Target type: biologicalprocess
The glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine. [RESID:AA0154]
O-linked glycosylation via serine is a crucial post-translational modification that adds sugar moieties to the hydroxyl group of serine residues within a protein. This process is facilitated by a family of enzymes known as glycosyltransferases, which specifically recognize and attach specific sugar molecules to the serine residue. The glycosylation process typically begins with the transfer of an N-acetylglucosamine (GlcNAc) sugar residue from a donor molecule, UDP-GlcNAc, to the hydroxyl group of serine. This initial step is catalyzed by an enzyme called O-GlcNAc transferase (OGT). Once the initial GlcNAc residue is attached, further modifications can occur, such as the addition of other sugars like galactose, fucose, or sialic acid. These modifications are catalyzed by specific glycosyltransferases that exhibit substrate specificity for both the protein and the sugar being added. O-linked glycosylation via serine plays a significant role in various cellular processes, including protein folding, trafficking, stability, and signaling. It can influence protein-protein interactions, modulate enzyme activity, and impact cellular localization. The specific function of O-linked glycosylation depends on the protein's structure, the site of glycosylation, and the nature of the attached sugar moieties. Disruptions in O-linked glycosylation have been implicated in various diseases, highlighting the importance of this process for normal cellular function.'
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Protein | Definition | Taxonomy |
---|---|---|
Polypeptide N-acetylgalactosaminyltransferase 13 | A polypeptide N-acetylgalactosaminyltransferase 13 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q8IUC8] | Homo sapiens (human) |
Polypeptide N-acetylgalactosaminyltransferase 3 | A polypeptide N-acetylgalactosaminyltransferase 3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q14435] | Homo sapiens (human) |
Polypeptide N-acetylgalactosaminyltransferase 1 | A polypeptide N-acetylgalactosaminyltransferase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q10472] | Homo sapiens (human) |
Polypeptide N-acetylgalactosaminyltransferase 2 | A polypeptide N-acetylgalactosaminyltransferase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q10471] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
gallic acid | gallate : A trihydroxybenzoate that is the conjugate base of gallic acid. | trihydroxybenzoic acid | antineoplastic agent; antioxidant; apoptosis inducer; astringent; cyclooxygenase 2 inhibitor; EC 1.13.11.33 (arachidonate 15-lipoxygenase) inhibitor; geroprotector; human xenobiotic metabolite; plant metabolite |
pyrene | pyrene : An ortho- and peri-fused polycyclic arene consisting of four fused benzene rings, resulting in a flat aromatic system. pyrene: structure in Merck Index, 9th ed, #7746 | ortho- and peri-fused polycyclic arene | fluorescent probe; persistent organic pollutant |
ellagic acid | catechols; cyclic ketone; lactone; organic heterotetracyclic compound; polyphenol | antioxidant; EC 1.14.18.1 (tyrosinase) inhibitor; EC 2.3.1.5 (arylamine N-acetyltransferase) inhibitor; EC 2.4.1.1 (glycogen phosphorylase) inhibitor; EC 2.5.1.18 (glutathione transferase) inhibitor; EC 2.7.1.127 (inositol-trisphosphate 3-kinase) inhibitor; EC 2.7.1.151 (inositol-polyphosphate multikinase) inhibitor; EC 2.7.4.6 (nucleoside-diphosphate kinase) inhibitor; EC 2.7.7.7 (DNA-directed DNA polymerase) inhibitor; EC 5.99.1.2 (DNA topoisomerase) inhibitor; EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor; food additive; fungal metabolite; geroprotector; plant metabolite; skin lightening agent | |
urolithin b | urolithin B: has antiproliferative activity; structure in first source | coumarins | |
urolithin d | urolithin D: has antiproliferative activity; structure in first source | hydroxycoumarin | |
3,3'-di-o-methylellagic acid | 3,3'-di-O-methylellagic acid: structure given in first source |