Version 5.4
Bos taurus Protein: NDUFV3
Summary
InnateDB Protein IDBP-691749.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol NDUFV3
Protein Name NADH dehydrogenase
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000028645
InnateDB Gene IDBG-639569 (NDUFV3)
Protein Structure
UniProt Annotation
Function Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 5 interaction(s) predicted by orthology.
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
Biological Process
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005747 mitochondrial respiratory chain complex I
GO:0016020 membrane
GO:0070469 respiratory chain
Protein Structure and Domains
PDB ID
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P25712
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 327717
UniGene Bt.43863
RefSeq NP_787024
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC103274 X59048
GenPept AAI03275 CAA41775

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