Version 5.4
Mus musculus Protein: Dak
Summary
InnateDB Protein IDBP-144463.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Dak
Protein Name dihydroxyacetone kinase 2 homolog (yeast)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000044556
InnateDB Gene IDBG-144461 (Dak)
Protein Structure
UniProt Annotation
Function Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 4 experimentally validated interaction(s) in this database.
They are also associated with 8 interaction(s) predicted by orthology.
Experimentally validated
Total 4 [view]
Protein-Protein 4 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 8 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004371 glycerone kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0034012 FAD-AMP lyase (cyclizing) activity
GO:0046872 metal ion binding
GO:0050354 triokinase activity
Biological Process
GO:0006071 glycerol metabolic process
GO:0016310 phosphorylation
GO:0044262 cellular carbohydrate metabolic process
GO:0045088 regulation of innate immune response
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005634 nucleus
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:2385084
InterPro IPR004006 Dak kinase
IPR004007 DhaL domain
IPR012734 Dihydroxyacetone kinase
PFAM PF02733
PF02734
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8VC30
PhosphoSite PhosphoSite-Q8VC30
TrEMBL
UniProt Splice Variant
Entrez Gene 225913
UniGene
RefSeq NP_663471
MGI ID
MGI Symbol Dak
OMIM
CCDS CCDS37914
HPRD
IMGT
EMBL BC021917
GenPept AAH21917

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca