UniProt Accession

 MDHM_MOUSE; P08249; Q0QF44; Q8CF79; Q8R1P0 

Genbank Protein ID

 M16229; X07295; X07296; X07297; X07298; X07299; X07300; X07301; AK002305; AK167809; AK160553; AK135162; BC023482; DQ402950 

Genbank Nucleotide ID

 AAA39509.1; CAA30274.1; CAA30274.1; CAA30274.1; CAA30274.1; CAA30274.1; CAA30274.1; CAA30274.1; BAC24986.1; BAE39836.1; BAE35869.1; BAE22447.1; AAH23482.1; ABD77283.1 

Protein Name

 Malate dehydrogenase, mitochondrial 

Protein Synonyms/Alias

  

Gene Name

 Mdh2 

Gene Synonyms/Alias

 Mor1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
26	TSAQNNAKVAVLGAS	acetylation	[1]
45	QPLSLLLKNSPLVSR	acetylation	[2]
78	IETRANVKGYLGPEQ	acetylation	[1, 2, 3, 4, 5, 6]
78	IETRANVKGYLGPEQ	succinylation	[5]
78	IETRANVKGYLGPEQ	ubiquitination	[7]
91	EQLPDCLKGCDVVVI	acetylation	[1, 2, 4, 5, 6]
91	EQLPDCLKGCDVVVI	succinylation	[5]
157	ITAEVFKKHGVYNPN	acetylation	[2, 5, 8]
165	HGVYNPNKIFGVTTL	acetylation	[1, 2, 3, 4, 5, 6]
165	HGVYNPNKIFGVTTL	succinylation	[5]
185	NTFVAELKGLDPARV	acetylation	[1, 2, 3, 4, 5, 6, 9, 10, 11]
185	NTFVAELKGLDPARV	succinylation	[5]
185	NTFVAELKGLDPARV	ubiquitination	[7]
203	VIGGHAGKTIIPLIS	acetylation	[2, 3, 4, 5, 6]
203	VIGGHAGKTIIPLIS	succinylation	[5]
215	LISQCTPKVDFPQDQ	acetylation	[1, 4, 5, 6, 10]
215	LISQCTPKVDFPQDQ	succinylation	[5]
239	EAGTEVVKAKAGAGS	acetylation	[2, 3, 4, 5, 6, 8]
239	EAGTEVVKAKAGAGS	succinylation	[5]
239	EAGTEVVKAKAGAGS	ubiquitination	[7]
269	LVDAMNGKEGVVECS	acetylation	[5]
269	LVDAMNGKEGVVECS	succinylation	[5]
281	ECSFVQSKETECTYF	acetylation	[3, 4, 5]
281	ECSFVQSKETECTYF	succinylation	[5]
296	STPLLLGKKGLEKNL	acetylation	[1, 2, 3, 4, 5, 6]
296	STPLLLGKKGLEKNL	succinylation	[5]
296	STPLLLGKKGLEKNL	ubiquitination	[7]
297	TPLLLGKKGLEKNLG	acetylation	[3]
301	LGKKGLEKNLGIGKI	acetylation	[1, 2, 3, 4, 5, 6, 12]
301	LGKKGLEKNLGIGKI	succinylation	[5]
301	LGKKGLEKNLGIGKI	ubiquitination	[7]
307	EKNLGIGKITPFEEK	acetylation	[1, 2, 3, 4, 5, 6, 9, 11]
307	EKNLGIGKITPFEEK	succinylation	[5]
307	EKNLGIGKITPFEEK	ubiquitination	[7]
314	KITPFEEKMIAEAIP	acetylation	[1, 2, 3, 4, 5, 6, 8, 9, 10]
314	KITPFEEKMIAEAIP	succinylation	[5]
314	KITPFEEKMIAEAIP	ubiquitination	[7]
324	AEAIPELKASIKKGE	acetylation	[1, 2, 3, 4, 5, 6, 11]
324	AEAIPELKASIKKGE	succinylation	[5]
324	AEAIPELKASIKKGE	ubiquitination	[7]
328	PELKASIKKGEDFVK	acetylation	[3, 4, 5]
328	PELKASIKKGEDFVK	succinylation	[5]
329	ELKASIKKGEDFVKN	acetylation	[1, 3, 4, 5, 9]
329	ELKASIKKGEDFVKN	succinylation	[5]
329	ELKASIKKGEDFVKN	succinylation	[5]
335	KKGEDFVKNMK****	acetylation	[1, 2, 3, 4, 5, 6, 9]
335	KKGEDFVKNMK****	succinylation	[5]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [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

  

Sequence Annotation

 NP_BIND 31 37 NAD (By similarity).
 NP_BIND 140 142 NAD (By similarity).
 ACT_SITE 200 200 Proton acceptor (By similarity).
 BINDING 57 57 NAD (By similarity).
 BINDING 104 104 Substrate.
 BINDING 110 110 Substrate.
 BINDING 117 117 NAD (By similarity).
 BINDING 142 142 Substrate.
 BINDING 176 176 Substrate.
 BINDING 251 251 NAD (By similarity).
 MOD_RES 157 157 N6-acetyllysine.
 MOD_RES 165 165 N6-acetyllysine (By similarity).
 MOD_RES 185 185 N6-acetyllysine (By similarity).
 MOD_RES 239 239 N6-acetyllysine; alternate (Probable).
 MOD_RES 239 239 N6-malonyllysine; alternate (By
 MOD_RES 239 239 N6-succinyllysine; alternate (By
 MOD_RES 301 301 N6-acetyllysine; alternate (By
 MOD_RES 301 301 N6-succinyllysine; alternate (By
 MOD_RES 307 307 N6-acetyllysine; alternate (By
 MOD_RES 307 307 N6-malonyllysine; alternate (By
 MOD_RES 314 314 N6-acetyllysine (Probable).
 MOD_RES 328 328 N6-acetyllysine; alternate (By
 MOD_RES 328 328 N6-succinyllysine; alternate (By
 MOD_RES 329 329 N6-acetyllysine; alternate (By
 MOD_RES 329 329 N6-malonyllysine; alternate (By
 MOD_RES 335 335 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide; Tricarboxylic acid cycle. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 338 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0030060; F:L-malate dehydrogenase activity; IDA:MGI.
 GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:Compara.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
 GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB.
 GO:0006108; P:malate metabolic process; ISA:MGI.
 GO:0006734; P:NADH metabolic process; IEA:Compara.
 GO:0006107; P:oxaloacetate metabolic process; IEA:Compara.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 

Interpro

 IPR001557; L-lactate/malate_DH.
 IPR022383; Lactate/malate_DH_C.
 IPR001236; Lactate/malate_DH_N.
 IPR015955; Lactate_DH/Glyco_Ohase_4_C.
 IPR001252; Malate_DH_AS.
 IPR010097; Malate_DH_type1.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF02866; Ldh_1_C
 PF00056; Ldh_1_N 

SMART

  

PROSITE

 PS00068; MDH 

PRINTS