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Q875L0 (HOG1_CRYPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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
OrganismCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifier5116 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Protein attributes

Sequence length358 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 By similarity. Involved in the virulence and conidia formation. Mediates tannic acid-induced laccase expression and cryparin expression. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation By similarity. Hypoviruses like CHV1-EP713 induce inactivation by lowering the degree of phosphorylation in response to various environmental stresses. Ref.1

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Domain

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

Post-translational modification

Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme By similarity. Phosphorylated in response of osmotic stress. Ref.1

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Mitogen-activated protein kinase HOG1
PRO_0000289686

Regions

Domain20 – 299280Protein kinase
Nucleotide binding26 – 349ATP By similarity
Motif171 – 1733TXY

Sites

Active site1411Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1711Phosphothreonine By similarity
Modified residue1731Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q875L0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D4B52064CF00B7C3

FASTA35840,945
        10         20         30         40         50         60 
MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAIKK IMKPFSTPVL 

        70         80         90        100        110        120 
AKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY 

       130        140        150        160        170        180 
FLYQIMRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR 

       190        200        210        220        230        240 
APEIMLTWQK YDVEVDIWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVINT 

       250        260        270        280        290        300 
IASENTLRFV KSLPKRERQP LASKFKNADE QAVDLLERML VFDPKKRITA SDALAHEYLA 

       310        320        330        340        350 
PYHDPTDEPV AEEKFDWSFN DADLPVDTWK IMMYSEILDY HNVDASGASA AMGEFNGQ 

« Hide

References

[1]"Characterization of HOG1 homologue, CpMK1, from Cryphonectria parasitica and evidence for hypovirus-mediated perturbation of its phosphorylation in response to hypertonic stress."
Park S.-M., Choi E.-S., Kim M.-J., Cha B.-J., Yang M.-S., Kim D.-H.
Mol. Microbiol. 51:1267-1277(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, ENZYME REGULATION.
Strain: ATCC 38755 / EP155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY166687 Genomic DNA. Translation: AAO27796.1.

3D structure databases

ProteinModelPortalQ875L0.
SMRQ875L0. Positions 3-343.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ875L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAPDDVIHT.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01773. P38MAPKINASE.
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_CRYPA
AccessionPrimary (citable) accession number: Q875L0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 67 of the entry and version 1 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