Search Results
Overview
| Uniprot ID | P29966 |
|---|---|
| Protein Name | Myristoylated alanine-rich C-kinase substrate |
| Gene Name | MARCKS |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 11 | QFSKTAAKGEAAAER |
| 165 | FSFKKSFKLSGFSFK |
| 173 | LSGFSFKKNKKEAGE |
| 176 | FSFKKNKKEAGEGGE |
Function
Membrane-associated protein that plays a role in the structural modulation of the actin cytoskeleton, chemotaxis, motility, cell adhesion, phagocytosis, and exocytosis through lipid sequestering and/or protein docking to membranes (PubMed:23704996, PubMed:36009319). Thus, exerts an influence on a plethora of physiological processes, such as embryonic development, tissue regeneration, neuronal plasticity, and inflammation. Sequesters phosphatidylinositol 4,5-bisphosphate (PIP2) at lipid rafts in the plasma membrane of quiescent cells, an action reversed by protein kinase C, ultimately inhibiting exocytosis (PubMed:23704996). During inflammation, promotes the migration and adhesion of inflammatory cells and the secretion of cytokines such as tumor necrosis factor (TNF), particularly in macrophages (PubMed:37949888). Plays an essential role in bacteria-induced intracellular reactive oxygen species (ROS) formation in the monocytic cell type. Participates in the regulation of neurite initiation and outgrowth by interacting with components of cellular machinery including CDC42 that regulates cell shape and process extension through modulation of the cytoskeleton (By similarity). Plays also a role in axon development by mediating docking and fusion of RAB10-positive vesicles with the plasma membrane (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Biological Process | GO:0007015 | actin filament organization |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0007417 | central nervous system development |
| Biological Process | GO:0007005 | mitochondrion organization |
| Biological Process | GO:0021915 | neural tube development |
| Biological Process | GO:0022008 | neurogenesis |
| Biological Process | GO:0034976 | response to endoplasmic reticulum stress |
| Cellular Component | GO:0032432 | actin filament bundle |
| Cellular Component | GO:0005938 | cell cortex |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0042585 | germinal vesicle |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0005080 | protein kinase C binding |
| Biological Process | GO:0051764 | actin crosslink formation |
| Biological Process | GO:0051017 | actin filament bundle assembly |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.