PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12530983-2 2003 Here, we show that antigen-induced formation of T cell:APC conjugates and synapses is abrogated in WASp-deficient T cells and that CD2 engagement evokes interactions between the proline-rich region required for WASp translocation to the synapse and the PSTPIP1 adaptor SH3 domain and between the PSTPIp1 coiled-coil domain and both CD2 and another CD2-binding adaptor, CD2AP. Proline 178-185 CD2 molecule Homo sapiens 332-335 16941565-1 2006 The cytoplasmic region of the CD2 receptor of lymphocytes contains proline-rich motifs, which are involved in T cell activation and interleukin-2 production. Proline 67-74 CD2 molecule Homo sapiens 30-33 17467737-2 2007 U5-52K binds to the CD2 receptor via its GYF-domain specifically recognizing a proline-rich motif on the cytoplasmic surface of the receptor. Proline 79-86 CD2 molecule Homo sapiens 20-23 12530983-2 2003 Here, we show that antigen-induced formation of T cell:APC conjugates and synapses is abrogated in WASp-deficient T cells and that CD2 engagement evokes interactions between the proline-rich region required for WASp translocation to the synapse and the PSTPIP1 adaptor SH3 domain and between the PSTPIp1 coiled-coil domain and both CD2 and another CD2-binding adaptor, CD2AP. Proline 178-185 CD2 molecule Homo sapiens 131-134 12530983-2 2003 Here, we show that antigen-induced formation of T cell:APC conjugates and synapses is abrogated in WASp-deficient T cells and that CD2 engagement evokes interactions between the proline-rich region required for WASp translocation to the synapse and the PSTPIP1 adaptor SH3 domain and between the PSTPIp1 coiled-coil domain and both CD2 and another CD2-binding adaptor, CD2AP. Proline 178-185 CD2 molecule Homo sapiens 332-335 10404223-1 1999 T cell activation through the CD2 cell surface receptor is transmitted by proline-rich sequences within its cytoplasmic tail. Proline 74-81 CD2 molecule Homo sapiens 30-33 12426371-2 2002 In T cells, the CD2BP2 adaptor binds two membrane-proximal proline-rich motifs in the CD2 cytoplasmic tail via its GYF domain, thereby regulating interleukin-2 production. Proline 59-66 CD2 molecule Homo sapiens 16-19 12426371-5 2002 NMR analysis shows that the Fyn but not the Lck tyrosine kinase SH3 domain competes with CD2BP2 GYF-domain binding to the same CD2 proline-rich sequence in vitro. Proline 131-138 CD2 molecule Homo sapiens 89-92 12426371-6 2002 To test the in vivo significance of this competition, we used co-immunoprecipitation experiments and found that CD2BP2 is the ligand of the membrane-proximal proline-rich tandem repeat of CD2 in detergent-soluble membrane compartments, but is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering. Proline 158-165 CD2 molecule Homo sapiens 112-115 12426371-6 2002 To test the in vivo significance of this competition, we used co-immunoprecipitation experiments and found that CD2BP2 is the ligand of the membrane-proximal proline-rich tandem repeat of CD2 in detergent-soluble membrane compartments, but is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering. Proline 158-165 CD2 molecule Homo sapiens 188-191 12426371-6 2002 To test the in vivo significance of this competition, we used co-immunoprecipitation experiments and found that CD2BP2 is the ligand of the membrane-proximal proline-rich tandem repeat of CD2 in detergent-soluble membrane compartments, but is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering. Proline 158-165 CD2 molecule Homo sapiens 188-191 10430626-5 1999 Here we demonstrate that Lck and Fyn can be activated by proline motifs in the CD28 and CD2 proteins, respectively. Proline 57-64 CD2 molecule Homo sapiens 79-82 10404223-2 1999 A membrane-proximal proline-rich tandem repeat, involved in cytokine production, is recognized by the intracellular CD2 binding protein CD2BP2. Proline 20-27 CD2 molecule Homo sapiens 116-119 2820751-4 1987 The cytoplasmic region of T11 is a lengthy, proline-rich segment; secondary structural analysis predicts it to have a nonglobular conformation. Proline 44-51 CD2 molecule Homo sapiens 26-29 8551220-0 1996 The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2. Proline 34-41 CD2 molecule Homo sapiens 86-89 8551220-7 1996 Thus, proline-rich sequences in the cytoplasmic domain of CD2 allow this transmembrane receptor to bind to the SH3 domain of p56lck. Proline 6-13 CD2 molecule Homo sapiens 58-61 8562067-7 1995 Amino acid analysis, Edman degradation, and FAB-MS identified T11 as the N-blocked decapeptide pyro-Gln-Pro-Val-Trp-Gln-Asp-Glu-Gly-Gln-Arg derived from the N-terminus of pZPC. Proline 104-107 CD2 molecule Homo sapiens 62-65 9843987-0 1998 Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation. Proline 20-27 CD2 molecule Homo sapiens 53-56 9710614-0 1998 Identification of a proline-rich sequence in the CD2 cytoplasmic domain critical for regulation of integrin-mediated adhesion and activation of phosphoinositide 3-kinase. Proline 20-27 CD2 molecule Homo sapiens 49-52 9710614-6 1998 A proline-rich sequence, K-G-P-P-L-P (amino acids 299 to 305), is essential for CD2-mediated regulation of beta1 integrin activity. Proline 2-9 CD2 molecule Homo sapiens 80-83 9710614-10 1998 Mutation of the proline residues in the K-G-P-P-L-P motif to alanines prevented CD2-mediated activation of integrin function and PI 3-K activity but not mitogen-activated protein (MAP) kinase activity. Proline 16-23 CD2 molecule Homo sapiens 80-83 9710614-12 1998 These studies identify a proline-rich sequence in CD2 critical for PI 3-K-dependent regulation of beta1 integrin adhesion by CD2. Proline 25-32 CD2 molecule Homo sapiens 50-53 9710614-12 1998 These studies identify a proline-rich sequence in CD2 critical for PI 3-K-dependent regulation of beta1 integrin adhesion by CD2. Proline 25-32 CD2 molecule Homo sapiens 125-128 9485403-1 1998 The N-terminal domain of phosphoglycerate kinase (N-PGK) and domain 1 of the T-cell adhesion protein CD2 (CD2.d1) fold through rapidly formed and transiently populated intermediate states in reactions which have no kinetic complications arising from proline isomerization or disulfide bonding. Proline 250-257 CD2 molecule Homo sapiens 101-104 9485403-1 1998 The N-terminal domain of phosphoglycerate kinase (N-PGK) and domain 1 of the T-cell adhesion protein CD2 (CD2.d1) fold through rapidly formed and transiently populated intermediate states in reactions which have no kinetic complications arising from proline isomerization or disulfide bonding. Proline 250-257 CD2 molecule Homo sapiens 106-112 7213661-0 1980 Hemoglobin Milledgeville (alpha 44 (CD2) Pro leads to Leu): a new variant with increased oxygen affinity. Proline 41-44 CD2 molecule Homo sapiens 36-39 7213661-7 1980 The alpha CD2 proline residue normally participates in the formation of the alpha 1 beta 2 subunit interface in the deoxy quaternary conformation, but not in oxyhemoglobin; the leucine substitution may produce destabilization of the deoxy conformation with a resulting shift in equilibrium toward the oxy conformation. Proline 14-21 CD2 molecule Homo sapiens 10-13 23663663-0 2013 Multimeric and differential binding of CIN85/CD2AP with two atypical proline-rich sequences from CD2 and Cbl-b*. Proline 69-76 CD2 molecule Homo sapiens 45-48 23663663-2 2013 Using NMR, isothermal titration calorimetry and small-angle X-ray scattering methods, we have characterized several binding modes of the N-terminal SH3 domain (SH3A) of CD2AP and CIN85 with two natural atypical proline-rich regions in CD2 (cluster of differentiation 2) and Cbl-b (Casitas B-lineage lymphoma), and compared these data with previous studies and published crystal structures. Proline 211-218 CD2 molecule Homo sapiens 169-172