Search results

Dynein light chain roadblock-type 2 (DYNLRB2) functions as one of several non-catalytic accessory components of the cytoplasmic dynein complex which are considered to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.

Single-strand-selective monofunctional uracil-DNA glycosylase (SMUG1) is an enzyme responsible for recognizing base lesions in the genome and initiating base excision DNA repair. SMUG1 participates in base excision repair by removing uracil from single- and double-stranded DNA. SMUG1 serves as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has inclination for single-stranded DNA substrates. SMUG1 activity is greater against mismatches (U/G) than against matches (U/A).

Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.

SULT1B1 enzyme in humans is encoded by the SULT1B1 gene. SULT1B1 holds a binding site for 3-prime-phosphoadenosine 5-prime-phosphosulfate, a sulfate donor, in addition to a cysteine residue conserved in the ST1 gene family of sulfotransferases. Sulfotransferases like SULT1B1 catalyze the biotransformation of a great amount of endogenous amalgams such as bile acids, neurotransmitters, steroids, and thyroid hormones, in addition to drugs and xenobiotics.

PECI is an enzyme that localized to the peroxisomal matrix and encloses one ACB (acyl-CoA-binding) domain. PECI is expressed abundantly in liver, heart and skeletal muscle. PECI functions to catalyze the isomerization of both 3-cis and 3-trans double bonds into the 2-trans form in an array of enoyl-CoA species. PECI takes part in the beta-oxidation of unsaturated fatty acids.

The protein kinase A holoenzyme is a heterotetramer composed of two types of subunits: Catalytic and Regulatory. The Catalyticsubunit contains the enzyme's active site. It also contains a domain that binds ATP and a domain that binds the regulatory subunit. The Regulatory subunit consists oftwo molecules which bind one another in an anti-parallel orientation to form a homodimer; for type I subunits- this binding is covalent via disulfide bonds. This subunit also has has two domains that bind cyclic AMP, a domain that interacts with a catalytic subunit, and an "auto-inhibitory" domain that serves as a substrate or pseudosubstrate for the catalytic subunit. Regulatory subunits may also have biologic activity distinct from their role in modulating catalytic subunit activity. Regulatory subunits exist in two major forms, RI and RII, with each form having two subtypes designated alpha and beta. Each of the four isotypes of the regulatory subunit is encoded by a different gene. In addition, three isotypes of the catalytic subunit have been identified (alpha, beta and gamma). The different isotypes tend to have different distributions within cells and among tissues. Type I enzymes inhabit cytoplasmic, soluble fractions of the cell, whereas type II enzymes tend to associate with cellular membranes.

PNMT is an enzyme located in the adrenal medulla and it catalyzes the final step of the catecholamine biosynthesis pathway. PNMT has beta-carboline 2N-methyltransferase activity. PNMT takes part in regulating epinephrine production. Glucocorticoid receptors form multimers of PNMT independent of the DNA binding domain. PNMT expression is regulated late in mouse gestation by AP2-alpha and glucocorticoids.

TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

Protein Phosphatase 1, Regulatory Subunit 3B (PPP1R3B) is the catalytic subunit of the serine/theonine phosphatase, protein phosphatase-1. PPP1R3B, which is expressed both in liver and in skeletal muscle tissue, regulates glycogen synthesis in these tissues. PPP1R3B is involved in type 2 diabetes and maturity-onset diabetes of the young.

Glycerol-3-phosphate dehydrogenase 1-like protein (GPD1L) converts sn-glycerol 3-phosphate to glycerone phosphate. GPD1L is found in the cytoplasm, associated with the plasma membrane, where it binds the sodium channel, voltage-gated, type V, alpha subunit (SCN5A). Mutations in the GPD1L gene are the cause of SIDS (sudden infant death syndrome) and Brugada syndrome type 2 (an autosomal dominant tachyarrhythmia).

Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.

Prostaglandin Reductase 1 (PTGR1) is a member of the NADP-dependent oxidoreductase L4BD family. PTGR1 catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4, thus being a primary step of metabolic inactivation of leukotriene B4. PTGR1 is highly expressed in the kidney, liver, and intestine but not in leukocytes.

PTPN6 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.

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.

QPRT is a key enzyme in the catabolism of quinolinate. QPRT is in between the tryptophannicotinamide adenine dinucleotide (NAD) pathway, resulting in the production of nicotinic acid, carbon dioxide and pyrophosphate. Rise of QPRT levels in the brain is related to the pathogenesis of neurodegenerative disorders such as epilepsy, Alzheimer's disease, and Huntington's disease.

REV1 Polymerase (REV1) contains a BRCT domain, which is imperative in protein-protein interactions. REV1 is a deoxycytidyl transferase involved in DNA repair. REV1 assists in the 1st step in the bypass of abasic lesions by the incorporation of a nucleotide opposite the lesion. REV1 is essential for normal generation of mutations by physical and chemical agents. REV1 transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. A role for the human Rev1-like protein has been suggested as a scaffold which recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA.

CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.

Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3) belongs to the cyclophilin family which catalyzes the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. PPIL3 acts either as catalyst or as molecular chaperone in protein-folding events.

UDP Glycosyltransferase 8 (UGT8) is a member of the UDP-glycosyltransferase family. UGT8 catalyzes the transfer of galactose to ceramide, a crucial enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.

SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Flagellin FliA (H), also known as RNA polymerase sigma factor for flagellar operon, Sigma F and Sigma-28, is a part of the FliA subfamily or sigma-70 factor family. This sigma factor controls the expression of flagella-related genes. Flagellin FliA (H) regulates the expression of genes involved in virulence. Flagellin FliA (H) is an initiation factors which endorses the attachment of RNA polymerase to specific initiation sites and are then released.