Search Results

Overview

Uniprot IDO60218
Protein NameAldo-keto reductase family 1 member B10
Gene NameAKR1B10
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 TFVELSTKAKMPIVG
117 IHWPQGFKSGDDLFP
12 VELSTKAKMPIVGLG
125 SGDDLFPKDDKGNAI
128 DLFPKDDKGNAIGGK
169 FSHFQIEKLLNKPGL
173 QIEKLLNKPGLKYKP
177 LLNKPGLKYKPVTNQ
179 NKPGLKYKPVTNQVE
195 HPYLTQEKLIQYCHS
203 LIQYCHSKGITVTAY
22 IVGLGTWKSPLGKVK
222 SPDRPWAKPEDPSLL
233 PSLLEDPKIKEIAAK
243 EIAAKHKKTAAQVLI
263 RNVIVIPKSVTPARI
27 TWKSPLGKVKEAVKV
33 GKVKEAVKVAIDAGY
62 VGEAIQEKIQEKAVK
66 IQEKIQEKAVKREDL
78 EDLFIVSKLWPTFFE
95 LVRKAFEKTLKDLKL

Function

Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:12732097, PubMed:18087047, PubMed:19013440, PubMed:19563777, PubMed:9565553). Displays strong enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:18087047). Plays a critical 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:19013440, PubMed:19563777). Displays no reductase activity towards glucose (PubMed:12732097)

Protein Sequence

10 MATFVELSTK 20 AKMPIVGLGT 30 WKSPLGKVKE 40 AVKVAIDAGY 50 RHIDCAYVYQ 60 NEHEVGEAIQ 70 EKIQEKAVKR 80 EDLFIVSKLW 90 PTFFERPLVR 100 KAFEKTLKDL 110 KLSYLDVYLI 120 HWPQGFKSGD 130 DLFPKDDKGN 140 AIGGKATFLD 150 AWEAMEELVD 160 EGLVKALGVS 170 NFSHFQIEKL 180 LNKPGLKYKP 190 VTNQVECHPY 200 LTQEKLIQYC 210 HSKGITVTAY 220 SPLGSPDRPW 230 AKPEDPSLLE 240 DPKIKEIAAK 250 HKKTAAQVLI 260 RFHIQRNVIV 270 IPKSVTPARI 280 VENIQVFDFK 290 LSDEEMATIL 300 SFNRNWRACN 310 VLQSSHLEDY PFNAEY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005764 lysosome
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0008106 alcohol dehydrogenase (NADP+) activity
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:0045550 geranylgeranyl reductase activity
Molecular Function GO:0047718 indanol dehydrogenase activity
Molecular Function GO:0001758 retinal dehydrogenase (NAD+) activity
Biological Process GO:0110095 cellular detoxification of aldehyde
Biological Process GO:0044597 daunorubicin metabolic process
Biological Process GO:0044598 doxorubicin metabolic process
Biological Process GO:0016488 farnesol catabolic process
Biological Process GO:0001523 retinoid 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 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.