Search results

NUDT5 is part of the nudix hydrolase family which remove toxic nucleotide derivatives from the cell. NUDT5 hydrolyzes ADP-ribose and ADP-mannose in the presence of magnesium, and in addition hydrolyzes nucleotide sugars with decreasing activity such as ADP-glucose and diadenosine diphosphate. As a nudix hydrolase, NUDT5 holds a central nudix motif and functions to eliminate toxic nucleotide metabolites from the cell while maintaining the levels of signaling nucleotides.
NUDT5 is broadly expressed but is most abundant in liver as a homodimer.

PARP1 takes part in the base excision repair pathway, by catalyzing the poly ADP-ribosyl of a restricted number of acceptor proteins involved in chromatin architecture and in DNA metabolism.. PARP1 mediates the poly ADP-ribosy of APLF and CHFR. PARP1 positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. PARP1 is a chromatin-associated enzyme, poly (ADP-ribosyl) transferase, which modifies various nuclear proteins by poly ADP-ribosyl. PARP1 takes part in the regulation of various significant cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. PARP1 is a site of mutation in Fanconi anemia, and is involved in the pathophysiology of type I diabetes.

Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily.

Immunity-related GTPase family M protein (IRGM) is essential for clearance of severe protozoan and bacterial infections. IRGM belongs to the p47 immunity-related GTPase family. IRGM serves in innate immune response possibly via regulation of autophagy. IRGM regulates proinflammatory cytokine production and inhibit endotoxemia upon infection and also has a part in macrophages adhesion and motility. Polymorphisms which modify the natural expression of the IRGM gene are associated with a susceptibility to Crohn's disease and tuberculosis.

FGFR1OP N-terminal like (FOPNL) is a member of the FGFR1OP family and contains 1 LisH domain. FOPNL is participates in the biogenesis of cilia. FOPNL is extensively expressed and detected in the brain, heart, kidney, liver, lung, skeletal muscle, placenta and the intestine.

Tumor Protein P53 Regulated Apoptosis Inducing Protein 1 (TP53AIP1) is expressed mainly in the thymus, and is localized to the mitochondrion. p53 induces TP53AIP1 production which then mediates p53- dependent apoptosis. Alternatively spliced transcript variants encoding diverse isoforms are known for TP53AIP1.

Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

CENPH is a member of the centromere protein H family. CENPH protein is a component of the CENPA-NAC (nucleosome-associated) complex which has a vital part in assembly of kinetochore proteins. The CENPA-NAC complex utilizes the CENPA-CAD (nucleosome distal) complex and is involved in integration of freshly synthesized CENPA into centromeres.

GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 (PRPSAP2) is a protein which relates with the enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes the formation of phosphoribosylpyrophosphate which is a substrate for synthesis of purine, pyrimidine, histidine, tryptophan and NAD. PRS is a complex with 2 catalytic subunits and 2 associated subunits. PRPSAP2 encodes a non-catalytic associated subunit of PRS.

UFM1 is a ubiquitin-like protein which is conjugated to target proteins by E1-like activating enzyme UBA5 and E2-like conjugating enzyme UFC1 in a manner equivalent to ubiquitylation. UFM1 localizes principally to the nucleus, but is also present in diffuse amounts in the cytoplasm. UFM1 is expressed in a variety of tissues, including kidney, brain, heart, liver and lung.

GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.

PSMG4 is a chaperone protein that enhances assembly of the 20S proteasome. PSMG4 cooperates with alpha and beta subunits of the 20S proteasome and with PSMG3 but disconnects when the POMP is recruited before the formation of half-proteasomes.

Synaptobrevin 1(Vehicle-associated membrane, VAMP1) is one of the key proteins in the SNARE complex which is involved in regulated exocytosis. Synaptobrevin1 binds to t-SNAREs, syntaxin (STX) and SNAP25, after the fusion of synaptic vesicles to plasma membrane.

VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.

Microtubule-associated proteins 1A/1B light chain 3 beta 2 (MAP1LC3B2) is a member of the MAP1LC3 family. MAP1LC3B2 is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and essential for neurogenesis. The MAP1LC3B2 protein is possibly involved in formation of autophagosomal vacuoles (autophagosomes). MAP1LC3B2 is expressed primarily in the heart, testis, brain and skeletal muscle.

RBBP9, restricts to the nucleus and cytoplasm, is a retinoblastoma binding protein which takes part in the regulation of cell proliferation and differentiation. RBBP9 cooperates with retinoblastoma (Rb) and offers cellular resistance to the growth-inhibitory effects of TGFbeta1, therefore enabling the cellular transformation process.

Ribosomes are the organelles which catalyze protein synthesis, they’re comprised of a small 40S subunit and a large 60S subunit. Ribosomal Protein L11 (RPL11) is a member of the L5P family of ribosomal proteins. RPL11 is a ribosomal protein which is a component of the 60S subunit. RPL11 is found in the cytoplasm. The RPL11 protein most likely associates with the 5S rRNA.

HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

NHP2L1 is a member of the ribosomal protein L7Ae family. NHP2L1 protein limited to the nucleus, primarily focused in the dense fibrillar component of the nucleolus. NHP2L1 directly binds to the 5' stem-loop of U4 snRNA and has a vital part in the late stage of spliceosome assembly, prior to step I of splicing catalysis.

Glycolipid transfer protein (GLTP) accelerates the intermembrane transfer of different glycolipids. GLTP catalyzes the transfer of various glycosphingolipids between membranes however does not catalyze the transfer of phospholipids. GLTP is involved in the intracellular translocation of glucosylceramides. The GLTP protein is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. GLTP is assumed to be a cytoplasmic protein. GLTP is detected in fibroblasts and in various cancer cell lines.

GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.