UniProt Accession

 NDUA8_HUMAN; P51970; B1AM93; Q9Y6N0 

Genbank Protein ID

 AF044953; AK314135; AL162423; CH471090; BC001016 

Genbank Nucleotide ID

 AAD42056.1; BAG36825.1; CAH73980.1; EAW87511.1; AAH01016.1 

Protein Name

 NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 

Protein Synonyms/Alias

 Complex I-19kD; CI-19kD; Complex I-PGIV; CI-PGIV; NADH-ubiquinone oxidoreductase 19 kDa subunit 

Gene Name

 NDUFA8 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
14	LPTLEELKVDEVKIS	ubiquitination	[1]
19	ELKVDEVKISSAVLK	ubiquitination	[2]
41	AQCDKPNKEFMLCRW	ubiquitination	[1]
51	MLCRWEEKDPRRCLE	ubiquitination	[1]
61	RRCLEEGKLVNKCAL	ubiquitination	[1, 3]
65	EEGKLVNKCALDFFR	ubiquitination	[1, 2, 3]
102	QLFRHCRKQQAKFDE	ubiquitination	[3, 4]
106	HCRKQQAKFDECVLD	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
114	FDECVLDKLGWVRPD	ubiquitination	[1, 9]
127	PDLGELSKVTKVKTD	ubiquitination	[1, 3, 7, 9, 10]
132	LSKVTKVKTDRPLPE	ubiquitination	[7]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] 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]
 [9] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [10] 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] 

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. 

Sequence Annotation

 DOMAIN 29 69 CHCH 1.
 DOMAIN 71 113 CHCH 2.
 MOTIF 36 46 C-X9-C motif 1.
 MOTIF 56 66 C-X9-C motif 2.
 MOTIF 78 88 C-X9-C motif 3.
 MOTIF 100 110 C-X9-C motif 4.
 DISULFID 36 66 Potential.
 DISULFID 46 56 Potential.
 DISULFID 78 110 Potential.
 DISULFID 88 100 Potential.  

Keyword

 Complete proteome; Direct protein sequencing; Disulfide bond; Electron transport; Mitochondrion; Polymorphism; Reference proteome; Repeat; Respiratory chain; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 172 AA 

Protein Sequence

Gene Ontology

 GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
 GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
 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. 

Interpro

 IPR010625; CHCH.
 IPR016680; NADH_Ub_cplx-1_asu_su-8. 

Pfam

 PF06747; CHCH 

SMART

  

PROSITE

  

PRINTS