Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14681 (KSS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 filamentation 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.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18

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 POF1, 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.13

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.7

Miscellaneous

Present with 5480 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
Periplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.8. Source: GOC

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

invasive growth in response to glucose limitation

Inferred from mutant phenotype PubMed 8001818. Source: SGD

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.10. Source: SGD

pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from mutant phenotype Ref.12. Source: SGD

protein phosphorylation

Inferred from direct assay Ref.8. Source: SGD

signal transduction involved in filamentous growth

Inferred from mutant phenotype Ref.9. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 18417610PubMed 7579701. Source: SGD

periplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from direct assay Ref.8. Source: SGD

protein binding

Inferred from physical interaction PubMed 10688190PubMed 18719252PubMed 19303851PubMed 20489023PubMed 23267104PubMed 23953117PubMed 7851759PubMed 8062390PubMed 8668180. Source: IntAct

transcription factor binding

Inferred from physical interaction Ref.10. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368Mitogen-activated protein kinase KSS1
PRO_0000186333

Regions

Domain13 – 313301Protein kinase
Nucleotide binding19 – 279ATP By similarity
Motif183 – 1853TXY
Compositional bias345 – 3495Poly-Glu

Sites

Active site1431Proton acceptor By similarity
Binding site421ATP By similarity

Amino acid modifications

Modified residue1831Phosphothreonine Ref.17
Modified residue1851Phosphotyrosine Ref.17

Sequences

Sequence LengthMass (Da)Tools
P14681 [UniParc].

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

FASTA36842,692
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPLEX WITH DIG1; DIG2 AND STE12.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INHIBITION OF FILAMENTATION.
[10]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STE12.
[11]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, FUNCTIONAL DEPENDENCE ON DIG1/DIG2.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, REGULATION OF ACTIVITY BY FUS3.
[13]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, REGULATION OF STE12 PROMOTER SELECTIVITY.
[15]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, STE12 STABILITY.
[16]"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].
[17]"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 THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[18]"Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes."
Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M., Gerstein M., Snyder M.
Genes Dev. 25:767-778(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POF1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26398 Genomic DNA. Translation: AAA34882.1.
DQ115391 Genomic DNA. Translation: AAZ22456.1.
Z72825 Genomic DNA. Translation: CAA97038.1.
AY557773 Genomic DNA. Translation: AAS56099.1.
BK006941 Genomic DNA. Translation: DAA08139.1.
PIRA33297.
RefSeqNP_011554.3. NM_001181169.3.

3D structure databases

ProteinModelPortalP14681.
SMRP14681. Positions 1-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33287. 176 interactions.
DIPDIP-60N.
IntActP14681. 18 interactions.
MINTMINT-411417.
STRING4932.YGR040W.

Proteomic databases

MaxQBP14681.
PaxDbP14681.
PeptideAtlasP14681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR040W; YGR040W; YGR040W.
GeneID852931.
KEGGsce:YGR040W.

Organism-specific databases

CYGDYGR040w.
SGDS000003272. KSS1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOGENOMHOG000233024.
KOK04371.
OMAGPRYTDL.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-30760-MONOMER.
BRENDA2.7.11.24. 984.

Gene expression databases

GenevestigatorP14681.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_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. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972657.
PROP14681.

Entry information

Entry nameKSS1_YEAST
AccessionPrimary (citable) accession number: P14681
Secondary accession number(s): D6VUH8, Q45U43
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families