CPLM-005321

Genbank Nucleotide ID

Acetyl-CoA acetyltransferase, mitochondrial

Protein Synonyms/Alias

Acetoacetyl-CoA thiolase; T2

Homo sapiens (Human)

Position	Peptide	Type	References
83	IEKAGIPKEEVKEAY	acetylation	[1]
87	GIPKEEVKEAYMGNV	ubiquitination	[2]
174	STPYGGVKLEDLIVK	acetylation	[1, 3]
174	STPYGGVKLEDLIVK	ubiquitination	[4, 5]
181	KLEDLIVKDGLTDVY	acetylation	[1]
181	KLEDLIVKDGLTDVY	ubiquitination	[2, 4, 5, 6]
190	GLTDVYNKIHMGSCA	acetylation	[1, 7]
202	SCAENTAKKLNIARN	acetylation	[1]
230	KAAWEAGKFGNEVIP	ubiquitination	[2]
251	GQPDVVVKEDEEYKR	acetylation	[1, 7, 8]
263	YKRVDFSKVPKLKTV	acetylation	[1, 7, 8, 9]
263	YKRVDFSKVPKLKTV	ubiquitination	[2, 10]
302	LMTADAAKRLNVTPL	ubiquitination	[2]

[1] 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]
[2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[3] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[4] 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]
[5] 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]
[6] 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]
[7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[10] 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]

Functional Description

Plays a major role in ketone body metabolism.

REGION 258 260 Coenzyme A binding.
ACT_SITE 126 126 Acyl-thioester intermediate (Probable).
ACT_SITE 385 385 Proton acceptor (Probable).
ACT_SITE 413 413 Proton acceptor (Probable).
METAL 219 219 Potassium.
METAL 280 280 Potassium; via carbonyl oxygen.
METAL 281 281 Potassium; via carbonyl oxygen.
METAL 283 283 Potassium; via carbonyl oxygen.
METAL 381 381 Potassium; via carbonyl oxygen.
BINDING 219 219 Coenzyme A.
BINDING 263 263 Coenzyme A.
BINDING 284 284 Coenzyme A.
MOD_RES 174 174 N6-acetyllysine.
MOD_RES 181 181 N6-acetyllysine.
MOD_RES 190 190 N6-acetyllysine (By similarity).
MOD_RES 230 230 N6-acetyllysine (By similarity).
MOD_RES 251 251 N6-acetyllysine.
MOD_RES 263 263 N6-acetyllysine.
MOD_RES 338 338 N6-acetyllysine (By similarity).

3D-structure; Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Disease mutation; Metal-binding; Mitochondrion; Polymorphism; Potassium; Reference proteome; Transferase; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO:0003985; F:acetyl-CoA C-acetyltransferase activity; EXP:Reactome.
GO:0050662; F:coenzyme binding; IEA:Compara.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0060612; P:adipose tissue development; IEA:Compara.
GO:0007420; P:brain development; IEA:Compara.
GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO:0046951; P:ketone body biosynthetic process; TAS:Reactome.
GO:0046952; P:ketone body catabolic process; TAS:Reactome.
GO:0001889; P:liver development; IEA:Compara.
GO:0072229; P:metanephric proximal convoluted tubule development; IEA:Compara.
GO:0051260; P:protein homooligomerization; IEA:Compara.
GO:0009725; P:response to hormone stimulus; IEA:Compara.
GO:0014070; P:response to organic cyclic compound; IEA:Compara.
GO:0042594; P:response to starvation; IEA:Compara.

IPR002155; Thiolase.
IPR016039; Thiolase-like.
IPR016038; Thiolase-like_subgr.
IPR020615; Thiolase_acyl_enz_int_AS.
IPR020610; Thiolase_AS.
IPR020617; Thiolase_C.
IPR020613; Thiolase_CS.
IPR020616; Thiolase_N.

PF02803; Thiolase_C
PF00108; Thiolase_N

PS00098; THIOLASE_1
PS00737; THIOLASE_2
PS00099; THIOLASE_3