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CSGALNACT2

Gene
CSGALNACT2
Protein
Chondroitin sulfate N-acetylgalactosaminyltransferase 2
Organism
Homo sapiens
Length
542 amino acids
Function
Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains.
Similarity
Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Mass
62.572 kDa
Sequence
MPRRGLILHTRTHWLLLGLALLCSLVLFMYLLECAPQTDGNASLPGVVGENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQEMSEKMRSLQERRNVGANGIGYQSNKEQAPSDLLEFLHSQIDKAEVSIGAKLPSEYGVIPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGLEVINNPDEDDEQEDEEGPLGEKLIFNENDFVEGYYRTERDKGTQYELFFKKADLTEYRHVTLFRPFGPLMKVKSEMIDITRSIINIIVPLAERTEAFVQFMQNFRDVCIHQDKKIHLTVVYFGKEGLSKVKSILESVTSESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANQEVPPPVEQQLVHKKDSGFWRDFGFGMTCQYRSDFLTIGGFDMEVKGWGGEDVHLYRKYLHGDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEASHSHLGMLVFREEIETHLHKQAYRTNSEAVG

Gene
Csgalnact2
Protein
Chondroitin sulfate N-acetylgalactosaminyltransferase 2
Organism
Mus musculus
Length
542 amino acids
Function
Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains (By similarity).
Similarity
Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Mass
62.53 kDa
Sequence
MSRRGSILHSRTQWLLLGLALLFSLVLFMYLLECAPQTDGNASLPGVVRENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQDMSEKMRALQERKKLGANGVGYPGNREQAPSDLLEFLHSQIDRAEVSVGAKLPSEYGVVPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGVEVINNPDEDDAQEDEEGPLGEKLIFNENDFIEGYYRTERDKGTQYELFFKKADLMEYRHVTLFRPFGPLMKVKNELIDITRSVINIIVPLAERTEAFSQFMQNFRDVCIHQDKRIHLTVVYFGKEGLSKVKSILESVSSESDFHNYTLVSLDEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANQDVPPPVEQQLVHKKDSGFWRDFGFGMTCQYQSDFLSVGGFDMEVKGWGGEDVHLYRKYLHGDLIVIRTPVPGLFHLWHEKHCADELTPEQYRMCIQSKAMNEASHSHLGMMVFREEIEMHLRKQAYRTNSETAG

Gene
CSGALNACT2
Protein
Chondroitin sulfate N-acetylgalactosaminyltransferase 2
Organism
Homo sapiens
Length
542 amino acids
Function
Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains.
Similarity
Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Mass
62.572 kDa
Sequence
MPRRGLILHTRTHWLLLGLALLCSLVLFMYLLECAPQTDGNASLPGVVGENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQEMSEKMRSLQERRNVGANGIGYQSNKEQAPSDLLEFLHSQIDKAEVSIGAKLPSEYGVIPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGLEVINNPDEDDEQEDEEGPLGEKLIFNENDFVEGYYRTERDKGTQYELFFKKADLTEYRHVTLFRPFGPLMKVKSEMIDITRSIINIIVPLAERTEAFVQFMQNFRDVCIHQDKKIHLTVVYFGKEGLSKVKSILESVTSESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANQEVPPPVEQQLVHKKDSGFWRDFGFGMTCQYRSDFLTIGGFDMEVKGWGGEDVHLYRKYLHGDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEASHSHLGMLVFREEIETHLHKQAYRTNSEAVG

Gene
Csgalnact2
Protein
Chondroitin sulfate N-acetylgalactosaminyltransferase 2
Organism
Mus musculus
Length
542 amino acids
Function
Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains (By similarity).
Similarity
Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Mass
62.53 kDa
Sequence
MSRRGSILHSRTQWLLLGLALLFSLVLFMYLLECAPQTDGNASLPGVVRENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQDMSEKMRALQERKKLGANGVGYPGNREQAPSDLLEFLHSQIDRAEVSVGAKLPSEYGVVPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGVEVINNPDEDDAQEDEEGPLGEKLIFNENDFIEGYYRTERDKGTQYELFFKKADLMEYRHVTLFRPFGPLMKVKNELIDITRSVINIIVPLAERTEAFSQFMQNFRDVCIHQDKRIHLTVVYFGKEGLSKVKSILESVSSESDFHNYTLVSLDEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANQDVPPPVEQQLVHKKDSGFWRDFGFGMTCQYQSDFLSVGGFDMEVKGWGGEDVHLYRKYLHGDLIVIRTPVPGLFHLWHEKHCADELTPEQYRMCIQSKAMNEASHSHLGMMVFREEIEMHLRKQAYRTNSETAG