| 词条 | HECT domain |
| 释义 |
| Symbol = HECT | Name = HECT-domain (ubiquitin-transferase) | image = PDB 1d5f EBI.jpg | width = | caption = structure of an e6ap-ubch7 complex: insights into the ubiquitination pathway | Pfam = PF00632 | Pfam_clan = | InterPro = IPR000569 | SMART = | PROSITE = | MEROPS = | SCOP = 1d5f | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, the HECT domain is a protein domain found in ubiquitin-protein ligases. The name HECT comes from 'Homologous to the E6-AP Carboxyl Terminus'.[1] Proteins containing this domain at the C terminus include ubiquitin-protein ligase, which regulates ubiquitination of CDC25. Ubiquitin-protein ligase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester, and then directly transfers the ubiquitin to targeted substrates. A cysteine residue is required for ubiquitin-thiolester formation. Human thyroid receptor interacting protein 12 (TRIP12), which also contains this domain, is a component of an ATP-dependent multisubunit protein that interacts with the ligand binding domain of the thyroid hormone receptor. It could be an E3 ubiquitin-protein ligase. Human ubiquitin-protein ligase E3A interacts with the E6 protein of the cancer-associated Human papillomavirus type 16 and Human papillomavirus type 18. The E6/E6-AP complex binds to and targets the p53 tumour-suppressor protein for ubiquitin-mediated proteolysis. References1. ^{{cite journal |vauthors=Huibregtse JM, Scheffner M, Beaudenon S, Howley PM | title = A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 7 | pages = 2563–7 |date=March 1995 | pmid = 7708685 | pmc = 42258 | doi = 10.1073/pnas.92.7.2563| url = }} {{InterPro content|IPR000569}} 1 : Protein domains |
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