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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: -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

Miscellaneous

Present with 8480 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Activity 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
  • identical protein binding Source: IntAct
  • MAP kinase activity Source: SGD

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Conjugation, Mitosis
LigandATP-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP16892
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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi32682, 427 interactors
DIPiDIP-714N
ELMiP16892
IntActiP16892, 35 interactors
MINTiP16892
STRINGi4932.YBL016W

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Phylogenomic databases

GeneTreeiENSGT00910000144035
HOGENOMiHOG000233024
InParanoidiP16892
KOiK04371
OMAiAYGMVSS
OrthoDBiEOG092C2FL8

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiFUS3_YEAST
AccessioniPrimary (citable) accession number: P16892
Secondary accession number(s): D6VPY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 1, 1993
Last modified: September 12, 2018
This is version 202 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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