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P16892

- FUS3_YEAST

UniProt

P16892 - FUS3_YEAST

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Protein
Mitogen-activated protein kinase FUS3
Gene
FUS3, DAC2, YBL016W, YBL03.21, YBL0303
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 STE12.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation after pheromone treatment.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATP By similarity
Active sitei137 – 1371Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: SGD
  3. identical protein binding Source: IntAct
  4. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. MAPK cascade Source: GOC
  2. cell cycle arrest Source: SGD
  3. invasive growth in response to glucose limitation Source: SGD
  4. mitotic nuclear division Source: UniProtKB-KW
  5. negative regulation of MAPK cascade Source: SGD
  6. negative regulation of transposition, RNA-mediated Source: SGD
  7. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  8. positive regulation of protein export from nucleus Source: SGD
  9. protein phosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Conjugation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28920-MONOMER.
BRENDAi2.7.11.24. 984.
ReactomeiREACT_191508. Signaling by FGFR.
REACT_205607. Regulation of HSF1-mediated heat shock response.
REACT_207653. Signal transduction by L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase FUS3 (EC:2.7.11.24)
Short name:
MAP kinase FUS3
Gene namesi
Name:FUS3
Synonyms:DAC2
Ordered Locus Names:YBL016W
ORF Names:YBL03.21, YBL0303
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBL016w.
SGDiS000000112. FUS3.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. mating projection tip Source: SGD
  3. nucleus Source: SGD
  4. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Mitogen-activated protein kinase FUS3
PRO_0000186326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Phosphothreonine1 Publication
Modified residuei182 – 1821Phosphotyrosine1 Publication

Post-translational modificationi

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 KSS1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16892.
PaxDbiP16892.
PeptideAtlasiP16892.

Expressioni

Gene expression databases

GenevestigatoriP16892.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7193,EBI-7193
BCK2P333062EBI-7193,EBI-3480
Kpol_1061p54A7TJH82EBI-7193,EBI-8783719From a different organism.
STE11P235616EBI-7193,EBI-18259
STE5P3291710EBI-7193,EBI-18373
STE7P0678415EBI-7193,EBI-18389
TIM12P328302EBI-7193,EBI-11303

Protein-protein interaction databases

BioGridi32682. 293 interactions.
DIPiDIP-714N.
IntActiP16892. 29 interactions.
MINTiMINT-376832.
STRINGi4932.YBL016W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Beta strandi13 – 219
Beta strandi23 – 3210
Turni33 – 353
Beta strandi38 – 447
Helixi50 – 6516
Beta strandi74 – 774
Turni83 – 853
Beta strandi89 – 935
Beta strandi97 – 993
Helixi100 – 1067
Helixi111 – 13020
Helixi140 – 1423
Beta strandi143 – 1453
Beta strandi151 – 1533
Helixi156 – 1583
Beta strandi182 – 1843
Helixi186 – 1883
Helixi191 – 1955
Helixi202 – 21817
Helixi228 – 23912
Turni245 – 2506
Helixi254 – 2618
Helixi271 – 2744
Helixi280 – 28910
Helixi294 – 2963
Helixi300 – 3045
Helixi307 – 3093
Turni310 – 3123
Helixi326 – 3327
Helixi340 – 35112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP16892.
SMRiP16892. Positions 1-353.

Miscellaneous databases

EvolutionaryTraceiP16892.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 309297Protein kinase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1823TXY

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
KOiK04371.
OMAiNDEPEGE.
OrthoDBiEOG7K3TWD.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16892-1 [UniParc]FASTAAdd to Basket

« Hide

MPKRIVYNIS SDFQLKSLLG EGAYGVVCSA THKPTGEIVA IKKIEPFDKP    50
LFALRTLREI KILKHFKHEN IITIFNIQRP DSFENFNEVY IIQELMQTDL 100
HRVISTQMLS DDHIQYFIYQ TLRAVKVLHG SNVIHRDLKP SNLLINSNCD 150
LKVCDFGLAR IIDESAADNS EPTGQQSGMT EYVATRWYRA PEVMLTSAKY 200
SRAMDVWSCG CILAELFLRR PIFPGRDYRH QLLLIFGIIG TPHSDNDLRC 250
IESPRAREYI KSLPMYPAAP LEKMFPRVNP KGIDLLQRML VFDPAKRITA 300
KEALEHPYLQ TYHDPNDEPE GEPIPPSFFE FDHYKEALTT KDLKKLIWNE 350
IFS 353
Length:353
Mass (Da):40,772
Last modified:October 1, 1993 - v2
Checksum:i5117980D20A1E7E2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti334 – 3341Y → H in AAA34613. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS28548.
RefSeqiNP_009537.1. NM_001178256.1.

Genome annotation databases

EnsemblFungiiYBL016W; YBL016W; YBL016W.
GeneIDi852265.
KEGGisce:YBL016W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S28548.
RefSeqi NP_009537.1. NM_001178256.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B9F X-ray 1.80 A 1-353 [» ]
2B9H X-ray 1.55 A 1-353 [» ]
2B9I X-ray 2.50 A 1-353 [» ]
2B9J X-ray 2.30 A 1-353 [» ]
2F49 X-ray 1.90 A/B 1-353 [» ]
2F9G X-ray 2.10 A 1-353 [» ]
2FA2 X-ray 2.85 A/B 1-353 [» ]
ProteinModelPortali P16892.
SMRi P16892. Positions 1-353.
ModBasei Search...

Protein-protein interaction databases

BioGridi 32682. 293 interactions.
DIPi DIP-714N.
IntActi P16892. 29 interactions.
MINTi MINT-376832.
STRINGi 4932.YBL016W.

Proteomic databases

MaxQBi P16892.
PaxDbi P16892.
PeptideAtlasi P16892.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBL016W ; YBL016W ; YBL016W .
GeneIDi 852265.
KEGGi sce:YBL016W.

Organism-specific databases

CYGDi YBL016w.
SGDi S000000112. FUS3.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074298.
HOGENOMi HOG000233024.
KOi K04371.
OMAi NDEPEGE.
OrthoDBi EOG7K3TWD.

Enzyme and pathway databases

BioCyci YEAST:G3O-28920-MONOMER.
BRENDAi 2.7.11.24. 984.
Reactomei REACT_191508. Signaling by FGFR.
REACT_205607. Regulation of HSF1-mediated heat shock response.
REACT_207653. Signal transduction by L1.

Miscellaneous databases

EvolutionaryTracei P16892.
NextBioi 970865.
PROi P16892.

Gene expression databases

Genevestigatori P16892.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. 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. 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].

Entry informationi

Entry nameiFUS3_YEAST
AccessioniPrimary (citable) accession number: P16892
Secondary accession number(s): D6VPY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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