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Identification
HMDB Protein ID HMDBP01041
Secondary Accession Numbers
  • 6330
Name Quinone oxidoreductase
Synonyms
  1. NADPH:quinone reductase
  2. Zeta-crystallin
Gene Name CRYZ
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding.
Pathways Not Available
Reactions
NADPH + Quinone → NADP + semiquinone details
GO Classification
Biological Process
xenobiotic catabolic process
visual perception
protein homotetramerization
Cellular Component
cytosol
Golgi apparatus
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
oxidoreductase activity
Molecular Function
NADPH:quinone reductase activity
zinc ion binding
mRNA 3'-UTR binding
NADPH binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 1
Locus 1p31.1
SNPs CRYZ
Gene Sequence
>990 bp
ATGGCGACTGGACAGAAGTTGATGAGAGCTGTTAGAGTTTTTGAATTTGGTGGGCCAGAA
GTCCTGAAATTGCGATCAGATATTGCAGTACCGATTCCAAAAGACCATCAGGTTCTAATC
AAGGTCCATGCATGTGGTGTCAACCCCGTGGAGACATACATTCGCTCTGGTACTTATAGT
AGAAAACCACTCTTACCCTATACTCCTGGCTCAGATGTGGCTGGGGTGATAGAAGCTGTT
GGAGATAATGCATCTGCTTTCAAGAAAGGTGACAGAGTTTTCACTAGCAGCACGATCTCT
GGGGGTTATGCAGAGTATGCTCTTGCAGCAGACCACACTGTTTACAAACTACCTGAAAAA
CTGGACTTTAAACAAGGAGCTGCCATCGGCATTCCATATTTTACTGCTTATCGAGCTCTG
ATCCACAGTGCCTGTGTGAAAGCTGGAGAGAGTGTTCTGGTTCATGGGGCAAGTGGAGGA
GTTGGATTAGCAGCATGCCAAATTGCTAGAGCTTATGGCTTAAAGATTTTGGGCACTGCT
GGTACTGAGGAAGGACAAAAGATTGTTTTGCAAAATGGAGCCCATGAAGTGTTCAATCAC
AGAGAAGTGAATTACATTGATAAAATTAAGAAGTATGTTGGTGAGAAAGGAATTGATATA
ATTATTGAAATGTTAGCTAATGTAAATCTTAGTAAAGACTTGAGTCTTCTGTCACATGGA
GGACGAGTGATAGTTGTTGGCAGCAGAGGTACTATTGAAATAAACCCACGAGACACCATG
GCAAAGGAGTCGAGTATAATTGGAGTTACTCTCTTTTCCTCAACCAAGGAGGAATTTCAG
CAATATGCAGCAGCCCTTCAAGCTGGAATGGAAATTGGCTGGTTGAAACCTGTGATAGGT
TCTCAATATCCATTGGAGAAGGTGGCCGAGGCTCATGAAAATATCATTCATGGTAGTGGG
GCTACTGGAAAAATGATTCTTCTCTTATGA
Protein Properties
Number of Residues 329
Molecular Weight 35206.36
Theoretical pI 8.444
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Quinone oxidoreductase
MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYS
RKPLLPYTPGSDVAGVIEAVGDNASAFKKGDRVFTSSTISGGYAEYALAADHTVYKLPEK
LDFKQGAAIGIPYFTAYRALIHSACVKAGESVLVHGASGGVGLAACQIARAYGLKILGTA
GTEEGQKIVLQNGAHEVFNHREVNYIDKIKKYVGEKGIDIIIEMLANVNLSKDLSLLSHG
GRVIVVGSRGTIEINPRDTMAKESSIIGVTLFSSTKEEFQQYAAALQAGMEIGWLKPVIG
SQYPLEKVAEAHENIIHGSGATGKMILLL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q08257
UniProtKB/Swiss-Prot Entry Name QOR_HUMAN
PDB IDs
GenBank Gene ID L13278
GeneCard ID CRYZ
GenAtlas ID CRYZ
HGNC ID HGNC:2419
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Gonzalez P, Rao PV, Zigler JS Jr: Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver. Biochem Biophys Res Commun. 1993 Mar 31;191(3):902-7. [PubMed:8466529 ]
  4. Gonzalez P, Rao PV, Zigler JS Jr: Organization of the human zeta-crystallin/quinone reductase gene (CRYZ). Genomics. 1994 May 15;21(2):317-24. [PubMed:8088825 ]
  5. Fernandez MR, Porte S, Crosas E, Barbera N, Farres J, Biosca JA, Pares X: Human and yeast zeta-crystallins bind AU-rich elements in RNA. Cell Mol Life Sci. 2007 Jun;64(11):1419-27. [PubMed:17497241 ]
  6. Lapucci A, Lulli M, Amedei A, Papucci L, Witort E, Di Gesualdo F, Bertolini F, Brewer G, Nicolin A, Bevilacqua A, Schiavone N, Morello D, Donnini M, Capaccioli S: zeta-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2 overexpression in T-cell acute lymphocytic leukemia. FASEB J. 2010 Jun;24(6):1852-65. doi: 10.1096/fj.09-140459. Epub 2010 Jan 26. [PubMed:20103721 ]