Version 5.4
Mus musculus Protein: Acsf2
Summary
InnateDB Protein IDBP-209108.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Acsf2
Protein Name acyl-CoA synthetase family member 2
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000099453
InnateDB Gene IDBG-209106 (Acsf2)
Protein Structure
UniProt Annotation
Function Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation. {ECO:0000269PubMed:17762044}.
Subcellular Localization Mitochondrion {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 7 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 7 [view]
Protein-Protein 6 [view]
Protein-DNA 0
Protein-RNA 1 [view]
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0008150 biological_process
GO:0008152 metabolic process
Cellular Component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:2388287
InterPro IPR000873 AMP-dependent synthetase/ligase
PFAM PF00501
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8VCW8
PhosphoSite PhosphoSite-Q8VCW8
TrEMBL
UniProt Splice Variant
Entrez Gene 264895
UniGene Mm.386885
RefSeq NP_722502
MGI ID
MGI Symbol Acsf2
OMIM
CCDS CCDS25259
HPRD
IMGT
EMBL AK034209 AK153582 AK169987 AL645764 AL645809 BC018371 BC063269
GenPept AAH18371 AAH63269 BAC28632 BAE32109 BAE41499 CAI24962 CAI25585

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