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P16892 (FUS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. 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:
Mitogen-activated protein kinase FUS3

Short name=MAP kinase FUS3
EC=2.7.11.24
Gene names
Name:FUS3
Synonyms:DAC2
Ordered Locus Names:YBL016W
ORF Names:YBL03.21, YBL0303
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Together with closely related KSS1, FUS3 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 FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12. Ref.8 Ref.9 Ref.10 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation after pheromone treatment.

Subunit structure

In the nucleus, FUS3 forms a complex with DIG1, DIG2 and STE12. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. During its activation and phosphorylation, FUS3 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.

Subcellular location

Nucleus. Cytoplasm. Periplasm. Note: FUS3 shuttles rapidly between the cytoplasm and the nucleus independent of pheromone treatment or FUS3 phosphorylation level. Activated FUS3 translocates rapidly to the nucleus. Ref.11

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response to pheromone induction, which activates the enzyme. Activated FUS3 initiates a feedback signal, down-regulating phosphorylation of both, FUS3 and KSS1. Ref.7

Miscellaneous

Present with 8480 molecules/cell in log phase SD medium.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Conjugation
Mitosis
   Cellular componentCytoplasm
Nucleus
Periplasm
   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

Inferred from direct assay PubMed 15620357PubMed 8384702. Source: GOC

cell cycle arrest

Inferred from mutant phenotype PubMed 10049917. Source: SGD

invasive growth in response to glucose limitation

Inferred from mutant phenotype PubMed 10652102PubMed 15620357PubMed 8001818. Source: SGD

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of MAPK cascade

Inferred from physical interaction PubMed 16424299. Source: SGD

negative regulation of transposition, RNA-mediated

Inferred from mutant phenotype PubMed 9566871. Source: SGD

pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from direct assay PubMed 15620357PubMed 8384702. Source: SGD

positive regulation of protein export from nucleus

Inferred from mutant phenotype PubMed 22588722. Source: SGD

protein phosphorylation

Inferred from direct assay PubMed 22588722PubMed 8384702. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10233162. Source: SGD

mating projection tip

Inferred from direct assay Ref.11PubMed 17952059. Source: SGD

nucleus

Inferred from direct assay PubMed 10233162PubMed 18417610. 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 PubMed 15620357PubMed 8384702. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 15020407PubMed 23953117. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353Mitogen-activated protein kinase FUS3
PRO_0000186326

Regions

Domain13 – 309297Protein kinase
Nucleotide binding19 – 279ATP By similarity
Motif180 – 1823TXY

Sites

Active site1371Proton acceptor By similarity
Binding site421ATP By similarity

Amino acid modifications

Modified residue1801Phosphothreonine Ref.7
Modified residue1821Phosphotyrosine Ref.7

Experimental info

Sequence conflict3341Y → H in AAA34613. Ref.1

Secondary structure

........................................................... 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16892 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 5117980D20A1E7E2

FASTA35340,772
        10         20         30         40         50         60 
MPKRIVYNIS SDFQLKSLLG EGAYGVVCSA THKPTGEIVA IKKIEPFDKP LFALRTLREI 

        70         80         90        100        110        120 
KILKHFKHEN IITIFNIQRP DSFENFNEVY IIQELMQTDL HRVISTQMLS DDHIQYFIYQ 

       130        140        150        160        170        180 
TLRAVKVLHG SNVIHRDLKP SNLLINSNCD LKVCDFGLAR IIDESAADNS EPTGQQSGMT 

       190        200        210        220        230        240 
EYVATRWYRA PEVMLTSAKY SRAMDVWSCG CILAELFLRR PIFPGRDYRH QLLLIFGIIG 

       250        260        270        280        290        300 
TPHSDNDLRC IESPRAREYI KSLPMYPAAP LEKMFPRVNP KGIDLLQRML VFDPAKRITA 

       310        320        330        340        350 
KEALEHPYLQ TYHDPNDEPE GEPIPPSFFE FDHYKEALTT KDLKKLIWNE IFS 

« Hide

References

« Hide 'large scale' references
[1]"FUS3 encodes a cdc2+/CDC28-related kinase required for the transition from mitosis into conjugation."
Elion E.A., Grisafi P.L., Fink G.R.
Cell 60:649-664(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The DAC2/FUS3 protein kinase is not essential for transcriptional activation of the mating pheromone response pathway in Saccharomyces cerevisiae."
Fujimura H.A.
Mol. Gen. Genet. 235:450-452(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative ARS."
van Dyck L., Purnelle B., Skala J., Goffeau A.
Yeast 8:769-776(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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 AT THR-180 AND TYR-182.
[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] [Europe PMC] [Abstract]
Cited for: FUNCTION, REGULATION OF STE12 ACTIVITY.
[9]"Regulation of the mating pheromone and invasive growth responses in yeast by two MAP kinase substrates."
Tedford K., Kim S., Sa D., Stevens K., Tyers M.
Curr. Biol. 7:228-238(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPLEX WITH DIG1; DIG2 AND STE12.
[10]"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 KSS1 ACTIVITY.
[11]"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.
[12]"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.
[13]"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].
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31132 Genomic DNA. Translation: AAA34613.1.
X69572 Genomic DNA. Translation: CAA49292.1.
X68577 Genomic DNA. Translation: CAA48569.1.
Z35777 Genomic DNA. Translation: CAA84835.1.
AY693096 Genomic DNA. Translation: AAT93115.1.
BK006936 Genomic DNA. Translation: DAA07104.1.
PIRS28548.
RefSeqNP_009537.1. NM_001178256.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B9FX-ray1.80A1-353[»]
2B9HX-ray1.55A1-353[»]
2B9IX-ray2.50A1-353[»]
2B9JX-ray2.30A1-353[»]
2F49X-ray1.90A/B1-353[»]
2F9GX-ray2.10A1-353[»]
2FA2X-ray2.85A/B1-353[»]
ProteinModelPortalP16892.
SMRP16892. Positions 1-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32682. 293 interactions.
DIPDIP-714N.
IntActP16892. 29 interactions.
MINTMINT-376832.
STRING4932.YBL016W.

Proteomic databases

PaxDbP16892.
PeptideAtlasP16892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL016W; YBL016W; YBL016W.
GeneID852265.
KEGGsce:YBL016W.

Organism-specific databases

CYGDYBL016w.
SGDS000000112. FUS3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOGENOMHOG000233024.
KOK04371.
OMAHENINRI.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-28920-MONOMER.
BRENDA2.7.11.24. 984.

Gene expression databases

GenevestigatorP16892.

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

EvolutionaryTraceP16892.
NextBio970865.
PROP16892.

Entry information

Entry nameFUS3_YEAST
AccessionPrimary (citable) accession number: P16892
Secondary accession number(s): D6VPY4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: 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