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Q9P419 (HOG1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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, sakA
ORF Names:AN1017
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length379 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.2 Ref.5

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. Phosphorylated by pbsB in response to osmotic and oxidative stresses. Ref.2 Ref.5

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_processMAPK cascade

Inferred from sequence alignment PubMed 11918796. Source: GOC

cellular hyperosmotic response

Inferred from mutant phenotype PubMed 11918796. Source: ASPGD

cellular response to oxidative stress

Inferred from direct assay Ref.2. Source: ASPGD

establishment or maintenance of cell polarity

Inferred from mutant phenotype PubMed 11918796. Source: ASPGD

hyperosmotic response

Inferred from sequence alignment PubMed 11918796. Source: ASPGD

osmosensory signaling pathway

Inferred from mutant phenotype PubMed 19596074. Source: ASPGD

protein phosphorylation

Inferred from sequence alignment PubMed 11918796. 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 direct assay PubMed 17617716PubMed 21320182. Source: ASPGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from sequence alignment PubMed 11918796. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Mitogen-activated protein kinase hog1
PRO_0000289687

Regions

Domain20 – 313294Protein 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 conflict1321V → C in AAF81523. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9P419 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 93DB6A450ECAB8E5

FASTA37943,183
        10         20         30         40         50         60 
MAEFVRAQIF GTTFEITSRY TDLQPVGMGA FGLVCSARDQ LTAQPVAVKK IMKPFSTPVL 

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

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

       190        200        210        220        230        240 
APEIMLTWQK YDAKVDVWSA ACIFAEMLLG APLFPGKDHV NQFSIITELL GTPPDDVIQT 

       250        260        270        280        290        300 
ICSENTLRFV KSLPKREPQD LAKLPKFLAL VHPDKKPEED EDYKNTINLL KAMLVYNPKD 

       310        320        330        340        350        360 
RISAEAALAA PYLAPYHDET DEPVAEEKFD WSFNDADLPV DTWKIMMYSE ILDFHNIDQG 

       370 
GDINPALVEG AGLNQQGFQ 

« Hide

References

« Hide 'large scale' references
[1]"The Aspergillus nidulans hogA MAP kinase gene, homologous to the yeast HOG1 gene, is regulated by salt stress."
Han K., Prade R.A.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"SakA MAP kinase is involved in stress signal transduction, sexual development and spore viability in Aspergillus nidulans."
Kawasaki L., Sanchez O., Shiozaki K., Aguirre J.
Mol. Microbiol. 45:1153-1163(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION.
[3]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[5]"Aspergillus nidulans HOG pathway is activated only by two-component signalling pathway in response to osmotic stress."
Furukawa K., Hoshi Y., Maeda T., Nakajima T., Abe K.
Mol. Microbiol. 56:1246-1261(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF270498 Genomic DNA. Translation: AAF81523.1.
AF282891 Genomic DNA. Translation: AAF97243.1.
AACD01000015 Genomic DNA. Translation: EAA65585.1.
BN001308 Genomic DNA. Translation: CBF88327.1.
RefSeqXP_658621.1. XM_653529.1.

3D structure databases

ProteinModelPortalQ9P419.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9P419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001630; CADANIAP00001630; CADANIAG00001630.
GeneID2876793.
KEGGani:AN1017.2.

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_EMENI
AccessionPrimary (citable) accession number: Q9P419
Secondary accession number(s): C8VU47, Q5BEL3, Q9P454
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 93 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