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Q00772

- SLT2_YEAST

UniProt

Q00772 - SLT2_YEAST

Protein

Mitogen-activated protein kinase SLT2/MPK1

Gene

SLT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Serine/threonine protein kinase involved in a signal transduction pathway that play 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

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541ATPPROSITE-ProRule annotation
    Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: SGD
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: SGD

    GO - Biological processi

    1. barrier septum assembly Source: SGD
    2. endoplasmic reticulum unfolded protein response Source: SGD
    3. fungal-type cell wall biogenesis Source: SGD
    4. MAPK cascade Source: GOC
    5. peroxisome degradation Source: SGD
    6. protein phosphorylation Source: SGD
    7. regulation of cell size Source: SGD
    8. regulation of fungal-type cell wall organization Source: SGD
    9. regulation of transcription factor import into nucleus Source: SGD
    10. response to acid chemical Source: SGD
    11. signal transduction Source: SGD
    12. UFP-specific transcription factor mRNA processing involved in endoplasmic reticulum unfolded protein response Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-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
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR030c.
    SGDiS000001072. SLT2.

    Subcellular locationi

    GO - Cellular componenti

    1. cellular bud neck Source: SGD
    2. cellular bud tip Source: SGD
    3. mating projection tip Source: SGD
    4. nucleus Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Mitogen-activated protein kinase SLT2/MPK1PRO_0000186338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei190 – 1901Phosphothreonine1 Publication
    Modified residuei192 – 1921Phosphotyrosine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ00772.
    PaxDbiQ00772.
    PeptideAtlasiQ00772.
    PRIDEiQ00772.

    Expressioni

    Gene expression databases

    GenevestigatoriQ00772.

    Interactioni

    Subunit structurei

    Interacts with RLM1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADA2Q023362EBI-17372,EBI-2186
    CDC73Q066972EBI-17372,EBI-29913
    CTR9P891052EBI-17372,EBI-5283
    GCN5Q033302EBI-17372,EBI-7458
    HSP82P028294EBI-17372,EBI-8659
    KIC1P386922EBI-17372,EBI-12253
    LEO1P384392EBI-17372,EBI-10108
    MKK2P324914EBI-17372,EBI-10973
    PAF1P383512EBI-17372,EBI-12855
    RTF1P530642EBI-17372,EBI-16303
    SSK2P535992EBI-17372,EBI-18191
    STE12P135742EBI-17372,EBI-18264

    Protein-protein interaction databases

    BioGridi36461. 620 interactions.
    DIPiDIP-1448N.
    IntActiQ00772. 39 interactions.
    MINTiMINT-395773.
    STRINGi4932.YHR030C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00772.
    SMRiQ00772. Positions 12-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 318296Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi190 – 1923TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi370 – 39122Poly-GlnAdd
    BLAST

    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

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000112267.
    HOGENOMiHOG000233024.
    KOiK04464.
    OMAiFMPKKPF.
    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.

    Q00772-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADKIERHTF KVFNQDFSVD KRFQLIKEIG HGAYGIVCSA RFAEAAEDTT    50
    VAIKKVTNVF SKTLLCKRSL RELKLLRHFR GHKNITCLYD MDIVFYPDGS 100
    INGLYLYEEL MECDMHQIIK SGQPLTDAHY QSFTYQILCG LKYIHSADVL 150
    HRDLKPGNLL VNADCQLKIC DFGLARGYSE NPVENSQFLT EYVATRWYRA 200
    PEIMLSYQGY TKAIDVWSAG CILAEFLGGK PIFKGKDYVN QLNQILQVLG 250
    TPPDETLRRI GSKNVQDYIH QLGFIPKVPF VNLYPNANSQ ALDLLEQMLA 300
    FDPQKRITVD EALEHPYLSI WHDPADEPVC SEKFEFSFES VNDMEDLKQM 350
    VIQEVQDFRL FVRQPLLEEQ RQLQLQQQQQ QQQQQQQQQQ QPSDVDNGNA 400
    AASEENYPKQ MATSNSVAPQ QESFGIHSQN LPRHDADFPP RPQESMMEMR 450
    PATGNTADIP PQNDNGTLLD LEKELEFGLD RKYF 484
    Length:484
    Mass (Da):55,636
    Last modified:February 1, 1995 - v2
    Checksum:i559A3E0D3EBDE5F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561V → L in CAA41954. (PubMed:1779770)Curated
    Sequence conflicti467 – 4671T → S in CAA41954. (PubMed:1779770)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59262 Genomic DNA. Translation: CAA41954.1 .
    U00062 Genomic DNA. Translation: AAB68912.1 .
    BK006934 Genomic DNA. Translation: DAA06721.1 .
    PIRi S43737.
    RefSeqi NP_011895.1. NM_001179160.1.

    3D structure databases

    ProteinModelPortali Q00772.
    SMRi Q00772. Positions 12-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36461. 620 interactions.
    DIPi DIP-1448N.
    IntActi Q00772. 39 interactions.
    MINTi MINT-395773.
    STRINGi 4932.YHR030C.

    Proteomic databases

    MaxQBi Q00772.
    PaxDbi Q00772.
    PeptideAtlasi Q00772.
    PRIDEi Q00772.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR030C ; YHR030C ; YHR030C .
    GeneIDi 856425.
    KEGGi sce:YHR030C.

    Organism-specific databases

    CYGDi YHR030c.
    SGDi S000001072. SLT2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000112267.
    HOGENOMi HOG000233024.
    KOi K04464.
    OMAi FMPKKPF.
    OrthoDBi EOG7K3TWD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31090-MONOMER.
    BRENDAi 2.7.11.24. 984.

    Miscellaneous databases

    NextBioi 982003.

    Gene expression databases

    Genevestigatori Q00772.

    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

    1. "A protein kinase gene complements the lytic phenotype of Saccharomyces cerevisiae lyt2 mutants."
      Torres L., Martin H., Garcia-Saez M.I., Arroyo J., Molina M., Sanchez M., Nombela C.
      Mol. Microbiol. 5:2845-2854(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204510 / AB320.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The SLT2 (MPK1) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae."
      Mazzoni C., Zarzov P., Rambourg A., Mann C.
      J. Cell Biol. 123:1821-1833(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway."
      Watanabe Y., Takaesu G., Hagiwara M., Irie K., Matsumoto K.
      Mol. Cell. Biol. 17:2615-2623(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RLM1.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates."
      Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.
      Mol. Biol. Cell 21:3475-3486(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiSLT2_YEAST
    AccessioniPrimary (citable) accession number: Q00772
    Secondary accession number(s): D3DKX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 145 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 3230 molecules/cell in log phase SD medium.1 Publication

    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

    External Data

    Dasty 3