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Ubiquitin-conjugating enzyme E2S

Ubiquitin-Protein Ligases
This gene encodes a member of the ubiquitin-conjugating enzyme family. The encoded protein is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a characteristic property of ubiquitin carrier proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, Rsp5, Cbl, E4
Papers on Ubiquitin-Protein Ligases
Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction.
Gardner et al., Seattle, United States. In Mol Biol Cell, 2013
Ubiquitin-protein ligases (E3s) that ubiquitinate substrates for proteasomal degradation are often in the position of ubiquitinating themselves due to interactions with a charged ubiquitin-conjugating enzyme (E2).
The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2.
Impact
GeneRIF
Rape et al., Berkeley, United States. In Cell, 2011
Linkage-specific ubiquitin chain formation by Ube2S is the result of substrate-assisted catalysis.
Deregulation of E2-EPF ubiquitin carrier protein in papillary renal cell carcinoma.
GeneRIF
Ohh et al., Toronto, Canada. In Am J Pathol, 2011
These findings reveal deregulation of the oxygen-sensing pathway impinging on the positive feedback mechanism of HIF1-mediated regulation of E2-EPF in papillary renal cell carcinoma.
Use of proteome arrays to globally identify substrates for E3 ubiquitin ligases.
Rotin et al., Toronto, Canada. In Methods Mol Biol, 2010
Ubiquitin-protein ligases (E3s) are responsible for target recognition and subsequent modification of selected substrates within the ubiquitin proteasomal system (UPS).
UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex.
GeneRIF
Kirschner et al., Boston, United States. In Proc Natl Acad Sci U S A, 2010
K11 specificity is determined by an E2 enzyme, UBE2S/E2-EPF, that elongates ubiquitin chains after the substrates are pre-ubiquitinated by UbcH10 or UbcH5.
UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit.
Impact
GeneRIF
Venkitaraman et al., Cambridge, United Kingdom. In Nat Cell Biol, 2009
UBE2S functions with the APC/C in a two-step mechanism to control substrate ubiquitylation that is essential for mitotic exit after prolonged SAC activation, providing a new model for APC/C function in human cells
Identification of a physiological E2 module for the human anaphase-promoting complex.
GeneRIF
Rape et al., Berkeley, United States. In Proc Natl Acad Sci U S A, 2009
UbcH10 and Ube2S constitute a physiological E2-module for anaphase-promoting complex, the activity of which is required for spindle assembly and cell division.
Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast.
Rotin et al., Toronto, Canada. In Mol Syst Biol, 2006
Ubiquitin-protein ligases (E3s) are responsible for target recognition and regulate stability, localization or function of their substrates.
Ubiquitin-protein ligases in muscle wasting.
Review
Lecker et al., Boston, United States. In Int J Biochem Cell Biol, 2005
Recent studies demonstrate that two ubiquitin-protein ligases (E3s), atrogin-1/MAFbx and MuRF1 are critical in the development of muscle atrophy.
A high throughput screen to identify substrates for the ubiquitin ligase Rsp5.
Rotin et al., Toronto, Canada. In J Biol Chem, 2005
Ubiquitin-protein ligases (E3s) are implicated in various human disorders and are attractive targets for therapeutic intervention.
Ubiquitin-protein ligases--novel therapeutic targets?
Review
Ardley et al., Leeds, United Kingdom. In Curr Protein Pept Sci, 2004
The key components that regulate substrate ubiquitylation are the ubiquitin-protein ligases.
Ubiquitylation as a quality control system for intracellular proteins.
Review
Nakayama et al., Fukuoka, Japan. In J Biochem, 2003
Ubiquitin-protein ligases (E3s) determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families.
Proteolytic targeting of transcriptional regulator TIP120B by a HECT domain E3 ligase.
Pickart et al., Baltimore, United States. In J Biol Chem, 2003
Ubiquitin-protein ligases (E3s) of the HECT family share a conserved catalytic region that is homologous to the E6-AP C terminus.
Ubiquitin-protein ligases in muscle wasting: multiple parallel pathways?
Review
Lecker, Boston, United States. In Curr Opin Clin Nutr Metab Care, 2003
RECENT FINDINGS: Recent experiments have shown that two newly identified ubiquitin-protein ligases (E3s), atrogin-1/MAFbx and MURF-1, are critical in the development of muscle atrophy.
U-box proteins as a new family of ubiquitin ligases.
Review
Nakayama et al., Fukuoka, Japan. In Biochem Biophys Res Commun, 2003
Ubiquitin-protein ligases (E3s) determine the substrate specificity of ubiquitylation and, until recently, had been classified into two families, the HECT and RING-finger families.
Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation.
Impact
Hampton et al., San Diego, United States. In Nat Cell Biol, 2001
Ubiquitin-protein ligases (E3s) play a crucial role in this process by recognizing target proteins and initiating their ubiquitination.
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.
Impact
Pavletich et al., New York City, United States. In Cell, 2000
Ubiquitin-protein ligases (E3s) regulate diverse cellular processes by mediating protein ubiquitination.
The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase.
Impact
Liu et al., Los Angeles, United States. In Science, 1999
Ubiquitin-protein ligases (or E3s) are the components of ubiquitination pathways that recognize target substrates and promote their ligation to ubiquitin.
Effect of stress on protein degradation: role of the ubiquitin system.
Review
Kulka et al., Jerusalem, Israel. In Acta Biol Hung, 1990
Ubiquitin-protein ligases (E3's) which attach multi-ubiquitin chains to proteins are thought to be responsible for the selection of proteins for degradation.
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