Version 5.4
Bos taurus Protein: ACLY
Summary
InnateDB Protein IDBP-692300.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ACLY
Protein Name ATP-citrate synthase
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000022258
InnateDB Gene IDBG-640080 (ACLY)
Protein Structure
UniProt Annotation
Function ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}.
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 24 interaction(s) predicted by orthology.
Predicted by orthology
Total 24 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003878 ATP citrate synthase activity
GO:0004775 succinate-CoA ligase (ADP-forming) activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0046912 transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
GO:0048037 cofactor binding
Biological Process
GO:0006629 lipid metabolic process
GO:0008152 metabolic process
GO:0008610 lipid biosynthetic process
GO:0044262 cellular carbohydrate metabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR002020 Citrate synthase-like
IPR003781 CoA-binding
IPR005811 ATP-citrate lyase/succinyl-CoA ligase
IPR013650 ATP-grasp fold, succinyl-CoA synthetase-type
IPR014608 ATP-citrate synthase
IPR016102 Succinyl-CoA synthetase-like
IPR016141 Citrate synthase-like, core
PFAM PF00285
PF02629
PF13380
PF00549
PF08442
PRINTS PR00143
PIRSF PIRSF036511
SMART SM00881
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q32PF2
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 511135
UniGene Bt.41387
RefSeq NP_001032534
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC108138
GenPept AAI08139

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