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SH3-domain binding protein 2

SH3BP2, 3BP2
The protein encoded by this gene has an N-terminal pleckstrin homology (PH) domain, an SH3-binding proline-rich region, and a C-terminal SH2 domain. The protein binds to the SH3 domains of several proteins including the ABL1 and SYK protein tyrosine kinases , and functions as a cytoplasmic adaptor protein to positively regulate transcriptional activity in T, natural killer (NK), and basophilic cells. Mutations in this gene result in cherubism. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009] (from NCBI)
Top mentioned proteins: Src, ABL, NBS1, Syk, ACID
Papers on SH3BP2
The adaptor 3BP2 is required for KIT receptor expression and human mast cell survival.
Martín et al., Barcelona, Spain. In J Immunol, Jun 2015
SH3-binding protein 2 (3BP2) is a cytoplasmic adaptor protein that acts as a positive regulator in mast cell FcεRI-dependent signaling.
The calcineurin inhibitor tacrolimus as a new therapy in severe cherubism.
Coudert et al., Paris, France. In J Bone Miner Res, May 2015
Cherubism is caused by gain-of-function mutations in the SH3BP2 gene, leading to overactivation of nuclear factor of activated T cells, cytoplasmic 1 (NFATc1)-dependent osteoclastogenesis.
Cherubism allele heterozygosity amplifies microbe-induced inflammatory responses in murine macrophages.
Deckert et al., In J Clin Invest, Apr 2015
Cherubism is a rare autoinflammatory bone disorder that is associated with point mutations in the SH3-domain binding protein 2 (SH3BP2) gene, which encodes the adapter protein 3BP2.
Loss of SH3 domain-binding protein 2 function suppresses bone destruction in tumor necrosis factor-driven and collagen-induced arthritis in mice.
Ueki et al., Kansas City, United States. In Arthritis Rheumatol, Mar 2015
OBJECTIVE: SH3 domain-binding protein 2 (SH3BP2) is a signaling adapter protein that regulates the immune and skeletal systems.
Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal.
Xu et al., Seattle, United States. In Nature, Feb 2015
Recent studies have shown that PARylation can serve as a signal for the polyubiquitination and degradation of several crucial regulatory proteins, including Axin and 3BP2 (refs 7, 8, 9).
Cherubism misdiagnosed as giant cell tumor: a case report and review of literature.
Duan et al., Xi'an, China. In Int J Clin Exp Med, 2014
The family history suggested us to perform sequence analysis of the SH3BP2 gene, a candidate marker for cherubism, in the family, and it was found that both the proband and the son had a missense mutation in SH3BP2 in exon 9 (p.
A c.1244G>A (p.Arg415Gln) mutation in SH3BP2 gene causes cherubism in a Turkish family: report of a family with review of the literature.
Bayrakdar et al., Kayseri, Turkey. In Med Oral Patol Oral Cir Bucal, 2014
Overall, a total of four family members were tested for SH3BP2 mutations, namely two siblings and their parents.
[Syk inhibitors].
Sada et al., Fukui, Japan. In Nihon Rinsho, 2013
Furthermore, we will introduce our findings of the adaptor protein 3BP2 (c-Abl SH3 domain-binding protein-2), as a novel target of Syk.
The 3BP2 adapter protein is required for chemoattractant-mediated neutrophil activation.
Rottapel et al., Toronto, Canada. In J Immunol, 2012
Adapter protein 3BP2 links chemoattractant fMLF-induced receptor signaling events to neutrophil actin cytoskeleton and NADPH oxidase complex, a requirement for effective bactericidal function in vivo.
The role of SH3BP2 in the pathophysiology of cherubism.
Lietman et al., Farmington, United States. In Orphanet J Rare Dis, 2012
Most patients with cherubism have germline mutations in the gene encoding SH3BP2, an adapter protein involved in adaptive and innate immune response signaling.
Cherubism: best clinical practice.
Reichenberger et al., Boston, United States. In Orphanet J Rare Dis, 2012
In most patients, cherubism is due to dominant mutations in the SH3BP2 gene on chromosome 4p16.3.
Loss of Tankyrase-mediated destruction of 3BP2 is the underlying pathogenic mechanism of cherubism.
Rottapel et al., Toronto, Canada. In Cell, 2012
Study shows that TNKS2, regulates 3BP2 stability through ADP-ribosylation and subsequent ubiquitylation in osteoclasts; cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction.
Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease.
Sicheri et al., Toronto, Canada. In Cell, 2012
This 8-residue consensus allows us to rationalize all known Tankyrase substrates and explains the basis for cherubism-causing mutations in the Tankyrase substrate 3BP2.
Tankyrase loses its grip on SH3BP2 in cherubism.
Olsen et al., Boston, United States. In Cell, 2012
Cherubism, a case of bone remodeling gone haywire, is associated with mutations in the adaptor protein SH3BP2.
Enhancement of B-cell receptor signaling by a point mutation of adaptor protein 3BP2 identified in human inherited disease cherubism.
Sada et al., Fukui, Japan. In Genes Cells, 2011
P416R mutation of 3BP2 causes the gain of function in B cells by increasing the interaction with specific signaling molecules.
3BP2-deficient mice are osteoporotic with impaired osteoblast and osteoclast functions.
Rottapel et al., Toronto, Canada. In J Clin Invest, 2011
3BP2 adapter protein has an unanticipated role in osteoblast function and in coordinating bone homeostatic signals in both osteoclast and osteoblast lineages
A concerted HIF-1α/MT1-MMP signalling axis regulates the expression of the 3BP2 adaptor protein in hypoxic mesenchymal stromal cells.
Annabi et al., Montréal, Canada. In Plos One, 2010
Data provide evidence for a concerted HIF-1alpha/MT1-MMP signalling axis that explains the induction of adaptor protein 3BP2 and which may link protein binding partners together and stimulate oncogenic MSC migration.
Ray et al., Seattle, United States. In Unknown Journal, 2007
SH3BP2 is the only gene in which mutation is currently known to cause cherubism.
Increased myeloid cell responses to M-CSF and RANKL cause bone loss and inflammation in SH3BP2 "cherubism" mice.
Olsen et al., Boston, United States. In Cell, 2007
These results indicate that the mutant phenotype reflects gain of SH3BP2 function and suggests that SH3BP2 is a critical regulator of myeloid cell responses to M-CSF and RANKL stimulation.
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