSS1.
Phylogenomic databases
HOGENOM	P14681.
OMA	TTAMDIW.
Enzyme and pathway databases
BRENDA	2.7.11.24. 250.
Gene expression databases
ArrayExpress	P14681.
Genevestigator	P14681.
GermOnline	YGR040W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003527. MAP_kinase_CS. 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	PS01351. MAPK. 1 hit. 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	972657.

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Entry information

Entry name

KSS1_YEAST

Accession

Primary (citable) accession number: P14681
Secondary accession number(s): Q45U43

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 3, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents