CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011580
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Quinone oxidoreductase 
Protein Synonyms/Alias
 NADPH:quinone reductase; Zeta-crystallin 
Gene Name
 CRYZ 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MATGQKLMRAVRVubiquitination[1, 2]
23FGGPEVLKLRSDIAVacetylation[3, 4]
23FGGPEVLKLRSDIAVubiquitination[2, 5, 6]
62RSGTYSRKPLLPYTPubiquitination[2, 7, 8]
88GDNASAFKKGDRVFTubiquitination[7, 8]
89DNASAFKKGDRVFTSubiquitination[2]
175IARAYGLKILGTAGTubiquitination[2]
187AGTEEGQKIVLQNGAubiquitination[2]
208REVNYIDKIKKYVGEacetylation[3]
208REVNYIDKIKKYVGEubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 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. 
Sequence Annotation
 NP_BIND 158 161 NADP.
 NP_BIND 246 249 NADP.
 NP_BIND 269 271 NADP.
 BINDING 53 53 NADP.
 BINDING 181 181 NADP; via amide nitrogen.
 BINDING 200 200 NADP.
 BINDING 229 229 NADP.
 MOD_RES 23 23 N6-acetyllysine.
 MOD_RES 248 248 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 329 AA 
Protein Sequence
MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS 60
RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK 120
LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA 180
GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG 240
GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG 300
SQYPLEKVAE AHENIIHGSG ATGKMILLL 329 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
 GO:0070402; F:NADPH binding; IDA:UniProtKB.
 GO:0003960; F:NADPH:quinone reductase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
 GO:0007601; P:visual perception; TAS:ProtInc.
 GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB. 
Interpro
 IPR013149; ADH_C.
 IPR013154; ADH_GroES-like.
 IPR002085; ADH_SF_Zn-type.
 IPR011032; GroES-like.
 IPR016040; NAD(P)-bd_dom.
 IPR002364; Quin_OxRdtase/zeta-crystal_CS. 
Pfam
 PF08240; ADH_N
 PF00107; ADH_zinc_N 
SMART
  
PROSITE
 PS01162; QOR_ZETA_CRYSTAL 
PRINTS