Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Quinone oxidoreductase  

UniProtKB / Swiss-Prot ID :  QOR_HUMAN

Gene Name (Synonyms) : 
CRYZ  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein 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. 

Protein Sequence MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYSRKPLLPYTPG...
Predicted Secondary Structure CCCHHHHHEEEEEECCCCCEEEEEEEECCCCCCCCCEEEEEEEEEECCHHHHHHHHCCCCCCCCCCEEEC...
Protein Variant
LocationDescription
66P -> S (in dbSNP:rs11551729). VAR_022913
176I -> V (in dbSNP:rs3819946). VAR_022914
183E -> K (in dbSNP:rs17095822). VAR_048200
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEVLKLRSD
CEEEEEEEE
47.21Phosphositeplus
Link
23N6-acetyllysinePEVLKLRSD
CEEEEEEEE
47.21HPRD
Link
23N6-acetyllysinePEVLKLRSD
CEEEEEEEE
47.21Phosphositeplus
Link
23N6-acetyllysine.PEVLKLRSD
CEEEEEEEE
47.21UniProtKB
Link
53PhosphotyrosinePVETYIRSG
HHHHHHHHC
4.84Phosphositeplus
Link
62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TYSRKPLLP
CCCCCCCCC
33.79Phosphositeplus
Link
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ASAFKKGDR
CCCCCCCCE
56.41Phosphositeplus
Link
133PhosphotyrosineIGIPYFTAY
HCCHHHHHH
16.19Phosphositeplus
Link
135PhosphothreonineIPYFTAYRA
CHHHHHHHH
19.55Phosphositeplus
Link
137PhosphotyrosineYFTAYRALI
HHHHHHHHH
8.05Phosphositeplus
Link
208N6-acetyllysineNYIDKIKKY
CHHHHHHHH
47.03HPRD
Link
208N6-acetyllysineNYIDKIKKY
CHHHHHHHH
47.03Phosphositeplus
Link
208N6-acetyllysine.NYIDKIKKY
CHHHHHHHH
47.03UniProtKB
Link
248PhosphoserineIVVGSRGTI
EEEECCCCC
18.87HPRD
Link
248PhosphoserineIVVGSRGTI
EEEECCCCC
18.87Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CRYAA_HUMANin vitroHPRD:00437HPRD11672428
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00266Dicoumarol
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-208, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures