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AP1G1
AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the ''AP1G1'' gene. Function Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two transcript variants encoding different isoforms have been found for this gene. Interactions AP1G1 has been shown to interact with: * AP1B1, * AP1GBP1, * AP1M1, * AP1S1, * NECAP2, * RABEP1 Rab GTPase-binding effector protein 1 is an enzyme that in humans is encoded by the ''RABEP ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AP1GBP1
Synergin gamma also known as AP1 subunit gamma-binding protein 1 (AP1GBP1) is a protein that in humans is encoded by the ''SYNRG'' gene. Function This gene encodes a protein that interacts with the gamma subunit of AP1 clathrin adaptor proteins, clathrin-adaptor complex. The AP1 complex is located at the trans-Golgi network and associates specific proteins with clathrin-coated vesicles. This encoded protein may act to connect the AP1 complex to other proteins. Alternatively spliced transcript variants that encode different isoforms have been described for this gene. Interactions AP1GBP1 has been shown to Protein-protein interaction, interact with AP1G1 and SCAMP1. References Further reading * * * * * * * * * * * {{gene-17-stub EH-domain-containing proteins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AP1B1
AP-1 complex subunit beta-1 is a protein that in humans is encoded by the ''AP1B1'' gene. Adaptor protein complex 1 is found at the cytoplasmic face of coated vesicles located at the Golgi complex, where it mediates both the recruitment of clathrin to the membrane and the recognition of sorting signals within the cytosolic tails of transmembrane receptors. This complex is a heterotetramer composed of two large, one medium, and one small adaptin subunit. The protein encoded by this gene serves as one of the large subunits of this complex and is a member of the adaptin protein family. This gene is a candidate meningioma gene. Two transcript variants encoding different isoforms have been found for this gene, and variants utilizing alternative polyadenylation signals exist. Interactions AP1B1 has been shown to interact with KIF13A and AP1G1 AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the ''AP1G1'' gene. Function Adaptins are important components of cla ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AP1M1
AP-1 complex subunit mu-1 is a protein that in humans is encoded by the ''AP1M1'' gene. Function The protein encoded by this gene is the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. The other components of this complex are beta-prime-adaptin, gamma-adaptin, and the small chain AP1S1. This complex is located at the Golgi vesicle and links clathrin to receptors in coated vesicles. These vesicles are involved in endocytosis and Golgi processing. Interactions AP1M1 has been shown to interact with VAMP4 and AP1G1 AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the ''AP1G1'' gene. Function Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans .... References Further reading * * * * * * * * * * * * * * * * * * * External links * {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AP1S1
AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the ''AP1S1'' gene. Function The protein encoded by this gene is part of the clathrin coat assembly complex which links clathrin to receptors in coated vesicles. These vesicles are involved in endocytosis and Golgi processing. This protein, as well as beta-prime-adaptin, gamma-adaptin, and the medium (mu) chain AP47, form the AP-1 assembly protein complex located at the Golgi vesicle. Two alternatively spliced transcript variants of this gene, which encode distinct isoforms, have been reported. A mutation in the AP1S1 causes the rare familial MEDNIK syndrome described in 2008. Interactions AP1S1 has been shown to interact with AP1G1 and RAB10 Ras-related protein Rab-10 is a protein that in humans is encoded by the ''RAB10'' gene. Interactions RAB10 has been shown to interact with AP1S1 AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the ''AP1S1'' gene. F .... Referen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NECAP2
Adaptin ear-binding coat-associated protein 2 is a protein that in humans is encoded by the ''NECAP2'' gene. Interactions NECAP2 has been shown to interact with AP1G1 AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the ''AP1G1'' gene. Function Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans .... References Further reading * * * * * * * * * Human proteins {{gene-1-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RABEP1
Rab GTPase-binding effector protein 1 is an enzyme that in humans is encoded by the ''RABEP1'' gene. It belongs to rabaptin protein family. Interactions RABEP1 has been shown to interact with: * AP1G1, * GGA1, * GGA2, * RAB4A, and * RAB5A Ras-related protein Rab-5A is a protein that in humans is encoded by the ''RAB5A'' gene. Function RAB5A localizes to early endosomes where it is involved in the recruitment of RAB7A and the maturation of these compartments to late endosomes. I .... References Further reading * * * * * * * * * * * * * * * {{Gene-17-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Synaptophysin
Synaptophysin, also known as the major synaptic vesicle protein p38, is a protein that in humans is encoded by the ''SYP'' gene. Genomics The gene is located on the short arm of X chromosome (Xp11.23-p11.22). It is 12,406 bases in length and lies on the minus strand. The encoded protein has 313 amino acids with a predicted molecular weight of 33.845 kDa. Molecular biology The protein is a synaptic vesicle glycoprotein with four transmembrane domains weighing 38kDa. It is present in neuroendocrine cells and in virtually all neurons in the brain and spinal cord that participate in synaptic transmission. It acts as a marker for neuroendocrine tumors, and its ubiquity at the synapse has led to the use of synaptophysin immunostaining for quantification of synapses. The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gene
In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a basic unit of heredity and the molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and noncoding genes. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes (many different genes) as well as gen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adaptin
Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These proteins are synthesized in the ribosomes, processed in the endoplasmic reticulum and transported from the Golgi apparatus to the trans-Golgi network, and from there via small carrier vesicles to their final destination compartment. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Clathrin
Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated and named by Barbara Pearse in 1976. It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they form a polyhedral lattice that surrounds the vesicle, hence the protein's name, which is derived from the Latin ''clathrum'' meaning lattice. Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis and exocytosis of vesicles allows cells to communicate, to transfer nutrients, to import signaling receptors, to mediate an immune response after sampling the extracellular world, and to clean up the cell debris left by tissue inflammation. The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection. Structure The clathrin triskelion is composed of three clathrin heavy chains inter ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Trans-Golgi Network
The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus. It was identified in 1897 by the Italian scientist Camillo Golgi and was named after him in 1898. Discovery Owing to its large size and distinctive structure, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was discovered in 1898 by Italian physician Camillo Golgi during an investigation of the nervous system. After first observing it under his ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
