PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15094065-1 2004 The three genes hTAF(II)68, EWS, and TLS (called the TET family) encode related RNA binding proteins containing an RNA recognition motif and three glycine-, arginine-, and proline-rich regions in the C-terminus and a degenerated repeat containing the consensus sequence Ser-Tyr-Gly-Gln-Ser in the N-terminus. Glycine 147-154 FUS RNA binding protein Homo sapiens 37-40 15094065-1 2004 The three genes hTAF(II)68, EWS, and TLS (called the TET family) encode related RNA binding proteins containing an RNA recognition motif and three glycine-, arginine-, and proline-rich regions in the C-terminus and a degenerated repeat containing the consensus sequence Ser-Tyr-Gly-Gln-Ser in the N-terminus. Glycine 278-281 FUS RNA binding protein Homo sapiens 37-40 34537246-6 2021 LARKS have high glycine content, which enables kinks to form as exemplified by the known LARKS-rich amyloidogenic structures of TDP43, FUS, and hnRNPA2, three proteins that are known to participate in MLOs. Glycine 16-23 FUS RNA binding protein Homo sapiens 135-138 9795213-6 1998 The RBP56/hTAFII68, FUS/TLS and EWS proteins comprise a sub-family of RNA binding proteins, which consist of an N-terminal Ser, Gly, Gln and Tyr-rich region, an RNA binding domain, a Cys2/Cys2 zinc finger motif and a C-terminal RGG-containing region. Glycine 128-131 FUS RNA binding protein Homo sapiens 20-27 7987849-9 1994 As a consequence the normally nontranslated exon 2 is translated and in both types there is in the junction between FUS and CHOP a shift from a FUS glycine codon to a valine codon in the chimeric mRNA. Glycine 148-155 FUS RNA binding protein Homo sapiens 116-119 7987849-9 1994 As a consequence the normally nontranslated exon 2 is translated and in both types there is in the junction between FUS and CHOP a shift from a FUS glycine codon to a valine codon in the chimeric mRNA. Glycine 148-155 FUS RNA binding protein Homo sapiens 144-147 33580145-8 2021 FUS(R495X) uses its C-terminal tandem arginine-glycine-glycine regions, RGG2 and RGG3, to bind the PY-NLS binding site of Kapbeta2 for nuclear localization in cells when arginine methylation is inhibited. Glycine 47-54 FUS RNA binding protein Homo sapiens 0-3 33411976-0 2021 Cytoplasmic granule formation by FUS-R495X is attributable to arginine methylation in all Gly-rich, RGG1 and RGG2 domains. Glycine 90-93 FUS RNA binding protein Homo sapiens 33-36 33580145-8 2021 FUS(R495X) uses its C-terminal tandem arginine-glycine-glycine regions, RGG2 and RGG3, to bind the PY-NLS binding site of Kapbeta2 for nuclear localization in cells when arginine methylation is inhibited. Glycine 55-62 FUS RNA binding protein Homo sapiens 0-3 33338404-0 2020 ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS. Glycine 33-40 FUS RNA binding protein Homo sapiens 29-32 33338404-0 2020 ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS. Glycine 33-40 FUS RNA binding protein Homo sapiens 117-120 29784880-6 2018 We also report that an arginine residue within the Arg-Gly-Gly domain of TLS, Arg-476, serves as the major determinant for binding to pncRNA. Glycine 55-58 FUS RNA binding protein Homo sapiens 73-76 33110735-6 2020 The N-terminal LC sequence of FUS is made up of Ser, Tyr, Gly, and Gln, which form a labile cross-beta polymer core while the C-terminal Arg-Gly-Gly repeats accelerate LLPS. Glycine 58-61 FUS RNA binding protein Homo sapiens 30-33 33159856-0 2020 ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS. Glycine 33-40 FUS RNA binding protein Homo sapiens 29-32 33159856-0 2020 ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS. Glycine 33-40 FUS RNA binding protein Homo sapiens 117-120 32915994-6 2020 RNA-seq analysis using the Gly-rich domain-deleted mutant coupled with snRNP70 knockdown revealed that FUS has a potential to regulate gene expression in both snRNP70-dependent and -independent manners through the Gly-rich domain. Glycine 27-30 FUS RNA binding protein Homo sapiens 103-106 29800261-3 2018 TLS/FUS binding to G-quadruplex telomere DNA and telomeric repeat-containing RNA depends especially on RGG3, comprising Arg-Gly-Gly repeats with proline- and arginine-rich regions. Glycine 124-127 FUS RNA binding protein Homo sapiens 0-3 29800261-3 2018 TLS/FUS binding to G-quadruplex telomere DNA and telomeric repeat-containing RNA depends especially on RGG3, comprising Arg-Gly-Gly repeats with proline- and arginine-rich regions. Glycine 124-127 FUS RNA binding protein Homo sapiens 4-7 29800261-3 2018 TLS/FUS binding to G-quadruplex telomere DNA and telomeric repeat-containing RNA depends especially on RGG3, comprising Arg-Gly-Gly repeats with proline- and arginine-rich regions. Glycine 128-131 FUS RNA binding protein Homo sapiens 0-3 29800261-3 2018 TLS/FUS binding to G-quadruplex telomere DNA and telomeric repeat-containing RNA depends especially on RGG3, comprising Arg-Gly-Gly repeats with proline- and arginine-rich regions. Glycine 128-131 FUS RNA binding protein Homo sapiens 4-7 29784880-6 2018 We also report that an arginine residue within the Arg-Gly-Gly domain of TLS, Arg-476, serves as the major determinant for binding to pncRNA. Glycine 59-62 FUS RNA binding protein Homo sapiens 73-76 25447237-3 2015 It has been shown in cell culture that the nuclear import of FUS is mediated by transportin, which binds the PY-NLS and the last arginine/glycine/glycine-rich (RGG) domain of FUS. Glycine 138-145 FUS RNA binding protein Homo sapiens 61-64 25447237-3 2015 It has been shown in cell culture that the nuclear import of FUS is mediated by transportin, which binds the PY-NLS and the last arginine/glycine/glycine-rich (RGG) domain of FUS. Glycine 138-145 FUS RNA binding protein Homo sapiens 175-178 25447237-3 2015 It has been shown in cell culture that the nuclear import of FUS is mediated by transportin, which binds the PY-NLS and the last arginine/glycine/glycine-rich (RGG) domain of FUS. Glycine 146-153 FUS RNA binding protein Homo sapiens 61-64 25447237-3 2015 It has been shown in cell culture that the nuclear import of FUS is mediated by transportin, which binds the PY-NLS and the last arginine/glycine/glycine-rich (RGG) domain of FUS. Glycine 146-153 FUS RNA binding protein Homo sapiens 175-178 23635657-2 2013 FUS contains a methylated arginine-glycine-glycine domain that is required for transport into the nucleus. Glycine 35-42 FUS RNA binding protein Homo sapiens 0-3 24268778-3 2013 Both the low-complexity domain and the arginine-glycine rich domain of FUS contribute to assembly. Glycine 48-55 FUS RNA binding protein Homo sapiens 71-74 25453086-8 2014 The N-terminal QGSY (glutamine-glycine-serine-tyrosine)-rich region (amino acids 1-164) mediates FUS self-assembly in the nucleus of mammalian cells and the self-assembly is essential for its chromatin binding and transcription activation. Glycine 31-38 FUS RNA binding protein Homo sapiens 97-100 23635657-2 2013 FUS contains a methylated arginine-glycine-glycine domain that is required for transport into the nucleus. Glycine 43-50 FUS RNA binding protein Homo sapiens 0-3 23833192-4 2013 FUS recruitment is mediated by the arginine/glycine-rich domains, which interact directly with PAR. Glycine 44-51 FUS RNA binding protein Homo sapiens 0-3 20541619-2 2010 FUS/TLS belongs to a sub-family of RNA binding proteins, encoding an N-terminal serine-tyrosine-glycine-glutamine (SYGQ) region, an RNA recognition motif (RRM) flanked by glycine rich (G-rich) regions, a cysteine(2)/cysteine(2) zinc finger motif and multiple RGG repeats. Glycine 96-103 FUS RNA binding protein Homo sapiens 0-7 23521792-3 2013 Here, we show that the Arg-Gly-Gly domain in the C-terminal region of TLS forms a ternary complex with human telomere G-quadruplex DNA and TERRA in vitro. Glycine 27-30 FUS RNA binding protein Homo sapiens 70-73 23521792-3 2013 Here, we show that the Arg-Gly-Gly domain in the C-terminal region of TLS forms a ternary complex with human telomere G-quadruplex DNA and TERRA in vitro. Glycine 31-34 FUS RNA binding protein Homo sapiens 70-73 22563080-5 2012 For FUS, the arginine-glycine-glycine zinc finger domain, which is the protein"s main RNA binding domain, is most important for SG recruitment, whereas the glycine-rich domain and RNA recognition motif (RRM) domain have a minor contribution and the glutamine-rich domain is dispensable. Glycine 22-29 FUS RNA binding protein Homo sapiens 4-7 22563080-5 2012 For FUS, the arginine-glycine-glycine zinc finger domain, which is the protein"s main RNA binding domain, is most important for SG recruitment, whereas the glycine-rich domain and RNA recognition motif (RRM) domain have a minor contribution and the glutamine-rich domain is dispensable. Glycine 30-37 FUS RNA binding protein Homo sapiens 4-7 20541619-2 2010 FUS/TLS belongs to a sub-family of RNA binding proteins, encoding an N-terminal serine-tyrosine-glycine-glutamine (SYGQ) region, an RNA recognition motif (RRM) flanked by glycine rich (G-rich) regions, a cysteine(2)/cysteine(2) zinc finger motif and multiple RGG repeats. Glycine 171-178 FUS RNA binding protein Homo sapiens 0-7 20124201-10 2010 While insertions/deletions of 2 glycines (G) were suggested to be pathogenic in the initial FUS reports, we observed an identical GG-deletion in 2 healthy individuals and similar G-insertions/deletions in 4 other control individuals, suggesting that G-insertions/deletions within this G-rich region may be tolerated. Glycine 32-40 FUS RNA binding protein Homo sapiens 92-95