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P32485

- HOG1_YEAST

UniProt

P32485 - HOG1_YEAST

Protein

Mitogen-activated protein kinase HOG1

Gene

HOG1

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 151 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription via the stress response element (STRE) in promoters of target genes. Upon osmotic shock, associates with the SKO1-SSN6-TUP1 complex, phosphorylates SKO1, and converts it into an activator that subsequently recruits Swi/Snf and SAGA complexes. Activates the SMP1 transcription factor and the RCK2 kinase, both also involved in the regulation of the expression of a subset of osmotic stress-related genes. Phosphorylation of HSL1 by HOG1 leads to a G2 arrest essential for cell survival at high osmolarity. Mediates also cell-cycle arrest in G1 phase by the dual targeting of SIC1. Regulates MFA2 ARE-mediated translation in response to carbon source. Targets RDP3 histone deacetylase to osmoresponsive promoters to induce gene expression on stress. Plays an essential role in maintaining water homeostasis, arsenite detoxification, copper-resistance, hydrogen peroxide response, adaptation to citric acid stress, and repression of the mating pathway activity. Required for the Golgi apparatus localization of MNN1.36 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation. Is phosphorylated on Tyr-176 by PBS2. Inactivated by dephosphorylation by NBP2 after adaptation to osmotic stress. PTP2 and PTP3 inactivate HOG1 by dephosphorylating Tyr-176, while the PP2Cs PTC1 and PTC2 or PTC3 dephosphorylate Thr-174 in the activation loop.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521ATPPROSITE-ProRule annotation
    Active sitei144 – 1441Proton 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. chromatin binding Source: SGD
    3. MAP kinase activity Source: SGD
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to heat Source: SGD
    2. cellular response to osmotic stress Source: SGD
    3. hyperosmotic response Source: SGD
    4. MAPK cascade Source: GOC
    5. osmosensory signaling pathway Source: SGD
    6. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    7. positive regulation of transcription from RNA polymerase II promoter in response to osmotic stress Source: SGD
    8. protein phosphorylation Source: SGD
    9. regulation of nuclear cell cycle DNA replication Source: SGD
    10. regulation of transcription from RNA polymerase II promoter in response to osmotic stress Source: SGD
    11. response to arsenic-containing substance Source: SGD
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32258-MONOMER.
    BRENDAi2.7.11.24. 984.
    ReactomeiREACT_188484. Oxidative Stress Induced Senescence.
    REACT_189013. NOD1/2 Signaling Pathway.
    REACT_212004. p38MAPK events.
    REACT_96987. activated TAK1 mediates p38 MAPK activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase HOG1 (EC:2.7.11.24)
    Short name:
    MAP kinase HOG1
    Alternative name(s):
    High osmolarity glycerol response protein 1
    Gene namesi
    Name:HOG1
    Synonyms:SSK3
    Ordered Locus Names:YLR113W
    ORF Names:L2931, L9354.2
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR113w.
    SGDiS000004103. HOG1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521K → R: Impairs catalytic activity, nuclear translocation, expression of CTT1 and increases sensitivity to osmotic shock. 4 Publications
    Mutagenesisi68 – 681Y → H: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi144 – 1441D → A: Impairs catalytic activity and nuclear translocation. 1 Publication
    Mutagenesisi170 – 1701D → A: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi174 – 1741T → A: Impairs catalytic activity, expression of CTT1 and increases sensitivity to osmotic shock. 2 Publications
    Mutagenesisi176 – 1761Y → F: Impairs expression of CTT1 and increases sensitivity to osmotic shock. 2 Publications
    Mutagenesisi314 – 3141A → T: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi318 – 3181F → L or S: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi320 – 3201W → R: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi322 – 3221F → L: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi332 – 3321W → R: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication
    Mutagenesisi391 – 3911N → D: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 435434Mitogen-activated protein kinase HOG1PRO_0000186331Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei174 – 1741Phosphothreonine1 Publication
    Modified residuei176 – 1761Phosphotyrosine2 Publications

    Post-translational modificationi

    Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme.15 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP32485.
    PaxDbiP32485.
    PeptideAtlasiP32485.

    Expressioni

    Inductioni

    By osmotic stress, cold stress, citric acid, and in presence of bacterial lipopolysaccharides (LPS).1 Publication

    Gene expression databases

    GenevestigatoriP32485.

    Interactioni

    Subunit structurei

    Interacts with CDC37, HOT1, KIN28, PTP2, PTP3, RBP1, RCK2, RPD3, SIC1, SMP1 and SIN4.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HOT1Q032134EBI-8437,EBI-27376
    HSL1P342442EBI-8437,EBI-9771
    SIC1P386344EBI-8437,EBI-17127
    STE7P067842EBI-8437,EBI-18389
    UBP3Q014773EBI-8437,EBI-19834

    Protein-protein interaction databases

    BioGridi31384. 331 interactions.
    DIPiDIP-1558N.
    IntActiP32485. 29 interactions.
    MINTiMINT-404719.

    Structurei

    3D structure databases

    ProteinModelPortaliP32485.
    SMRiP32485. Positions 5-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 302280Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi174 – 1763TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi364 – 37916Ala-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074271.
    HOGENOMiHOG000233024.
    KOiK04441.
    OMAiPDDVIHT.
    OrthoDBiEOG7K3TWD.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    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]
    PRINTSiPR01773. P38MAPKINASE.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P32485-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTNEEFIRT QIFGTVFEIT NRYNDLNPVG MGAFGLVCSA TDTLTSQPVA    50
    IKKIMKPFST AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT 100
    ELQGTDLHRL LQTRPLEKQF VQYFLYQILR GLKYVHSAGV IHRDLKPSNI 150
    LINENCDLKI CDFGLARIQD PQMTGYVSTR YYRAPEIMLT WQKYDVEVDI 200
    WSAGCIFAEM IEGKPLFPGK DHVHQFSIIT DLLGSPPKDV INTICSENTL 250
    KFVTSLPHRD PIPFSERFKT VEPDAVDLLE KMLVFDPKKR ITAADALAHP 300
    YSAPYHDPTD EPVADAKFDW HFNDADLPVD TWRVMMYSEI LDFHKIGGSD 350
    GQIDISATFD DQVAAATAAA AQAQAQAQAQ VQLNMAAHSH NGAGTTGNDH 400
    SDIAGGNKVS DHVAANDTIT DYGNQAIQYA NEFQQ 435
    Length:435
    Mass (Da):48,858
    Last modified:November 1, 1997 - v2
    Checksum:iD95A20242587CE06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91R → G in AAB67558. (PubMed:9090053)Curated
    Sequence conflicti409 – 43527VSDHV…NEFQQ → GQRSCSCK in AAA34680. (PubMed:7681220)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06279 Genomic DNA. Translation: AAA34680.1.
    U53878 Genomic DNA. Translation: AAB67558.1.
    Z73285 Genomic DNA. Translation: CAA97680.1.
    X89514 Genomic DNA. Translation: CAA61691.1.
    BK006945 Genomic DNA. Translation: DAA09427.1.
    PIRiS64950.
    RefSeqiNP_013214.1. NM_001182000.1.

    Genome annotation databases

    EnsemblFungiiYLR113W; YLR113W; YLR113W.
    GeneIDi850803.
    KEGGisce:YLR113W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06279 Genomic DNA. Translation: AAA34680.1 .
    U53878 Genomic DNA. Translation: AAB67558.1 .
    Z73285 Genomic DNA. Translation: CAA97680.1 .
    X89514 Genomic DNA. Translation: CAA61691.1 .
    BK006945 Genomic DNA. Translation: DAA09427.1 .
    PIRi S64950.
    RefSeqi NP_013214.1. NM_001182000.1.

    3D structure databases

    ProteinModelPortali P32485.
    SMRi P32485. Positions 5-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31384. 331 interactions.
    DIPi DIP-1558N.
    IntActi P32485. 29 interactions.
    MINTi MINT-404719.

    Proteomic databases

    MaxQBi P32485.
    PaxDbi P32485.
    PeptideAtlasi P32485.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR113W ; YLR113W ; YLR113W .
    GeneIDi 850803.
    KEGGi sce:YLR113W.

    Organism-specific databases

    CYGDi YLR113w.
    SGDi S000004103. HOG1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074271.
    HOGENOMi HOG000233024.
    KOi K04441.
    OMAi PDDVIHT.
    OrthoDBi EOG7K3TWD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32258-MONOMER.
    BRENDAi 2.7.11.24. 984.
    Reactomei REACT_188484. Oxidative Stress Induced Senescence.
    REACT_189013. NOD1/2 Signaling Pathway.
    REACT_212004. p38MAPK events.
    REACT_96987. activated TAK1 mediates p38 MAPK activation.

    Miscellaneous databases

    NextBioi 967026.
    PROi P32485.

    Gene expression databases

    Genevestigatori P32485.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    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 ]
    PRINTSi PR01773. P38MAPKINASE.
    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. "An osmosensing signal transduction pathway in yeast."
      Brewster J.L., de Valoir T., Dwyer N.D., Winter E., Gustin M.C.
      Science 259:1760-1763(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found."
      Verhasselt P., Volckaert G.
      Yeast 13:241-250(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 90840 / EAY235 / FY23.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The HOG pathway controls osmotic regulation of transcription via the stress response element (STRE) of the Saccharomyces cerevisiae CTT1 gene."
      Schueller C., Brewster J.L., Alexander M.R., Gustin M.C., Ruis H.
      EMBO J. 13:4382-4389(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF LYS-52; THR-174 AND TYR-176.
    6. "Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway."
      Norbeck J., Paehlman A.-K., Akhtar N., Blomberg A., Adler L.
      J. Biol. Chem. 271:13875-13881(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The osmoregulatory pathway represses mating pathway activity in Saccharomyces cerevisiae: isolation of a FUS3 mutant that is insensitive to the repression mechanism."
      Hall J.P., Cherkasova V., Elion E., Gustin M.C., Winter E.
      Mol. Cell. Biol. 16:6715-6723(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-52.
    8. "Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases."
      Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H.
      Mol. Cell. Biol. 17:1289-1297(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTP2, ENZYME REGULATION.
    9. "Two protein-tyrosine phosphatases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1."
      Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M.
      J. Biol. Chem. 272:17749-17755(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTP2 AND PTP3, ENZYME REGULATION.
    10. "The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae."
      O'Rourke S.M., Herskowitz I.
      Genes Dev. 12:2874-2886(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The high osmolarity glycerol response (HOG) MAP kinase pathway controls localization of a yeast Golgi glycosyltransferase."
      Reynolds T.B., Hopkins B.D., Lyons M.R., Graham T.R.
      J. Cell Biol. 143:935-946(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Kinase activity-dependent nuclear export opposes stress-induced nuclear accumulation and retention of Hog1 mitogen-activated protein kinase in the budding yeast Saccharomyces cerevisiae."
      Reiser V., Ruis H., Ammerer G.
      Mol. Biol. Cell 10:1147-1161(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    13. "Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway."
      Raitt D.C., Posas F., Saito H.
      EMBO J. 19:4623-4631(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast."
      Mattison C.P., Ota I.M.
      Genes Dev. 14:1229-1235(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Rck2 kinase is a substrate for the osmotic stress-activated mitogen-activated protein kinase Hog1."
      Bilsland-Marchesan E., Arino J., Saito H., Sunnerhagen P., Posas F.
      Mol. Cell. Biol. 20:3887-3895(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RCK2.
    16. "Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress."
      Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.
      EMBO J. 20:1123-1133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SKO1.
    17. "Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate Hog1 kinase and confer copper-resistance in Saccharomyces cerevisisae."
      Toh-e A., Oguchi T.
      Genes Genet. Syst. 76:393-410(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation."
      Bell M., Capone R., Pashtan I., Levitzki A., Engelberg D.
      J. Biol. Chem. 276:25351-25358(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-68; ASP-170; ALA-314; PHE-318; TRP-320; PHE-322; TRP-332 AND ASN-391.
    19. "Stress-induced map kinase Hog1 is part of transcription activation complexes."
      Alepuz P.M., Jovanovic A., Reiser V., Ammerer G.
      Mol. Cell 7:767-777(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1."
      Warmka J., Hanneman J., Lee J., Amin D., Ota I.M.
      Mol. Cell. Biol. 21:51-60(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    21. "Low external pH induces HOG1-dependent changes in the organization of the Saccharomyces cerevisiae cell wall."
      Kapteyn J.C., ter Riet B., Vink E., Blad S., De Nobel H., Van Den Ende H., Klis F.M.
      Mol. Microbiol. 39:469-479(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress."
      Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K., Ota I.M.
      Eukaryot. Cell 1:163-173(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    23. "Role of Ptc2 type 2C Ser/Thr phosphatase in yeast high-osmolarity glycerol pathway inactivation."
      Young C., Mapes J., Hanneman J., Al-Zarban S., Ota I.M.
      Eukaryot. Cell 1:1032-1040(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    24. "Transient inhibition of translation initiation by osmotic stress."
      Uesono Y., Toh-e A.
      J. Biol. Chem. 277:13848-13855(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Hog1 kinase converts the Sko1-Cyc8-Tup1 repressor complex into an activator that recruits SAGA and SWI/SNF in response to osmotic stress."
      Proft M., Struhl K.
      Mol. Cell 9:1307-1317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "Osmostress-induced transcription by Hot1 depends on a Hog1-mediated recruitment of the RNA Pol II."
      Alepuz P.M., de Nadal E., Zapater M., Ammerer G., Posas F.
      EMBO J. 22:2433-2442(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HOT1; KIN28; RBP1 AND SIN4.
    27. "Phosphorylation of Tyr-176 of the yeast MAPK Hog1/p38 is not vital for Hog1 biological activity."
      Bell M., Engelberg D.
      J. Biol. Chem. 278:14603-14606(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-174 AND TYR-176, MUTAGENESIS OF THR-174 AND TYR-176.
    28. "Targeting the MEF2-like transcription factor Smp1 by the stress-activated Hog1 mitogen-activated protein kinase."
      de Nadal E., Casadome L., Posas F.
      Mol. Cell. Biol. 23:229-237(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMP1.
    29. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    30. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    31. "Expression of YAP4 in Saccharomyces cerevisiae under osmotic stress."
      Nevitt T., Pereira J., Azevedo D., Guerreiro P., Rodrigues-Pousada C.
      Biochem. J. 379:367-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "The Hog1 MAP kinase pathway and the Mec1 DNA damage checkpoint pathway independently control the cellular responses to hydrogen peroxide."
      Haghnazari E., Heyer W.-D.
      DNA Repair 3:769-776(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "Evidence of a new role for the high-osmolarity glycerol mitogen-activated protein kinase pathway in yeast: regulating adaptation to citric acid stress."
      Lawrence C.L., Botting C.H., Antrobus R., Coote P.J.
      Mol. Cell. Biol. 24:3307-3323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    34. "The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes."
      De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F.
      Nature 427:370-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPD3.
    35. "Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1."
      Escote X., Zapater M., Clotet J., Posas F.
      Nat. Cell Biol. 6:997-1002(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIC1.
    36. "Evidence that C-terminal non-kinase domain of Pbs2p has a role in high osmolarity-induced nuclear localization of Hog1p."
      Sharma P., Mondal A.K.
      Biochem. Biophys. Res. Commun. 328:906-913(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    37. "p38 mitogen-activated protein kinase/Hog1p regulates translation of the AU-rich-element-bearing MFA2 transcript."
      Vasudevan S., Garneau N., Tu Khounh D., Peltz S.W.
      Mol. Cell. Biol. 25:9753-9763(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    38. "The HOG MAP kinase pathway is required for the induction of methylglyoxal-responsive genes and determines methylglyoxal resistance in Saccharomyces cerevisiae."
      Aguilera J., Rodriguez-Vargas S., Prieto J.A.
      Mol. Microbiol. 56:228-239(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    39. "In yeast, loss of Hog1 leads to osmosensitivity of autophagy."
      Prick T., Thumm M., Koehrer K., Haeussinger D., Vom Dahl S.
      Biochem. J. 394:153-161(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    40. "Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity."
      Clotet J., Escote X., Adrover M.A., Yaakov G., Gari E., Aldea M., de Nadal E., Posas F.
      EMBO J. 25:2338-2346(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    41. "Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae."
      Chasse S.A., Flanary P., Parnell S.C., Hao N., Cha J.Y., Siderovski D.P., Dohlman H.G.
      Eukaryot. Cell 5:330-346(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    42. "Analysis of mitogen-activated protein kinase signaling specificity in response to hyperosmotic stress: use of an analog-sensitive HOG1 allele."
      Westfall P.J., Thorner J.
      Eukaryot. Cell 5:1215-1228(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-52 AND ASP-144.
    43. "Mitogen-activated protein kinase Hog1 is essential for the response to arsenite in Saccharomyces cerevisiae."
      Sotelo J., Rodriguez-Gabriel M.A.
      Eukaryot. Cell 5:1826-1830(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    44. "A downshift in temperature activates the high osmolarity glycerol (HOG) pathway, which determines freeze tolerance in Saccharomyces cerevisiae."
      Panadero J., Pallotti C., Rodriguez-Vargas S., Randez-Gil F., Prieto J.A.
      J. Biol. Chem. 281:4638-4645(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    45. "Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin."
      Marques J.M., Rodrigues R.J., de Magalhaes-Sant'ana A.C., Goncalves T.
      J. Biol. Chem. 281:24687-24694(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    46. Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    47. "The stress-activated Hog1 kinase is a selective transcriptional elongation factor for genes responding to osmotic stress."
      Proft M., Mas G., de Nadal E., Vendrell A., Noriega N., Struhl K., Posas F.
      Mol. Cell 23:241-250(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPB1.
    48. "A systems-biology analysis of feedback inhibition in the Sho1 osmotic-stress-response pathway."
      Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H., Elston T.C., Dohlman H.G.
      Curr. Biol. 17:659-667(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-52.
    49. "Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)."
      Hawle P., Horst D., Bebelman J.-P., Yang X.X., Siderius M., van der Vies S.M.
      Eukaryot. Cell 6:521-532(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC37, PHOSPHORYLATION.
    50. "Dissecting yeast Hog1 MAP kinase pathway using a chemical genetic approach."
      Kim S., Shah K.
      FEBS Lett. 581:1209-1216(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    51. "Plc1p is required for SAGA recruitment and derepression of Sko1p-regulated genes."
      Guha N., Desai P., Vancura A.
      Mol. Biol. Cell 18:2419-2428(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    52. "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].
    53. "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 TYR-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    54. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHOG1_YEAST
    AccessioniPrimary (citable) accession number: P32485
    Secondary accession number(s): D6VYB1, Q06232, Q12294
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 151 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 6780 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 XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3