FEATURES

FAMILY

DESCRIPTION

Also known as UBA5_HUMAN, UBA5, UBE1DC1. E1-like enzyme which specifically catalyzes the first step in ufmylation (PubMed:15071506, PubMed:18442052, PubMed:25219498, PubMed:20368332, PubMed:27653677, PubMed:26929408, PubMed:27545674, PubMed:30412706, PubMed:27545681). 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:27653677, PubMed:26929408, 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). Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:32160526). Ufmylation is essential for erythroid differentiation of both megakaryocytes and erythrocytes (By similarity). Homodimer; homodimerization is required for UFM1 activation (PubMed:29295865, PubMed:27653677). Interacts (via UIS motif) with UFM1; binds UFM1 via a trans-binding mechanism in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer (PubMed:29295865, PubMed:27653677, PubMed:26929408, PubMed:28360427, PubMed:30412706, PubMed:26872069). Interacts (via UIS motif) with GABARAPL2 and, with lower affinity, with GABARAP and GABARAPL1 (PubMed:26929408, PubMed:30990354). Interacts (via C-terminus) with UFC1 (PubMed:17825256, PubMed:29868776, PubMed:27653677).

Also known as UBA5_HUMAN, UBA5, UBE1DC1. E1-like enzyme which specifically catalyzes the first step in ufmylation (PubMed:15071506, PubMed:18442052, PubMed:25219498, PubMed:20368332, PubMed:2765 ...

EXTERNAL LINKS

UBA5

Mutations

Mutation(s) distribution

Mutations table