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Protein

Mitogen-activated protein kinase FUS3

Gene

FUS3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

Mg2+By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation after pheromone treatment.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42ATPPROSITE-ProRule annotation1
Active sitei137Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 27ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: SGD

GO - Biological processi

  • cell cycle arrest Source: SGD
  • cell division Source: UniProtKB-KW
  • invasive growth in response to glucose limitation Source: SGD
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of MAPK cascade Source: SGD
  • negative regulation of transposition, RNA-mediated Source: SGD
  • pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  • positive regulation of protein export from nucleus Source: SGD
  • protein autophosphorylation Source: SGD
  • 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.
ReactomeiR-SCE-110056. MAPK3 (ERK1) activation.
R-SCE-112409. RAF-independent MAPK1/3 activation.
R-SCE-112411. MAPK1 (ERK2) activation.
R-SCE-1169408. ISG15 antiviral mechanism.
R-SCE-198753. ERK/MAPK targets.
R-SCE-198765. Signalling to ERK5.
R-SCE-202670. ERKs are inactivated.
R-SCE-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-375165. NCAM signaling for neurite out-growth.
R-SCE-4086398. Ca2+ pathway.
R-SCE-444257. RSK activation.
R-SCE-445144. Signal transduction by L1.
R-SCE-5673001. RAF/MAP kinase cascade.
R-SCE-5674135. MAP2K and MAPK activation.
R-SCE-5674499. Negative feedback regulation of MAPK pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-881907. Gastrin-CREB signalling pathway via PKC and MAPK.

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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL016W.
SGDiS000000112. FUS3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic stress granule Source: SGD
  • mating projection tip Source: SGD
  • nucleus Source: SGD
  • periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863261 – 353Mitogen-activated protein kinase FUS3Add BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei180Phosphothreonine1 Publication1
Modified residuei182Phosphotyrosine1 Publication1
Cross-linki345Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

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

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16892.
PRIDEiP16892.

PTM databases

iPTMnetiP16892.

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. 305 interactors.
DIPiDIP-714N.
IntActiP16892. 30 interactors.
MINTiMINT-376832.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi13 – 21Combined sources9
Beta strandi23 – 32Combined sources10
Turni33 – 35Combined sources3
Beta strandi38 – 44Combined sources7
Helixi50 – 65Combined sources16
Beta strandi74 – 77Combined sources4
Turni83 – 85Combined sources3
Beta strandi89 – 93Combined sources5
Beta strandi97 – 99Combined sources3
Helixi100 – 106Combined sources7
Helixi111 – 130Combined sources20
Helixi140 – 142Combined sources3
Beta strandi143 – 145Combined sources3
Beta strandi151 – 153Combined sources3
Helixi156 – 158Combined sources3
Beta strandi182 – 184Combined sources3
Helixi186 – 188Combined sources3
Helixi191 – 195Combined sources5
Helixi202 – 218Combined sources17
Helixi228 – 239Combined sources12
Turni245 – 250Combined sources6
Helixi254 – 261Combined sources8
Helixi271 – 274Combined sources4
Helixi280 – 289Combined sources10
Helixi294 – 296Combined sources3
Helixi300 – 304Combined sources5
Helixi307 – 309Combined sources3
Turni310 – 312Combined sources3
Helixi326 – 332Combined sources7
Helixi340 – 351Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16892.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 309Protein kinasePROSITE-ProRule annotationAdd BLAST297

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi180 – 182TXY3

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
InParanoidiP16892.
KOiK04371.
OMAiDEFHAIT.
OrthoDBiEOG092C2FL8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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

        10         20         30         40         50
MPKRIVYNIS SDFQLKSLLG EGAYGVVCSA THKPTGEIVA IKKIEPFDKP
60 70 80 90 100
LFALRTLREI KILKHFKHEN IITIFNIQRP DSFENFNEVY IIQELMQTDL
110 120 130 140 150
HRVISTQMLS DDHIQYFIYQ TLRAVKVLHG SNVIHRDLKP SNLLINSNCD
160 170 180 190 200
LKVCDFGLAR IIDESAADNS EPTGQQSGMT EYVATRWYRA PEVMLTSAKY
210 220 230 240 250
SRAMDVWSCG CILAELFLRR PIFPGRDYRH QLLLIFGIIG TPHSDNDLRC
260 270 280 290 300
IESPRAREYI KSLPMYPAAP LEKMFPRVNP KGIDLLQRML VFDPAKRITA
310 320 330 340 350
KEALEHPYLQ TYHDPNDEPE GEPIPPSFFE FDHYKEALTT KDLKKLIWNE

IFS
Length:353
Mass (Da):40,772
Last modified:October 1, 1993 - v2
Checksum:i5117980D20A1E7E2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti334Y → H in AAA34613 (PubMed:2406028).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32682. 305 interactors.
DIPiDIP-714N.
IntActiP16892. 30 interactors.
MINTiMINT-376832.

PTM databases

iPTMnetiP16892.

Proteomic databases

MaxQBiP16892.
PRIDEiP16892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YBL016W.
SGDiS000000112. FUS3.

Phylogenomic databases

GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
InParanoidiP16892.
KOiK04371.
OMAiDEFHAIT.
OrthoDBiEOG092C2FL8.

Enzyme and pathway databases

BioCyciYEAST:G3O-28920-MONOMER.
BRENDAi2.7.11.24. 984.
ReactomeiR-SCE-110056. MAPK3 (ERK1) activation.
R-SCE-112409. RAF-independent MAPK1/3 activation.
R-SCE-112411. MAPK1 (ERK2) activation.
R-SCE-1169408. ISG15 antiviral mechanism.
R-SCE-198753. ERK/MAPK targets.
R-SCE-198765. Signalling to ERK5.
R-SCE-202670. ERKs are inactivated.
R-SCE-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-375165. NCAM signaling for neurite out-growth.
R-SCE-4086398. Ca2+ pathway.
R-SCE-444257. RSK activation.
R-SCE-445144. Signal transduction by L1.
R-SCE-5673001. RAF/MAP kinase cascade.
R-SCE-5674135. MAP2K and MAPK activation.
R-SCE-5674499. Negative feedback regulation of MAPK pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-881907. Gastrin-CREB signalling pathway via PKC and MAPK.

Miscellaneous databases

EvolutionaryTraceiP16892.
PROiP16892.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 185 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.