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GORASP2
Golgi reassembly-stacking protein 2 ( GRS2) also known as Golgi reassembly-stacking protein of 55 Dalton (unit), kDa (GRASP55) is a protein that in humans is encoded by the ''GORASP2'' gene. It was identified by its homology with GORASP1 and the protein primary structure, protein's amino acid sequence was determined by analysis of a Molecular cloning, molecular clone of its complementary DNA. The first (N-terminus) 212 Protein structure#Amino acid residues, amino acid residues of GORASP2 are highly homologous to those of GORASP1, but the remainder of the 454 amino acid residues are highly diverged from GORASP1. The conserved region is known as the GRASP domain, and it is conserved among GRASPs of a wide variety of eukaryotes, but not plants. The C-terminus portion of the molecule is called the ''SPR domain'' (serine, proline-rich). GORASP2 is more closely related to homologues in other species, suggesting that GORASP2 is ancestral to GORASP1. GORASP2 is found associated with th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TMED2
Transmembrane emp24 domain-containing protein 2 is a protein that in humans is encoded by the ''TMED2'' gene. Interactions TMED2 has been shown to Protein-protein interaction, interact with GORASP1 and GORASP2. References Further reading * * * * * * * {{Gene-12-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TGF Alpha
Transforming growth factor alpha (TGF-α) is a protein that in humans is encoded by the TGFA gene. As a member of the epidermal growth factor (EGF) family, TGF-α is a mitogenic polypeptide. The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling. TGF-α is a transforming growth factor that is a ligand for the epidermal growth factor receptor, which activates a signaling pathway for cell proliferation, differentiation and development. This protein may act as either a transmembrane-bound ligand or a soluble ligand. This gene has been associated with many types of cancers, and it may also be involved in some cases of cleft lip/palate. Synthesis TGF-α is synthesized internally as part of a 160 (human) or 159 (rat) amino acid transmembrane precursor. The precursor is composed of an extracellular domain containing a hydrophobic transmembrane domain, 50 amino acids of TGF-α, and a 35-residue-long cytoplasmic domain. In its ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
BLZF1
Golgin-45 is a protein that in humans is encoded by the ''BLZF1'' gene. Interactions Golgin-45 has been shown to interact with GORASP2 Golgi reassembly-stacking protein 2 ( GRS2) also known as Golgi reassembly-stacking protein of 55 Dalton (unit), kDa (GRASP55) is a protein that in humans is encoded by the ''GORASP2'' gene. It was identified by its homology with GORASP1 and .... References Further reading * * * * * * * * External links * * Transcription factors {{gene-1-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphorylation
In biochemistry, phosphorylation is described as the "transfer of a phosphate group" from a donor to an acceptor. A common phosphorylating agent (phosphate donor) is ATP and a common family of acceptor are alcohols: : This equation can be written in several ways that are nearly equivalent that describe the behaviors of various protonated states of ATP, ADP, and the phosphorylated product. As is clear from the equation, a phosphate group per se is not transferred, but a phosphoryl group (PO3-). Phosphoryl is an electrophile. This process and its inverse, dephosphorylation, are common in biology. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License. Protein phosphorylation often activates (or deactivates) many enzymes. During respiration Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mitosis
Mitosis () is a part of the cell cycle in eukaryote, eukaryotic cells in which replicated chromosomes are separated into two new Cell nucleus, nuclei. Cell division by mitosis is an equational division which gives rise to genetically identical cells in which the total number of chromosomes is maintained. Mitosis is preceded by the S phase of interphase (during which DNA replication occurs) and is followed by telophase and cytokinesis, which divide the cytoplasm, organelles, and cell membrane of one cell into two new cell (biology), cells containing roughly equal shares of these cellular components. The different stages of mitosis altogether define the mitotic phase (M phase) of a cell cycle—the cell division, division of the mother cell into two daughter cells genetically identical to each other. The process of mitosis is divided into stages corresponding to the completion of one set of activities and the start of the next. These stages are preprophase (specific to plant ce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rab (G-protein)
The Rab family of proteins is a member of the Ras superfamily of small G proteins. Approximately 70 types of Rabs have now been identified in humans. Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices. Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface. Function Rab proteins are peripheral membrane proteins, anchored to a membrane via a lipid group covalently linked to an amino acid. Spec ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lipid Bilayer
The lipid bilayer (or phospholipid bilayer) is a thin polar membrane made of two layers of lipid molecules. These membranes form a continuous barrier around all cell (biology), cells. The cell membranes of almost all organisms and many viruses are made of a lipid bilayer, as are the nuclear envelope, nuclear membrane surrounding the cell nucleus, and biological membrane, membranes of the membrane-bound organelles in the cell. The lipid bilayer is the barrier that keeps ions, proteins and other molecules where they are needed and prevents them from diffusing into areas where they should not be. Lipid bilayers are ideally suited to this role, even though they are only a few nanometers in width, because they are impermeable to most water-soluble (hydrophilic) molecules. Bilayers are particularly impermeable to ions, which allows cells to regulate salt concentrations and pH by transporting ions across their membranes using proteins called Ion transporter, ion pumps. Biological bilaye ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Myristoylation
Myristoylation is a lipidation modification where a myristoyl group, derived from myristic acid, is covalently attached by an amide bond to the alpha-amino group of an ''N''-terminal glycine residue. Myristic acid is a 14-carbon saturated fatty acid (14:0) with the systematic name of ''n''-tetradecanoic acid. This modification can be added either co-translationally or post-translationally. ''N''-myristoyltransferase (NMT) catalyzes the myristic acid addition reaction in the cytoplasm of cells. This lipidation event is the most common type of fatty acylation and is present in many organisms, including animals, plants, fungi, protozoans and viruses. Myristoylation allows for weak protein–protein and protein–lipid interactions and plays an essential role in membrane targeting, protein–protein interactions and functions widely in a variety of signal transduction pathways. Discovery In 1982, Koiti Titani's lab identified an "''N''-terminal blocking group" on the catal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein–protein Interaction
Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context. Proteins rarely act alone as their functions tend to be regulated. Many molecular processes within a cell are carried out by molecular machines that are built from numerous protein components organized by their PPIs. These physiological interactions make up the so-called Interactome, interactomics of the organism, while aberrant PPIs are the basis of multiple aggregation-related diseases, such as Creutzfeldt–Jakob disease, Creutzfeldt–Jakob and Alzheimer's diseases. PPIs have been studied with Methods to investigate protein–protein interactions, many methods and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
