Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Carbonyl reductase [NADPH] 1  

UniProtKB / Swiss-Prot ID :  CBR1_HUMAN

Gene Name (Synonyms) : 
CBR1, CBR, CRN  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. 

Protein Sequence MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSI...
Predicted Secondary Structure CCCCCCEEEEEECCCHHHHHHHHHHHHHCCCEEEEEECCHHHHHHHHHHHHHCCCCEEEEECCCCCHHHH...
Protein Variant
LocationDescription
88V -> I (reduced affinity for NADPH andreduced activity towards daunorubicin and
131P -> S (in dbSNP:rs41557318). VAR_031706
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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
2N-acetylserine---MSSGIH
---CCCCCC
36.95HPRD
Link
2N-acetylserine.---MSSGIH
---CCCCCC
36.95UniProtKB
Link
2Phosphoserine---MSSGIH
---CCCCCC
36.95HPRD
Link
148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VRALKSCSP
HCCCCCCCH
48.72Phosphositeplus
Link
160PhosphoserineQKFRSETIT
HHHHHHHCC
42.07Phosphositeplus
Link
162PhosphothreonineFRSETITEE
HHHHHCCHH
34.15Phosphositeplus
Link
174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLMNKFVED
HHCCCCCCC
36.50Phosphositeplus
Link
186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GVHQKEGWP
CCCCCCCCC
43.23Phosphositeplus
Link
194PhosphotyrosinePSSAYGVTK
CCHHHHHHH
17.68HPRD
Link
194PhosphotyrosinePSSAYGVTK
CCHHHHHHH
17.68PhosphoELM
Link
194PhosphotyrosinePSSAYGVTK
CCHHHHHHH
17.68Phosphositeplus
Link
194Phosphotyrosine.PSSAYGVTK
CCHHHHHHH
17.68UniProtKB
Link
205PhosphoserineVTVLSRIHA
HHHHHHHHH
25.50HPRD
Link
213PhosphoserineARKLSEQRK
HHHHHHHHC
34.42HPRD
Link
213PhosphoserineARKLSEQRK
HHHHHHHHC
34.42Phosphositeplus
Link
239N6-1-carboxyethyl lysine.MAGPKATKS
CCCCCCCCC
68.70UniProtKB
Link
253PhosphotyrosineETPVYLALL
HHHHHHHCC
6.35Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ERCC8_HUMANphysical interactionEBI-736451
intact16169070
ERCC8_HUMANyeast 2-hybridHPRD:00267HPRD16169070
PTGES_HUMANENSP00000290349STRING
PGES2_HUMANENSP00000290349STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00997Doxorubicin
DB00502Haloperidol
DB01046Lubiprostone
DB04844Tetrabenazine
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Related Literatures of Post-Translational Modification
N6-1-carboxyethyl lysine
ReferencePubMed
"Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase.";
Krook M., Ghosh D., Stroemberg R., Carlquist M., Joernvall H.;
Proc. Natl. Acad. Sci. U.S.A. 90:502-506(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND N6-1-CARBOXYETHYLATION AT LYS-239.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-194, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures