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Protein

Mitogen-activated protein kinase SLT2/MPK1

Gene

SLT2

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

Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the SLT2/MPK1 kinase which itself then phosphorylates and activates the transcription factor RLM1. Directly phosphorylates BCY1 upon TOR complex 1 (TORC1) inhibition.2 Publications

Miscellaneous

Present with 3230 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation by MKK1 and MKK2.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54ATPPROSITE-ProRule annotation1
Active sitei153Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 37ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • autophagy of peroxisome Source: SGD
  • cellular response to osmotic stress Source: GO_Central
  • endoplasmic reticulum unfolded protein response Source: SGD
  • fungal-type cell wall biogenesis Source: SGD
  • mRNA splicing via endonucleolytic cleavage and ligation involved in unfolded protein response Source: SGD
  • positive regulation of division septum assembly Source: SGD
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: GO_Central
  • protein phosphorylation Source: SGD
  • regulation of cell size Source: SGD
  • regulation of fungal-type cell wall organization Source: SGD
  • regulation of proteasome assembly Source: SGD
  • regulation of transcription factor import into nucleus Source: SGD
  • response to acidic pH Source: SGD
  • response to endoplasmic reticulum stress Source: SGD
  • signal transduction Source: SGD

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31090-MONOMER.
BRENDAi2.7.11.24. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase SLT2/MPK1 (EC:2.7.11.24)
Short name:
MAP kinase MPK1
Gene namesi
Name:SLT2
Synonyms:MPK1
Ordered Locus Names:YHR030C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR030C.
SGDiS000001072. SLT2.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863381 – 484Mitogen-activated protein kinase SLT2/MPK1Add BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei190PhosphothreonineCombined sources1
Modified residuei192PhosphotyrosineCombined sources1

Post-translational modificationi

Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ00772.
PRIDEiQ00772.

PTM databases

iPTMnetiQ00772.

Interactioni

Subunit structurei

Interacts with RLM1.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi36461. 894 interactors.
DIPiDIP-1448N.
ELMiQ00772.
IntActiQ00772. 98 interactors.
MINTiMINT-395773.
STRINGi4932.YHR030C.

Structurei

3D structure databases

ProteinModelPortaliQ00772.
SMRiQ00772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 318Protein kinasePROSITE-ProRule annotationAdd BLAST296

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi190 – 192TXY3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi370 – 391Poly-GlnAdd BLAST22

Domaini

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

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00900000140938.
HOGENOMiHOG000233024.
InParanoidiQ00772.
KOiK04464.
OMAiASDEPDC.
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.

Q00772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKIERHTF KVFNQDFSVD KRFQLIKEIG HGAYGIVCSA RFAEAAEDTT
60 70 80 90 100
VAIKKVTNVF SKTLLCKRSL RELKLLRHFR GHKNITCLYD MDIVFYPDGS
110 120 130 140 150
INGLYLYEEL MECDMHQIIK SGQPLTDAHY QSFTYQILCG LKYIHSADVL
160 170 180 190 200
HRDLKPGNLL VNADCQLKIC DFGLARGYSE NPVENSQFLT EYVATRWYRA
210 220 230 240 250
PEIMLSYQGY TKAIDVWSAG CILAEFLGGK PIFKGKDYVN QLNQILQVLG
260 270 280 290 300
TPPDETLRRI GSKNVQDYIH QLGFIPKVPF VNLYPNANSQ ALDLLEQMLA
310 320 330 340 350
FDPQKRITVD EALEHPYLSI WHDPADEPVC SEKFEFSFES VNDMEDLKQM
360 370 380 390 400
VIQEVQDFRL FVRQPLLEEQ RQLQLQQQQQ QQQQQQQQQQ QPSDVDNGNA
410 420 430 440 450
AASEENYPKQ MATSNSVAPQ QESFGIHSQN LPRHDADFPP RPQESMMEMR
460 470 480
PATGNTADIP PQNDNGTLLD LEKELEFGLD RKYF
Length:484
Mass (Da):55,636
Last modified:February 1, 1995 - v2
Checksum:i559A3E0D3EBDE5F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56V → L in CAA41954 (PubMed:1779770).Curated1
Sequence conflicti467T → S in CAA41954 (PubMed:1779770).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59262 Genomic DNA. Translation: CAA41954.1.
U00062 Genomic DNA. Translation: AAB68912.1.
BK006934 Genomic DNA. Translation: DAA06721.1.
PIRiS43737.
RefSeqiNP_011895.1. NM_001179160.1.

Genome annotation databases

EnsemblFungiiYHR030C; YHR030C; YHR030C.
GeneIDi856425.
KEGGisce:YHR030C.

Similar proteinsi

Entry informationi

Entry nameiSLT2_YEAST
AccessioniPrimary (citable) accession number: Q00772
Secondary accession number(s): D3DKX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: November 22, 2017
This is version 178 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

Complete proteome, Reference proteome

Documents

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