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Description:
Sorting nexin (SNX) proteins are members of a large family of hydrophilic PX (phospholipid-binding motif) domain-containing proteins that interact with a variety of receptor types. SNXs are widely expressed, although the tissue distribution of each SNX mRNA varies. The ability of SNXs to bind specific phospholipids, as well as their tendency to form protein-protein complexes, suggests a role for these proteins in cellular membrane trafficking and protein sorting. SNXs may also function specifically in pro-degradative sorting, internalization, endosomal recycling or simply in endosomal sorting. SNX10 (Sorting nexin-10) is a 201 amino acid protein that contains one phox domain and belongs to the SNX family. Like other members of the SNX family, SNX10 is thought to play a role in intracellular trafficking events throughout the cell.
Description:
Sorting nexin (SNX) proteins are members of a large family of hydrophilic PX (phospholipid-binding motif) domain-containing proteins that interact with a variety of receptor types. SNXs are widely expressed, although the tissue distribution of each SNX mRNA varies. The ability of SNXs to bind specific phospholipids, as well as their tendency to form protein-protein complexes, suggests a role for these proteins in cellular membrane trafficking and protein sorting. SNXs may also function specifically in pro-degradative sorting, internalization, endosomal recycling or simply in endosomal sorting. SNX10 (Sorting nexin-10) is a 201 amino acid protein that contains one phox domain and belongs to the SNX family. Like other members of the SNX family, SNX10 is thought to play a role in intracellular trafficking events throughout the cell.
Description:
The product of this gene is a member of the nuclear factors of activated T cells family of transcription factors. Proteins belonging to this family play a central role in inducible gene transcription during the immune response. This protein regulates gene expression induced by osmotic stress in mammalian cells. Unlike monomeric members of this protein family, this protein exists as a homodimer and forms stable dimers with DNA elements. Multiple transcript variants encoding different isoforms have been found for this gene.
Description:
The product of this gene is a member of the nuclear factors of activated T cells family of transcription factors. Proteins belonging to this family play a central role in inducible gene transcription during the immune response. This protein regulates gene expression induced by osmotic stress in mammalian cells. Unlike monomeric members of this protein family, this protein exists as a homodimer and forms stable dimers with DNA elements. Multiple transcript variants encoding different isoforms have been found for this gene.
Description:
Endothelins (ET) show potent constrictor activity in vascular and non-vascular smooth muscle. This family of 21-amino acid peptides exists in at least three isoforms - ET-1, ET-2, and ET-3, and is produced in endothelial and epithelial cells. ET's can mediate biological effects in cells and tissues, and have been shown to bind to an ET receptor in the lung, kidney, heart, and liver. Endothelin 1 is expressed in lung, placental stem villi vessels and in cultured placental vascular smooth muscle cells.
Description:
Cytidine is a nucleoside formed by a cytosine attached to a ribose ring via a beta-N1-glycosidic bond. DNA is methylated on cytidines by DNA methylases (DNMTs)to generate 5-methylcytidine (5-mC), a potent epigenetics marker and regulator of gene expression. The reverse reaction (cytidine demethylation) starts with its oxidation to hydroxymethyl- (5-hmC), formyl- (5-fC), and carboxy- (5-caC) cytidine. Several enzymes, including the Tet family of proteins have been implicated in cytidine demethylation.
Description:
DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate.The loss of DMP-1 can result in hypomineralized bone.
Description:
The protein encoded by this gene is a member of the dual specificity protein kinase family, which acts as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This protein kinase lies upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As an essential component of MAP kinase signal transduction pathway, this kinase is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development.
Description:
Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs (also designated synaptobrevins), including VAMP-1 and VAMP-2, and synaptotagmin, a protein that may function as an inhibitor of exocytosis, are vesicular proteins.
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF185 (ring finger protein 185), also known as FLJ38628, is a 192 amino acid multi-pass membrane protein containing one RING-type zinc finger. Two RNF185 isoforms exist as a result of alternative splicing, and the gene encoding RNF185 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.
Description:
Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs (also designated synaptobrevins), including VAMP-1 and VAMP-2, and synaptotagmin, a protein that may function as an inhibitor of exocytosis, are vesicular proteins.
Description:
The ring finger is a specialized type of zinc finger of 40 to 60 residues that binds two atoms of zinc and mediates protein-protein interactions. There are five known isoforms of RNF170.
Description:
MYBPC3 encodes the cardiac isoform of the thick-filament myosin-binding protein C. It is found in the crossbridge-bearing zone (C region) of A bands in vertebrate striated muscle. Regulatory phosphorylation of MYBPC3 by cAMP-dependent protein kinase (PKA) upon adrenergic stimulation may be linked to modulation of cardiac contraction. MYBPC3 binds F-Actin, MHC and native thin filaments, and modifies the activity of Actin-activated myosin ATPase. Mutations in the MYBPC3 gene lead mainly to truncation of the protein, which results in one cause of familial hypertrophic cardiomyopathy type 4 (CMH4), a heart disorder characterised by ventricular hypertrophy, which often involves the interventricular septum and is usually asymmetric. The MYBPC3 gene maps to chromosome 11p11.2.
Description:
COPA (alpha-coat protein) is processed to produce Xenin. Xenin stimulates exocrine pancreatic secretion to affect small and large intestinal motility, and inhibits pentagastrin-stimulated secretion of acid. In the gut, Xenin interacts with the neurotensin receptor. Membrane and vesicular trafficking in the early secretory pathway are mediated by non-Clathrin COP (coat protein) I-coated vesicles. COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, is composed of two subcomplexes. The first consists of the COPB, COPG, COPD and COPZ subunits (also known as b-, g-, d- and z-COP, respectively), which are distantly homologous to AP Clathrin adaptor subunits. The second consists of the COPA, b'-COP and COPE subunits (also known as a-COP, COPP and e-COP, respectively).
Description:
E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation.
Description:
May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth (By similarity). Overexpression of HYAL1 suppressed the growth rate of colon carcinoma cell tumors in an experimental model.
UOM:
1 * 100 µl
Promotion
,BOSSBS-1235R-CY5EA
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