Related MeSH Hierarchy (8)
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Peptides » Intracellular Signaling Peptides and Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Carrier Proteins » Calmodulin-Binding Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Carrier Proteins » Poly-ADP-Ribose Binding Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Cytoskeletal Proteins » Microfilament Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Intracellular Signaling Peptides and Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Membrane Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Nuclear Proteins » Poly-ADP-Ribose Binding Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Chemicals and Drugs [D] » Macromolecular Substances [D05] » Polymers » Biopolymers » Microfilament Proteins » Myristoylated Alanine-Rich C Kinase Substrate
Description
A membrane and ACTIN CYTOSKELETON associated, N-terminal myristoylated protein that binds CALMODULIN and is a prominent substrate for PROTEIN KINASE C. Both phosphorylation and poly(ADP)-ribosylation inhibit its F-ACTIN crosslinking activity; phosphorylation also causes MARCKS to relocate from the membrane to cytoplasm. MeSH
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