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CD2BP2 gene

Known as: LIN1, CD2 (Cytoplasmic Tail) Binding Protein 2 Gene, PPP1R59 
This gene plays a role in both spliceosome assembly and T-cell activation.
National Institutes of Health

Related topics

Related topics

5 relations
CD2 Antigen Cytoplasmic Tail-Binding Protein 2CD2BP2 wt AlleleLigand BindingRNA Splicing

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2016
Highly Cited
2016
The Dengue Virus NS5 Protein Intrudes in the Cellular Spliceosome and Modulates Splicing
Dengue virus NS5 protein plays multiple functions in the cytoplasm of infected cells, enabling viral RNA replication and… 
Highly Cited
2013
Highly Cited
2013
Src activation by b-adrenoreceptors is a key switch for tumour metastasis
Guillermo N. Armaiz-Pena1, Julie K. Allen1,2, Anthony Cruz3, Rebecca L. Stone1, Alpa M. Nick1, Yvonne G. Lin1, Liz Y. Han1… 
Highly Cited
2011
Highly Cited
2011
Chloroplast Genome Variation in Upland and Lowland Switchgrass
Switchgrass (Panicum virgatum L.) exists at multiple ploidies and two phenotypically distinct ecotypes. To facilitate… 
Highly Cited
2010
Highly Cited
2010
Linear relationship between increasing amounts of extruded linseed in dairy cow diet and milk fatty acid composition and butter properties.
The aim of this experiment was to compare the effects of increasing amounts of extruded linseed in dairy cow diet on milk fat… 
Highly Cited
2005
Highly Cited
2005
The putative high-affinity nitrate transporter NRT2.1 represses lateral root initiation in response to nutritional cues.
Lateral root initiation is strongly repressed in Arabidopsis by the combination of high external sucrose and low external nitrate… 
Highly Cited
2005
Highly Cited
2005
The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation.
The U5 snRNP plays an essential role in both U2- and U12-dependent splicing. Here, we have characterized a 52-kDa protein… 
2004
2004
Recognition Sequences for the GYF Domain Reveal a Possible Spliceosomal Function of CD2BP2*
Protein-protein interactions are often mediated by small domains that recognize solvent-exposed peptide sequences. Deciphering… 
Highly Cited
2002
Highly Cited
2002
Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules
Intracellular protein interaction domains are essential for eukaryotic signaling. In T cells, the CD2BP2 adaptor binds two… 
Highly Cited
1999
Highly Cited
1999
The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences
T cell activation through the CD2 cell surface receptor is transmitted by proline-rich sequences within its cytoplasmic tail. A… 
Highly Cited
1998
Highly Cited
1998
Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation.
An intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two PPPGHR segments within the… 
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