The enzymes of the ubiquitylation pathway play a pivotal role in a number of cellular processes including regulated and targeted proteosomal degradation of substrate proteins. Three classes of enzymes are involved in the process of ubiquitylation; activating enzymes (E1s), conjugating enzymes (E2s) and protein ligases (E3s). UBE2Q1 is a member of the E2 conjugating enzyme family. Cloning of human UBE2Q1 was first described by Marenholz et al. (2001). UBE2Q1 shares 50-75% sequence identity to its homologues in, Mus musculus, Drosophila, C. elegans and Xenopus. Murine UBE2Q1 has a conserved sequence for ubiquitin binding shared by all the ubiquitin-conjugating enzymes and its NH2-terminal domain appears critical for the binding and internalization of cell surface galactosyltransferase 1 (GalT1) in embryonic stem cells. UBE2Q1 regulates GalT1-associated laminin-dependent embryonic cell adhesion and the formation of embryoid bodies (Wassler et al., 2008).
Marenholz I, Zirra M, Fischer DF, Backendorf C, Ziegler A, Mischke D (2001) Identification of human epidermal differentiation complex (EDC)-encoded genes by subtractive hybridization of entire YACs to a gridded keratinocyte cDNA library. Genome Res 11, 341-55.
Wassler MJ, Shur BD, Zhou W, Geng YJ (2008) Characterization of a novel ubiquitin-conjugating enzyme that regulates beta1,4-galactosyltransferase-1 in embryonic stem cells. Stem Cells 26, 2006-18.