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Q9UV50 (HOG1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names:DEHA2E20944g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces

Protein attributes

Sequence length387 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. Ref.1 Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation.

Subcellular location

Cytoplasm. Nucleus. Note: In contrast to other yeasts, the nuclear translocation is delayed under severe osmotic conditions although it is activated rapidly. Ref.3

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 of osmotic stress, oxidative stress and UV stress, but not heat stress. Ref.3

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
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Mitogen-activated protein kinase HOG1
PRO_0000186330

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 conflict2721S → T in AAF24231. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UV50 [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: 710908EC58AA0828

FASTA38744,357
        10         20         30         40         50         60 
MVSDGEFTRT QIFGTVFEIT NRYTDLNPVG MGAFGLVCSA IDKLTGQNVA VKKIMKPFST 

        70         80         90        100        110        120 
SVLAKRTYRE LKLLKHLRHE NLITLDDIFL SPLEDIYFVT ELQGTDLHRL LTSRPLEKQF 

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

       190        200        210        220        230        240 
YYRAPEIMLT WQKYDTEVDL WSVGCILSEM IEGKPLFPGK DHVHQFSIIT ELLGSPPPDV 

       250        260        270        280        290        300 
IETICSENTL RFVQSLPHRD PIPFSERFAQ CSHVEPEAID LLAKMLIFDP KKRISALDAL 

       310        320        330        340        350        360 
SHPYMEPYHD PTDEPVCEVK FDWSFNDADL PVDTWRVMMY SEILDFHQII GAGANGTTQE 

       370        380 
QMAQIQQEGI QAPSSQYQQT NQEQKVE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence of the HOG1 homolog from Debaryomyces hansenii by complementation of hog1 Delta strain of Saccharomyces cerevisiae."
Bansal P.K., Mondal A.K.
Yeast 16:81-88(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: MTCC 234.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.
[3]"Debaryomyces hansenii, a highly osmo-tolerant and halo-tolerant yeast, maintains activated Dhog1p in the cytoplasm during its growth under severe osmotic stress."
Sharma P., Meena N., Aggarwal M., Mondal A.K.
Curr. Genet. 48:162-170(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF185278 Genomic DNA. Translation: AAF24231.2.
CR382137 Genomic DNA. Translation: CAG88486.2.
RefSeqXP_460213.2. XM_460213.1.

3D structure databases

ProteinModelPortalQ9UV50.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9UV50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2902985.
KEGGdha:DEHA2E20944g.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04441.
OMAPDDVIHT.
OrthoDBEOG7K3TWD.

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_DEBHA
AccessionPrimary (citable) accession number: Q9UV50
Secondary accession number(s): Q6BNK7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 97 of the entry and version 3 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