CPLM-001528

Genbank Nucleotide ID

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

Protein Synonyms/Alias

Complex I-B17; CI-B17; NADH-ubiquinone oxidoreductase B17 subunit

Homo sapiens (Human)

Position	Peptide	Type	References
9	TGYTPDEKLRLQQLR	ubiquitination	[1, 2, 3]
24	ELRRRWLKDQELSPR	ubiquitination	[2, 3, 4, 5, 6]
49	PMEKFWNKFLENKSP	acetylation	[7]
49	PMEKFWNKFLENKSP	ubiquitination	[2, 3, 4, 5, 6, 8]
54	WNKFLENKSPWRKMV	ubiquitination	[2, 4, 5, 6]
93	MKYHVSEKPYGIVEK	ubiquitination	[4, 5, 6]

[1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]

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.

MOD_RES 2 2 N-acetylthreonine.

Acetylation; Alternative splicing; Complete proteome; Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:HPA.
GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
GO:0044281; P:small molecule metabolic process; TAS:Reactome.

IPR019174; NADH_DH_b-subcmplx_su6.