PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21576243-7 2011 The most crucial residue within the beta1-beta2 linker (Asp(110)), when mutated from aspartate to cysteine, can be altered by cysteine-modifying reagents much more readily when channels are closed than when they are desensitized. Aspartic Acid 56-59 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 36-41 24581800-7 2014 Based on these analyses, the residues His122 and Lys140 of beta1 and Glu 66, Asn 131, Asp 118, Glu 120, Glu133, Asn135, Ser 137 of beta3 were predicted to play a functional role. Aspartic Acid 86-89 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 59-75 2527855-8 1989 Laminin-binding by the alpha beta 1 complex was independent of Arg-Gly-Asp or Tyr-Ile-Gly-Ser-Arg-like sequences, but required the presence of divalent cations. Aspartic Acid 71-74 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 29-35 26020686-8 2015 (4) Yeast beta1 and human beta1c subunits preferentially bind Asp and Leu in their S1 pockets, while Glu and large hydrophobic residues are not accepted. Aspartic Acid 62-65 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 10-15 21576243-7 2011 The most crucial residue within the beta1-beta2 linker (Asp(110)), when mutated from aspartate to cysteine, can be altered by cysteine-modifying reagents much more readily when channels are closed than when they are desensitized. Aspartic Acid 85-94 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 36-41 18650446-5 2008 Mode 1 expression results from a single amino acid change at residue hbeta1 Asp-37. Aspartic Acid 76-79 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 69-75 9585419-1 1998 The amyloid-beta peptide (Abeta) can mediate cell attachment by binding to beta1 integrins through an arg-his-asp sequence. Aspartic Acid 110-113 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 75-80