Genomewide analysis of sperm whale E2 ubiquitin conjugating enzyme genes

We present classical molecular dynamics (MD), Born-Oppenheimer molecular dynamics (BOMD), and hybrid quantum mechanics/molecular mechanics (QM/MM) data. MD was performed using the GPU accelerated pmemd module of the AMBER14MD package. BOMD was performed using CP2K version 2.6. The reaction rates in BOMD were accelerated using the Metadynamics method. QM/MM was performed using ONIOM in the Gaussian09 suite of programs. Relevant input files for BOMD and QM/MM are available.

Download Full-text

Ubiquitin-conjugating enzyme E2 R1

Targeted Protein Database ◽

10.2970/tpdb.2007.79 ◽

2007 ◽

Author(s):

Gracia Diez-Roux

Keyword(s):

Ubiquitin Conjugating Enzyme ◽

Conjugating Enzyme

Download Full-text

Targeting neddylation E2s: a novel therapeutic strategy in cancer

Journal of Hematology & Oncology ◽

10.1186/s13045-021-01070-w ◽

2021 ◽

Vol 14 (1) ◽

Author(s):

Yi-Chao Zheng ◽

Yan-Jia Guo ◽

Bo Wang ◽

Chong Wang ◽

M. A. A. Mamun ◽

...

Keyword(s):

Posttranslational Modification ◽

Therapeutic Strategy ◽

Neural Precursor Cell ◽

Catalytic Core Domain ◽

Catalytic Core ◽

Core Domain ◽

E3 Ligases ◽

Ubiquitin Conjugating Enzyme ◽

E2 Enzymes ◽

Conjugating Enzyme

AbstractUbiquitin-conjugating enzyme E2 M (UBE2M) and ubiquitin-conjugating enzyme E2 F (UBE2F) are the two NEDD8-conjugating enzymes of the neddylation pathway that take part in posttranslational modification and change the activity of target proteins. The activity of E2 enzymes requires both a 26-residue N-terminal docking peptide and a conserved E2 catalytic core domain, which is the basis for the transfer of neural precursor cell-expressed developmentally downregulated 8 (NEDD8). By recruiting E3 ligases and targeting cullin and non-cullin substrates, UBE2M and UBE2F play diverse biological roles. Currently, there are several inhibitors that target the UBE2M-defective in cullin neddylation protein 1 (DCN1) interaction to treat cancer. As described above, this review provides insights into the mechanism of UBE2M and UBE2F and emphasizes these two E2 enzymes as appealing therapeutic targets for the treatment of cancers.

Download Full-text

Cell Cycle-Dependent Expression of Mammalian E2-C Regulated by the Anaphase-Promoting Complex/Cyclosome

Molecular Biology of the Cell ◽

10.1091/mbc.11.8.2821 ◽

2000 ◽

Vol 11 (8) ◽

pp. 2821-2831 ◽

Cited By ~ 36

Author(s):

Atsushi Yamanaka ◽

Shigetsugu Hatakeyama ◽

Kin-ichiro Kominami ◽

Masatoshi Kitagawa ◽

Masaki Matsumoto ◽

...

Keyword(s):

Cell Cycle ◽

Substrate Specificity ◽

Critical Role ◽

Anaphase Promoting Complex ◽

Polyubiquitin Chain ◽

M Phase ◽

Ubiquitin Conjugating Enzyme ◽

Recognition Motifs ◽

Cycle Dependent ◽

Conjugating Enzyme

Progression through mitosis requires the precisely timed ubiquitin-dependent degradation of specific substrates. E2-C is a ubiquitin-conjugating enzyme that plays a critical role with anaphase-promoting complex/cyclosome (APC/C) in progression of and exit from M phase. Here we report that mammalian E2-C is expressed in late G2/M phase and is degraded as cells exit from M phase. The mammalian E2-C shows an autoubiquitinating activity leading to covalent conjugation to itself with several ubiquitins. The ubiquitination of E2-C is strongly enhanced by APC/C, resulting in the formation of a polyubiquitin chain. The polyubiquitination of mammalian E2-C occurs only when cells exit from M phase. Furthermore, mammalian E2-C contains two putative destruction boxes that are believed to act as recognition motifs for APC/C. The mutation of this motif reduced the polyubiquitination of mammalian E2-C, resulting in its stabilization. These results suggest that mammalian E2-C is itself a substrate of the APC/C-dependent proteolysis machinery, and that the periodic expression of mammalian E2-C may be a novel autoregulatory system for the control of the APC/C activity and its substrate specificity.

Download Full-text