Version 5.4
Homo sapiens Protein: CARKD
Summary
InnateDB Protein IDBP-373575.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CARKD
Protein Name carbohydrate kinase domain containing
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000413191
InnateDB Gene IDBG-235905 (CARKD)
Protein Structure
UniProt Annotation
Function Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. {ECO:0000255HAMAP-Rule:MF_03157}.
Subcellular Localization Mitochondrion {ECO:0000255HAMAP- Rule:MF_03157}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0005524 ATP binding
GO:0047453 ATP-dependent NAD(P)H-hydrate dehydratase activity
Biological Process
GO:0008150 biological_process
GO:0046496 nicotinamide nucleotide metabolic process
Cellular Component
GO:0005575 cellular_component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID
InterPro IPR000631 YjeF C-terminal domain
IPR029056 Ribokinase-like
PFAM PF01256
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8IW45
PhosphoSite PhosphoSite-Q8IW45
TrEMBL
UniProt Splice Variant
Entrez Gene 55739
UniGene Hs.408324
RefSeq NP_001229812
HUGO HGNC:25576
OMIM 615910
CCDS CCDS55903
HPRD 07698
IMGT
EMBL AK001631 AK024260 AK302117 AL139385 BC041028 CH471085
GenPept AAH41028 BAA91797 BAB14863 BAG63496 CAI17008 EAX09121 EAX09125

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