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Ubiquitin-like modifier activating enzyme 7

UBE1L, D-8, Ube-2
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 is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ISG15, Ubiquitin, UbcH8, ACID, HAD
Papers on UBE1L
Mechanism of Dose-Dependent Regulation of UBE1L by Polyphenols in Human Bronchial Epithelial Cells.
Feng et al., Nanjing, China. In J Cell Biochem, Aug 2015
Ubiquitin activating enzyme E1-like (UBE1L) is the activating enzyme for ISG15ylation (ISG15, interferon stimulated gene 15).
Murine Herc6 Plays a Critical Role in Protein ISGylation In Vivo and Has an ISGylation-Independent Function in Seminal Vesicles.
Shimotohno et al., San Diego, United States. In J Interferon Cytokine Res, May 2015
ISG15 conjugation (ISGylation) to proteins is a multistep process involving interferon (IFN)-inducible UBE1L (E1), UbcH8 (E2), and ISG15 E3 ligases (E3s).
Protein interferon-stimulated gene 15 conjugation delays but does not overcome coronavirus proliferation in a model of fulminant hepatitis.
McGilvray et al., Toronto, Canada. In J Virol, 2014
Decreasing ISGylation by knockdown of the ISG15 E1 enzyme, Ube1L, in primary USP18(+/+) and USP18(-/-) hepatocytes led to increased MHV-3 replication.
Down-regulation of epidermal growth factor receptor by curcumin-induced UBE1L in human bronchial epithelial cells.
Feng et al., Nanjing, China. In J Nutr Biochem, 2014
UBE1L, ubiquitin-activating enzyme E1-like, is the activating enzyme of ISG15ylation (ISG15, interferon stimulated gene 15).
Repression of exogenous gene expression by the retinoic acid target gene G0S2.
Dmitrovsky et al., United States. In Int J Oncol, 2013
Transient G0S2 transfection repressed the activities of multiple reporter constructs (including the retinoid-regulated species RARβ, UBE1L and G0S2); this occurred in diverse cell contexts.
Molecular epidemiological survey of hemoglobinopathies in the Wuxi region of Jiangsu Province, eastern China.
Yang et al., Chaozhou, China. In Hemoglobin, 2012
Eight genotypes of Hb variants were found, including Hb E [β26(B8)Glu→Lys, GAG>AAG; HBB: c.79G>A], Hb J-Bangkok [β56(D7)Gly→Asp (GGC>GAC); HBB; c.170G>A], Hb G-Coushatta [β22(4)Glu→Ala (GAA>GCA); HBB: c.68A>C], Hb Queens [α34(B15)Leu→Arg (CTG>CGG) (α2 or α1); HBA2: c.104T>G (or HBA1)], Hb I [α16(A14)Lys→Glu, AAG>GAG (α1); HBA1: c.49A>G], Hb Beijing [α16(A14)Lys→Asn (AAG>AAC or AAT) (α2 or α1); HBA2: c.51G>C (or HBA1) or 51G>T (or HBA1)], Hb Ube-2 [α68(E17)Asn→Asp (AAC>GAC) (α2 or α1); HBA2: c.205A>G (or HBA1)] and Hb G-Taipei [β22(B4)Glu→Gly (GAA>GGA); HBB: c.68A>G].
Evidence for the ubiquitin protease UBP43 as an antineoplastic target.
Dmitrovsky et al., United States. In Mol Cancer Ther, 2012
One candidate pathway to target is composed of the E1-like ubiquitin-activating enzyme (UBE1L) that associates with interferon-stimulated gene 15 (ISG15), which complexes with and destabilizes cyclin D1.
[Advances in ubiquitin-like protein ISG15-mediated anti-viral response].
Ma et al., Shanghai, China. In Bing Du Xue Bao, 2012
ISGylation system contains ISG15, UBE1L, UBCH8 and HERC5 proteins, which are all essential for ISGylation.
The ISG15 conjugation system.
Huibregtse et al., Austin, United States. In Methods Mol Biol, 2011
The core E1, E2, and E3 enzymes for ISG15 are Ube1L, UbcH8, and Herc5, respectively, and these are all also induced at the transcriptional level by IFN-α/β.
Covalent protein modification with ISG15 via a conserved cysteine in the hinge region.
Praefcke et al., Köln, Germany. In Plos One, 2011
While the ISG15 activating enzyme UBE1L is conjugated by ISG15 in the classical way, we show that the ubiquitin conjugating enzyme Ubc13 can either be classically conjugated by ISG15 or can form a disulphide bridge with ISG15 at the active site cysteine 87.
ISG15 is critical in the control of Chikungunya virus infection independent of UbE1L mediated conjugation.
Lenschow et al., Saint Louis, United States. In Plos Pathog, 2011
Chikungunya virus (CHIKV) is a re-emerging alphavirus that has caused significant disease in the Indian Ocean region since 2005.
The defective nuclear lamina in Hutchinson-gilford progeria syndrome disrupts the nucleocytoplasmic Ran gradient and inhibits nuclear localization of Ubc9.
Paschal et al., Charlottesville, United States. In Mol Cell Biol, 2011
the cellular effects of progerin expression in Hutchinson-Gilford progeria syndrome are transduced, at least in part, through reduced function of the Ran GTPase and E2 SUMOylation pathways.
Hematopoietic cells from Ube1L-deficient mice exhibit an impaired proliferation defect under the stress of bone marrow transplantation.
Zhang et al., San Diego, United States. In Blood Cells Mol Dis, 2010
Bone marrow transplantation experiment revealed a 50% reduction in repopulation potential of Ube1L-deficient cells at 3weeks posttransplantation, but no differences at 6 and 12weeks.
ISG15 and immune diseases.
Chung et al., Seoul, South Korea. In Biochim Biophys Acta, 2010
A set of three-step cascade enzymes, an E1 enzyme (UBE1L), an E2 enzyme (UbcH8), and one of several E3 ligases (e.g., EFP and HERC5), catalyzes ISG15 conjugation (ISGylation) of a specific protein.
Identification and Validation of ISG15 Target Proteins.
Huibregtse et al., Austin, United States. In Subcell Biochem, 2009
The core E1, E2 and E3 enzymes for conjugation of human ISG15 are Ube1L, UbcH8 and Herc5, all of which are induced at the transcriptional level by Type 1 interferon signaling.
ISG15 Arg151 and the ISG15-conjugating enzyme UbE1L are important for innate immune control of Sindbis virus.
Virgin et al., Saint Louis, United States. In J Virol, 2009
The importance of UbE1L was confirmed by demonstrating that mice lacking this ISG15 E1 enzyme were highly susceptible to Sindbis virus infection.
Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection.
Lenschow et al., Saint Louis, United States. In J Virol, 2009
Both UbE1L(-/-) and ISG15(-/-) mice display increased susceptibility to influenza B virus infection, including non-mouse-adapted strains.
UBE1L causes lung cancer growth suppression by targeting cyclin D1.
Dmitrovsky et al., United States. In Mol Cancer Ther, 2008
UBE1L-ISG15 preferentially inhibits cyclin D1 in lung cancer
Uncovering novel targets for cancer chemoprevention.
Dmitrovsky et al., United States. In Recent Results Cancer Res, 2006
Gene profiling experiments highlighted the E1-like ubiquitin-activating enzyme (UBE1L) in the retinoid regulation of cyclin D1.
Retinoid targets in cancer therapy and chemoprevention.
Dmitrovsky et al., United States. In Cancer Biol Ther, 2003
Microarray analysis revealed involvement of an E1-like ubiquitin-activating enzyme, UBE1L, in this induction.
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