UniProt Accession

 BACH_HUMAN; O00154; A8K0K7; A8K232; A8K6B8; A8K837; B3KQ12; O43703; Q53Y78; Q5JYL2; Q5JYL3; Q5JYL4; Q5JYL5; Q5JYL6; Q5TGR4; Q9UJM9; Q9Y539; Q9Y540 

Genbank Protein ID

 D88894; AB074415; AB074416; AB074417; AB074418; AB074419; U91316; BT006888; AK289572; AK290097; AK291583; AK292202; AK057168; AL031847; AL031848; AL031847; AL031848; AL031847; AL031848; AL031847; AL031848; AL031848; AL031847; AL031848; AL031847; AL031848; AL031847; AL031848; AL031847; CH471130; CH471130; CH471130; BC017365 

Genbank Nucleotide ID

 BAA24350.1; BAC20174.1; BAC20175.1; BAC20176.1; BAC20177.1; BAC20178.1; AAB61211.1; AAP35534.1; BAF82261.1; BAF82786.1; BAF84272.1; BAF84891.1; BAG51874.1; CAI19440.1; CAI19440.1; CAI19435.1; CAI19435.1; CAI19442.1; CAI19442.1; CAI19443.1; CAI19443.1; CAI19774.1; CAI19774.1; CAI19777.1; CAI19777.1; CAI19778.1; CAI19778.1; CAI19779.1; CAI19779.1; EAW71528.1; EAW71529.1; EAW71530.1; AAH17365.2 

Protein Name

 Cytosolic acyl coenzyme A thioester hydrolase 

Protein Synonyms/Alias

 Acyl-CoA thioesterase 7; Brain acyl-CoA hydrolase; BACH; CTE-IIa; CTE-II; Long chain acyl-CoA thioester hydrolase 

Gene Name

 ACOT7 

Gene Synonyms/Alias

 BACH 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
2	******MKLLARALR	ubiquitination	[1]
78	VHGGTILKMIEEAGA	acetylation	[2]
157	GAKKLTNKATLWYVP	ubiquitination	[3, 4]
168	WYVPLSLKNVDKVLE	acetylation	[2]
168	WYVPLSLKNVDKVLE	ubiquitination	[1, 3, 4, 5]
172	LSLKNVDKVLEVPPV	ubiquitination	[1, 6]
198	RKRYEAQKLERMETK	acetylation	[2]
198	RKRYEAQKLERMETK	ubiquitination	[1]
205	KLERMETKWRNGDIV	ubiquitination	[1]
267	IVAARHCKTNIVTAS	ubiquitination	[1]
283	DAINFHDKIRKGCVI	acetylation	[2]
283	DAINFHDKIRKGCVI	ubiquitination	[1, 3, 4]
286	NFHDKIRKGCVITIS	ubiquitination	[1]
321	PVVDSSQKRYRAASA	ubiquitination	[7]
369	KGRYLQMKAKRQGHA	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 

Functional Description

 Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA. 

Sequence Annotation

 DOMAIN 56 151 Acyl coenzyme A hydrolase 1.
 DOMAIN 242 319 Acyl coenzyme A hydrolase 2.
 ACT_SITE 66 66 By similarity.
 ACT_SITE 255 255 By similarity.
 MOD_RES 168 168 N6-acetyllysine.
 MOD_RES 198 198 N6-acetyllysine.
 MOD_RES 283 283 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion; Reference proteome; Repeat; Serine esterase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 380 AA 

Protein Sequence

Gene Ontology

 GO:0044297; C:cell body; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
 GO:0003824; F:catalytic activity; TAS:ProtInc.
 GO:0000062; F:fatty-acyl-CoA binding; TAS:ProtInc.
 GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:EC.
 GO:0009062; P:fatty acid catabolic process; IEA:Compara.
 GO:0006629; P:lipid metabolic process; TAS:ProtInc. 

Interpro

 IPR006683; Thioestr_supf. 

Pfam

 PF03061; 4HBT 

SMART

  

PROSITE

  

PRINTS