CPLM-007274

Genbank Nucleotide ID

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
6	**MEGYHKPDQQKLQ	acetylation	[1]
6	**MEGYHKPDQQKLQ	ubiquitination	[2]
11	YHKPDQQKLQALKDT	acetylation	[1]
16	QQKLQALKDTANRLR	ubiquitination	[2]
102	AELLNLRKISSDLDG	ubiquitination	[2]
114	LDGHPVPKQAFTDVA	ubiquitination	[2]
144	YTGKYFDKASYRVYC	acetylation	[3]
144	YTGKYFDKASYRVYC	ubiquitination	[2]
204	HQVDIYQKRCEAFGW	acetylation	[3, 4]
232	CKAFGQAKHQPTAII	acetylation	[1, 3, 5]
232	CKAFGQAKHQPTAII	ubiquitination	[2]
241	QPTAIIAKTFKGRGI	acetylation	[3]
241	QPTAIIAKTFKGRGI	ubiquitination	[2]
254	GITGIEDKEAWHGKP	acetylation	[4]
254	GITGIEDKEAWHGKP	ubiquitination	[2]
260	DKEAWHGKPLPKNMA	acetylation	[1]
260	DKEAWHGKPLPKNMA	ubiquitination	[2]
264	WHGKPLPKNMAEQII	ubiquitination	[2]
281	IYSQVQSKKKILATP	ubiquitination	[2]
282	YSQVQSKKKILATPP	ubiquitination	[2]
283	SQVQSKKKILATPPQ	ubiquitination	[2]
310	MPTPPSYKVGDKIAT	acetylation	[3]
310	MPTPPSYKVGDKIAT	ubiquitination	[2]
314	PSYKVGDKIATRKAY	acetylation	[1, 5, 6]
314	PSYKVGDKIATRKAY	succinylation	[5]
319	GDKIATRKAYGLALA	acetylation	[3]
319	GDKIATRKAYGLALA	ubiquitination	[2]
327	AYGLALAKLGHASDR	acetylation	[3]
327	AYGLALAKLGHASDR	ubiquitination	[2]
343	IALDGDTKNSTFSEL	acetylation	[3]
343	IALDGDTKNSTFSEL	ubiquitination	[2]
456	SDGVATEKAVELAAN	ubiquitination	[2]
493	DFQVGQAKVVLKSKD	ubiquitination	[2]
499	AKVVLKSKDDQVTVI	acetylation	[1]
499	AKVVLKSKDDQVTVI	ubiquitination	[2]
538	VLDPFTIKPLDRKLI	acetylation	[3, 5]
538	VLDPFTIKPLDRKLI	ubiquitination	[2]
543	TIKPLDRKLILDSAR	acetylation	[3]
543	TIKPLDRKLILDSAR	ubiquitination	[2]
597	SQVPRSGKPAELLKM	ubiquitination	[2]
603	GKPAELLKMFGIDKD	acetylation	[4]
609	LKMFGIDKDAIVQAV	acetylation	[3, 5]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (By similarity).

NP_BIND 123 125 Thiamine pyrophosphate (By similarity).
ACT_SITE 366 366 Proton donor (By similarity).
METAL 155 155 Magnesium (By similarity).
METAL 185 185 Magnesium (By similarity).
METAL 187 187 Magnesium; via carbonyl oxygen (By
BINDING 37 37 Substrate (By similarity).
BINDING 40 40 Thiamine pyrophosphate (By similarity).
BINDING 77 77 Thiamine pyrophosphate (By similarity).
BINDING 156 156 Thiamine pyrophosphate; via amide
BINDING 185 185 Thiamine pyrophosphate (By similarity).
BINDING 244 244 Thiamine pyrophosphate (By similarity).
BINDING 258 258 Substrate (By similarity).
BINDING 258 258 Thiamine pyrophosphate (By similarity).
BINDING 318 318 Substrate (By similarity).
BINDING 345 345 Substrate (By similarity).
BINDING 392 392 Thiamine pyrophosphate (By similarity).
BINDING 416 416 Substrate (By similarity).
BINDING 424 424 Substrate (By similarity).
BINDING 428 428 Thiamine pyrophosphate (By similarity).
BINDING 474 474 Substrate (By similarity).
MOD_RES 1 1 N-acetylmethionine (By similarity).
MOD_RES 6 6 N6-acetyllysine (By similarity).
MOD_RES 11 11 N6-acetyllysine (By similarity).
MOD_RES 144 144 N6-acetyllysine (By similarity).
MOD_RES 204 204 N6-acetyllysine (By similarity).
MOD_RES 241 241 N6-acetyllysine (By similarity).
MOD_RES 260 260 N6-acetyllysine (By similarity).
MOD_RES 275 275 Phosphotyrosine.
MOD_RES 287 287 Phosphothreonine (By similarity).
MOD_RES 295 295 Phosphoserine (By similarity).
MOD_RES 603 603 N6-acetyllysine (By similarity).

Acetylation; Calcium; Complete proteome; Direct protein sequencing; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Thiamine pyrophosphate; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; IEA:Compara.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0004802; F:transketolase activity; IDA:MGI.
GO:0040008; P:regulation of growth; IMP:MGI.

IPR009014; Transketo_C/Pyr-ferredox_oxred.
IPR015941; Transketolase-like_C.
IPR005475; Transketolase-like_Pyr-bd.
IPR020826; Transketolase_BS.
IPR005476; Transketolase_C.
IPR005474; Transketolase_N.

PF02779; Transket_pyr
PF02780; Transketolase_C
PF00456; Transketolase_N

SM00861; Transket_pyr

PS00801; TRANSKETOLASE_1
PS00802; TRANSKETOLASE_2