Search results for ST3GAL3

Showing 13 results out of 13

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Protein (4 results from a total of 4)

Identifier: R-HSA-981488
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: ST3GAL3: Q11203
Identifier: R-HSA-3702142
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: ST3GAL3: Q11203
Identifier: R-HSA-3702112
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: Q11203
Identifier: R-HSA-3702102
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: Q11203

Set (3 results from a total of 3)

Identifier: R-HSA-3702117
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-1499957
Species: Homo sapiens
Compartment: Golgi membrane
Identifier: R-HSA-9605640
Species: Homo sapiens
Compartment: Golgi membrane

Pathway (2 results from a total of 2)

Identifier: R-HSA-3656243
Species: Homo sapiens
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (ST3GAL3) mediates the transfer of sialic acid from CMP-sialic acid to galactose-containing glycoproteins and forms the sialyl Lewis a epitope on proteins which are required for attaining and/or maintaining higher cognitive functions. Some defects in ST3GAL3 result in mental retardation, autosomal recessive 12 (MRT12; MIM:611090), a disorder characterised by below average general intellectual function and impaired adaptive behaviour (Najmabadi et al. 2007, Hu et al. 2011). Another defect of ST3GAL3 can cause early infantile epileptic encephalopathy-15 (EIEE15: MIM:615006), resulting in severe mental retardation (Edvardson et al. 2012).
Identifier: R-HSA-1912420
Species: Homo sapiens
Compartment: Golgi membrane, endoplasmic reticulum membrane, Golgi lumen, plasma membrane
NOTCH undergoes final posttranslational processing in the Golgi apparatus (Lardelli et al. 1994, Blaumueller et al. 1997, Weinmaster et al. 1991, Weinmaster et al. 1992, Uyttendaele et al. 1996). Movement of NOTCH precursors from the endoplasmic reticulum to Golgi is controlled by SEL1L protein, a homolog of C. elegans sel-1. SEL1L localizes to the endoplasmic reticulum membrane and prevents translocation of misfolded proteins, therefore serving as a quality control check (Li et al. 2010, Sundaram et al. 1993, Francisco et al. 2010). Similarly, C. elegans sel-9 and its mammalian homolog TMED2 are Golgi membrane proteins that participate in quality control of proteins transported from Golgi to the plasma membrane. Translocation of a mutant C. elegans NOTCH homolog lin-12 from the Golgi to the plasma membrane is negatively regulated by sel-9 (Wen et al. 1999). A GTPase RAB6 positively controls NOTCH trafficking through Golgi (Purcell et al. 1999).


Processing of mammalian NOTCH precursors in the Golgi typically involves the cleavage by FURIN convertase. Pre-NOTCH is a ~300 kDa protein, and cleavage by FURIN produces two fragments with approximate sizes of 110 kDa and 180 kDa. The 110 kDa fragment contains the transmembrane and intracellular domains of NOTCH and is known as NTM or NTMICD. The 189 kDa fragment contains NOTCH extracellular sequence and is known as NEC or NECD. The NTM and NEC fragments heterodimerize (Blaumueller et al. 1997, Logeat et al. 1998, Chan et al. 1998) and are held together by disulfide bonds and calcium ions (Rand et al. 2000, Gordon et al. 2009).


An optional step in Pre-NOTCH processing in the Golgi is modification by fringe enzymes. Fringe enzymes are glycosyl transferases that initiate elongation of O-linked fucose on fucosylated peptides by addition of a beta 1,3 N-acetylglucosaminyl group, resulting in formation of disaccharide chains on NOTCH EGF repeats (GlcNAc-bet1,3-fucitol). Three fringe enzymes are known in mammals: LFNG (lunatic fringe), MFNG (manic fringe) and RFNG (radical fringe). LFNG shows the highest catalytic activity in modifying NOTCH (Bruckner et al. 2000, Moloney et al. 2000). Fringe-created disaccharide chains on NOTCH EGF repeats are further extended by B4GALT1 (beta-1,4-galactosyltransferase 1), which adds galactose to the N-acetylglucosaminyl group, resulting in formation of trisaccharide Gal-beta1,4-GlcNAc-beta1,3-fucitol chains (Moloney et al. 2000, Chen et al. 2001). Formation of trisaccharide chains is the minimum requirement for fringe-mediated modulation of NOTCH signaling, although fringe-modified NOTCH expressed on the cell surface predominantly contains tetrasaccharide chains on EGF repeats. The tetrasaccharide chains are formed by sialyltransferase(s) that add sialic acid to galactose, resulting in formation of Sia-alpha2,3-Gal-beta1,4-GlcNAc-beta1,3-fucitol (Moloney et al. 2000). Three known Golgi membrane sialyltransferases could be performing this function: ST3GAL3, ST3GAL4 and ST3GAL6 (Harduin-Lepers et al. 2001). The modification of NOTCH by fringe enzymes modulates NOTCH-signaling by increasing the affinity of NOTCH receptors for delta-like ligands, DLL1 and DLL4, while decreasing affinity for jagged ligands, JAG1 and JAG2.

Reaction (4 results from a total of 4)

Identifier: R-HSA-3656258
Species: Homo sapiens
Compartment: Golgi membrane, Golgi lumen
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (ST3GAL3) mediates the transfer of sialic acid from CMP-sialic acid to galactose-containing glycoproteins and forms the sialyl Lewis, an epitope on proteins which are required for attaining and/or maintaining higher cognitive functions. Some defects in ST3GAL3 result in mental retardation, autosomal recessive 12 (MRT12; MIM:611090), a disorder characterised by below average general intellectual function and impaired adaptative behaviour. Another defect of ST3GAL3 can cause early infantile epileptic encephalopathy-15 (EIEE15: MIM:615006), resulting in severe mental retardation.

In two ST3GAL3 homozygous mutations causing MRT12, A13D and D370Y, most of the mutant protein was improperly localized to the endoplasmic reticulum. This prevented the protein from interacting with its substrates in the Golgi, resulting in a loss of function and loss of the sialyl Lewis, an epitope important for higher cognative functions (Najmabadi et al. 2007, Hu et al. 2011). Another homozygous mutation, A320P, causing EIEE15, functional expression studies showed a 75% reduction in the secretion of the mutant protein and no detectable enzymatic activity (Edvardson et al. 2012). This mutation affects the highly conserved sialyl motif S, which is crucial for binding both donor and acceptor substrates.
Identifier: R-HSA-9603987
Species: Homo sapiens
Compartment: Golgi lumen, Golgi membrane
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (ST3GAL3), located on the Golgi membrane, mediates the transfer of sialic acid (Neu5Ac, N-acetylneuraminic acid) in an α2,3 linkage to the terminal galactose of Gal-beta-1,3-GlcNAc- and Gal-beta-1,4-GalNAc- sequences found on glycoproteins and glycolipids (Kitagawa & Paulson 1993). The product, Type 1 monosialylgalactosylgloboside (Type 1 MSGG) is the precursor to sialyl Lewis a (sLeA) (also known as the CA19-9 antigen), a tumour marker that is used primarily in the management of pancreatic cancer. Increased sialylation has been observed to be associated with malignant transformation and metastasis.
Identifier: R-HSA-9605600
Species: Homo sapiens
Compartment: Golgi lumen, Golgi membrane
The alpha-2,3-sialyltransferases ST3GAL3,4 and 6 (Kitagawa & Paulson 1993, Okajima et al. 1999, Kitagawa & Paulson 1994) located on the Golgi membrane, mediate the transfer of sialic acid (Neu5Ac, N-acetylneuraminic acid) in an α2,3 linkage to the terminal galactose of Gal-beta-1,4-GlcNAc- sequences found on glycoproteins and glycolipids to form Type 2 monosialylgalactosylgloboside (Type 2 MSGG).

Increased sialylation has been associated with malignant transformation and metastasis. ST3GAL6 is highly expressed in patients with multiple myeloma (MM). Knockdown of ST3GAL6 has been shown to prolong survival in mice (Glavey et al. 2014).
Identifier: R-HSA-1912378
Species: Homo sapiens
Compartment: Golgi membrane, Golgi lumen
Mature fringe-modified NOTCH usually has a tetrasaccharide attached to conserved fucosylated serine and threonine residues in EGF repeats. The chemical structure of these tetrasaccharides is Sia-alpha2,3-Gal-beta1,4-GlcNAc-beta1,3-fucitol (Moloney et al. 2000). The identity of sialyltransferase(s) that add sialic acid to galactose remains unknown in this context. Based on the type of chemical bonds in the tetrasaccharide, there are three known Golgi membrane sialyltransferases that could perform this function: ST3GAL3, ST3GAL4, ST3GAL6 (Harduin-Lepers et al. 2001).
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