UBE2F is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by an ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.
UBE2F ELISA Pair sets
UBE2F cDNA Clones
NCE2 [Homo sapiens]
2510010F15Rik, AI851109 [Mus musculus]
NEDD8-conjugating enzyme UBE2F
Protein modification; protein neddylation.
Belongs to the ubiquitin-conjugating enzyme family.
ATP + NEDD8 + protein lysine = AMP + diphosphate + protein N-NEDD8yllysine.
Interacts with UBA3 and RBX2.
Widely expressed (at protein level).
General information above from UniProt
UBE2F accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.
- UBE2F is ligase activity
- UBE2F is ubiquitin conjugation enzyme activity