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Q56R42 (HOG1_CRYNH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length365 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. Also involved in response to UV radiations, heat stress and oxidative stress. Mediates the sensitivity to fludioxonil, an agricultural fungicide. Ref.1 Ref.3 Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by dephosphorylation after osmotic stress or in presence of the fludioxonil fungicide.

Subcellular location

Cytoplasm. Nucleus. Note: Concentration into the nucleus in response to hyperosmotic conditions is transient and moderate. Ref.1

Domain

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

Post-translational modification

Contrary to what happens in most fungi, is constitutively phosphorylated during non-stress conditions and dephosphorylated after osmotic stress or in presence of the fludioxonil fungicide. Ref.1 Ref.3 Ref.4

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 – 365365Mitogen-activated protein kinase HOG1
PRO_0000289685

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

Experimental info

Mutagenesis491K → S: Confers resistance to fludioxonil; when associated with N-50. Ref.3
Mutagenesis501K → N: Confers resistance to fludioxonil; when associated with S-49. Ref.3
Mutagenesis1711T → A: Confers resistance to fludioxonil; when associated with A-173. Ref.3
Mutagenesis1731Y → A: Confers resistance to fludioxonil; when associated with A-171. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q56R42 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: F28E2E95B6DAD6B5

FASTA36541,213
        10         20         30         40         50         60 
MADFVKLSIF GTVFEVTTRY VDLQPVGMGA FGLVCSAKDQ LSGTSVAIKK IMKPFSTPVL 

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

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

       190        200        210        220        230        240 
APEIMLTWQK YDVAVDIWST GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVIQT 

       250        260        270        280        290        300 
IASENTLRFV QSLPKREKVP FSTKFPNADP VSLDLLEKML VFDPRTRISA AEGLAHEYLA 

       310        320        330        340        350        360 
PYHDPTDEPV AAEVFDWSFN DADLPVDTWK VMMYSEILDF HNLGDISQNE AEGPVTGEVP 


AAPAS 

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References

« Hide 'large scale' references
[1]"Specialization of the HOG pathway and its impact on differentiation and virulence of Cryptococcus neoformans."
Bahn Y.-S., Kojima K., Cox G.M., Heitman J.
Mol. Biol. Cell 16:2285-2300(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487.
[2]"Analysis of the genome and transcriptome of Cryptococcus neoformans var. grubii reveals complex RNA expression and microevolution leading to virulence attenuation."
Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V., Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F., Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A., Gaillardin C., Gerik K.J. expand/collapse author list , Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A., Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A., Cuomo C.A., Dietrich F.S.
PLoS Genet. 10:E1004261-E1004261(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487.
[3]"Calcineurin, Mpk1 and Hog1 MAPK pathways independently control fludioxonil antifungal sensitivity in Cryptococcus neoformans."
Kojima K., Bahn Y.-S., Heitman J.
Microbiology 152:591-604(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF LYS-49; LYS-50; THR-171 AND TYR-173.
[4]"A unique fungal two-component system regulates stress responses, drug sensitivity, sexual development, and virulence of Cryptococcus neoformans."
Bahn Y.-S., Kojima K., Cox G.M., Heitman J.
Mol. Biol. Cell 17:3122-3135(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY775548 Genomic DNA. Translation: AAX08139.1.
CP003830 Genomic DNA. Translation: AFR97728.1.

3D structure databases

ProteinModelPortalQ56R42.
SMRQ56R42. Positions 3-342.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG7K3TWD.

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_CRYNH
AccessionPrimary (citable) accession number: Q56R42
Secondary accession number(s): J9VTY4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 10, 2005
Last modified: June 11, 2014
This is version 61 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