protein
Beta-1,3-glucosyltransferase
aka Beta3Glc-T
Gene
B3GLCT
Organism
Homo sapiens(9606)
Length
498 aa
Mass
56,564 Da
Beta-1,3-glucosyltransferase (B3GLCT) is a 498-amino acid transferase that catalyzes a key step in O-linked fucosylation of proteins containing thrombospondin type-1 repeats, a post-translational modification occurring in the endoplasmic reticulum (UniProt: Q6Y288). The enzyme extends fucosylated substrates by transferring glucose from UDP-glucose to the attached fucose residue, thereby regulating biological processes in cysteine-knotted proteins.
B3GLCT mutations cause Peters-plus syndrome (PTRPLS, MIM 261540), an autosomal recessive disorder featuring anterior eye abnormalities, short stature, developmental delay, and craniofacial features (UniProt: Q6Y288). The protein's role in endoplasmic reticulum protein modification suggests relevance to protein quality control and secretory pathway function.
In Alzheimer's Disease, B3GLCT is upregulated in post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics; mean log2FC = 0.46), indicating elevated expression in disease state. This upregulation was detected across subcellular fractions in TMT-labeled quantitative mass spectrometry analysis, suggesting potential involvement in AD-associated protein misfolding or glycosylation imbalances.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↑ Up in ADP3
not detected
P2
+0.455
S2
not detected
S3
not detected
Mean log₂FC across detected fractions: +0.4552 (1 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Beta-1,3-glucosyltransferase involved in one of the two pathways responsible for protein O-linked fucosylation, a unique post-translational modification of cysteine-knotted proteins that regulates various biological processes. This pathway targets proteins with Thrombospondin type-1 (TSP1) repeats (TSR) in the endoplasmic reticulum. It starts with POFUT2, which attaches fucose via an O-glycosidic bond to a conserved serine or threonine residue. B3GLCT extends this modification by transferring a glucose molecule from UDP-glucose to the fucose
Disease associations
Peters-plus syndromePTRPLS
An autosomal recessive disorder characterized by anterior eye-chamber abnormalities, disproportionate short stature, developmental delay, characteristic craniofacial features, cleft lip and/or palate.
Sources
Last updated 5/8/2026, 6:26:14 AM