Recombinant Human UBA5 protein (His tag)
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Recombinant Human UBA5 protein (His tag) is a Human Full Length protein, in the 1 to 404 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
UBE1DC1, UBA5, Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
UBA5 is implicated in the UFM1 conjugation system. This process modifies specific proteins and affects protein stability interaction and degradation. UBA5 operates in complex with UFC1 an E2 enzyme enabling the transfer of UFM1 to target proteins. Its activity is essential for maintaining cellular homeostasis particularly in the endoplasmic reticulum stress response through protein modification and regulation tasks.
Pathways
The UBA5-UFM1 axis integrates into the cellular stress response pathway and the endoplasmic reticulum-associated degradation (ERAD) pathway. Through these pathways UBA5 collaborates with proteins like UFL1 further connecting these pathways by tagging proteins with UFM1 to mark them for degradation or functional modification. The coordination between UBA5 and UFL1 supports efficient protein quality control and maintains cellular equilibrium under stress conditions.
Specifications
Form
Liquid
Additional notes
ab199575 is greater than 95% pure as determined by SEC-HPLC and reducing SDS-PAGE.
General info
Function
E1-like enzyme which specifically catalyzes the first step in ufmylation (PubMed : 15071506, PubMed : 18442052, PubMed : 20368332, PubMed : 25219498, PubMed : 26929408, PubMed : 27545674, PubMed : 27545681, PubMed : 27653677, PubMed : 30412706, PubMed : 30626644, PubMed : 34588452). Activates UFM1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP (PubMed : 20368332, PubMed : 26929408, PubMed : 27653677, PubMed : 30412706). Activates UFM1 via a trans-binding mechanism, in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer (PubMed : 27653677). Trans-binding also promotes stabilization of the UBA5 homodimer, and enhances ATP-binding (PubMed : 29295865). Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also takes place using a trans mechanism (PubMed : 27653677, PubMed : 34588452). Ufmylation plays a key role in various processes, such as ribosome recycling, response to DNA damage, interferon response or reticulophagy (also called ER-phagy) (PubMed : 30412706, PubMed : 32160526, PubMed : 35394863). Ufmylation is essential for erythroid differentiation of both megakaryocytes and erythrocytes (By similarity).
Sequence similarities
Belongs to the ubiquitin-activating E1 family. UBA5 subfamily.
Subcellular localisation
Nucleus
Target data
Product promise
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