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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Ring finger protein 115

BCA2, RNF115, ZNF364
Top mentioned proteins: Ubiquitin, BST2, CAN, Ubc9, ACID
Papers on BCA2
Characterization and expression analysis of BCA2 gene in large yellow croaker, Larimichthys crocea.
Wang et al., Xiamen, China. In Fish Shellfish Immunol, Oct 2015
BCA2, as an E3 ubiquitin ligase, is an important anti-virus immune factor in mammals.
Genome-wide association analysis of more than 120,000 individuals identifies 15 new susceptibility loci for breast cancer.
Easton et al., Brisbane, Australia. In Nat Genet, Apr 2015
Combining association analysis with ChIP-seq chromatin binding data in mammary cell lines and ChIA-PET chromatin interaction data from ENCODE, we identified likely target genes in two regions: SETBP1 at 18q12.3 and RNF115 and PDZK1 at 1q21.1.
BCA2/Rabring7 targets HIV-1 Gag for lysosomal degradation in a tetherin-independent manner.
Serra-Moreno et al., United States. In Plos Pathog, 2014
BCA2 (Rabring7, RNF115 or ZNF364) is a RING-finger E3 ubiquitin ligase that was identified as a co-factor in the restriction imposed by tetherin/BST2 on HIV-1.
ATLs and BTLs, plant-specific and general eukaryotic structurally-related E3 ubiquitin ligases.
Guzmán, Irapuato, Mexico. In Plant Sci, 2014
Arabidopsis Tóxicos en Levadura (ATLs) and BCA2 zinc finger ATLs (BTLs) are two families of ubiquitin ligases that share some common structural features.
Regulation of metformin response by breast cancer associated gene 2.
Dou et al., Detroit, United States. In Neoplasia, 2013
Breast cancer associated gene 2 (BCA2/Rabring7/RNF115), a novel Really Interesting New Gene (RING) finger ubiquitin E3 ligase, is overexpressed in >50% of breast tumors.
RNF115/BCA2 E3 ubiquitin ligase promotes breast cancer cell proliferation through targeting p21Waf1/Cip1 for ubiquitin-mediated degradation.
Chen et al., Kunming, China. In Neoplasia, 2013
The E3 ubiquitin ligase RING finger protein 115 (RNF115), also known as breast cancer-associated gene 2 (BCA2), has previously been reported to be overexpressed in estrogen receptor α (ERα)-positive breast tumors and to promote breast cell proliferation; however, its mechanism is unknown.
Novel inhibitors of Rad6 ubiquitin conjugating enzyme: design, synthesis, identification, and functional characterization.
Shekhar et al., Detroit, United States. In Mol Cancer Ther, 2013
SMI #9 inhibition of Rad6 was selective as BCA2 ubiquitination by E2 UbcH5 was unaffected by SMI #9.
BCA2 is differentially expressed in renal oncocytoma: an analysis of 158 renal neoplasms.
Osunkoya et al., Atlanta, United States. In Tumour Biol, 2013
All RING E3 ligases, including BCA2, contain a consensus protein sequence that would complex two or more zinc ions in the expressed protein.
Expansion and diversification of BTL ring-H2 ubiquitin ligases in angiosperms: putative Rabring7/BCA2 orthologs.
Guzmán et al., Irapuato, Mexico. In Plos One, 2012
BTLs are putative orthologs of the mammalian Rabring7/BCA2 RING-H2 E3s that have expanded in angiosperms.
Transcriptional activation of breast cancer-associated gene 2 by estrogen receptor.
Dou et al., Detroit, United States. In Breast Cancer Res Treat, 2012
RNF115, or Breast Cancer-Associated Gene 2 (BCA2), encodes a RING-finger ubiquitin E3 ligase, expression of which was associated with estrogen receptor (ER)-positive status in human breast tumors.
Effects of partner proteins on BCA2 RING ligase activity.
Seth et al., Toronto, Canada. In Bmc Cancer, 2011
BACKGROUND: BCA2 is an E3 ligase linked with hormone responsive breast cancers.
Early in vitro passages of breast cancer cells are differentially susceptible to retinoids and differentially express RARβ isoforms.
Christov et al., Chicago, United States. In Int J Oncol, 2011
However, only one EPBCC (BCA-2) expressed RARβ5 at mRNA and protein level and it was resistant to retinoids, both in vitro and in a xenograft tumor assay.
Roles of E3 ubiquitin ligases in cell adhesion and migration.
Huang, Chapel Hill, United States. In Cell Adh Migr, 2010
Recent studies have demonstrated that a number of E3 ubiquitin ligases, including Cbl, Smurf1, Smurf2, HDM2, BCA2, SCF(beta-TRCP) and XRNF185, play important roles in cell adhesion and migration.
Role of the BCA2 ubiquitin E3 ligase in hormone responsive breast cancer.
Seth et al., Detroit, United States. In Open Cancer J, 2009
The BCA2 protein contains a RING H2 finger and a Zn finger near the N-terminus and has E3 ligase activity.
BCA2/Rabring7 promotes tetherin-dependent HIV-1 restriction.
Yamamoto et al., Tokyo, Japan. In Plos Pathog, 2009
BCA2 accelerates the internalization and degradation of viral particles following their tethering to the cell surface and is a co-factor or enhancer for the tetherin-dependent restriction of HIV-1 release from infected cells.
Involvement of Rabring7 in EGF receptor degradation as an E3 ligase.
Sasaki et al., Tokushima, Japan. In Biochem Biophys Res Commun, 2007
These results suggest that Rabring7 is involved in the endocytic trafficking of EGFR through its E3 ligase activity.
Novel RING E3 ubiquitin ligases in breast cancer.
Seth et al., Toronto, Canada. In Neoplasia, 2006
BCA2 E3 ligase is coregulated with estrogen receptor and plays a role in the regulation of epidermal growth factor receptor (EGF-R) trafficking
A novel RING-type ubiquitin ligase breast cancer-associated gene 2 correlates with outcome in invasive breast cancer.
Seth et al., Toronto, Canada. In Cancer Res, 2005
The autoubiquitination activity of BCA2 indicates that it is a novel RING-type E3 ligase.
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