Ub-Cys632-UBA1 adenylates ubiquitin in the nucleus

Stable Identifier
R-HSA-8852131
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
UBA1 is located in both the cytoplasm and nucleus (Grenfell et al. 1994). Activation of ubiquitin by UBA1 proceeds through 3 steps: adenylation of ubiquitin, conjugation of ubiquitin from adenyl-ubiquitin to an internal cysteine residue of UBA1, and adenylation of a second molecule of ubiquitin. In the third step, the UBA1-ubiquitin conjugate adenylates the C-terminal glycine of a second ubiquitin molecule. This results in UBA1 loaded with 2 ubiquitin molecules, one of which is conjugated to an internal cysteine residue of UBA1 and one of which is adenylated and non-covalently bound to UBA1 (Jin et al. 2007, inferred from the rabbit homologue in Haas et al. 1982, Hershko et al. 1983, reviewed in Groettrup et al. 2008)
Literature References
PubMed ID Title Journal Year
17597759 Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging

Li, X, Gygi, SP, Jin, J, Harper, JW

Nature 2007
18353650 Activating the ubiquitin family: UBA6 challenges the field

Hofmann, K, Pelzer, C, Groettrup, M, Schmidtke, G

Trends Biochem. Sci. 2008
6277905 Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation

Rose, IA, Hershko, A, Haas, AL, Warms, JV

J. Biol. Chem. 1982
6305978 Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown

Ciechanover, A, Elias, S, Heller, H, Hershko, A

J. Biol. Chem. 1983
8010951 Nuclear localization of the ubiquitin-activating enzyme, E1, is cell-cycle-dependent

Schwartz, AL, Ciechanover, A, Grenfell, SJ, Handley-Gearhart, PM, Trausch-Azar, JS

Biochem. J. 1994
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!