Literature summary for 2.4.1.175 extracted from

Izumikawa, T.; Okuura, Y.; Koike, T.; Sakoda, N.; Kitagawa, H.
Chondroitin 4-O-sulfotransferase-1 regulates the chain length of chondroitin sulfate in co-operation with chondroitin N-acetylgalactosaminyltransferase-2 (2011), Biochem. J., 434, 321-331.

Search for more literature for 2.4.1.175

Cloned(Commentary)

Cloned (Comment)	Organism
ChGn-2, expression analysis by quantitative real-time RT-PCR, co-expression of ChGn-1 or ChGn-2 into sog9 and L cells, sog9 is a mutant L cell line are deficient in the expression of chondroitin 4-O-sulfotransferase-1, C4ST-1, disaccharide composition of chondroitin sulfate in control and transfected L cells, overview	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
D367A	site-directed mutagenesis, a soluble mutant is generated by replacing the first 36 amino acids of ChGn-2 D367A with a cleavable insulin signal sequence and the protein A IgG-binding domain, inactive mutant	Mus musculus
additional information	silencing of ChGn-2 in L cells by shRNA	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Synonyms

Synonyms	Comment	Organism
ChGn-2	-	Mus musculus
chondroitin N-acetylgalactosaminyltransferase-2	-	Mus musculus

General Information

General Information	Comment	Organism
malfunction	overexpression of ChGn-2 increases the length and amount of chondroitin sulfate chains in L cells, but not in sog9 mutant cells. Knockdown of ChGn-2 results in a decrease in the amount of CS in L cells in a manner proportional to ChGn-2 expression levels, whereas the introduction of mutated ChGn-2 lacking enzyme activity fails to increase the amount of chondroitin sulfate	Mus musculus
physiological function	chondroitin 4-O-sulfotransferase-1, C4ST-1 regulates the chain length and amount of chondroitin sulfate in co-operation with ChGn-2 the enzymes play a critical role in chondroitin sulfate chain elongation	Mus musculus

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Release 2023.1 (January 2023)