Search Results

Overview

Uniprot IDP15121
Protein NameAldo-keto reductase family 1 member B1
Gene NameAKR1B1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
179 NKPGLKYKPAVNQIE
243 AIAAKHNKTTAQVLI
263 RNLVVIPKSVTPERI
308 LLSCTSHKDYPFHEE
62 VGVAIQEKLREQVVK
86 LWCTYHEKGLVKGAC
90 YHEKGLVKGACQKTL
95 LVKGACQKTLSDLKL

Function

Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates (PubMed:10510318, PubMed:12732097, PubMed:1332968, PubMed:21329684, PubMed:8245005, PubMed:4402695, PubMed:1936586). It catalyzes the reduction of glucose to sorbitol, the first step of the polyol pathway, an alternative route of glucose metabolism that converts glucose to fructose (PubMed:4402695, PubMed:1936586). This pathway becomes highly active under elevated glucose levels, such as during hyperglycemia (PubMed:1936586). Reduces steroids and their derivatives and prostaglandins. Displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:19010934, PubMed:8343525). Catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides (PubMed:17381426). Plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:21329684)

Protein Sequence

10 MASRLLLNNG 20 AKMPILGLGT 30 WKSPPGQVTE 40 AVKVAIDVGY 50 RHIDCAHVYQ 60 NENEVGVAIQ 70 EKLREQVVKR 80 EELFIVSKLW 90 CTYHEKGLVK 100 GACQKTLSDL 110 KLDYLDLYLI 120 HWPTGFKPGK 130 EFFPLDESGN 140 VVPSDTNILD 150 TWAAMEELVD 160 EGLVKAIGIS 170 NFNHLQVEMI 180 LNKPGLKYKP 190 AVNQIECHPY 200 LTQEKLIQYC 210 QSKGIVVTAY 220 SPLGSPDRPW 230 AKPEDPSLLE 240 DPRIKAIAAK 250 HNKTTAQVLI 260 RFPMQRNLVV 270 IPKSVTPERI 280 AENFKVFDFE 290 LSSQDMTTLL 300 SYNRNWRVCA 310 LLSCTSHKDY PFHEEF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Biological Process GO:0046370 fructose biosynthetic process
Biological Process GO:0001523 retinoid metabolic process
Biological Process GO:0006060 sorbitol metabolic process
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0004032 aldose reductase (NADPH) activity
Molecular Function GO:0052650 all-trans-retinol dehydrogenase (NADP+) activity
Molecular Function GO:0047655 allyl-alcohol dehydrogenase activity
Molecular Function GO:0009055 electron transfer activity
Molecular Function GO:0043795 glyceraldehyde oxidoreductase activity
Molecular Function GO:0047956 glycerol dehydrogenase (NADP+) activity
Molecular Function GO:0047939 L-glucuronate reductase activity
Molecular Function GO:0036130 prostaglandin H2 endoperoxidase reductase activity
Molecular Function GO:0001758 retinal dehydrogenase (NAD+) activity
Biological Process GO:0006700 C21-steroid hormone biosynthetic process
Biological Process GO:0005975 carbohydrate metabolic process
Biological Process GO:0071475 cellular hyperosmotic salinity response
Biological Process GO:0044597 daunorubicin metabolic process
Biological Process GO:0044598 doxorubicin metabolic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[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] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[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.