CPLM-020982

Genbank Nucleotide ID

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

Protein Synonyms/Alias

Complex I-39kD; CI-39kD; NADH-ubiquinone oxidoreductase 39 kDa subunit

Mus musculus (Mouse)

Position	Peptide	Type	References
113	LEWDARDKDSIRKAV	acetylation	[1]
157	RAIAQASKEAGVERF	acetylation	[2]
157	RAIAQASKEAGVERF	succinylation	[2]
175	SHLNASMKSSSKSLR	acetylation	[2]
175	SHLNASMKSSSKSLR	succinylation	[2]
189	RSKAVGEKEVRSVFP	acetylation	[1, 3, 4]
254	KGIVNATKDPDAVGK	acetylation	[1]
254	KGIVNATKDPDAVGK	ubiquitination	[5]
370	SSEIEETKPAKTVNY	acetylation	[1, 3, 4, 6, 7]

[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] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]

Functional Description

Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).

MOD_RES 370 370 N6-acetyllysine.

Acetylation; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Mitochondrion; Reference proteome; Respiratory chain; Transit peptide; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.

IPR016040; NAD(P)-bd_dom.
IPR008030; NmrA.