UBA7 Antibody – Rabbit Polyclonal

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein. [provided by RefSeq, Jul 2008]

UBE1L: Activates ubiquitin by first adenylating with ATP its C- terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP. Belongs to the ubiquitin-activating E1 family.

Protein type: EC 6.3.2.19; Ubiquitin ligase; Ubiquitin conjugating system

Chromosomal Location of Human Ortholog: 3p21

Cellular Component: cytosol; nucleus

Molecular Function: ISG15 activating enzyme activity; ubiquitin-protein ligase activity; ubiquitin activating enzyme activity; ATP binding

Biological Process: ISG15-protein conjugation; modification-dependent protein catabolic process; cytokine and chemokine mediated signaling pathway; protein modification process; innate immune response; protein ubiquitination; negative regulation of interferon type I production