Search Results

Overview

Uniprot IDP16152
Protein NameCarbonyl reductase [NADPH] 1
Gene NameCBR1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
148 IMSVRALKSCSPELQ
157 CSPELQQKFRSETIT
180 NKFVEDTKKGVHQKE
186 TKKGVHQKEGWPSSA
239 RTDMAGPKATKSPEE

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 (PubMed:15799708, PubMed:17344335, PubMed:17912391, PubMed:18449627, PubMed:18826943, PubMed:1921984, PubMed:7005231). Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (PubMed:17344335, PubMed:18826943). In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (PubMed:28878267)

Protein Sequence

10 MSSGIHVALV 20 TGGNKGIGLA 30 IVRDLCRLFS 40 GDVVLTARDV 50 TRGQAAVQQL 60 QAEGLSPRFH 70 QLDIDDLQSI 80 RALRDFLRKE 90 YGGLDVLVNN 100 AGIAFKVADP 110 TPFHIQAEVT 120 MKTNFFGTRD 130 VCTELLPLIK 140 PQGRVVNVSS 150 IMSVRALKSC 160 SPELQQKFRS 170 ETITEEELVG 180 LMNKFVEDTK 190 KGVHQKEGWP 200 SSAYGVTKIG 210 VTVLSRIHAR 220 KLSEQRKGDK 230 ILLNACCPGW 240 VRTDMAGPKA 250 TKSPEEGAET 260 PVYLALLPPD 270 AEGPHGQFVS EKRVEQW

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:1903561 extracellular vesicle
Molecular Function GO:0047021 15-hydroxyprostaglandin dehydrogenase (NADP+) activity
Molecular Function GO:0047020 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
Molecular Function GO:0004090 carbonyl reductase (NADPH) activity
Molecular Function GO:0016655 oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
Molecular Function GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Molecular Function GO:0050221 prostaglandin E2 9-reductase activity
Molecular Function GO:0160163 S-nitrosoglutathione reductase (NADPH) activity
Biological Process GO:0030855 epithelial cell differentiation
Biological Process GO:0008211 glucocorticoid metabolic process
Biological Process GO:2000379 positive regulation of reactive oxygen species metabolic process
Biological Process GO:0046457 prostanoid biosynthetic process
Biological Process GO:0042373 vitamin K metabolic process
Biological Process GO:0006805 xenobiotic metabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.