CHPF2 Gene - Chondroitin Polymerizing Factor 2 | Function, Mutations & Disease

CHPF2 encodes chondroitin polymerizing factor 2, a transmembrane protein that functions as a bifunctional glycosyltransferase involved in chondroitin sulfate (CS) chain elongation. It possesses both glucuronyltransferase and N-acetylgalactosaminyltransferase activities, adding alternating glucuronic acid and N-acetylgalactosamine residues to the growing CS chain. CHPF2 is essential for normal skeletal development and extracellular matrix composition. Mutations in CHPF2 are associated with skeletal dysplasias and altered CS expression in cancers.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Chondroitin sulfate/dermatan sulfate biosynthesis (Reactome: R-HSA-1971475)

• Glycosaminoglycan metabolism (KEGG: hsa00532)

CHPF2 is a 775-amino acid type II transmembrane protein localized to the Golgi apparatus. It contains a short N-terminal cytoplasmic tail, a transmembrane domain, and a large luminal catalytic region. The protein forms a hetero-oligomeric complex with CHPF (chondroitin polymerizing factor) to efficiently polymerize chondroitin sulfate chains. Its bifunctional glycosyltransferase activity is critical for the elongation of CS, a major component of cartilage extracellular matrix. Defects in CHPF2 lead to impaired CS synthesis, resulting in skeletal abnormalities and altered tumor microenvironment in cancers.