UniProt Accession

 CBR1_HUMAN; P16152; B2RBZ7; Q3LHW8 

Genbank Protein ID

 J04056; M62420; AB003151; AP000688; AB124848; BT019843; CR541708; AK314879; EF141836; AP001724; CH471079; BC002511; BC015640 

Genbank Nucleotide ID

 AAA52070.1; AAA17881.1; BAA33498.1; BAA89424.1; BAE45940.1; AAV38646.1; CAG46509.1; BAG37394.1; ABK97430.1; BAA95508.1; EAX09755.1; AAH02511.1; AAH15640.1 

Protein Name

 Carbonyl reductase [NADPH] 1 

Protein Synonyms/Alias

 15-hydroxyprostaglandin dehydrogenase [NADP(+)]; NADPH-dependent carbonyl reductase 1; Prostaglandin 9-ketoreductase; Prostaglandin-E(2) 9-reductase 

Gene Name

 CBR1 

Gene Synonyms/Alias

 CBR; CRN 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
148	IMSVRALKSCSPELQ	ubiquitination	[1]
157	CSPELQQKFRSETIT	acetylation	[2]
174	ELVGLMNKFVEDTKK	ubiquitination	[3]
186	TKKGVHQKEGWPSSA	ubiquitination	[4]

Reference

 [1] 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]
 [2] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [3] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [4] 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] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 10 34 NADP.
 NP_BIND 63 64 NADP.
 NP_BIND 194 198 NADP.
 NP_BIND 231 233 NADP.
 REGION 95 97 Glutathione binding.
 REGION 193 194 Glutathione binding.
 ACT_SITE 194 194 Proton acceptor.
 BINDING 90 90 NADP; via carbonyl oxygen.
 BINDING 106 106 Glutathione.
 BINDING 140 140 Substrate.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 239 239 N6-1-carboxyethyl lysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 277 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:EC.
 GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
 GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
 GO:0050221; F:prostaglandin-E2 9-reductase activity; IEA:EC.
 GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
 GO:0017144; P:drug metabolic process; IDA:UniProtKB.
 GO:0042373; P:vitamin K metabolic process; IDA:UniProtKB. 

Interpro

 IPR002198; DH_sc/Rdtase_SDR.
 IPR002347; Glc/ribitol_DH.
 IPR016040; NAD(P)-bd_dom.
 IPR020904; Sc_DH/Rdtase_CS. 

Pfam

 PF00106; adh_short 

SMART

  

PROSITE

 PS00061; ADH_SHORT 

PRINTS

 PR00081; GDHRDH.
 PR00080; SDRFAMILY.