Search results

SYT13 belongs to the great synaptotagmin protein family which contain 2 domains: cytoplasmic C terminus with two tandem C2 domains (C2A and C2B) and extracellular N-terminal transmembrane domain. Synaptotogmin family members have dissimilar biochemical properties and developmental profiles, and patterns of tissue distribution. Additionally, Synaptotogmins formulate homo- and heteromeric complexes with each other. Synaptotagmins operate as membrane traffickers in multicellular organisms.

Marginal zone B- and B1-cell-specific protein (MZB1) functions as a hormone-regulated adipokine/proinflammatory cytokine which is implicated in causing chronic inflammation and affecting cellular expansion. MZB1 links with immunoglobulin M (IgM) heavy and light chains and stimulate s IgM assembly and secretion. MZB1 exerts its effect by acting as a molecular chaperone or as an oxidoreductase as it exhibits a low level of oxidoreductase activity. MZB1 helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.

VCPKMT is a member of the methyltransferase superfamily. VCPKMT is a protein-lysine N-methyltransferase which specifically trimethylates 'Lys-315' of VCP/p97; this alteration reduces VCP ATPase activity.

Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

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.

Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

Bestrophin 1 (BEST1) is a part of the bestrophin gene family and is also forms calcium-activated chloride-ion channels in epithelial. This small gene family is characterized by proteins with a highly conserved N-terminus with 4-6 transmembrane domains. BEST1 is extremely permeable to bicarbonate.

Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.

UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.

RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.

STIM1 is a type-1 transmembrane protein that is necessary for store-operated Ca(2+) entry, a process of extracellular Ca(2+) influx in response to the depletion of Ca(2+) stores in the endoplasmic reticulum (ER). STIM1 localizes predominantly to the ER; upon Ca(2+) release from the ER, STIM1 translocates to the ER-plasma membrane junctions and activates Ca(2+) channels. STIM1 is an adhesion molecule involved in early hematopoiesis by mediating attachment to stromal cells. STIM1 controls the survival and/or proliferation of b-cell precursors. STIM1 gene is one of several genes located in the imprinted gene domain of 11p15.5, a significant tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. STIM1 is involved in malignancies as well as early hematopoiesis, by mediating attachment to stromal cells. STIM1 is oriented in a head-to-tail configuration with the ribonucleotide reductase 1 gene (RRM1), with the 3' end of this gene situated 1.6 kb from the 5' end of the RRM1 gene.

TPM1 is a member of the tropomyosin family which consists of a number of extremely conserved, extensively distributed 35-45 kDa actin-binding proteins that are involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin-1 is composed of 2 alpha-helical chains arranged as a coiled-coil. TPM1 is polymerized end to end alongside the two grooves of actin filaments and provides stability to the filaments. TPM1 binds to actin filaments in muscle and non-muscle cells. TPM1 also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In non-muscle cells TPM1 is implicated in stabilizing cytoskeleton actin filaments. Smooth muscle contraction is controlled by interaction with caldesmon.
Alternatively spliced transcript variants encoding a range of isoforms have been described in smooth muscle and non-muscle cells. TPM1 Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues, whereas Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle.
Mutations in the TPM1 gene are linked to type 3 familial hypertrophic cardiomyopathy.

Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.

Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.