background:
Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells, either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. Ubiquitin conjugating enzyme 8 (UBC8) is an E2 enzyme involved in the ubiquitin pathway for protein degradation. Like other E2 enzymes, UBC8 forms a thioester bond with ubiquitin in an E1-dependent manner. UBC8 binds to the human homolog of Drosophila ariadne (HHARI) and UBC7-associated protein (H7-AP1) as well as double ring-finger protein (Dorfin). UBC8 is enriched in the central nervous system and interacts with Parkin, a RING-finger-containing protein implicated in the pathogenesis of familial Parkinson’s disease. Parkin shares sequence homology with other UBC8 binding proteins such as HHARI and H7-AP1.
Function:
Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3.
Subunit:
Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3 (tyrosine phosphorylated).
Tissue Specificity:
Present in natural killer cells.
Post-translational modifications:
ISGylated.
Similarity:
Belongs to the ubiquitin-conjugating enzyme family.
Database links:
UniProtKB/Swiss-Prot: O14933.4
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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