UniProt Accession

 NDUA9_HUMAN; Q16795; Q14076; Q2NKX0 

Genbank Protein ID

 AF050641; BC009311; BC015837; BC111546; X76665; L04490 

Genbank Nucleotide ID

 AAD42055.1; AAH09311.1; AAH15837.1; AAI11547.1; CAA54099.1; AAA36350.1 

Protein Name

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

Protein Synonyms/Alias

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

Gene Name

 NDUFA9 

Gene Synonyms/Alias

 NDUFS2L 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
137	IGRDWETKNFDFEDV	ubiquitination	[1, 2, 3, 4, 5, 6]
147	DFEDVFVKIPQAIAQ	ubiquitination	[4]
157	QAIAQLSKEAGVEKF	ubiquitination	[4]
202	FPEAIIVKPSDIFGR	ubiquitination	[4]
234	PLGSLGWKTVKQPVY	ubiquitination	[1, 4, 5, 6, 7]
237	SLGWKTVKQPVYVVD	ubiquitination	[4, 7]
254	KGIVNAVKDPDANGK	ubiquitination	[2, 4, 7]
370	SAEIEDVKPAKTVNI	ubiquitination	[2, 4]
373	IEDVKPAKTVNI***	ubiquitination	[4, 7]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 

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

 MOD_RES 370 370 N6-acetyllysine (By similarity).  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 377 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
 GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
 GO:0050662; F:coenzyme binding; IEA:InterPro.
 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.
 GO:0006814; P:sodium ion transport; NAS:UniProtKB. 

Interpro

 IPR001509; Epimerase_deHydtase.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF01370; Epimerase 

SMART

  

PROSITE

  

PRINTS