UniProt Accession

 NDUS5_HUMAN; O43920 

Genbank Protein ID

 AF047434; AF020352; BC001884 

Genbank Nucleotide ID

 AAC39878.1; AAB87866.1; AAH01884.1 

Protein Name

 NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 

Protein Synonyms/Alias

 Complex I-15 kDa; CI-15 kDa; NADH-ubiquinone oxidoreductase 15 kDa subunit 

Gene Name

 NDUFS5 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MPFLDIQKRFGLNID	ubiquitination	[1, 2, 3, 4]
28	QSGEQPYKMAGRCHA	ubiquitination	[1, 2, 3, 5, 6, 7]
101	PPPHHIGKGEPRP**	ubiquitination	[1, 2, 3]

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] 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] 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]
 [4] 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]
 [5] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [6] 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]
 [7] 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] 

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

 MOTIF 33 43 C-X9-C motif 1.
 MOTIF 56 66 C-X9-C motif 2.
 DISULFID 33 66 Potential.
 DISULFID 43 56 Potential.  

Keyword

 Complete proteome; Disulfide bond; Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Polymorphism; Reference proteome; Respiratory chain; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 106 AA 

Protein Sequence

Gene Ontology

 GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
 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:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 

Interpro

 IPR019342; NADH_UbQ_OxRdtase_FeS-su5. 

Pfam

 PF10200; Ndufs5 

SMART

  

PROSITE

  

PRINTS