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Q9HG11 (MPKC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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 mpkC

Short name=MAP kinase C
EC=2.7.11.24
Gene names
Name:mpkC
ORF Names:AN4668
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 length415 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mitogen-activated protein kinase required for growth on media where sorbitol or mannitol is the sole carbon source By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation 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.

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 CBF77037.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA60710.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from sequence alignment PubMed 15882418. Source: GOC

ascospore formation

Inferred from mutant phenotype PubMed 21717328. Source: ASPGD

cellular response to osmotic stress

Inferred from mutant phenotype PubMed 10220889. Source: ASPGD

establishment of cell polarity

Inferred from mutant phenotype PubMed 23516554. Source: ASPGD

establishment or maintenance of cell polarity

Inferred from mutant phenotype PubMed 10220889. Source: ASPGD

hyperosmotic response

Inferred from sequence alignment PubMed 15882418. Source: ASPGD

osmosensory signaling pathway

Inferred from sequence alignment PubMed 15882418. Source: ASPGD

penicillin biosynthetic process

Inferred from mutant phenotype PubMed 18378656. Source: ASPGD

positive regulation of ascospore formation

Inferred from mutant phenotype PubMed 21717328. Source: ASPGD

positive regulation of penicillin metabolic process

Inferred from mutant phenotype PubMed 18378656. Source: ASPGD

positive regulation of sterigmatocystin biosynthetic process

Inferred from mutant phenotype PubMed 18378656. Source: ASPGD

protein phosphorylation

Inferred from sequence alignment PubMed 15882418. Source: ASPGD

regulation of ascospore formation

Inferred from mutant phenotype PubMed 23516554. Source: ASPGD

regulation of cleistothecium development

Inferred from mutant phenotype PubMed 23516554. Source: ASPGD

regulation of conidiophore development

Inferred from mutant phenotype PubMed 23516554. Source: ASPGD

regulation of secondary metabolite biosynthetic process

Inferred from mutant phenotype PubMed 18378656PubMed 22829779. Source: ASPGD

sexual sporulation

Inferred from mutant phenotype PubMed 17669651. Source: ASPGD

spore germination

Inferred from mutant phenotype PubMed 10220889. Source: ASPGD

sporocarp development involved in sexual reproduction

Inferred from mutant phenotype PubMed 21717328PubMed 22829779. Source: ASPGD

sterigmatocystin biosynthetic process

Inferred from mutant phenotype PubMed 18378656. Source: ASPGD

tube fusion

Inferred from mutant phenotype PubMed 21717328. Source: ASPGD

   Cellular_componenthyphal tip

Inferred from direct assay PubMed 22829779. Source: ASPGD

nuclear envelope

Inferred from direct assay PubMed 22829779. Source: ASPGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from sequence alignment PubMed 15882418. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Mitogen-activated protein kinase mpkC
PRO_0000289717

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
Q9HG11 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 9EB7A07F88F66FF8

FASTA41546,990
        10         20         30         40         50         60 
MAEFIRSDIL GTTFETTSRY ANLQPVGLGT AGVVCSAYDL ISEQVVAIKK MMKPFHSTSV 

        70         80         90        100        110        120 
AKRTYREVKL LRHLRHDNLI NMSDIFISPL EDVYLVTELL GTDLHRLLNG KPLESKFAQY 

       130        140        150        160        170        180 
FTYQILRGLK YIHSAGVIHR DLKPGNLLIN ENCDLKICDF GLARVQEPQM TGYVSTRYYR 

       190        200        210        220        230        240 
APEIMLTWQR YGSKVDLWSV GCILAEMLLG RPLFPGTDHI NQFWLITDLL GNPPDEVIDR 

       250        260        270        280        290        300 
ITTNNTRRVV KSMAKRNPRP LKEILPAAED AALNLLDNLL VFDPDRRISA EQGLMHPWMA 

       310        320        330        340        350        360 
PYHDPTDEPV ATEQFDWSFN DADLPLDTWK IMIYSEVLDF FQLTTNAEPS GEQSQNQSQS 

       370        380        390        400        410 
QSQAFTSSQD LQLASMLNLG EGELLPDFAA TIDPNKFGSV DYLMDGQSLD PNSFS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a gene encoding a MAPK homolog from Aspergillus nidulans."
Jahng K.-Y., Lee S.-J., Park H.-J., Chae K.-S., Han D.M.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"Isolation of a gene encoding a MAPK homolog from Aspergillus nidulans."
Im Y.-E., Lee S.-J., Jahng K.-Y.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Novel mitogen-activated protein kinase MpkC of Aspergillus fumigatus is required for utilization of polyalcohol sugars."
Reyes G., Romans A., Nguyen C.K., May G.S.
Eukaryot. Cell 5:1934-1940(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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.
[5]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF195773 Genomic DNA. Translation: AAG28463.2.
EF137429 mRNA. Translation: ABL85065.1.
DQ402476 mRNA. Translation: ABD64614.1.
AACD01000080 Genomic DNA. Translation: EAA60710.1. Sequence problems.
BN001303 Genomic DNA. Translation: CBF77037.1. Sequence problems.
RefSeqXP_662272.1. XM_657180.1.

3D structure databases

ProteinModelPortalQ9HG11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00005765.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00005765; CADANIAP00005765; CADANIAG00005765.
GeneID2872468.
KEGGani:AN4668.2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04441.
OrthoDBEOG7K3TWD.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
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.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPKC_EMENI
AccessionPrimary (citable) accession number: Q9HG11
Secondary accession number(s): C8VB11, Q208R0, Q5B462
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 86 of the entry and version 2 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