InterPro : IPR018075

Name  Ubiquitin-activating enzyme, E1 Short Name  UBQ-activ_enz_E1
Type  Family Description  The post-translational attachment of ubiquitin () to proteins (ubiquitinylation) alters the function, location or trafficking of a protein, or targets it to the 26S proteasome for degradation [, , ]. Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2, ), and a ubiquitin ligase (E3, , ), which work sequentially in a cascade []. The E1 enzyme is responsible for activating ubiquitin, the first step in ubiquitinylation. The E1 enzyme hydrolyses ATP and adenylates the C-terminal glycine residue of ubiquitin, and then links this residue to the active site cysteine of E1, yielding a ubiquitin-thioester and free AMP. To be fully active, E1 must non-covalently bind to and adenylate a second ubiquitin molecule. The E1 enzyme can then transfer the thioester-linked ubiquitin molecule to a cysteine residue on the ubiquitin-conjugating enzyme, E2, in an ATP-dependent reaction.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

6 Contains

Id Name Short Name Type
IPR000594 UBA/THIF-type NAD/FAD binding fold ThiF_NAD_FAD-bd Domain
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR019572 Ubiquitin-activating enzyme Ubiquitin-activating_enzyme Domain
IPR009036 Molybdenum cofactor biosynthesis, MoeB Molybdenum_cofac_synth_MoeB Domain
IPR018074 Ubiquitin-activating enzyme, E1, active site UBQ-activ_enz_E1_AS Active_site
IPR000127 Ubiquitin-activating enzyme repeat UBact_repeat Repeat

0 Found In

1 Parent Features

Id Name Short Name Type
IPR000011 Ubiquitin/SUMO-activating enzyme E1 UBQ/SUMO-activ_enz_E1-like Family

4 Publications

First Author Title Year Journal Volume Pages
Burger AM The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications. 2004 Eur J Cancer 40 2217-29
Passmore LA Getting into position: the catalytic mechanisms of protein ubiquitylation. 2004 Biochem J 379 513-25
Pickart CM Polyubiquitin chains: polymeric protein signals. 2004 Curr Opin Chem Biol 8 610-6
Sun L The novel functions of ubiquitination in signaling. 2004 Curr Opin Cell Biol 16 119-26

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)