PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20109515-1 2010 Src kinase activity is regulated by the interaction of SH3 domain with protein sequences that are rich in proline residues. Proline 106-113 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 0-3 23169783-2 2013 Conventionally, activation of c-Src is often induced by the binding of proline-rich sequences to its SH3 domain. Proline 71-78 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 30-35 22078467-6 2011 Cortactin, an F-actin associated protein and a substrate of Src kinase, was found to interact with FAK through its SH3 domain and the C-terminal proline-rich regions of FAK. Proline 145-152 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 60-63 21236256-4 2011 Structural-functional studies suggest that the proline-rich motif in the N-terminus of AFAP is critical for c-Src activation, and subsequent SRE/AP-1 transactivation and the actin-binding domain in the AFAP C-terminus is negatively involved in the regulation of AFAP/c-Src mediated SRE/AP-1 transactivation. Proline 47-54 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 108-113 21236256-4 2011 Structural-functional studies suggest that the proline-rich motif in the N-terminus of AFAP is critical for c-Src activation, and subsequent SRE/AP-1 transactivation and the actin-binding domain in the AFAP C-terminus is negatively involved in the regulation of AFAP/c-Src mediated SRE/AP-1 transactivation. Proline 47-54 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 267-272 20173116-5 2010 We also demonstrate a novel and direct interaction between the SH3 domains of Lyn and Src with a conserved proline-rich motif in GMR-alpha and show a selective requirement for Src family kinases by the FIDelta mutant. Proline 107-114 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 86-89 20638934-8 2010 The mutation results in deletion of 11 amino acids in the N-terminus of the protein, a proline-rich region as a binding site for Src homology 3 (SH3) domains associated with Src-family protein tyrosine kinase (TK) pathway. Proline 87-94 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 129-132 20638934-8 2010 The mutation results in deletion of 11 amino acids in the N-terminus of the protein, a proline-rich region as a binding site for Src homology 3 (SH3) domains associated with Src-family protein tyrosine kinase (TK) pathway. Proline 87-94 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 174-178 20525694-3 2010 All have a highly conserved N-terminal tyrosine kinase binding domain, a catalytic RING finger domain, and a C-terminal proline-rich domain that mediates interactions with Src homology 3 (SH3) containing proteins. Proline 120-127 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 172-175 18342899-4 2008 SH2-Src interacts with a phosphotyrosine residue of ER and SH3-Src interacts with a proline rich sequence of AR. Proline 84-91 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 4-7 18342899-4 2008 SH2-Src interacts with a phosphotyrosine residue of ER and SH3-Src interacts with a proline rich sequence of AR. Proline 84-91 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 63-66 18571832-3 2008 The proline-rich regions contain several consensus PXXP motifs, which allow PELP1 to couple the ER with SH3 domain-containing kinase signaling proteins, such as Src and PI3K P85 regulatory subunit. Proline 4-11 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 161-164 17418139-1 2007 SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. Proline 163-170 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 21-24 17700527-3 2008 Here, we demonstrate that both hepatocytes growth factor (HGF) stimulation and v-Src transformation induce tyrosine phosphorylation of Dgk-alpha on Y335, through a mechanism requiring its proline-rich C-terminal sequence. Proline 188-195 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 81-84 17700527-4 2008 Moreover, we show that both proline-rich sequence and phosphorylation of Y335 of Dgk-alpha mediate: (i) its enzymatic activation, (ii) its ability to interact respectively with SH3 and SH2 domains of Src, (iii) its recruitment to the membrane. Proline 28-35 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 200-203 18083027-0 2008 In silico screening and biological evaluation of inhibitors of Src-SH3 domain interaction with a proline-rich ligand. Proline 97-104 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 63-66 18083027-2 2008 Here we report virtual screening for novel compounds that inhibit the Src-SH3 protein-protein interaction with a proline-rich peptide ligand. Proline 113-120 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 70-73 18083027-5 2008 A benzoquinoline derivative showed micromolar inhibition of binding between Src-SH3 and the proline-rich peptide. Proline 92-99 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 76-79 17178840-6 2007 We define the proline residues in hnRNP K in the proline-rich motifs P2 (amino acids [aa] 285 to 297) and P3 (aa 303 to 318), which are necessary and sufficient for the specific activation of c-Src, and we dissect the amino acid sequence (aa 216 to 226) of hnRNP K that mediates a second interaction with c-Src. Proline 14-21 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 192-197 17283076-6 2007 Pulldown analysis with glutathione S-transferase-fused proline-rich regions of PTP-PEST revealed coprecipitation of WASP, PYK2, c-Src, and PSTPIP proteins with the N-terminal region (amino acids 294-497) of PTP-PEST. Proline 55-62 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 128-133 17178840-6 2007 We define the proline residues in hnRNP K in the proline-rich motifs P2 (amino acids [aa] 285 to 297) and P3 (aa 303 to 318), which are necessary and sufficient for the specific activation of c-Src, and we dissect the amino acid sequence (aa 216 to 226) of hnRNP K that mediates a second interaction with c-Src. Proline 14-21 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 305-310 17178840-6 2007 We define the proline residues in hnRNP K in the proline-rich motifs P2 (amino acids [aa] 285 to 297) and P3 (aa 303 to 318), which are necessary and sufficient for the specific activation of c-Src, and we dissect the amino acid sequence (aa 216 to 226) of hnRNP K that mediates a second interaction with c-Src. Proline 49-56 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 192-197 17178840-6 2007 We define the proline residues in hnRNP K in the proline-rich motifs P2 (amino acids [aa] 285 to 297) and P3 (aa 303 to 318), which are necessary and sufficient for the specific activation of c-Src, and we dissect the amino acid sequence (aa 216 to 226) of hnRNP K that mediates a second interaction with c-Src. Proline 49-56 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 305-310 17189480-5 2007 The activity of Src, PI3, and Itk kinases, for example, is regulated by intramolecular interactions between their SH3 domain and internal proline-rich sequences. Proline 138-145 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 16-19 17094785-2 2006 We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl. Proline 135-142 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 58-61 17038311-0 2006 Proline-rich motifs in the parathyroid hormone (PTH)/PTH-related protein receptor C terminus mediate scaffolding of c-Src with beta-arrestin2 for ERK1/2 activation. Proline 0-7 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 116-121 17038311-12 2006 Subsequently, we identified and mutated to alanine four proline-rich motifs in the PTH1R distal C terminus, which resulted in loss of both c-Src and arrestin co-precipitation and significantly decreased ERK1/2 activation. Proline 56-63 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 139-144 17038311-13 2006 These data delineate the multiple PTH1R structural determinants for ERK1/2 activation and newly identify a unique mechanism involving proline-rich motifs in the receptor C terminus for reciprocal scaffolding of c-Src and beta-arrestin2 with a class II G-protein-coupled receptor. Proline 134-141 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 211-216 17094785-4 2006 Mutating prolines 543-548 reduced Src binding to the Cbl 479-636 fragment significantly more than mutating the prolines in the PPVPPR(494-499) motif, which was previously reported to bind Src SH3. Proline 9-17 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 34-37 17094785-5 2006 Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src-induced phosphorylation of Cbl, and the inhibition of Src kinase activity by Cbl. Proline 13-21 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 64-67 17094785-5 2006 Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src-induced phosphorylation of Cbl, and the inhibition of Src kinase activity by Cbl. Proline 13-21 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 84-87 17094785-5 2006 Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src-induced phosphorylation of Cbl, and the inhibition of Src kinase activity by Cbl. Proline 13-21 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 84-87 17094785-2 2006 We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl. Proline 135-142 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 89-92 17094785-2 2006 We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl. Proline 135-142 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 89-92 14670955-2 2004 We have identified two proline-rich, SH3 binding sites (PXXP) in the carboxyl-terminal tail of the human P2Y(2) nucleotide receptor that directly associate with the tyrosine kinase Src in protein binding assays. Proline 23-30 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 181-184 15784259-3 2005 As a homolog of the corresponding Src docking domain, the CAS SH3 domain binds to proline-rich sequences (PxxP) of its interacting partners that can adopt a polyproline type II helix. Proline 82-89 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 34-37 15994299-2 2005 p22phox associates with gp91phox and, through its proline-rich C terminus, provides a binding site for the tandem Src homology 3 domains of the activating subunit p47phox. Proline 50-57 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 114-117 15872089-5 2005 The association of dynamin with Cbl in osteoclasts was decreased by Src tyrosine kinase activity and we found that destabilization of the dynamin-Cbl complex involves the recruitment of Src through the proline-rich domain of Cbl. Proline 202-209 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 186-189 15723349-6 2005 This is induced by the replacement of a conserved Asp, Asn, or Glu residue by a Pro at one side of the N-Src loop. Proline 80-83 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 105-108 15557335-4 2005 A proline-rich region in the C terminus of Alix bound the Src SH3 domain, but this interaction was dependent on the release of the Src SH2 domain from its Src internal ligand either by interaction with Alix Tyr319 or by mutation of Src Tyr527. Proline 2-9 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 58-61 15615649-2 2005 Mediated by the proline-rich region of tau and the SH3 domain of fyn or src, this interaction has the potential to confer novel cellular activities for tau in the growth cone and in the membrane. Proline 16-23 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 72-75 15217616-3 2004 Five of these contained proline-rich sequences in their FG loop that resembled class I (i.e., +xxPxxP) peptide ligands for the Src SH3 domain. Proline 24-31 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 127-130 15217616-4 2004 The sixth clone lacked the proline-rich sequence and showed particularly high binding specificity to the Src SH3 domain among various SH3 domains tested. Proline 27-34 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 105-108 12529254-5 2003 Other results suggest that rP2X(7)-R-mediated ERK1/2 phosphorylation was linked to the phosphorylation of the proline-rich/Ca(2+)-activated tyrosine kinase Pyk2, c-Src, phosphatidylinositol 3"-kinase, and protein kinase Cdelta activities and was dependent on the presence of extracellular Ca(2+). Proline 110-117 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 162-167 12473651-4 2003 In this study, we further showed that the proline-rich domain of DOC-2/DAB2 could also interact with proteins containing the Src homology 3 domain, such as Src and Fgr. Proline 42-49 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 125-128 12473651-4 2003 In this study, we further showed that the proline-rich domain of DOC-2/DAB2 could also interact with proteins containing the Src homology 3 domain, such as Src and Fgr. Proline 42-49 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 156-159 12612073-4 2003 ERID-I and ERID-II flank a proline cluster responsible for binding of PRB to c-Src. Proline 27-34 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 77-82 12163161-9 2002 These results suggest that the proline rich region within the Tec homology domain of ITK regulates its basal activity and its response to Src family kinase signals. Proline 31-38 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 138-141 12223544-7 2002 SH3-dependent binding of Src leads to the suppression of both Kv1.5 and Kv1.4 (modified to contain proline-rich SH3 domain binding sites) macroscopic currents even in the absence of Src-catalyzed tyrosine phosphorylation, whereas binding-independent tyrosine phosphorylation by Src leads to the suppression of Kv1.5 macroscopic currents and the modulation of Kv1.4 inactivation kinetics. Proline 99-106 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 25-28 11753652-5 2001 Abl was regulated efficiently when its SH3 domain was replaced with a heterologous SH3 from c-Src that binds a different spectrum of proline-rich ligands, but not by substitution of a modular WW domain with similar ligand-binding specificity. Proline 133-140 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 92-97 12023880-9 2002 In contrast, both the C-terminal proline-rich region and the tandem tyrosine residues present in the N-terminal region are required for the activation of Src family kinases. Proline 33-40 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 154-157 11943772-2 2002 Molecular cloning of GPVI has revealed the presence of a proline-rich domain in the sequence of GPVI cytoplasmic tail which has the consensus for interaction with the Src homology 3 (SH3) domains of Fyn and Lyn. Proline 57-64 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 167-170 11943772-3 2002 A series of in vitro experiments demonstrated the ability of the SH3 domains of both Src kinases to bind the proline-rich domain of GPVI. Proline 109-116 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 85-88 11964172-2 2002 In order to study the role of Grb2 in blood platelet responses, we used a peptide containing two proline-rich sequences derived from Sos (peptidimer), which binds to Grb2-Src homology 3 domain (SH3) with a high affinity, and hence inhibits Grb2-SH3-mediated protein interactions. Proline 97-104 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 171-174 11509578-5 2001 The new protein mainly binds to the proline-rich region of mDia through its Src homology 3 domain and also binds to Grb2 through its proline-rich domain. Proline 36-43 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 76-79 11518702-6 2001 The binding involves a proline-rich region in pORF3 and the src homology 3 (SH3) domains in the cellular proteins. Proline 23-30 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 60-63 11509578-5 2001 The new protein mainly binds to the proline-rich region of mDia through its Src homology 3 domain and also binds to Grb2 through its proline-rich domain. Proline 133-140 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 76-79 11032808-7 2000 Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. Proline 102-109 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 0-3 11545730-0 2001 Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Proline 33-40 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 107-112 11032808-7 2000 Src SH2 interacts with phosphotyrosine 537 of oestradiol receptor alpha and the Src SH3 domain with a proline-rich stretch of the androgen receptor. Proline 102-109 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 80-83 10830300-7 2000 The association between p85 and c-src is due in part to a direct interaction between the proline-rich sequences of p85 and the SH3 domain of c-src. Proline 89-96 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 32-37 10830300-7 2000 The association between p85 and c-src is due in part to a direct interaction between the proline-rich sequences of p85 and the SH3 domain of c-src. Proline 89-96 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 141-146 10601992-1 1999 The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells. Proline 4-11 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 288-291 10753943-5 2000 This recruitment of c-SRC to the receptor involves an interaction between the amino-terminal proline-rich region of beta-arrestin1 and the Src homology 3 (SH3) domain of c-SRC, but deletion of the proline-rich domain does not totally ablate the interaction. Proline 93-100 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 20-25 10753943-5 2000 This recruitment of c-SRC to the receptor involves an interaction between the amino-terminal proline-rich region of beta-arrestin1 and the Src homology 3 (SH3) domain of c-SRC, but deletion of the proline-rich domain does not totally ablate the interaction. Proline 197-204 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 20-25 9763511-5 1998 Here we report that a proline rich sequence in the amino terminus of tau interacts with the SH3 domains of fyn and src non-receptor tyrosine kinases. Proline 22-29 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 115-118 10430626-0 1999 Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation. Proline 0-7 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 33-36 10430626-3 1999 Recent crystal structures of Src kinases suggest that an important mechanism of kinase activation is via engagement of the Src homology (SH)3 domain by proline-containing sequences. Proline 152-159 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 29-32 10430626-3 1999 Recent crystal structures of Src kinases suggest that an important mechanism of kinase activation is via engagement of the Src homology (SH)3 domain by proline-containing sequences. Proline 152-159 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 123-126 9819391-9 1998 Both coimmunoprecipitation and tyrosine phosphorylation depend on the same proline-rich class II Src SH3 binding site required for in vitro association. Proline 75-82 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 97-100 9856337-5 1998 In addition, the proline-rich domain of Sos also bound to the SH3 domains of other src-type tyrosine kinases, src and fyn, but not to that of PLC-gamma. Proline 17-24 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 83-86 9856337-5 1998 In addition, the proline-rich domain of Sos also bound to the SH3 domains of other src-type tyrosine kinases, src and fyn, but not to that of PLC-gamma. Proline 17-24 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 110-113 8953041-1 1996 The human Kv1.5 potassium channel (hKv1.5) contains proline-rich sequences identical to those that bind to Src homology 3 (SH3) domains. Proline 52-59 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 107-110 9525481-1 1998 It is well known that v-Src phosphorylates various substrates on tyrosine residue and associates with tyrosine-phosphorylated proteins as well as proline-rich ligands through its SH2 and SH3 domains, respectively, thereby inducing oncogenic transformation. Proline 146-153 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 24-27 9235918-7 1997 We also observed that the calpain-mediated digestion in vitro is dependent on the presence of a sequence containing a proline-rich region and multiple tyrosine residues that are phosphorylated by pp60(c-)src. Proline 118-125 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 196-207 9199323-2 1997 It also contains a tyrosine residue and a proline-rich sequence near the C terminus, which are the binding sites for the SH2 and SH3 domains of Src kinase, respectively. Proline 42-49 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 144-147 8953041-3 1996 This interaction was mediated by the proline-rich motif of hKv1.5 and the SH3 domain of Src. Proline 37-44 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 88-91 7516469-7 1994 All of these proteins contain proline-rich peptide motifs that could serve as SH3 domain ligands, and the binding of these proteins to the Src SH3 domain was inhibited with a proline-rich Src SH3 peptide ligand. Proline 30-37 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 139-142 8766817-6 1996 A peptide derived from residues 32-44 of Sam68 which fits the class II SH3 domain binding consensus sequence inhibited binding of Sam68 to both p85alpha SH3 domain and c-src SH3 domain, but with differential potency, suggesting a differential affinity of these SH3 domains for this proline-rich motif. Proline 282-289 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 168-173 8618911-0 1995 Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proline 34-41 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 70-73 7589480-3 1995 Here, we report that the Src homology 3 (SH3) domain of Fyn binds to the proline-rich cytoplasmic region of FasL. Proline 73-80 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 25-28 7565714-2 1995 Structural analysis of the Src SH3 domain (Src SH3) complexed with proline-rich peptide ligands revealed three binding sites involved in this interaction: two hydrophobic interactions (between aliphatic proline dipeptides in the SH3 ligand and highly conserved aromatic residues on the surface of the SH3 domain), and one salt bridge (between Asp-99 of Src and an Arg three residues upstream of the conserved Pro-X-X-Pro motif in the ligand). Proline 67-74 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 27-30 7565714-2 1995 Structural analysis of the Src SH3 domain (Src SH3) complexed with proline-rich peptide ligands revealed three binding sites involved in this interaction: two hydrophobic interactions (between aliphatic proline dipeptides in the SH3 ligand and highly conserved aromatic residues on the surface of the SH3 domain), and one salt bridge (between Asp-99 of Src and an Arg three residues upstream of the conserved Pro-X-X-Pro motif in the ligand). Proline 67-74 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 43-46 7565714-2 1995 Structural analysis of the Src SH3 domain (Src SH3) complexed with proline-rich peptide ligands revealed three binding sites involved in this interaction: two hydrophobic interactions (between aliphatic proline dipeptides in the SH3 ligand and highly conserved aromatic residues on the surface of the SH3 domain), and one salt bridge (between Asp-99 of Src and an Arg three residues upstream of the conserved Pro-X-X-Pro motif in the ligand). Proline 67-74 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 43-46 7565714-2 1995 Structural analysis of the Src SH3 domain (Src SH3) complexed with proline-rich peptide ligands revealed three binding sites involved in this interaction: two hydrophobic interactions (between aliphatic proline dipeptides in the SH3 ligand and highly conserved aromatic residues on the surface of the SH3 domain), and one salt bridge (between Asp-99 of Src and an Arg three residues upstream of the conserved Pro-X-X-Pro motif in the ligand). Proline 203-210 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 27-30 7565714-2 1995 Structural analysis of the Src SH3 domain (Src SH3) complexed with proline-rich peptide ligands revealed three binding sites involved in this interaction: two hydrophobic interactions (between aliphatic proline dipeptides in the SH3 ligand and highly conserved aromatic residues on the surface of the SH3 domain), and one salt bridge (between Asp-99 of Src and an Arg three residues upstream of the conserved Pro-X-X-Pro motif in the ligand). Proline 203-210 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 43-46 7565714-2 1995 Structural analysis of the Src SH3 domain (Src SH3) complexed with proline-rich peptide ligands revealed three binding sites involved in this interaction: two hydrophobic interactions (between aliphatic proline dipeptides in the SH3 ligand and highly conserved aromatic residues on the surface of the SH3 domain), and one salt bridge (between Asp-99 of Src and an Arg three residues upstream of the conserved Pro-X-X-Pro motif in the ligand). Proline 203-210 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 43-46 7988556-9 1994 We find that although the phage-displayed Abl and Src SH3 ligands are proline rich, they are distinct. Proline 70-77 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 50-53 7516469-7 1994 All of these proteins contain proline-rich peptide motifs that could serve as SH3 domain ligands, and the binding of these proteins to the Src SH3 domain was inhibited with a proline-rich Src SH3 peptide ligand. Proline 30-37 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 188-191 7516469-7 1994 All of these proteins contain proline-rich peptide motifs that could serve as SH3 domain ligands, and the binding of these proteins to the Src SH3 domain was inhibited with a proline-rich Src SH3 peptide ligand. Proline 175-182 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 139-142 7516469-7 1994 All of these proteins contain proline-rich peptide motifs that could serve as SH3 domain ligands, and the binding of these proteins to the Src SH3 domain was inhibited with a proline-rich Src SH3 peptide ligand. Proline 175-182 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 188-191 34688656-3 2021 As evidenced by transmission electron microscopy and fluorescence and CD spectroscopy, the proline-rich domain (PRD) of ALIX, which encodes binding epitopes of multiple cellular partners, formed rope-like beta-sheet-rich reversible amyloid fibrils that dissolved upon Src-mediated phosphorylation and were restored on PTP1B-mediated dephosphorylation of its conserved tyrosine residues. Proline 91-98 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 268-271 7510218-1 1994 A common RXL motif was found in proline-rich ligands that were selected from a biased combinatorial peptide library on the basis of their ability to bind specifically to the SH3 domains from phosphatidylinositol 3-kinase (PI3K) or c-Src. Proline 32-39 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 231-236 34582006-8 2021 RESULTS: We found that the Src homology 3 (SH3) domain of betaPix interacts with the proline-rich domain of Dynamin 2 (Dyn2), a large GTPase. Proline 85-92 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 27-30 33837725-11 2021 Furthermore, we show that the C-terminal portion of the Serine-Threonine-Proline-rich (STP) region, adjacent to the GAIN domain, was required for Src-Fak activation. Proline 73-80 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 146-149 2463376-6 1989 Insertion of two extra cytosines 23 bp before and 19 bp after the c-src stop codon resulted in an extension of the coding portion up to 587 amino acids, divergence of sequences after Pro-525 and replacement of Tyr-527 by a valine residue. Proline 183-186 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 66-71 30824759-6 2019 We revealed that the interaction between the SH3 domain of c-Src and the proline-rich region of Alix activates ESCRT-mediated intra-luminal vesicle (ILV) formation, resulting in the upregulation of exosome secretion in c-Src-transformed cells. Proline 73-80 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 59-64 30824759-6 2019 We revealed that the interaction between the SH3 domain of c-Src and the proline-rich region of Alix activates ESCRT-mediated intra-luminal vesicle (ILV) formation, resulting in the upregulation of exosome secretion in c-Src-transformed cells. Proline 73-80 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 219-224 28049762-8 2017 However, Src did not directly bind to recombinant TBK1 in vitro but instead bound to the proline-X-X-proline motifs within key PRR adaptor proteins, such as TRIF, MAVS, and STING, which formed complexes with TBK1 after PRR engagement. Proline 89-96 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 9-12 29254203-3 2017 PROS exerted significant cytotoxicity, induced sub-G1 phase and S phase arrest, increased apoptotic bodies, and attenuated the expression of pro-PARP, Bcl-2, Cyclin E, Cyclin A, CDK2, E2F1, p-Src, p-STAT3, p-ERK, p-AKT, COX-2 and SOCS-1 in A549 and H460 cells along with disrupted binding of STAT3 with CDK2 or VEGF. Proline 0-4 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 192-195 29254203-4 2017 Notably, PROS inhibited VEGF induced proliferation, migration and tube formation in HUVECs and suppressed angiogenesis in chorioallantoic membrane (CAM) assay via reduced phosphorylation of VEGFR2, Src and STAT3. Proline 9-13 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 198-201 29928795-4 2018 Results of GST pull-down and fluorescence polarization assays show that both a proline-rich SH3 binding motif (PSRPLPDAP, residues 466-474) and an adjacent phosphotyrosine-containing SH2 binding motif (pYEEI, residues 508-511) in Tks4 are responsible for Src binding. Proline 79-86 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 255-258 27480221-4 2016 Our results demonstrate that imatinib binding to the kinase domain effects dynamics of proline-rich or phosphorylated peptide ligand binding sites in distal c-Src SH3 and SH2 domains. Proline 87-94 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 157-162 25031324-5 2014 PKA-dependent proline resonances were lost in the presence of the Src homology 3 domain of c-Src, consistent with formation of a complex. Proline 14-21 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 91-96 25490095-8 2014 Changes in this hydrogen-bond network lead to the displacement of the c-Src-SH3 distal loop, resulting also in conformational changes of Leu100 that might be related to the binding of proline rich motifs. Proline 184-191 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 70-75 27227417-0 2016 Correction to Multiple Src Homology 3 Binding to the Ubiquitin Ligase Itch Conserved Proline-Rich Region. Proline 85-92 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 23-26 26613292-0 2015 Multiple Src Homology 3 Binding to the Ubiquitin Ligase Itch Conserved Proline-Rich Region. Proline 71-78 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 9-12 26613292-2 2015 In addition to these common domains, Itch also contains a conserved proline-rich region (PRR) allowing its interaction with Src homology 3 (SH3) domain-containing proteins. Proline 68-75 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 124-127 24706440-4 2014 By structure-function analysis of ROR1 mutants, we show that ROR1 encompasses two major substrate regions: one is located in the proline-rich domain and is directly phosphorylated by MET; the other resides in the pseudokinase domain and is phosphorylated through intermediate activation of SRC. Proline 129-136 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 290-293 24556574-1 2014 In the Src Homology 3 domain (SH3) the RT and n-Src loops form a pocket that accounts for the specificity and affinity in binding of proline rich motifs (PRMs), while the distal and diverging turns play a key role in the folding of the protein. Proline 133-140 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 7-10 24556574-1 2014 In the Src Homology 3 domain (SH3) the RT and n-Src loops form a pocket that accounts for the specificity and affinity in binding of proline rich motifs (PRMs), while the distal and diverging turns play a key role in the folding of the protein. Proline 133-140 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 48-51 24582589-7 2014 Src-aPKC interaction was essential; substitution of the proline residues in aPKC that associate with the Src-SH3 binding domain rendered the mutant kinase unable to induce macropinocytosis in transfected cells. Proline 56-63 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 0-3 24582589-7 2014 Src-aPKC interaction was essential; substitution of the proline residues in aPKC that associate with the Src-SH3 binding domain rendered the mutant kinase unable to induce macropinocytosis in transfected cells. Proline 56-63 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 105-108