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The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The ...
The 5′-end (pronounced "five prime end") designates the end of the DNA or RNA strand that has the fifth carbon in the sugar-ring of the deoxyribose or ribose at its terminus. A phosphate group attached to the 5′-end permits ligation of two nucleotides , i.e., the covalent binding of a 5′-phosphate to the 3′-hydroxyl group of another ...
The soluble resident protein will remain in the ER as long as it contains a KDEL signal sequence on the C-terminal end of the protein. However, since vesicle budding is such a dynamic process, and there is a high concentration of soluble proteins in the ER, soluble proteins are inadvertently transported to the cis-golgi via COPII coated vesicles.
56424 Ensembl ENSG00000103266 ENSMUSG00000039615 UniProt Q9UNE7 Q9WUD1 RefSeq (mRNA) NM_005861 NM_001293197 NM_019719 RefSeq (protein) NP_001280126 NP_005852 NP_062693 Location (UCSC) Chr 16: 0.68 – 0.68 Mb Chr 17: 26.05 – 26.05 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse STUB1 (ST IP1 homology and U - B ox containing protein 1) is a human gene that codes for the protein CHIP ...
A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of ...
Group I proteins have the N terminus on the far side and C terminus on the cytosolic side. Group II proteins have the C terminus on the far side and N terminus in the cytosol. Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuclear magnetic resonance ...
In molecular biology, the type IV collagen C4 domain (or collagen IV NC1 domain) is a duplicated domain present at the C-terminus of type IV collagens.Each type IV collagen contains a long triple-helical collagenous domain flanked by a short 7S domain of 25 amino acids and a globular non-collagenous C4 domain of ~230 amino acids at the N and C terminus, respectively.
[1] [5] [6] and was the only epitope tag to be patented. [7] [8] It has since become one of the most commonly used protein tags in laboratories worldwide. Unlike some other tags (e.g. myc, HA), where a monoclonal antibody was first isolated against an existing protein, then the epitope was characterized and used as a tag, the FLAG epitope was ...