UBA1 conjugates ubiquitin to nuclear E2 enzymes

Stable Identifier
Reaction [transition]
Homo sapiens
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In the nucleus (Grenfell et al. 1994), the UBA1-ubiquitin thiol ester conjugate transfers ubiquitin from UBA1 to an internal cysteine residue of the E2 enzyme, forming a thiol ester conjugate between ubiquitin and the cysteine residue of E2 (Jin et al. 2007, inferred from the rabbit homologue in Hershko et al. 1983, reviewed in Groettrup et al. 2008). The E2 then disengages from UBA1 (Eletr et al. 2005).

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
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
16142244 E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer

Huang, DT, Kuhlman, B, Duda, DM, Schulman, BA, Eletr, ZM

Nat. Struct. Mol. Biol. 2005
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