CATH Superfamily 2.80.10.50
The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 101: Polypeptide N-acetylgalactosaminyltransferase
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 3 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Polypeptide N-acetylgalactosaminyltransferase activity GO:0004653
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis.
|
1 | Q9Y117 (/IDA) |
|
Acetylgalactosaminyltransferase activity GO:0008376
Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an oligosaccharide.
|
1 | Q9Y117 (/IDA) |
|
Transferase activity, transferring glycosyl groups GO:0016757
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
|
1 | Q9Y117 (/IDA) |
There are 7 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
|
1 | Q9Y117 (/IDA) |
|
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
|
1 | Q9Y117 (/IMP) |
|
Oligosaccharide biosynthetic process GO:0009312
The chemical reactions and pathways resulting in the formation of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
|
1 | Q9Y117 (/IDA) |
|
O-glycan processing GO:0016266
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form a core O-glycan structure.
|
1 | Q9Y117 (/IDA) |
|
Cell-substrate adhesion GO:0031589
The attachment of a cell to the underlying substrate via adhesion molecules.
|
1 | Q9Y117 (/IMP) |
|
Regulation of cell adhesion mediated by integrin GO:0033628
Any process that modulates the frequency, rate, or extent of cell adhesion mediated by integrin.
|
1 | Q9Y117 (/IMP) |
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Extracellular matrix constituent secretion GO:0070278
The controlled release of molecules that form the extracellular matrix, including carbohydrates and glycoproteins by a cell.
|
1 | Q9Y117 (/IMP) |
There are 2 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
1 | Q9Y117 (/IDA) |
|
Golgi stack GO:0005795
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
|
1 | Q9Y117 (/NAS) |
