Search results

SNRPB is one of several nuclear proteins which are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the SNRPB protein may also have a role in pre-mRNA splicing or snRNP structure. SNRPB binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner. SNRPB functions in the U7 snRNP complex which is involved in histone 3'-end processing.

NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.

PGK2 is a testis-specific form of phosphoglycerate kinase. Originally presumed to be a pseudogene, the PGK2 protein is actually a functional phosphoglycerate kinase which catalyzes the reversible conversion of 1,3-bisphosphoglycerate to 3-phosphoglycerate, during the Embden-Meyerhof-Parnas pathway of glycolysis, in the later stages of spermatogenesis. The PGK2 gene is intronless, results from retrotransposition of the phosphoglycerate kinase 1 gene, and is expressed specifically in the testis.

PSMA6 belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. PSMA6 is spread all over eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway.

HINT1, also known as Histidine triad nucleotide-binding protein 1 is part of the superfamily named for a near C-terminal HXHXHXX motif (H:Histidine, X:a hydrophobic amino acid) positioned at the ?-phosphate of nucleotide substrates. HINT1 hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. Though it was initially considered to be a protein kinase C inhibitor and act as a haplod-insufficient tumor suppressor including spontaneous tumor formation in Hint+/- and Hint-/- , its actual physiologic function is not known.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

Nucleophosmin (NPM1) is a phosphoprotein which shuffles between the nucleus and the cytoplasm. NPM1 is assumed to be involved in a number of processes including regulation of the ARF/p53 pathway. Several genes fusion partners have been described, particularly the anaplastic lymphoma kinase gene on chromosome 2. NPM1 gene mutations are linked with acute myeloid leukemia.

Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

Lymphokine-activated killer T-cell-originated protein kinase (PBK) is a serine/threonine kinase related to the dual specific mitogen-activated protein kinase (MAPKK) family. PBK is abundant in placenta (is also found in the testis’ outer cell layer of seminiferous tubules) and absent from adult brain tissue. PBK is involved in the activation of lymphoid cells and supports testicular functions, with a possible role in the process of spermatogenesis. Mitotic phosphorylation is required for PBK’s catalytic activity. Once phosphorylated,PBK forms a complex with TP53, leading to TP53 destabilization and weakening of G2/M checkpoint during some kind of DNA damage. PBK is active only during mitosis. In addition, a PDZ domain in the tumor suppressor protein Dlg can coordinate with the T/SXV motif of PBK. PBK also phosphorylates MAP kinase p38, and may have a role in the activation of lymphoid cells.

PCDHGL4 belongs to one of three related clusters tandemly linked on chromosome five - the protocadherin gamma gene cluster. These gene clusters have an immunoglobulin-like organization, which indicates that a novel mechanism takes part in their regulation and expression. These neural cadherin-like cell adhesion proteins have a vital role in the establishment and function of specific cell-cell connections in the brain.

CBX5 belongs to the heterochromatin protein family. CBX5 is enriched in the heterochromatin and linked with centromeres. CBX5 takes part in the creation of functional kinetochore by interaction with important kinetochore proteins. CBX5 has a pseudogene situated on chromosome 3. Additionaly, The CBX5 proteins reconnect with chromatin at the end of mitosis, as Histone H3 is dephosphorylated.

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.

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

Polymerase (RNA) II (DNA directed) Polypeptide C (POLR2C) is the 3rd largest subunit of RNA polymerase II. The product of POLR2C consists of a cysteine rich area and exists as a heterodimer with an additional polymerase subunit, POLR2J. Those 2 subunits shape a core subassembly unit of the polymerase.

PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. Inhibition of PPP1R14A results to increased myosin phosphorylation and enhances smooth muscle contraction in the absence of increased intracellular Ca(2+) concentration. Myosin phosphatase can reverse MYL (myosin light chain) phosphorylation to induce a state of relaxation. However, during agonist-induced contraction at constant Ca2+ concurrent inhibition of myosin phosphatase leads to increases in MYL phosphorylation and tension. These calcium-independent increases in myosin phosphorylation and tension are termed calcium sensitization.
Human pregnancy is characterized by the increases of PKN1 expression and CPI-17 phosphorylation in the myometrium. PPP1R14A is mapped to chromosome 19q13.13-q13.2.
PPP1R14A binds directly to protein kinase C and casein kinase I.
PPP1R14A siRNA decreased the level of merlin phosphorylation and consequently Ras and ERK activity in human tumor cell lines.
PKC/CPI-17 mediated pathway in histamine, triggeres cytoskeletal rearrangements causing lung microvascular barrier compromise.

Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.

cAMP-dependent protein kinase type II-alpha regulatory subunit (PRKAR2A) can be phosphorylated by the activated catalytic subunit. PRKAR2A interacts with numerous A-kinase anchoring proteins and regulates the subcellular localization of cAMP-dependent protein kinase.

RAC2 is a small signaling G protein/GTPase which is part of the RAS superfamily of small GTP-binding proteins which regulate cell growth, actin cytoskeletal organization, cell proliferation, survival, cell cycle progression, gene transcription rgulation and the activation of protein kinases. RAC2 cycles between an active gtp-bound and inactive gdp-bound state. In active state, RAC2 binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. RAC2 is involved in the regulation of the nadph oxidase.

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.

NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

Nicotinamide Nucleotide Adenylyltransferase 2, also known as NMNAT2 is a member of the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze a vital step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; NMNAT2 is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for NMNAT2. Among the diseases associated with NMNAT2 are tauopathy, and systemic lupus erythematosus.

Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).

Serine/Threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA) is crucial for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. The PPP1CA protein may have a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.