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Protein

Mitogen-activated protein kinase HOG1

Gene

HOG1

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

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

Mg2+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

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: SGD
  • MAP kinase activity Source: SGD

GO - Biological processi

  • cellular response to heat Source: SGD
  • cellular response to osmotic stress Source: SGD
  • hyperosmotic response Source: SGD
  • osmosensory signaling pathway Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to osmotic stress Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of macroautophagy Source: SGD
  • regulation of nuclear cell cycle DNA replication Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to osmotic stress Source: SGD
  • response to arsenic-containing substance Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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.
ReactomeiR-SCE-168638. NOD1/2 Signaling Pathway.
R-SCE-171007. p38MAPK events.
R-SCE-193648. NRAGE signals death through JNK.
R-SCE-198753. ERK/MAPK targets.
R-SCE-2559580. Oxidative Stress Induced Senescence.
R-SCE-2871796. FCERI mediated MAPK activation.
R-SCE-375170. CDO in myogenesis.
R-SCE-418592. ADP signalling through P2Y purinoceptor 1.
R-SCE-4420097. VEGFA-VEGFR2 Pathway.
R-SCE-450302. activated TAK1 mediates p38 MAPK activation.
R-SCE-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR113W.
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

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

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 methionineiRemovedCombined sources
Chaini2 – 435434Mitogen-activated protein kinase HOG1PRO_0000186331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Modified residuei174 – 1741Phosphothreonine1 Publication
Modified residuei176 – 1761PhosphotyrosineCombined sources1 Publication

Post-translational modificationi

Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme.14 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32485.

PTM databases

iPTMnetiP32485.

Expressioni

Inductioni

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

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. 343 interactions.
DIPiDIP-1558N.
IntActiP32485. 29 interactions.
MINTiMINT-404719.

Structurei

3D structure databases

ProteinModelPortaliP32485.
SMRiP32485. Positions 7-345.
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

GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiP32485.
KOiK04441.
OMAiLSHEYLA.
OrthoDBiEOG092C2FL8.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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

        10         20         30         40         50
MTTNEEFIRT QIFGTVFEIT NRYNDLNPVG MGAFGLVCSA TDTLTSQPVA
60 70 80 90 100
IKKIMKPFST AVLAKRTYRE LKLLKHLRHE NLICLQDIFL SPLEDIYFVT
110 120 130 140 150
ELQGTDLHRL LQTRPLEKQF VQYFLYQILR GLKYVHSAGV IHRDLKPSNI
160 170 180 190 200
LINENCDLKI CDFGLARIQD PQMTGYVSTR YYRAPEIMLT WQKYDVEVDI
210 220 230 240 250
WSAGCIFAEM IEGKPLFPGK DHVHQFSIIT DLLGSPPKDV INTICSENTL
260 270 280 290 300
KFVTSLPHRD PIPFSERFKT VEPDAVDLLE KMLVFDPKKR ITAADALAHP
310 320 330 340 350
YSAPYHDPTD EPVADAKFDW HFNDADLPVD TWRVMMYSEI LDFHKIGGSD
360 370 380 390 400
GQIDISATFD DQVAAATAAA AQAQAQAQAQ VQLNMAAHSH NGAGTTGNDH
410 420 430
SDIAGGNKVS DHVAANDTIT DYGNQAIQYA NEFQQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP32485.
SMRiP32485. Positions 7-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31384. 343 interactions.
DIPiDIP-1558N.
IntActiP32485. 29 interactions.
MINTiMINT-404719.

PTM databases

iPTMnetiP32485.

Proteomic databases

MaxQBiP32485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR113W.
SGDiS000004103. HOG1.

Phylogenomic databases

GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiP32485.
KOiK04441.
OMAiLSHEYLA.
OrthoDBiEOG092C2FL8.

Enzyme and pathway databases

BioCyciYEAST:G3O-32258-MONOMER.
BRENDAi2.7.11.24. 984.
ReactomeiR-SCE-168638. NOD1/2 Signaling Pathway.
R-SCE-171007. p38MAPK events.
R-SCE-193648. NRAGE signals death through JNK.
R-SCE-198753. ERK/MAPK targets.
R-SCE-2559580. Oxidative Stress Induced Senescence.
R-SCE-2871796. FCERI mediated MAPK activation.
R-SCE-375170. CDO in myogenesis.
R-SCE-418592. ADP signalling through P2Y purinoceptor 1.
R-SCE-4420097. VEGFA-VEGFR2 Pathway.
R-SCE-450302. activated TAK1 mediates p38 MAPK activation.
R-SCE-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.

Miscellaneous databases

PROiP32485.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 171 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.