Search results

GGPS1 is PART of the prenyltransferase family. GGPS1 is widely expressed in testis, heart and skeletal muscle, GGPS1 is localized in the cytoplasm and catalyzes the formation of geranylgeranyl pyrophosphate, a precursor of geranylgeranylated proteins and carotenoids. GGPS1 is a significant enzyme that is responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor.

Protein Phosphatase 4 Catalytic subunit (PPP4C), is a part of the Serine/threonine-protein phosphatase catalytic subunits which tskes part in dephosphorylation and regulation of HDAC3. The protein phosphatase (PP) holoenzyme is a trimeric complex compound of a regulatory subunit, a variable subunit and a catalytic subunit. 4 major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C.

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.

Mediator complex subunit 4 (MED4) is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. MED4 is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is able to activate nuclear receptors in a ligand-dependent manner. MED4 functions as a link to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. MED4 is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

RLBP1 is a 36-kD water-soluble protein that transports 11-cis-retinal or 11-cis-retinaldehyde as physiologic ligands. RLBP1 is a functional element of the visual cycle. RLBP1 gene mutations cause retinitis punctata albescens, severe rod-cone dystrophy and Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa).

Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

Phl p 12.0101 a profilin, is a minor grass pollen allergen which is involved in cytoskeleton mobility by interacting with actin filaments. It is well recognized that IgE binding can cause immune cross-reactivity with profilins of plant-derived foods and pollen profilin.

GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH act directly on pituitary somatotrophs to stimulate GH release. Growth hormone (GH) release is stimulated by a variety of synthetic secretagogues, of which growth hormone-releasing hexapeptide (GHRP-6) has been most thoroughly studied; it is thought to have actions at both pituitary and hypothalamic site.

RING1- and YY1-binding protein (RYBP) belongs to the polycomb group (PcG). RYBP interacts with MDM2 and decreases MDM2-mediated p53 ubiquitination, which leads to stabilization of p53 and an increase in p53 activity. RYBP causes cell-cycle arrest and is involved in the p53 response to DNA damage. RYBP interacts with RING1, YY1, Caspase 10, E2F3, E2F2, Mdm2, Abl gene and CBX2. RYBP inhibits ubiquitination and subsequent degradation of TP53, and thus has a role in regulating transcription of TP53 target genes. RYBP may also be involved in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. RYBP may bind to DNA, and promote apoptosis.

SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

Bone Morphogenetic protein Receptor-1B, also known as BMPR1B belongs to the TKL Ser/Thr protein kinase family. BMPR1Bis on ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate as well as activate type I receptors which autophosphorylate, afterward bind and activate SMAD transcriptional regulators. BMPR1B is receptor for BMP7/OP-1 as well as GDF5.

Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

Charged multivesicular body protein 1b (CHMP1B) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. CHMP1B is a possible peripherally associated component of the ESCRT-III (endosomal sorting required for transport complex III) which is involved in MVBs (multivesicular bodies) formation and sorting of endosomal cargo proteins into MVBs. The MVBs contain ILVs (intraluminal vesicles) which are created by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.

CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

The human cytomegalovirus UL99-encoded pp28 is a myristylated phosphoprotein that is a constituent of the virion. The pp28 protein is positioned within the tegument of the virus particle, a protein structure that resides between the capsid and envelope. In the infected cell, pp28 is found in a cytoplasmic compartment derived from the Golgi apparatus, where the virus buds into vesicles to acquire its final membrane.

GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.

Human Mucin-1 (CA15-3), aka MUC1, is a glycoprotein with extensive O-linked glycosylation of its extracellular domain. This protein has alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit roles in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Mucins line the apical surface of epithelial cells in the stomach, lungs, intestines, eyes and other tissues. Mucins protect the body from infection by pathogen binding to oligosaccharides in the extracellular domain, preventing the pathogen from reaching the cell surface. Overexpression of CA15-3 is often associated with colon, breast, ovarian, lung and pancreatic cancers.

SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.

A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.

Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.

TPMT, thiopurine S-methyltransferase, is a cytosolic enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. TPMT activity exhibits autosomal codominant genetic polymorphism, and patients inheriting TPMT-deficiency are at high risk of potentially fatal hematopoietic toxicity.

Protein Phosphatase 1F (PPM1F) is a part of the PP2C family of Ser/Thr protein phosphatases whose members are known to be negative regulators of cell stress response pathways. PPM1F interacts with Rho guanine nucleotide exchange factors (PIX), and as a result blocks the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is one of the substrates of PPM1F. PPM1F is found to be an apoptosis Promoter.