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Literature summary extracted from

  • Yoshimura, Y.; Nudelman, A.S.; Levery, S.B.; Wandall, H.H.; Bennett, E.P.; Hindsgaul, O.; Clausen, H.; Nishimura, S.
    Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates (2012), Glycobiology, 22, 429-438.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.41 His tagged truncated protein expressed in High Five cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.41 D519H inactivated lectin domain Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.41 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.41 ion exchange chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine + (glycosylated GTTPSPVPTTSTTSAP) natural-type (alpha-GalNAc-O-Thr) and unnatural-type (beta-GalNAc-O-Thr, alpha-Fuc-O-Thr and beta-GlcNAc-O-Thr) glycosylated Homo sapiens UDP + ?
-
 ?
2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
-
 Homo sapiens UDP + ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.41 UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
-
 Homo sapiens
2.4.1.41 uridine diphosphate-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.4.1.41 physiological function the lectin domain strictly recognizes GalNAc on the substrate and this specificity controls the glycosylation pathway Homo sapiens