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Q92207 (HOG1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase HOG1

Short name=MAP kinase HOG1
EC=2.7.11.24
Gene names
Name:HOG1
ORF Names:CaO19.8514, CaO19.895
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence 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 of target genes. Regulates stress-induced production and accumulation of glycerol and D-arabitol. HOG1 is also involved in virulence, morphogenesis and oxidative stress response especially through its role in chlamydospore formation, an oxygen-dependent morphogenetic program. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation By similarity.

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation. Ref.6 Ref.7 Ref.12

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 By similarity. Phosphorylated in response to oxidative and salt stress. Ref.4 Ref.5 Ref.6 Ref.8 Ref.12

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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-mediated signaling

Inferred from genetic interaction PubMed 15813744. Source: CGD

cellular response to cadmium ion

Inferred from mutant phenotype Ref.11. Source: CGD

cellular response to drug

Inferred from mutant phenotype PubMed 15813744. Source: CGD

cellular response to heat

Inferred from mutant phenotype Ref.10PubMed 17804815. Source: CGD

cellular response to osmotic stress

Inferred from mutant phenotype Ref.4Ref.7Ref.11Ref.10PubMed 17804815Ref.1. Source: CGD

cellular response to oxidative stress

Inferred from mutant phenotype Ref.7Ref.9Ref.11Ref.10PubMed 16939537PubMed 17804815PubMed 19759180. Source: CGD

cellular response to pH

Inferred from mutant phenotype Ref.10. Source: CGD

chlamydospore formation

Inferred from mutant phenotype Ref.4Ref.10. Source: CGD

filamentous growth

Inferred from mutant phenotype Ref.3Ref.7PubMed 17182857. Source: CGD

filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype Ref.3. Source: CGD

filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype Ref.3. Source: CGD

filamentous growth of a population of unicellular organisms in response to chemical stimulus

Inferred from mutant phenotype PubMed 17182857. Source: CGD

filamentous growth of a population of unicellular organisms in response to heat

Inferred from mutant phenotype Ref.10. Source: CGD

fungal-type cell wall organization

Inferred from mutant phenotype Ref.7Ref.10. Source: CGD

intracellular accumulation of glycerol

Inferred from mutant phenotype Ref.9. Source: CGD

negative regulation of filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype Ref.3. Source: CGD

negative regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype Ref.3Ref.10. Source: CGD

negative regulation of filamentous growth of a population of unicellular organisms in response to heat

Inferred from mutant phenotype Ref.10. Source: CGD

pathogenesis

Inferred from mutant phenotype Ref.3PubMed 16939537. Source: CGD

polyol biosynthetic process

Inferred from mutant phenotype Ref.9. Source: CGD

positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus

Inferred from mutant phenotype PubMed 17182857. Source: CGD

protein phosphorylation

Inferred from direct assay PubMed 12075460Ref.6. Source: CGD

regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype Ref.10. Source: CGD

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to salt stress

Inferred from mutant phenotype PubMed 23261427. Source: CGD

stress-activated MAPK cascade

Inferred from direct assay Ref.6. Source: CGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6Ref.7. Source: CGD

nucleus

Inferred from direct assay Ref.6Ref.7. Source: CGD

protein kinase CK2 complex

Inferred from sequence or structural similarity PubMed 15813744. Source: CGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from direct assay PubMed 12075460. Source: CGD

protein kinase activity

Inferred from direct assay Ref.6. Source: CGD

protein serine/threonine kinase activity

Inferred from sequence or structural similarity PubMed 15813744. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Mitogen-activated protein kinase HOG1
PRO_0000186328

Regions

Domain23 – 305283Protein kinase
Nucleotide binding29 – 379ATP By similarity
Motif174 – 1763TXY

Sites

Active site1441Proton acceptor By similarity
Binding site521ATP By similarity

Amino acid modifications

Modified residue1741Phosphothreonine By similarity
Modified residue1761Phosphotyrosine By similarity

Experimental info

Sequence conflict2981E → Q in CAA62214. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q92207 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: 8DB21BD497A4F52E

FASTA37742,947
        10         20         30         40         50         60 
MSADGEFTRT QIFGTVFEIT NRYTELNPVG MGAFGLVCSA VDRLTGQNVA VKKVMKPFST 

        70         80         90        100        110        120 
SVLAKRTYRE LKLLKHLKHE NLITLDDIFI SPLEDIYFVN ELQGTDLHRL LNSRPLEKQF 

       130        140        150        160        170        180 
IQYFTYQIMR GLKYIHSAGV IHRDLKPSNI LINENCDLKI CDFGLARLQD PQMTGYVSTR 

       190        200        210        220        230        240 
YYRAPEIMLT WQKYDTEVDL WSVGCILAEM IEGKPLFPGK DHVHQFSIIT ELLGSPPADV 

       250        260        270        280        290        300 
IDTICSENTL RFVQSLPHRD PIPFSERFAS CTHVEPEAID LLAKLLVFDP KKRISAVEGL 

       310        320        330        340        350        360 
THPYMEAYHD PTDEPVCESK FDWSFNDADL PVDTWRVMMY SEILDFHQTV GVANETEGSE 

       370 
QPDSQVEQNN LDSANGA 

« Hide

References

« Hide 'large scale' references
[1]"The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans."
San Jose C., Monge R.A., Perez-Diaz R., Pla J., Nombela C.
J. Bacteriol. 178:5850-5852(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 64385 / 1001.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[3]"Role of the mitogen-activated protein kinase Hog1p in morphogenesis and virulence of Candida albicans."
Alonso-Monge R., Navarro-Garcia F., Molero G., Diez-Orejas R., Gustin M.C., Pla J., Sanchez M., Nombela C.
J. Bacteriol. 181:3058-3068(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The Hog1 mitogen-activated protein kinase is essential in the oxidative stress response and chlamydospore formation in Candida albicans."
Alonso-Monge R., Navarro-Garcia F., Roman E., Negredo A.I., Eisman B., Nombela C., Pla J.
Eukaryot. Cell 2:351-361(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[5]"Candida albicans response regulator gene SSK1 regulates a subset of genes whose functions are associated with cell wall biosynthesis and adaptation to oxidative stress."
Chauhan N., Inglis D., Roman E., Pla J., Li D., Calera J.A., Calderone R.
Eukaryot. Cell 2:1018-1024(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[6]"A conserved stress-activated protein kinase regulates a core stress response in the human pathogen Candida albicans."
Smith D.A., Nicholls S., Morgan B.A., Brown A.J.P., Quinn J.
Mol. Biol. Cell 15:4179-4190(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]"The Pbs2 MAP kinase kinase is essential for the oxidative-stress response in the fungal pathogen Candida albicans."
Arana D.M., Nombela C., Alonso-Monge R., Pla J.
Microbiology 151:1033-1049(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"The MAP kinase Mkc1p is activated under different stress conditions in Candida albicans."
Navarro-Garcia F., Eisman B., Fiuza S.M., Nombela C., Pla J.
Microbiology 151:2737-2749(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[9]"The MAP kinase Hog1p differentially regulates stress-induced production and accumulation of glycerol and D-arabitol in Candida albicans."
Kayingo G., Wong B.
Microbiology 151:2987-2999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The Cek1 and Hog1 mitogen-activated protein kinases play complementary roles in cell wall biogenesis and chlamydospore formation in the fungal pathogen Candida albicans."
Eisman B., Alonso-Monge R., Roman E., Arana D.M., Nombela C., Pla J.
Eukaryot. Cell 5:347-358(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Role of the Hog1 stress-activated protein kinase in the global transcriptional response to stress in the fungal pathogen Candida albicans."
Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P., Quinn J.
Mol. Biol. Cell 17:1018-1032(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Functional studies of the Ssk1p response regulator protein of Candida albicans as determined by phenotypic analysis of receiver domain point mutants."
Menon V., Li D., Chauhan N., Rajnarayanan R., Dubrovska A., West A.H., Calderone R.
Mol. Microbiol. 62:997-1013(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X90586 Genomic DNA. Translation: CAA62214.1.
AACQ01000018 Genomic DNA. Translation: EAL02326.1.
AACQ01000019 Genomic DNA. Translation: EAL02199.1.
RefSeqXP_721016.1. XM_715923.1.
XP_721137.1. XM_716044.1.

3D structure databases

ProteinModelPortalQ92207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1220487. 2 interactions.
STRING5476.CAL0002931.

Proteomic databases

PRIDEQ92207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3637270.
3637393.
KEGGcal:CaO19.8514.
cal:CaO19.895.

Organism-specific databases

CGDCAL0002931. HOG1.

Phylogenomic databases

eggNOGCOG0515.
KOK04441.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BRENDA2.7.11.24. 1096.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHOG1_CANAL
AccessionPrimary (citable) accession number: Q92207
Secondary accession number(s): Q5AHA1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Candida albicans

Candida albicans: entries and gene names