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Description:
Eph receptor A2 is the receptor for members of the ephrin-A family. It binds to ephrin-A1, -A3, -A4 and -A5. Eph receptor A3 is also a receptor for members of the ephrin-A family. It binds to ephrin-A2, -A3, -A4 and -A5 and is thought to play a role in lymphoid function. Eph receptor A4 is a receptor for members of the ephrin-A family. It binds to ephrin-A1, -A4 and -A5. It binds more poorly to ephrin-A2 and -A3. It may play a role in a signal transduction process involved in hindbrain pattern formation.
Description:
PLSCR3 (phospholipid scramblase 3) may mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. Members of this family, PLS1 and PLS3 are both substrates of Protein kinase C (PKC) delta and are phosphorylated by PKC-delta during apoptosis. PKC-delta translocates to mitochondria during apoptosis and phosphorylates PLS3. Overexpression of PLS3 in the HEK293 cells enhanced apoptosis induced by UV-irradiation.
Description:
As a major event in type â… allergic reaction,degranulation of mast cells is triggered by the interaction between specific IgEs and high affinity IgE receptors (FcεRIs) on mast cell membrane,and is followed by the release of a battery of inflammatory mediators,such as histamine,leukotrienes and arachidonic acid,and these inflammatory mediators in turn induce a series of allergic symptoms.Recently,Allergin-1 has been found to be an immunoglobulin-like receptor preferentially expressed on mast cells.The crosslinking of Allergin-1 to FcεRIs on mast cells may inhibit the signal transduction from FcεRIs to intracellular immunoreceptor tyrosine-based inhibitory motif (ITIM),generate ITIM inhibitory signals,which then participate in the regulation of mast cell degranulation,and finally block the initiation of allergic inflammation.
Description:
Tau proteins are important Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Tau proteins subcellular located in the axons of neurons, in the cytoso l and in association with plasma membrane components. It expressed in neurons. PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.
Description:
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains.
Description:
The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq].
Description:
C9 is a plasma protein synthesized in the liver and monocytes consisting of a single polypeptide chain. C9 is a part of the membrane attack complex (MAC), an important component of the immune system. The MAC forms upon complement system activation by invading pathogenic bacteria and consists of the four major complement proteins: C5b, C6, C7 and C8. These complement proteins bind to the outer surface of the plasma membrane of the invading cell. C9 binds to the membrane associated C5b-8 protein, which leads to the circular polymerization of 12-18 C9 molecules. These polymerized C9 molecules form a ring structure in the membrane. Molecules can then diffuse freely through this transmembrane channel, causing cell lysis and destruction of the invading bacterial cell.
Description:
Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2.
Description:
Integrin alpha-M/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain.
Description:
HD-PTP is a 1636 amino acid protein encoded by the human gene PTPN23. HD-PTP belongs to the protein-tyrosine phosphatase family, non-receptor class subfamily. It contains one BRO1 domain, two TPR repeats and one tyrosine-protein phosphatase domain. The C-terminal region contains the PTP-like domain, whereas the N-terminal region contains the two TPR regions. These regions are homologous to the yeast protein, BRO1, which is involved in the mitogen-activated protein kinase signaling pathway. Similarly, HD-PTP is believed to act as a negative regulator of Ras-mediated mitogenic activity and is phosphorylated upon DNA damage, probably by ATM or ATR. HD-PTP protein is differentially modulated by two angiogenic growth factors. While Vascular Endothelial Growth Factor (VEGF) has no affect on protein levels, Fibroblast Growth Factor-2 (FGF-2) induces HD-PTP degradation via the proteasome system.
Description:
HD-PTP is a 1636 amino acid protein encoded by the human gene PTPN23. HD-PTP belongs to the protein-tyrosine phosphatase family, non-receptor class subfamily. It contains one BRO1 domain, two TPR repeats and one tyrosine-protein phosphatase domain. The C-terminal region contains the PTP-like domain, whereas the N-terminal region contains the two TPR regions. These regions are homologous to the yeast protein, BRO1, which is involved in the mitogen-activated protein kinase signaling pathway. Similarly, HD-PTP is believed to act as a negative regulator of Ras-mediated mitogenic activity and is phosphorylated upon DNA damage, probably by ATM or ATR. HD-PTP protein is differentially modulated by two angiogenic growth factors. While Vascular Endothelial Growth Factor (VEGF) has no affect on protein levels, Fibroblast Growth Factor-2 (FGF-2) induces HD-PTP degradation via the proteasome system.
Description:
HD-PTP is a 1636 amino acid protein encoded by the human gene PTPN23. HD-PTP belongs to the protein-tyrosine phosphatase family, non-receptor class subfamily. It contains one BRO1 domain, two TPR repeats and one tyrosine-protein phosphatase domain. The C-terminal region contains the PTP-like domain, whereas the N-terminal region contains the two TPR regions. These regions are homologous to the yeast protein, BRO1, which is involved in the mitogen-activated protein kinase signaling pathway. Similarly, HD-PTP is believed to act as a negative regulator of Ras-mediated mitogenic activity and is phosphorylated upon DNA damage, probably by ATM or ATR. HD-PTP protein is differentially modulated by two angiogenic growth factors. While Vascular Endothelial Growth Factor (VEGF) has no affect on protein levels, Fibroblast Growth Factor-2 (FGF-2) induces HD-PTP degradation via the proteasome system.
Description:
Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.
Description:
Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.
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