PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22013076-5 2011 We find that MARCKS-ED dissociation is prevented by mutation of four serine residues that are potential sites of phosphorylation by PKC. Serine 69-75 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 21762971-9 2011 Four serine residues in the myristoylated alanine-rich C kinase substrate (MARCKS)-phosphorylation site domain were mutated to identify the function of MARCKS in TRPM8-mediated airway mucus hypersecretion. Serine 5-11 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-73 21762971-9 2011 Four serine residues in the myristoylated alanine-rich C kinase substrate (MARCKS)-phosphorylation site domain were mutated to identify the function of MARCKS in TRPM8-mediated airway mucus hypersecretion. Serine 5-11 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-81 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Serine 208-211 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 15703821-9 2005 Furthermore, MARCKS was serine-phosphorylated in liver cirrhosis and HCC, and phosphorylated MARCKS was detected in a cytosolic fraction of these tissues. Serine 24-30 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 15052337-2 2004 The most prominent structural feature of MARCKS and MRP is a central basic effector domain (ED) that binds F-actin, Ca2+-calmodulin, and acidic phospholipids; phosphorylation of key serine residues within the ED by protein kinase C (PKC) prevents the above interactions. Serine 182-188 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-47 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Serine 105-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Serine 208-211 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 10736562-3 2000 MARCKS (and MRP) interact inter alia with lipid bilayer membranes (via the myristoyl group and the ED), with protein kinases (which phosphorylate the serines in the ED), and with calmodulin (via the ED); synergies between these diverse interactions present an unusually rich array of possibilities for a variety of regulatory roles. Serine 150-157 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Serine 220-227 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Serine 220-227 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 9112755-4 1997 The wild-type MARCKS and MRP peptides induced significant increases in the Ca2+ affinity of CaM (pCa 6.1 and 5.8, respectively, compared to 5.2, for CaM in the absence of bound peptides), whereas a modified MARCKS peptide, in which the four serine residues susceptible to phosphorylation in the wild-type sequence have been replaced with aspartate residues to mimic phosphorylation, had smaller effect (pCa 5.6). Serine 241-247 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 9808756-3 1998 To detect the activation of protein kinase C in vivo, we produced a specific antibody against MARCKS phosphorylated at serines 152 and 156. Serine 119-126 myristoylated alanine rich protein kinase C substrate Homo sapiens 94-100 9679146-5 1998 A polyclonal antibody specific to the phosphorylated state of the RTPS-serine, which is the major PKC phosphorylation site in the MARCKS-related domain, was used to evaluate phosphorylation of adducin in cells. Serine 71-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 8557118-0 1996 PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Serine 57-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 8601451-6 1996 However, in contrast to other PKCs, a peptide derived from the MARCKS phosphorylation domain is phosphorylated only at serine 156, and not at serines 152 and 163, implicating a differential regulation by PKC mu. Serine 119-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 63-69 8557118-0 1996 PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Serine 45-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 7720702-6 1995 MARCKS phosphorylation is required for its translocation to lysosomes since mutating either the serine residues phosphorylated by PKC (phos-) or the PKC inhibitor staurosporine, prevented MARCKS phosphorylation, its release from the plasma membrane, and its subsequent association with lysosomes. Serine 96-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8557118-0 1996 PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Serine 57-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 7667880-3 1995 For MARCKS, and perhaps other proteins, phosphorylation of serines within its basic cluster reduces the electrostatic attraction, producing translocation of the protein from the membrane to the cytosol by a simple "electrostatic switch" mechanism. Serine 59-66 myristoylated alanine rich protein kinase C substrate Homo sapiens 4-10 7720702-6 1995 MARCKS phosphorylation is required for its translocation to lysosomes since mutating either the serine residues phosphorylated by PKC (phos-) or the PKC inhibitor staurosporine, prevented MARCKS phosphorylation, its release from the plasma membrane, and its subsequent association with lysosomes. Serine 96-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-194 1650359-1 1991 The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain. Serine 113-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 33-78 1650359-1 1991 The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain. Serine 113-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 1650359-10 1991 Thus, the phosphorylation site domain peptide of the MARCKS protein is a high affinity substrate for protein kinase C in vitro; the cognate peptide containing no serines is a potent but not completely specific inhibitor of both protein kinase C and its catalytic fragment. Serine 162-169 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59