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Description:
Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107). During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (By similarity). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity).
Description:
FUNCTION: Involved in the production of GD3 and GT3 from GM3. CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-N-acetylneuraminyl-2,3-beta-D-galactosyl-R = CMP + beta-N-acetylneuraminyl-2,8-beta-N-acetylneuraminyl-2,3-beta-D-galactosyl-R. SIMILARITY: Belongs to the glycosyltransferase 29 family. PATHWAY: Glycosylation. SUBCELLULAR LOCATION: Golgi apparatus; Golgi membrane; single-pass type II membrane protein
Description:
ST3GAL2 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A.
Description:
CMPK2 Antibody: UMP-CMP kinase 2 (CMPK2) is the first nucleoside monophosphate kinase that has been identified in human mitochondria. It is a component of the salvage pathway for nucleotide synthesis that may participate in terminal differentiation of monocytic cells. There are two distinct domains of CMPK2: the N-terminal domain with unknown function and the C-terminal domain with the kinase function, suggesting that CMPK2 may be a bifunctional protein with other biological functions in addition to its UMP-CMP kinase activity. CMPK2 may participate in dUTP and dCTP synthesis and is responsible for phosphorylation of dCMP and dUMP in mitochondria. CMPK2 is actively involved in macrophage activation and the inflammatory response
Description:
ST3GAL3 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. ST3GAL3 is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Multiple transcript variants encoding several different isoforms have been found for this gene.
Description:
Pyrimidine 5-prime-nucleotidase (P5N), also called uridine 5-prime monophosphate hydrolase (UMPH), catalyzes the dephosphorylation of the pyrimidine 5-prime monophosphates UMP and CMP to the corresponding nucleosides. There are 2 isozymes of pyrimidine 5-prime nucleotidase in red blood cells, referred to as type I (UMPH1) and type II (UMPH2). The 2 enzymes are not separable by electrophoresis in humans but have distinct kinetic properties, and the proteins show no homology. Pyrimidine 5-prime-nucleotidase (P5N; EC 3.1.3.5), also called uridine 5-prime monophosphate hydrolase (UMPH), catalyzes the dephosphorylation of the pyrimidine 5-prime monophosphates UMP and CMP to the corresponding nucleosides. There are 2 isozymes of pyrimidine 5-prime nucleotidase in red blood cells, referred to as type I (UMPH1) and type II (UMPH2; MIM 191720). The 2 enzymes are not separable by electrophoresis in humans but have distinct kinetic properties, and the proteins show no homology.
Description:
ST3GAL3 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. ST3GAL3 is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Multiple transcript variants encoding several different isoforms have been found for this gene.
Description:
ST8SIA2 is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. ST8SIA2 may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.
Description:
CMAS is an enzyme that catalyzes the activation of Neu5Ac to Cytidine 5-prime-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), which provides the substrate required for the addition of sialic acid. Sialic acids of cell surface glycoproteins and glycolipids play a pivotal role in the structure and function of animal tissues. The pattern of cell surface sialylation is highly regulated during embryonic development, and changes with stages of differentiation. Studies of a similar murine protein suggest that this protein localizes to the nucleus.The enzyme encoded by this gene catalyzes the activation of Neu5Ac to Cytidine 5-prime-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), which provides the substrate required for the addition of sialic acid. Sialic acids of cell surface glycoproteins and glycolipids play a pivotal role in the structure and function of animal tissues. The pattern of cell surface sialylation is highly regulated during embryonic development, and changes with stages of differentiation. Studies of a similar murine protein suggest that this protein localizes to the nucleus.
Description:
alpha-N-Acetylneuraminide alpha-2,8-Sialyltransferase (ST8SIA1) belongs to the glycosyltransferase 29 family. ST8SIA1 is a sialytransferase that catalyzes the transfer of sialic acid from CMP-sialic acid to GM3 to produce GD3 and GT3. ST8SIA1 is highly expressed in melanoma cell lines, adult and fetal brain, low expressed in adult and fetal lung. ST8SIA1 may act as a type II transmembrane protein with a short N-termianl cytoplasmic domain and a single-pass transmembrane domain folowed by an enzymatic domain in the lument of the Golgi apparatus.
Description:
ST6GALNAC4 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. ST6GALNAC4 prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. ST6GALNAC4 is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. It is a member of glycosyltransferase family 29.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Transcript variants encoding different isoforms have been found for this gene.
Description:
ST3gal6 Antibody: Sialyltransferases catalyze the transfer of sialic acid from cytidine 5-prime monophospho-N-acetylneuraminic acid (CMP-NeuAc) to terminal positions of glycoprotein and glycolipid carbohydrate groups. Terminal NeuAc residues are key determinants of carbohydrate structures, such as the sialyl-Lewis X determinants, and are widely distributed in many cell types. However, cancer cells often express more heavily sialylated glycans on their cell surface and this feature sometimes correlates with invasiveness. In contrast, expression of ST3gal6, a member of the sialyltransferase family that sialylates type II lactosamine structures on glycoproteins and glycolipids, was found to be significantly decreased by hypermethylation of the gene in gastrointestinal cancer. At least three isoforms of ST3gal6 are known to exist.
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