Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4WSF6 (HOG1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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
Synonyms:hogA, osm1, sakA
ORF Names:AfA5C11.10, AFUA_1G12940
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length366 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. Ref.3

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 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. 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.

Sequence caution

The sequence CAF32009.1 differs from that shown. Reason: Erroneous gene model prediction.

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_processcellular heat acclimation

Inferred from mutant phenotype PubMed 19715768. Source: ASPGD

cellular hyperosmotic response

Inferred from mutant phenotype PubMed 16998074. Source: ASPGD

cellular response to alkalinity

Inferred from mutant phenotype PubMed 22220813. Source: ASPGD

cellular response to drug

Inferred from mutant phenotype PubMed 17981060PubMed 22220813PubMed 22438852. Source: ASPGD

cellular response to heat

Inferred from mutant phenotype PubMed 22220813PubMed 22678624. Source: ASPGD

cellular response to osmotic stress

Inferred from mutant phenotype PubMed 16998074. Source: ASPGD

cellular response to oxidative stress

Inferred from mutant phenotype Ref.3. Source: ASPGD

fungal-type cell wall organization or biogenesis

Inferred from mutant phenotype PubMed 17981060. Source: ASPGD

hyphal growth

Inferred from mutant phenotype PubMed 17981060PubMed 19715768. Source: ASPGD

regulation of melanin biosynthetic process

Inferred from mutant phenotype PubMed 19715768. Source: ASPGD

regulation 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 – 366366Mitogen-activated protein kinase hog1
PRO_0000289674

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

Sequence conflict21 – 222TD → N in CAD28436. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q4WSF6 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 45B8F9234DAD334A

FASTA36641,960
        10         20         30         40         50         60 
MAEFVRAQIF GTTFEITSRY TDLQPVGMGA FGLVCSARDQ LTGQPVAVKK IMKPFSTPVL 

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

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

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

       250        260        270        280        290        300 
ICSENTLRFV KSLPKRERQP LANKFKNADP EAVDLLERML VFDPKKRIRA GEALAHEYLS 

       310        320        330        340        350        360 
PYHDPTDEPE AEEKFDWSFN DADLPVDTWK IMMYSEILDF HNIDQGNDAG QVLMEGGVAQ 


AQQNYA 

« Hide

References

« Hide 'large scale' references
[1]"Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb region encompassing the nitrate assimilation gene cluster."
Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M., Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S., O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A., Salzberg S.L. expand/collapse author list , Saunders D., Seeger K., Sharp S., Warren T., Denning D.W., Barrell B.G., Hall N.
Fungal Genet. Biol. 41:443-453(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[3]"The role of the sakA (Hog1) and tcsB (sln1) genes in the oxidant adaptation of Aspergillus fumigatus."
Du C., Sarfati J., Latge J.-P., Calderone R.
Med. Mycol. 44:211-218(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL713629 Genomic DNA. Translation: CAD28436.1.
BX649606 Genomic DNA. Translation: CAF32009.1. Sequence problems.
AAHF01000004 Genomic DNA. Translation: EAL90626.1.
RefSeqXP_752664.1. XM_747571.1.

3D structure databases

ProteinModelPortalQ4WSF6.
SMRQ4WSF6. Positions 3-342.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00006975; CADAFUAP00006975; CADAFUAG00006975.
GeneID3510276.
KEGGafm:AFUA_1G12940.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04441.
OMAPDDVIHT.
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_ASPFU
AccessionPrimary (citable) accession number: Q4WSF6
Secondary accession number(s): Q6MYJ4, Q8TFX5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 5, 2005
Last modified: May 14, 2014
This is version 81 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