EC Number   |
General Information   |
Reference   |
|---|
 6.2.1.45 | physiological function |
isoform Uba6 forms a covalent link with ubiquitin in vitro and in vivo, which is sensitive to reducing conditions. In an in vitro polyubiquitylation assay, recombinant Uba6 can activate ubiquitin and transfer it onto the ubiquitin-conjugating enzyme UbcH5B. Ubiquitin activated by Uba6 can be used for ubiquitylation of p53 by MDM2 and supports the autoubiquitylation of the E3 ubiquitin ligases HectH9 and E6-AP |
674842 |
 6.2.1.45 | physiological function |
knockdown of E1 decreases the abundance of ubiquitinated proteins in leukemia and myeloma cells and induces cell death. Inhibitor 1-(3-chloro-4-fluorophenyl)-4-[(5-nitro-2-furyl)methylene]-3,5-pyrazolidinedione, i.e. PYZD-4409, induces cell death in malignant cells and preferentially inhibits the clonogenic growth of primary acute myeloid leukemia cells compared with normal hematopoietic cells. Mechanistically, genetic or chemical inhibition of E1 increases expression of E1 stress markers. ER membrane protein BI-1 overexpression blocks cell death after E1 inhibition |
707854 |
 6.2.1.45 | physiological function |
plays an important role in the first step of the proteasome pathway to activate ubiquitin. The UBE1 is a two-step intramolecular and ATP-dependent reaction to generate a high-energy E1-thiol-ester-ubiquitin intermediate. The activated ubiquitin are then transferred to ubiquitin-conjugating enzyme E2 |
709881 |
 6.2.1.45 | physiological function |
a lysine 48-linked polyubiquitin chain, assembled upon an internal lysine residue of a substrate protein, becomes the principle signal for recognition and target degradation by the 26S proteasome. E1 is not only essential for the initial ATP-dependent activation of ubiquitin in the ubiquitin degradtion pathway, but also capable of the catalytic extension of the polyubiquitin chain on a mono-ubiquitinated substrate |
725376 |
 6.2.1.45 | physiological function |
in mouse embryo fibroblast cell A31N-ts20, which is thermosensitive for ubiquitin-activating enzyme E1, the enzymatic activity of the enzyme is heat-inactivatable in vitro; and a major mechanism responsible for E1 inactivation in vivo consists of accelerated destruction. In vivo, ubiquitination of the various protein substrates in A31N-ts20 cells requires different amounts of E1 enzyme |
727412 |
 6.2.1.45 | malfunction |
lethality of RNA antisense silencing of Giardia E1 |
-, 733043 |
 6.2.1.45 | physiological function |
enzyme E1 is an essential gene for parasite viability and is implicated in encystation.Enzyme overexpression greatly increases the encystation rate, indicating a relationship between E1 and Giardia differentiation |
-, 733043 |
 6.2.1.45 | more |
sequence and structure comparisons, overview |
733532 |
 6.2.1.45 | physiological function |
ubiquitin-activating enzyme (E1) is a key regulator in protein ubiquitination, which lies on the upstream of the ubiquitin-related pathways and determines the activation of the downstream enzyme cascade |
733532 |
 6.2.1.45 | evolution |
5 amino acids and 8 bases are different in cDNA and DNA sequences of CrUBE1 between Wuzishatangju and Shatangju, respectively |
733931 |