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Ubiquitin-like modifier activating enzyme 6

Uba6, UBE1L2, ubiquitin-like modifier activating enzyme 6
Modification of proteins with ubiquitin (UBB; MIM 191339) or ubiquitin-like proteins controls many signaling networks and requires a ubiquitin-activating enzyme (E1), a ubiquitin conjugating enzyme (E2), and a ubiquitin protein ligase (E3). UBE1L2 is an E1 enzyme that initiates the activation and conjugation of ubiquitin-like proteins (Jin et al., 2007 [PubMed 17597759]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, USE1, UBE1, CAN, fibrillin-1
Papers on Uba6
Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery.
Rucktooa et al., Amsterdam, Netherlands. In J Biol Chem, Feb 2016
FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes.
Interstitial microdeletions including the chromosome band 4q13.2 and the UBA6 gene as possible causes of intellectual disability and behavior disorder.
Eiris et al., Santiago de Compostela, Spain. In Am J Med Genet A, Dec 2015
and includes 17 genes amongst of which we suggest UBA6 (ubiquitin-like modifier-activating enzyme 6) as a strong candidate gene for these phenotypes.
Impairment of social behavior and communication in mice lacking the Uba6-dependent ubiquitin activation system.
Lee et al., Seoul, South Korea. In Behav Brain Res, Apr 2015
The Uba6-Use1 ubiquitin enzyme cascade is a poorly understood arm of the ubiquitin-proteasome system required for mouse development.
Digital quantitation of HCC-associated stem cell markers and protein quality control factors using tissue arrays of human liver sections.
French et al., Torrance, United States. In Exp Mol Pathol, 2014
UBA6 was increased in both the HCCs and the parent livers, and the levels were higher in the HCCs compared to the parent livers.
Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation.
Aichem et al., Kreuzlingen, Switzerland. In Plos One, 2014
The conjugation machinery consists of the bispecific E1 activating enzyme Ubiquitin-like modifier activating enzyme 6 (UBA6), the likewise bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1 (USE1), and possibly E3 ligases.
Exploration of salivary proteins in buffalo: an approach to find marker proteins for estrus.
Gulyas et al., Tiruchchir─üppalli, India. In Faseb J, 2014
On the whole, 37 proteins are exclusively expressed in the estrus phase, which include ╬▓-enolase, Toll-like receptor (TLR) 4, clusterin, lactoperoxidase, serotransferrin, TGM3, UBA6, and transducin.
Ufmylation and FATylation pathways are downregulated in human alcoholic and nonalcoholic steatohepatitis, and mice fed DDC, where Mallory-Denk bodies (MDBs) form.
French et al., Torrance, United States. In Exp Mol Pathol, 2014
The FAT10-specific E1 and E2 enzymes Uba6 and USE1, however, were found to be downregulated both in patients' livers and in the liver of DDC re-fed mice.
Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1.
Groettrup et al., Kreuzlingen, Switzerland. In Febs J, 2014
FAT10 is conjugated to its substrates via the bispecific, ubiquitin-activating and FAT10-activating enzyme UBA6, the likewise bispecific conjugating enzyme UBA6-specific E2 enzyme 1 (USE1), and possibly E3 ligases.
Altered social behavior and neuronal development in mice lacking the Uba6-Use1 ubiquitin transfer system.
Harper et al., Boston, United States. In Mol Cell, 2013
The Uba6 (E1)-Use1 (E2) ubiquitin transfer cascade is a poorly understood alternative arm of the ubiquitin proteasome system (UPS) and is required for mouse embryonic development, independent of the canonical Uba1-E2-E3 pathway.
Specificity of the E1-E2-E3 enzymatic cascade for ubiquitin C-terminal sequences identified by phage display.
Yin et al., Chicago, United States. In Acs Chem Biol, 2013
In this study, we used phage display to profile the specificity of the two human E1 enzymes, Ube1 and Uba6, toward the C-terminal sequence of UB ending with (71)LRLRGG(76).
The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation.
Groettrup et al., Kreuzlingen, Switzerland. In J Cell Sci, 2012
In addition to two already known FAT10-interacting proteins, histone deacetylase 6 and UBA6, we identified 569 novel FAT10-interacting proteins involved in different functional pathways such as autophagy, cell cycle regulation, apoptosis and cancer.
Mechanistic studies on activation of ubiquitin and di-ubiquitin-like protein, FAT10, by ubiquitin-like modifier activating enzyme 6, Uba6.
Dick et al., Cambridge, United States. In J Biol Chem, 2012
Data indicate the potential role of cytokine-induced FAT10 expression in regulating Uba6 pathways.
Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage.
Bartek et al., Praha, Czech Republic. In Cell Cycle, 2012
We show that siRNA-mediated knockdown of UBA1, but not of another UBA family member UBA6, impaired formation of both ubiquitin conjugates at the sites of DNA damage and IR-induced foci (IRIF) by the downstream components of the DSB response pathway, 53BP1 and BRCA1.
Activating the ubiquitin family: UBA6 challenges the field.
Hofmann et al., Konstanz, Germany. In Trends Biochem Sci, 2008
Ubiquitin-like modifier activating enzyme 6 activates not only ubiquitin, but also the ubiquitin-like modifier FAT10[review]
E1-L2 activates both ubiquitin and FAT10.
Chen et al., Dallas, United States. In Mol Cell, 2007
The identification of an E1-like protein, termed E1-L2, that activates both ubiquitin and another ubiquitin-like protein, FAT10, is reported.
UBE1L2, a novel E1 enzyme specific for ubiquitin.
Groettrup et al., Konstanz, Germany. In J Biol Chem, 2007
UBE1L2 is a novel E1 enzyme specific for ubiquitin
Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging.
Harper et al., Boston, United States. In Nature, 2007
Human Uba6 and Ube1 have distinct preferences for E2 charging in vitro, and their specificity depends in part on their C-terminal ubiquitin-fold domains, which recruit E2s
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