5ajn: Difference between revisions

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== Function ==

[https://www.uniprot.org/uniprot/~~MUC5A_HUMAN MUC5A_HUMAN~~] ~~Gel~~-~~forming glycoprotein~~ of ~~gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding~~ to ~~inhaled microorganisms and particles that are subsequently removed by~~ the ~~mucociliary system (PubMed:14535999~~, ~~PubMed:14718370). Interacts with H~~.~~pylori~~ in ~~the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia~~ of the ~~duodenum (GMD)~~ (~~PubMed:14535999~~).<ref>PMID:~~14535999</ref> <ref>PMID:14535999~~</ref> <ref>PMID:~~14718370~~</ref>

[https://www.uniprot.org/uniprot/GALT2_HUMAN GALT2_HUMAN] Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region.<ref>PMID:9295285</ref> <ref>PMID:12438318</ref>

== Publication Abstract from PubMed ==

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 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/MUC5A_HUMAN MUC5A_HUMAN] Gel-forming glycoprotein of gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microorganisms and particles that are subsequently removed by the mucociliary system (PubMed:14535999, PubMed:14718370). Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD) (PubMed:14535999).<ref>PMID:14535999</ref> <ref>PMID:14535999</ref> <ref>PMID:14718370</ref>
+[https://www.uniprot.org/uniprot/GALT2_HUMAN GALT2_HUMAN] Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region.<ref>PMID:9295285</ref> <ref>PMID:12438318</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==