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Ubiquitin-like modifier activating enzyme 3

Uba3, hUba3
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme associates with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and then the enzyme complex activates NEDD8, a ubiquitin-like protein, which regulates cell division, signaling and embryogenesis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, NEDD8, NaeI, Cullin, Ubc12
Papers on Uba3
COP9-Signalosome deneddylase activity is enhanced by simultaneous neddylation: insights into the regulation of an enzymatic protein complex.
Grossman et al., Tel Aviv-Yafo, Israel. In Cell Div, 2014
Deneddylation rate was tested either simultaneous to neddylation or after termination of neddylation by using an ATP depleting reaction or by directly inhibiting the neddylation activation enzyme named APP-BP1/UBA3 by its specific inhibitor MLN-4924.
CBS9106-induced CRM1 degradation is mediated by cullin ring ligase activity and the neddylation pathway.
Kawabe et al., Numazu, Japan. In Mol Cancer Ther, 2014
Furthermore, RNAi-mediated knockdown of neddylation pathway proteins (NEDD8 and UBA3) or cullin ring ligase (CRL) component protein (Rbx1) attenuated CRM1 protein degradation and G1 phase cell-cycle arrest by CBS9106.
Neddylation pathway is up-regulated in human intrahepatic cholangiocarcinoma and serves as a potential therapeutic target.
Fan et al., Shanghai, China. In Oncotarget, 2014
Immunohistochemistry of neddylation pathway components in a cohort of 322 cases showed that E1 (NAE1 and UBA3) and E2 (UBC12) enzymes, as well as global NEDD8 conjugation, were upregulated in over 2/3 of human ICC.
Expression of neddylation-related proteins in melanoma cell lines and the effect of neddylation on melanoma proliferation.
Chen et al., Xingtai, China. In Oncol Lett, 2014
Downregulation of UBA3, a subunit of the E1 enzyme, by RNA interference caused cell cycle arrest at G0(/)G1 in the M14 cell line.
Mutations in UBA3 confer resistance to the NEDD8-activating enzyme inhibitor MLN4924 in human leukemic cells.
Schimmer et al., Toronto, Canada. In Plos One, 2013
R-K562(MLN) and R-U937(MLN) cells contain I310N and Y352H mutations in the NAE catalytic subunit UBA3, respectively.
Molecular dynamics investigation on the poor sensitivity of A171T mutant NEDD8-activating enzyme (NAE) for MLN4924.
Mishra et al., Benares, India. In J Biomol Struct Dyn, 2013
A single nucleotide transition that changes alanine 171 to threonine (A171T) of the NAE subunit UBA3 reduces the enzyme's sensitivity for MLN4924.
Dysfunction of the ubiquitin proteasome and ubiquitin-like systems in schizophrenia.
Meador-Woodruff et al., Birmingham, United States. In Neuropsychopharmacology, 2013
NEDD8ylation was also dysregulated in schizophrenia, with decreased levels of the E1 activase UBA3 and the E3 ligase Rnf7.
Neddylation dysfunction in Alzheimer's disease.
Liu et al., Little Rock, United States. In J Cell Mol Med, 2012
Central to the neddylation pathway is the amyloid precursor protein (APP)-binding protein APP-BP1, which together with Uba3, plays an analogous role to the ubiquitin-activating enzyme E1 in nedd8 activation.
E2-binding surface on Uba3 β-grasp domain undergoes a conformational transition.
Haas et al., Muğla, Turkey. In Proteins, 2012
The activating enzyme for neural-precursor-cell-expressed developmentally downregulated 8 (NEDD8) is a heterodimer composed of APPBP1 and Uba3 subunits.
A gatekeeper residue for NEDD8-activating enzyme inhibition by MLN4924.
Petroski et al., Los Angeles, United States. In Cell Rep, 2012
Here, we show that selective pressure results in HCT116 colorectal carcinoma cells with decreased MLN4924 sensitivity and identify a single-nucleotide transition that changes alanine 171 to threonine (A171T) of the NAE subunit UBA3.
A metal-based inhibitor of NEDD8-activating enzyme.
Ma et al., Aomen, Macao. In Plos One, 2011
Molecular modeling analysis suggested that the overall binding mode of 1 within the binding pocket of the APPBP1/UBA3 heterodimer resembled that for MLN4924.
Structural dissection of a gating mechanism preventing misactivation of ubiquitin by NEDD8's E1.
Schulman et al., Memphis, United States. In Biochemistry, 2008
X-ray crystallographic analysis of APPBP1-UBA3-NEDD8 shows that APPBP1-UBA3's preference for NEDD8's Ala72 appears to be indirect, due to proper positioning of UBA3's Arg190.
Basis for a ubiquitin-like protein thioester switch toggling E1-E2 affinity.
Schulman et al., Memphis, United States. In Nature, 2007
Here we report the structural analysis of a trapped UBL activation complex for the human NEDD8 pathway, containing NEDD8's heterodimeric E1 (APPBP1-UBA3), two NEDD8s (one thioester-linked to E1, one noncovalently associated for adenylation), a catalytically inactive E2 (Ubc12), and MgATP.
The cell cycle of early mammalian embryos: lessons from genetic mouse models.
Cohen-Tannoudji et al., Paris, France. In Cell Cycle, 2006
Here, we discuss the particularities of the mouse early embryonic cell cycle and review the mutations that result in cell cycle defects during mouse early embryogenesis, including deficiencies for genes of the cyclin family (cyclin A2 and B1), genes involved in cell cycle checkpoints (Mad2, Bub3, Chk1, Atr), genes involved in ubiquitin and ubiquitin-like pathways (Uba3, Ubc9, Cul1, Cul3, Apc2, Apc10, Csn2) as well as genes the function of which had not been previously ascribed to cell cycle regulation (Cdc2P1, E4F and Omcg1).
Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1.
Schulman et al., Memphis, United States. In Mol Cell, 2005
crystal structure of a complex between the C-terminal domain from NEDD8's heterodimeric E1 (APPBP1-UBA3) and the catalytic core domain of NEDD8's E2 (Ubc12)
APP induces neuronal apoptosis through APP-BP1-mediated downregulation of beta-catenin.
Chen, United States. In Apoptosis, 2004
This mini-review focuses on how the amyloid precursor protein (APP) plays a central role in AD and Down syndrome as the regulator of the APP-BP1/hUba3 activated neddylation pathway.
The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1.
Schulman et al., Memphis, United States. In Mol Cell, 2003
Data report the structure of the quaternary complex between human APPBP1-UBA3, a heterodimeric E1, its ubl NEDD8, and ATP.
Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer.
Haas et al., Milwaukee, United States. In J Biol Chem, 2003
Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer.
Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8.
Schulman et al., Memphis, United States. In Nature, 2003
structure and mutational analysis of human APPBP1-UBA3, the heterodimeric E1 enzyme for NEDD8
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