Mitogen-activated protein kinase HOG1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P32485 (HOG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 137. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase HOG1
Short name=MAP kinase HOG1
EC=2.7.11.24

Alternative name(s):
High osmolarity glycerol response protein 1

Gene names

Name:	HOG1
Synonyms:	SSK3
Ordered Locus Names:	YLR113W
ORF Names:	L2931, L9354.2

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.25 Ref.27 Ref.29 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	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. Ref.8 Ref.9 Ref.20 Ref.22 Ref.23
Subunit structure	Interacts with CDC37, HOT1, KIN28, PTP2, PTP3, RBP1, RCK2, RPD3, SIC1, SMP1 and SIN4. Ref.8 Ref.9 Ref.15 Ref.16 Ref.27 Ref.29 Ref.35 Ref.36 Ref.48 Ref.50
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation. Ref.12 Ref.14 Ref.30 Ref.37 Ref.43 Ref.46 Ref.47
Induction	By osmotic stress, cold stress, citric acid, and in presence of bacterial lipopolysaccharides (LPS). Ref.8 Ref.9 Ref.20 Ref.22 Ref.23 Ref.46
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme. Ref.5 Ref.12 Ref.16 Ref.28 Ref.34 Ref.37 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.50 Ref.51
Miscellaneous	Present with 6780 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to heat Inferred from mutant phenotype Ref.22. Source: SGD hyperosmotic response Inferred from mutant phenotype Ref.1. Source: SGD negative regulation of transcription from RNA polymerase II promoter by pheromones Inferred from expression pattern PubMed 10722658. Source: SGD osmosensory signaling pathway Inferred from mutant phenotype Ref.1. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.27. Source: SGD response to arsenic-containing substance Inferred from mutant phenotype Ref.47. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.14 PubMed 11914276. Source: SGD nucleus Inferred from direct assay Ref.14. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from direct assay Ref.15. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
HOT1	Q03213	4	EBI-8437,EBI-27376
RCK2	P38623	4	EBI-8437,EBI-14885
SIC1	P38634	4	EBI-8437,EBI-17127
STE7	P06784	2	EBI-8437,EBI-18389

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 435

435

Mitogen-activated protein kinase HOG1

PRO_0000186331

Regions

Domain

23 – 302

280

Protein kinase

Nucleotide binding

29 – 37

ATP By similarity

Motif

174 – 176

TXY

Compositional bias

364 – 379

Ala-rich

Sites

Active site

144

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

174

Phosphothreonine Ref.26 Ref.28

Modified residue

176

Phosphotyrosine Ref.26 Ref.28 Ref.53

Modified residue

178

Phosphoserine Ref.53

Modified residue

179

Phosphothreonine Ref.53

Experimental info

Mutagenesis

K → R: Impairs catalytic activity, nuclear translocation, expression of CTT1 and increases sensitivity to osmotic shock. Ref.5 Ref.7 Ref.43 Ref.49

Mutagenesis

Y → H: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

144

D → A: Impairs catalytic activity and nuclear translocation. Ref.43

Mutagenesis

170

D → A: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

174

T → A: Impairs catalytic activity, expression of CTT1 and increases sensitivity to osmotic shock. Ref.5 Ref.28

Mutagenesis

176

Y → F: Impairs expression of CTT1 and increases sensitivity to osmotic shock. Ref.5 Ref.28

Mutagenesis

314

A → T: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

318

F → L or S: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

320

W → R: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

322

F → L: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

332

W → R: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Mutagenesis

391

N → D: Activates HOG1 in a constitutive manner, without the need of a stimulating stress. Ref.18

Sequence conflict

R → G in AAB67558. Ref.2

Sequence conflict

409 – 435

VSDHV…NEFQQ → GQRSCSCK in AAA34680. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P32485 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D95A20242587CE06
Show »

FASTA

435

48,858

        10         20         30         40         50         60 
MTTNEEFIRT QIFGTVFEIT NRYNDLNPVG MGAFGLVCSA TDTLTSQPVA IKKIMKPFST 

        70         80         90        100        110        120 
AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT ELQGTDLHRL LQTRPLEKQF 

       130        140        150        160        170        180 
VQYFLYQILR GLKYVHSAGV IHRDLKPSNI LINENCDLKI CDFGLARIQD PQMTGYVSTR 

       190        200        210        220        230        240 
YYRAPEIMLT WQKYDVEVDI WSAGCIFAEM IEGKPLFPGK DHVHQFSIIT DLLGSPPKDV 

       250        260        270        280        290        300 
INTICSENTL KFVTSLPHRD PIPFSERFKT VEPDAVDLLE KMLVFDPKKR ITAADALAHP 

       310        320        330        340        350        360 
YSAPYHDPTD EPVADAKFDW HFNDADLPVD TWRVMMYSEI LDFHKIGGSD GQIDISATFD 

       370        380        390        400        410        420 
DQVAAATAAA AQAQAQAQAQ VQLNMAAHSH NGAGTTGNDH SDIAGGNKVS DHVAANDTIT 

       430 
DYGNQAIQYA NEFQQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND TYR-176, MASS SPECTROMETRY. Strain: 2124.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[31]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"The MAPK Hog1p modulates Fps1p-dependent arsenite uptake and tolerance in yeast." Thorsen M., Di Y., Taengemo C., Morillas M., Ahmadpour D., Van der Does C., Wagner A., Johansson E., Boman J., Posas F., Wysocki R., Tamas M.J. Mol. Biol. Cell 17:4400-4410(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-176; SER-178 AND THR-179, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S64950.
RefSeq	NP_013214.1. NM_001182000.1.
3D structure databases
ProteinModelPortal	P32485.
SMR	P32485. Positions 7-343.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1558N.
IntAct	P32485. 24 interactions.
MINT	MINT-404719.
Proteomic databases
PaxDb	P32485.
PeptideAtlas	P32485.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR113W; YLR113W; YLR113W.
GeneID	850803.
KEGG	sce:YLR113W.
Organism-specific databases
CYGD	YLR113w.
SGD	S000004103. HOG1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074271.
HOGENOM	HOG000233024.
KO	K04441.
OMA	RELIWNE.
OrthoDB	EOG496319.
Enzyme and pathway databases
BRENDA	2.7.11.24. 984.
Gene expression databases
Genevestigator	P32485.
GermOnline	YLR113W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR008352. MAPK_p38. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01773. P38MAPKINASE.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967026.

Entry information

Entry name

HOG1_YEAST

Accession

Primary (citable) accession number: P32485
Secondary accession number(s): D6VYB1, Q06232, Q12294

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents