Search Results

Overview

Uniprot IDP00387
Protein NameNADH-cytochrome b5 reductase 3
Gene NameCYB5R3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
120 YFKDTHPKFPAGGKM
154 GLLVYQGKGKFAIRP
156 LVYQGKGKFAIRPDK
163 KFAIRPDKKSNPIIR
164 FAIRPDKKSNPIIRT
42 TLESPDIKYPLRLID

Function

Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor

Protein Sequence

10 MGAQLSTLGH 20 MVLFPVWFLY 30 SLLMKLFQRS 40 TPAITLESPD 50 IKYPLRLIDR 60 EIISHDTRRF 70 RFALPSPQHI 80 LGLPVGQHIY 90 LSARIDGNLV 100 VRPYTPISSD 110 DDKGFVDLVI 120 KVYFKDTHPK 130 FPAGGKMSQY 140 LESMQIGDTI 150 EFRGPSGLLV 160 YQGKGKFAIR 170 PDKKSNPIIR 180 TVKSVGMIAG 190 GTGITPMLQV 200 IRAIMKDPDD 210 HTVCHLLFAN 220 QTEKDILLRP 230 ELEELRNKHS 240 ARFKLWYTLD 250 RAPEAWDYGQ 260 GFVNEEMIRD 270 HLPPPEEEPL 280 VLMCGPPPMI 290 QYACLPNLDH 300 VGHPTERCFV F

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035578 azurophil granule lumen
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005833 hemoglobin complex
Cellular Component GO:0005811 lipid droplet
Cellular Component GO:0016020 membrane
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0005741 mitochondrial outer membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:1903958 nitric-oxide synthase complex
Molecular Function GO:0004128 cytochrome-b5 reductase activity, acting on NAD(P)H
Molecular Function GO:0090524 cytochrome-b5 reductase activity, acting on NADH
Molecular Function GO:0071949 FAD binding
Biological Process GO:0008015 blood circulation
Biological Process GO:0006695 cholesterol biosynthetic process
Biological Process GO:0006809 nitric oxide biosynthetic 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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.