UBA7
UBA7 (ubiquitin like modifier activating enzyme 7, also known as UBE1L, UBA1B, D8 and UBE2) is the E1-activating enzyme for the ubiquitin-like protein ISG15. It drives protein ISGylation and contributes to antiviral immunity. Browse Assay Genie's current range of UBA7 research reagents below, or read on for the biology behind the target.
UBA7 is an E1-activating enzyme that catalyses the covalent conjugation of the ubiquitin-like protein encoded by ISG15 to interferon-stimulated proteins and to other cellular proteins, including P53, in a process termed protein ISGylation. Together with ISG15, it plays an essential role in antiviral immunity by restricting the replication of many viruses, including rabies virus, influenza virus, sindbis virus, rotavirus and human cytomegalovirus.
Antiviral ISGylation acts on viral proteins directly. ISG15 modification of the influenza A protein NS1 disrupts its association with importin-alpha, which inhibits NS1 nuclear import. ISGylation of the human cytomegalovirus protein UL26 regulates its stability and inhibits its activities, which suppresses NF-kappa-B signalling.
The UBA7 gene encodes a member of the ubiquitin-activating E1 family. Ubiquitin-pathway modification involves three enzyme classes: E1 activating enzymes, E2 conjugating enzymes and E3 ligases, and ubiquitination targets abnormal or short-lived proteins for degradation. The UBA7 protein is found in the cytoplasm and nucleus. HGNC places the gene in the ubiquitin like modifier activating enzymes group, and lists previous names including ubiquitin-activating enzyme E1-like, hence the alias UBE1L.
UBA7 is also a retinoid target. In acute promyelocytic leukaemia it triggers degradation of the PML/RARalpha fusion protein and apoptosis, and it is involved there in conjugation of ISG15. Researchers working on UBA7 often study it alongside other E1 enzymes and the wider ubiquitin-like modifier pathways.
UBA7 activates ISG15 and so supports ISGylation, which restricts replication of viruses such as influenza virus, rabies virus and human cytomegalovirus.
As the E1 enzyme for ISG15, UBA7 conjugates ISG15 to interferon-stimulated proteins and other targets, including P53.
UBA7 is a retinoid target that triggers PML/RARalpha degradation and apoptosis in acute promyelocytic leukaemia.
UBA7 belongs to the E1 family that initiates the E1, E2 and E3 cascade used to target proteins for modification and degradation.
UBA7 is an E1-activating enzyme that catalyses conjugation of the ubiquitin-like protein ISG15 to interferon-stimulated proteins and other cellular proteins such as P53. This ISGylation supports antiviral immunity by restricting replication of viruses including influenza virus, rabies virus and human cytomegalovirus.
UBA7 is also called UBE1L, UBA1B, D8 and UBE2. Earlier names include ubiquitin-activating enzyme E1-like. The UniProt entry names it ubiquitin-like modifier-activating enzyme 7, and it belongs to the ubiquitin-activating E1 family.
A mouse ortholog, Uba7, is recorded for the gene. In disease, UBA7 is a retinoid target that triggers PML/RARalpha degradation and apoptosis in acute promyelocytic leukaemia. Check the datasheet of any product for its validated reactivity.
Other ubiquitin-activating E1 enzymes and ubiquitin-pathway proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P41226; product specifications from Assay Genie datasheets.