Version 5.4
Bos taurus Protein: SDHAF2
Summary
InnateDB Protein IDBP-696016.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol SDHAF2
Protein Name Succinate dehydrogenase assembly factor 2, mitochondrial
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000020305
InnateDB Gene IDBG-643460 (SDHAF2)
Protein Structure
UniProt Annotation
Function Required for insertion of FAD cofactor into SDHA, the catalytic subunit of succinate dehydrogenase (SDH). SDH is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). In is unclear whether it participates in the chemistry of FAD attachment (enzymatic function) or acts as a chaperone that maintains SDHA in a conformation that is susceptible to autocatalytic FAD attachment. {ECO:0000255HAMAP- Rule:MF_03057}.
Subcellular Localization Mitochondrion {ECO:0000255HAMAP- Rule:MF_03057}.
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 15 interaction(s) predicted by orthology.
Predicted by orthology
Total 15 [view]
Gene Ontology

Molecular Function
Accession GO Term
Biological Process
GO:0006121 mitochondrial electron transport, succinate to ubiquinone
GO:0018293 protein-FAD linkage
Cellular Component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID
InterPro IPR005631 Flavinator of succinate dehydrogenase
PFAM PF03937
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3ZBC2
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 767983
UniGene
RefSeq NP_001070513
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC103446
GenPept AAI03447

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) 

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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