UniProt Accession

 NQO2_HUMAN; P16083; B2R492; Q5TD04 

Genbank Protein ID

 J02888; AY299456; AB050248; AY855291; AK311746; AL133351; CH471087; BC006096 

Genbank Nucleotide ID

 AAA60239.1; AAB60642.3; BAB16974.1; AAW29945.1; BAG34689.1; CAI23294.1; EAW55107.1; AAH06096.1 

Protein Name

 Ribosyldihydronicotinamide dehydrogenase [quinone] 

Protein Synonyms/Alias

 NRH dehydrogenase [quinone] 2; NRH:quinone oxidoreductase 2; Quinone reductase 2; QR2 

Gene Name

 NQO2 

Gene Synonyms/Alias

 NMOR2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
16	VYAHQEPKSFNGSLK	ubiquitination	[1]
23	KSFNGSLKNVAVDEL	ubiquitination	[2, 3]
54	LEPRATDKDITGTLS	ubiquitination	[2]
77	VETHEAYKQRSLASD	ubiquitination	[2]
90	SDITDEQKKVREADL	ubiquitination	[2, 4]
158	GTAEMYTKTGVNGDS	ubiquitination	[2, 4]
217	QRLQTIWKEEPIPCT	ubiquitination	[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] 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] 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]
 [4] 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

 The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. 

Sequence Annotation

 NP_BIND 18 21 FAD.
 NP_BIND 104 107 FAD.
 NP_BIND 148 151 FAD.
 REGION 127 129 Substrate binding.
 METAL 174 174 Zinc.
 METAL 178 178 Zinc.
 METAL 223 223 Zinc.
 BINDING 12 12 FAD.
 BINDING 156 156 FAD.
 BINDING 194 194 FAD.
 BINDING 201 201 FAD.
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 197 197 Phosphoserine.  

Keyword

 3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 231 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IEA:EC.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008753; F:NADPH dehydrogenase (quinone) activity; TAS:ProtInc.
 GO:0007613; P:memory; IEA:Compara. 

Interpro

 IPR003680; Flavodoxin_fold. 

Pfam

 PF02525; Flavodoxin_2 

SMART

  

PROSITE

  

PRINTS