UniProt Accession

 NDUA5_MOUSE; Q9CPP6; Q9CY90; Q9D2P2; Q9D703; Q9D739 

Genbank Protein ID

 AK008156; AK008286; AK008414; AK009338; AK009396; AK009461; AK009493; AK009608; AK009642; AK009652; AK009775; AK009840; AK009985; AK010024; AK010090; AK010092; AK011579; AK011947; AK019084; AK019201; AK019207; AK019215; AK019242; AK019245; AK019291; AK019301; AK019324; AK019354; AK019359; AK019364; AK019368; BC028633 

Genbank Nucleotide ID

 BAB25499.1; BAB25577.1; BAB25655.1; BAB26226.1; BAB26263.1; BAB26302.1; BAB26323.1; BAB26389.1; BAB26409.1; BAB26416.1; BAB26496.1; BAB26535.1; BAB26627.1; BAB26649.1; BAB26695.1; BAB26696.1; BAB27713.1; BAB27932.1; BAB31537.1; BAB31598.1; BAB31601.1; BAB31606.1; BAB31622.1; BAB31624.1; BAB31650.1; BAB31656.1; BAB31667.1; BAB31675.1; BAB31678.1; BAB31681.1; BAB31682.1; AAH28633.1 

Protein Name

 NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 

Protein Synonyms/Alias

 Complex I subunit B13; Complex I-13kD-B; CI-13kD-B; NADH-ubiquinone oxidoreductase 13 kDa-B subunit 

Gene Name

 Ndufa5 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
36	TKTLDILKHFPKHAA	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 9]
40	DILKHFPKHAAYRKY	acetylation	[5, 9, 10]
40	DILKHFPKHAAYRKY	succinylation	[10]
46	PKHAAYRKYTEQITN	acetylation	[1, 2, 4, 5, 8]
60	NEKLDMVKAEPDVKK	acetylation	[2, 5, 9]
66	VKAEPDVKKLEALLQ	acetylation	[9]
96	SLARKMLKWKPWEPL	acetylation	[5]
98	ARKMLKWKPWEPLVE	acetylation	[1, 5]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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] 

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). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 30 30 N6-acetyllysine (By similarity).
 MOD_RES 36 36 N6-acetyllysine.
 MOD_RES 46 46 N6-acetyllysine.
 MOD_RES 60 60 N6-acetyllysine (By similarity).
 MOD_RES 98 98 N6-acetyllysine.  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Respiratory chain; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 116 AA 

Protein Sequence

Gene Ontology

 GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
 GO:0022904; P:respiratory electron transport chain; IEA:InterPro. 

Interpro

 IPR006806; ETC_CI_29_9. 

Pfam

 PF04716; ETC_C1_NDUFA5 

SMART

  

PROSITE

  

PRINTS