PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Lysine 220-223 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. Lysine 109-112 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. Lysine 220-223 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. Lysine 220-223 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 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. Lysine 211-218 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 11018286-3 2000 In this report we show that macrophage extracts contain a protease which specifically cleaves human MARCKS, expressed in a cell-free system or in E. coli, between Lys-6 and Thr-7. Lysine 163-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 100-106 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. Lysine 211-218 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 30655546-3 2019 Here, we show that high maternal glucose induced MARCKS acetylation at lysine 165 by the acetyltransferase Tip60, which is a prerequisite for its phosphorylation, whereas Sirtuin 2 (SIRT2) deacetylated MARCKS. Lysine 71-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 27166806-4 2016 Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. Lysine 56-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-22 27166806-4 2016 Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. Lysine 56-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-113