CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021746
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
16VYAHQEPKSFNGSLKubiquitination[1]
23KSFNGSLKKVAVEELacetylation[2]
23KSFNGSLKKVAVEELubiquitination[1]
77IETHEAYKKKALTSDubiquitination[1]
79THEAYKKKALTSDIFubiquitination[1]
139FYDSGFLKGKLALLSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
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 (By similarity).
 NP_BIND 104 107 FAD (By similarity).
 NP_BIND 148 151 FAD (By similarity).
 REGION 127 129 Substrate binding (By similarity).
 METAL 174 174 Zinc (By similarity).
 METAL 178 178 Zinc (By similarity).
 METAL 223 223 Zinc (By similarity).
 BINDING 12 12 FAD (By similarity).
 BINDING 156 156 FAD (By similarity).
 BINDING 194 194 FAD (By similarity).
 BINDING 201 201 FAD (By similarity).
 MOD_RES 197 197 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 231 AA 
Protein Sequence
MAGKKVLIVY AHQEPKSFNG SLKKVAVEEL SKQGCTVTVS DLYSMNFEPR ATRNDITGAP 60
SNPDVFSYGI ETHEAYKKKA LTSDIFEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV 120
LCRGFAFDIP GFYDSGFLKG KLALLSLTTG GTAEMYTKDG VSGDFRYFLW PLQHGTLHFC 180
GFKVLAPQIS FGLDVSSEEE RKVMLASWAQ RLKSIWKEEP IHCTPPWYFQ E 231 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007613; P:memory; IEA:Compara. 
Interpro
 IPR003680; Flavodoxin_fold. 
Pfam
 PF02525; Flavodoxin_2 
SMART
  
PROSITE
  
PRINTS