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  2. Protein O-GlcNAc transferase - Wikipedia

    en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase

    O-GlcNAc transferase is a part of a host of biological functions within the human body. OGT is involved in the resistance of insulin in muscle cells and adipocytes by inhibiting the Threonine 308 phosphorylation of AKT1, increasing the rate of IRS1 phosphorylation (at serine 307 and serine 632/635), reducing insulin signaling, and glycosylating ...

  3. Paucimannosylation - Wikipedia

    en.wikipedia.org/wiki/Paucimannosylation

    The function of protein paucimannosylation remains largely unexplored in vertebrates. Recent literature however has emerged demonstrating that paucimannosylation play roles in mediating pathophysiological processes such as in inflammation, pathogen infection, cancer and in the development of stem cells and in normal homeostasis.

  4. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    These can be divided into four groups: disorders of protein N-glycosylation, disorders of protein O-glycosylation, disorders of lipid glycosylation and disorders of other glycosylation pathways and of multiple glycosylation pathways. No effective treatment is known for any of these disorders. 80% of these affect the nervous system.

  5. ALG1 - Wikipedia

    en.wikipedia.org/wiki/ALG1

    208211 Ensembl ENSG00000033011 ENSMUSG00000039427 UniProt Q9BT22 Q921Q3 RefSeq (mRNA) NM_019109 NM_001330504 NM_145362 RefSeq (protein) NP_001317433 NP_061982 NP_663337 Location (UCSC) Chr 16: 5.03 – 5.09 Mb Chr 16: 5.05 – 5.06 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Chitobiosyldiphosphodolichol beta-mannosyltransferase is an enzyme that is encoded by ALG1 whose structure ...

  6. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    The best characterised O-mannosylated human protein is α-dystroglycan. [16] O-Man sugars separate two domains of the protein, required to connect the extracellular and intracellular regions to anchor the cell in position. [18] Ribitol, xylose and glucuronic acid can be added to this structure in a complex modification that forms a long sugar ...

  7. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [3]

  8. Golgin subfamily A member 2 - Wikipedia

    en.wikipedia.org/wiki/Golgin_subfamily_A_member_2

    The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. [ 6 ]

  9. DPAGT1 - Wikipedia

    en.wikipedia.org/wiki/DPAGT1

    The protein encoded by this gene is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway (also see Genetic pathway) for glycoprotein biosynthesis. This enzyme belongs to the glycosyltransferase family 4. This protein is an integral membrane protein of the endoplasmic reticulum.