InterPro : IPR019572

Name  Ubiquitin-activating enzyme Short Name  Ubiquitin-activating_enzyme
Type  Domain Description  Ubiquitin-activating enzyme (E1 enzyme) 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 an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2) []. This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP []. Not all proteins in this entry contain a functional active site.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR018074 Ubiquitin-activating enzyme, E1, active site UBQ-activ_enz_E1_AS Active_site

4 Found In

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR009036 Molybdenum cofactor biosynthesis, MoeB Molybdenum_cofac_synth_MoeB Domain
IPR000011 Ubiquitin/SUMO-activating enzyme E1 UBQ/SUMO-activ_enz_E1-like Family
IPR018075 Ubiquitin-activating enzyme, E1 UBQ-activ_enz_E1 Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Handley PM Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1. 1991 Proc Natl Acad Sci U S A 88 258-62
Tokumoto M Molecular cloning of cDNA encoding a ubiquitin-activating enzyme (E1) from goldfish (Carassius auratus) and expression analysis of the cloned gene. 2000 Biochim Biophys Acta 1492 259-63



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)