BP

GO:0001574

ganglioside biosynthetic process

The chemical reactions and pathways resulting in the formation of ceramide oligosaccharides carrying in addition to other sugar residues, one or more sialic acid residues.

IBA

BP

GO:0006464

cellular protein modification process

The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

IDA

BP

GO:0006664

glycolipid metabolic process

The chemical reactions and pathways involving glycolipids, a class of 1,2-di-O-acylglycerols joined at oxygen 3 by a glycosidic linkage to a carbohydrate part (usually a mono-, di- or tri-saccharide). Some substances classified as bacterial glycolipids have the sugar group acylated by one or more fatty acids and the glycerol group may be absent.

IDA

BP

GO:0009311

oligosaccharide metabolic process

The chemical reactions and pathways involving oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.

IDA

BP

GO:0018146

keratan sulfate biosynthetic process

The chemical reactions and pathways resulting in the formation of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.

TAS

BP

GO:0018279

protein N-linked glycosylation via asparagine

The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

IBA

BP

GO:0071354

cellular response to interleukin-6

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-6 stimulus.

IEP

BP

GO:0097503

sialylation

The covalent attachment of sialic acid to a substrate molecule.

IEA

CC

GO:0000139

Golgi membrane

The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

TAS

CC

GO:0016021

integral component of membrane

The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

NAS

CC

GO:0030173

integral component of Golgi membrane

The component of the Golgi membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

IEA

CC

GO:0070062

extracellular exosome

A membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.

IDA

MF

GO:0003836

beta-galactoside (CMP) alpha-2,3-sialyltransferase activity

Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R.

IBA|TAS

MF

GO:0052798

beta-galactoside alpha-2,3-sialyltransferase activity

Catalysis of the transfer of sialyl residues alpha-2,3-linked to a beta galactosyl residue on the donor to form an alpha-2,3 linkage to a terminal beta galactosyl residue on the acceptor.

IDA