UBA7

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]

Ubiquitin Like Modifier Activating Enzyme 7

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 a ubiquitin-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein.

Biological Process cellular response to DNA damage stimulus Source:GO_Central1 Publication
Biological Process ISG15-protein conjugation Source:HGNC-UCL1 Publication
Biological Process modification-dependent protein catabolic process Source:Ensembl
Biological Process protein modification by small protein conjugation Source:GO_Central1 Publication
Biological Process protein modification process Source:HGNC-UCL1 Publication

cytoplasm
cytosol
nucleoplasm
nucleus

ISGylated.