CPLM-017762

Genbank Nucleotide ID

Acetyl-CoA acetyltransferase, mitochondrial

Protein Synonyms/Alias

Acetoacetyl-CoA thiolase

Mus musculus (Mouse)

Position	Peptide	Type	References
33	LERSYASKPTLNEVV	acetylation	[1]
63	LASQPATKLGTAAIQ	acetylation	[1, 2, 3]
63	LASQPATKLGTAAIQ	succinylation	[3]
75	AIQGAIEKAGIPKEE	acetylation	[2, 3, 4, 5, 6, 7]
75	AIQGAIEKAGIPKEE	succinylation	[3]
80	IEKAGIPKEEVKEVY	acetylation	[1, 6, 7, 8]
84	GIPKEEVKEVYMGNV	acetylation	[6, 7]
84	GIPKEEVKEVYMGNV	ubiquitination	[9]
121	TPCTTVNKVCASGMK	acetylation	[5]
171	ATPYGGVKLEDLIVK	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 10, 11, 12]
171	ATPYGGVKLEDLIVK	succinylation	[3]
171	ATPYGGVKLEDLIVK	ubiquitination	[9]
178	KLEDLIVKDGLTDVY	acetylation	[1, 3, 4, 5, 6, 7]
178	KLEDLIVKDGLTDVY	succinylation	[3]
178	KLEDLIVKDGLTDVY	ubiquitination	[9]
187	GLTDVYNKIHMGNCA	acetylation	[1, 2, 3, 4, 6, 7, 8, 10, 11, 12]
187	GLTDVYNKIHMGNCA	succinylation	[3]
199	NCAENTAKKMNISRQ	acetylation	[1, 3, 4, 6, 7]
199	NCAENTAKKMNISRQ	succinylation	[3]
220	LSSYTRSKEAWDAGK	acetylation	[1, 3, 6, 7]
220	LSSYTRSKEAWDAGK	succinylation	[3]
227	KEAWDAGKFASEITP	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 10, 11, 12]
227	KEAWDAGKFASEITP	succinylation	[3]
240	TPITISVKGKPDVVV	acetylation	[2, 3]
240	TPITISVKGKPDVVV	succinylation	[3]
242	ITISVKGKPDVVVKE	acetylation	[1, 2, 3, 4, 6, 7]
242	ITISVKGKPDVVVKE	succinylation	[3]
242	ITISVKGKPDVVVKE	succinylation	[3]
242	ITISVKGKPDVVVKE	ubiquitination	[9]
248	GKPDVVVKEDEEYKR	acetylation	[1, 2, 4, 6, 7, 8, 12]
254	VKEDEEYKRVDFSKV	acetylation	[1, 6, 7]
260	YKRVDFSKVPKLKTV	acetylation	[1, 2, 3, 5, 6, 7, 8]
260	YKRVDFSKVPKLKTV	succinylation	[3]
260	YKRVDFSKVPKLKTV	ubiquitination	[9]
263	VDFSKVPKLKTVFQK	acetylation	[2, 3, 6]
263	VDFSKVPKLKTVFQK	succinylation	[3]
263	VDFSKVPKLKTVFQK	succinylation	[3]
265	FSKVPKLKTVFQKEN	acetylation	[2, 3, 6]
265	FSKVPKLKTVFQKEN	succinylation	[3]
265	FSKVPKLKTVFQKEN	ubiquitination	[9]
270	KLKTVFQKENGTITA	acetylation	[1, 3, 8]
270	KLKTVFQKENGTITA	succinylation	[3]
304	AAQRLNVKPLARIAA	acetylation	[1, 6, 7]
304	AAQRLNVKPLARIAA	ubiquitination	[9]
332	APAYAVPKVLKYAGL	acetylation	[4]
335	YAVPKVLKYAGLKKE	acetylation	[1, 3, 4, 5, 6, 7, 8, 10]
335	YAVPKVLKYAGLKKE	succinylation	[3]
335	YAVPKVLKYAGLKKE	ubiquitination	[9]
340	VLKYAGLKKEDIAMW	acetylation	[6, 7]
370	MLEIDPQKVNIHGGA	ubiquitination	[9]

[1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[2] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
[3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[5] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[6] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[8] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[9] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[10] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[11] 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]
[12] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]

Functional Description

Plays a major role in ketone body metabolism (By similarity).

REGION 255 257 Coenzyme A binding (By similarity).
ACT_SITE 123 123 Acyl-thioester intermediate (By
ACT_SITE 382 382 Proton acceptor (By similarity).
ACT_SITE 410 410 Proton acceptor (By similarity).
METAL 216 216 Potassium (By similarity).
METAL 277 277 Potassium; via carbonyl oxygen (By
METAL 278 278 Potassium; via carbonyl oxygen (By
METAL 280 280 Potassium; via carbonyl oxygen (By
METAL 378 378 Potassium; via carbonyl oxygen (By
BINDING 216 216 Coenzyme A (By similarity).
BINDING 260 260 Coenzyme A (By similarity).
BINDING 281 281 Coenzyme A (By similarity).
MOD_RES 171 171 N6-acetyllysine.
MOD_RES 178 178 N6-acetyllysine (By similarity).
MOD_RES 187 187 N6-acetyllysine.
MOD_RES 227 227 N6-acetyllysine.
MOD_RES 248 248 N6-acetyllysine (By similarity).
MOD_RES 260 260 N6-acetyllysine (By similarity).
MOD_RES 335 335 N6-acetyllysine.

Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Metal-binding; Mitochondrion; Potassium; Reference proteome; Transferase; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
GO:0005759; C:mitochondrial matrix; IEA:Compara.
GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:MGI.
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: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