Recombinant Human NEDD8 E1 (APPBP1/UBA3) Protein, CF
Recombinant Human NEDD8 E1 (APPBP1/UBA3) Protein, CF Summary
60 kDa (APP-BP1)
52 kDa (UBA3)
Background: NEDD8 Activating Enzyme (APPBP1/UBA3)
Neural Precursor Cell Expressed Developmentally Downregulated Gene 8 (NEDD8) Activating Enzyme (APP-BP1/UBA3) is a heterodimeric NEDD8-activating (E1) enzyme with a predicted molecular weight of 112 kDa. It is responsible for the first step in the conjugation of NEDD8 to protein substrates. The NEDD8 Activating Enzyme heterodimer is composed of a regulatory subunit, Amyloid beta Precursor Protein Binding Protein 1 (APP-BP1), and a catalytic subunit, Ubiquitin-like Modifier Activating Enzyme 3 (UBA3). Human APP-BP1 is a 534 amino acid (aa) protein with a predicted molecular weight of 60 kDa that is expressed ubiquitously in fetal tissues and in the adult brain (1). APP-BP1 is required for UBA3 neddylation activity, regulates enzyme specificity, and is expressed as two isoforms, the full length protein and a second isoform with an alternate N-terminal, aa1-17, sequence (2). APP-BP1 has been shown to drive cell cycle progression, and its expression is increased in the hippocampus of Alzheimer's disease brains (3,4). Human UBA3 is a 463 aa protein with a predicted molecular weight of 52 kDa. It is ubiquitously expressed and shares high aa sequence identity with the C-terminal domain of human UBE1 (5). UBA3 contains an ATP-binding domain and an active site cysteine residue, Cys237 in humans, which are both common to E1 enzymes. Like APP-BP1, two isoforms of UBA3 have been identified in humans, the full length protein and a truncated isoform, which lacks aa 8-21. UBA3 is required for cell cycle progression and has been shown to downregulate steroid receptor activation (4,6). Neddylation and its associated enzymes have been implicated in the progression of Alzheimer's disease, via neddylation of APP, and cancer via post-translational modification of oncogenes (7,8).
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Citations for Recombinant Human NEDD8 E1 (APPBP1/UBA3) Protein, CF
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Citations: Showing 1 - 5
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Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophila
Authors: D Valleau, AT Quaile, H Cui, X Xu, E Evdokimova, C Chang, ME Cuff, ML Urbanus, S Houliston, CH Arrowsmith, AW Ensminger, A Savchenko
Cell Rep, 2018;23(2):568-583.
A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
Authors: H Zhou, J Lu, L Liu, D Bernard, CY Yang, E Fernandez-, K Chinnaswam, S Layton, J Stuckey, Q Yu, W Zhou, Z Pan, Y Sun, S Wang
Nat Commun, 2017;8(1):1150.
Sample Types: Recombinant Protein
SENP8 limits aberrant neddylation of NEDD8 pathway components to promote cullin-RING ubiquitin ligase function
Authors: KE Coleman, M Békés, JR Chapman, SB Crist, MJ Jones, BM Ueberheide, TT Huang
Sample Types: Whole Cells
The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity.
Authors: Huang G, Towe C, Choi L, Yonekawa Y, Bommelje C, Bains S, Rechler W, Hao B, Ramanathan Y, Singh B
J Biol Chem, 2015;290(1):296-309.
SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).
Authors: Huang G, Stock C, Bommelje C, Weeda V, Shah K, Bains S, Buss E, Shaha M, Rechler W, Ramanathan S, Singh B
Sample Types: Cell Lysates
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