54829 Results for: "Markery,+d\u0142ugopisy+i+grawery&pageNo=48"

Supplier: Bioss

The GGA family of proteins (Golgi-localized, g-Adaptin ear-containing, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin. Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multi-domain proteins that bind mannose 6-phosphate receptors (MPRs). GGAs have modular structures with an N-terminal VHS (VPS27, Hrs and STAM) domain followed by a GAT (GGA and Tom1) domain, a connecting hinge segment and a C-terminal GAE (g-Adaptin ear) domain. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences. The human GGA3 gene maps to chromosome 17 and encodes a 723 amino acid protein that shares 46% sequence identity with GGA1 and 38% with GGA2.

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The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells and is comprised of more than 100 different subunits. Many of the subunits belong to a family called nucleoporins (Nups), which are characterized by the presence of O-linked-N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). gp210, also known as Nup210 (nucleoporin 210kDa) or POM210, is a 1,887 amino acid single-pass type I membrane protein that localizes to both the endoplasmic reticulum and to the nucleus, specifically within the NPC. Expressed ubiquitously with highest expression in pancreas, testis, lung, ovary and liver, gp210 functions as a nucleoporin that is capable of dimerization and is essential for the assembly, fusion and structural integrity of the NPC. gp210 exists as multiple alternatively spliced isoforms and is subject to post-translational phosphorylation.

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Glycosylphosphatidylinositol (GPI) acts as a membrane anchor for cell surface proteins. Glycosylphosphatidylinositol anchor attachment 1 protein (GPAA1), also designated GPI anchor attachment protein 1 or GAA1 protein homolog, is a membrane protein localized to the endoplasmic reticulum which is involved in GPI-anchor biosynthesis. GPAA1 is crucial for GPI-anchoring of precursor proteins and catalyzes the attachment of GPI to proteins containing a C-terminal GPR attachment signal. GAA1 contains an N-terminal signal sequence, one cAMP- and cGMP-dependent protein kinase phosphorylation site, two potential N-glycosylation sites, one leucine zipper pattern and eight putative transmembrane domains. GPAA1 is ubiquitously expressed and shows higher levels of expression in fetal tissues than in adult tissues.

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Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type.

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The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

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Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.

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BCAR1, or CAS, is an Src (MIM 190090) family kinase substrate involved in various cellular events, including migration, survival, transformation, and invasion

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Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation in breast cancer cells through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS.

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Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex. May inhibit BACE1 activity and amyloid precursor protein processing.

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Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.

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Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade.

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Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.

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LRIG2

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Cell adhesion molecule with an important role in the development of the nervous system. Involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on neurons.

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Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals.

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The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium.

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Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum.

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EXTL3 is a member of the EXT (hereditary multiple exostosin) gene family of tumor suppressors encoding glycosyltransferases involved in heparan sulfate (HS) biosynthesis. Within this family, the C-terminus is conserved between all members from C. elegans to vertebrates. EXTL3 is a ubiquitously expressed, developmentally regulated, single-pass type II membrane protein that localizes to the endoplasmic reticulum membrane. EXTL3 adds N-acetylglucosamine (GlcNAc) to the polysaccharide-protein linkage region and to the growing HS chain suggesting that it plays a role in both the initiation and elongation of HS chains. In addition, EXTL3 may act as a Reg receptor, binding Reg via its N-terminus.

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Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts.

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Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity).

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Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor-suppressor activity.

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CXorf36

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Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity).

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Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor.

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Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate, glutarate, and to a lesser extent, pimelate, 2-oxopimelate, 2-aminoadipate, oxaloacetate, and citrate.

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The catenins are ubiquitously expressed, cytoplasmic proteins that associate with E-cadherin at cellular junctions. Catenin/cadherin complexes play an important role in mediating cellular adhesion. alpha T-catenin, also referred to as VR22, is a 895-amino acid protein that is most abundantally expressed in cardiomyocytes and in the peritubular myoid cells of the testis. alpha T-catenin binds to alpha E-catenin as well as to beta-catenin, and it functions to inhibit Wnt signaling. CTNNA3, the gene that encodes for alpha-T-catenin, is located on chromosome 10, and mutations in this gene show a strong correlation to late-onset Alzheimer's disease (LOAD) as well as to dilated cardiomyopathy.

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RAB proteins are GTPases that regulate vesicular trafficking and reside in specific intracellular compartments. RAB9 has been localized to components of the endocytic/exocytic pathway. It has been implicated in the recycling of membrane receptors, such as the mannose 6-phosphate receptor from early endosomes to the trans Golgi network.

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Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes.

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The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues of various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T10 (Polypeptide N-acetylgalactosaminyltransferase 10), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, is a 603 amino acid single-pass type II membrane protein that prefers Muc5Ac and EA2 peptide substrates. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T10 is widely expressed, with highest levels found in small intestine. There are four isoforms of GalNAc-T10 that are produced as a result of alternative splicing events.

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Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.