Search Results
Overview
| Uniprot ID | O00429 |
|---|---|
| Protein Name | Dynamin-1-like protein |
| Gene Name | DNM1L |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 597 | RGMLKTSKAEELLAE |
Function
Functions in mitochondrial and peroxisomal division (PubMed:11514614, PubMed:12499366, PubMed:17301055, PubMed:17460227, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:19342591, PubMed:19411255, PubMed:19638400, PubMed:23283981, PubMed:23530241, PubMed:23921378, PubMed:26992161, PubMed:27145208, PubMed:27145933, PubMed:27301544, PubMed:27328748, PubMed:29478834, PubMed:32439975, PubMed:32484300, PubMed:9570752, PubMed:9786947). Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism (PubMed:23530241, PubMed:23584531, PubMed:33850055). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:23283981, PubMed:23921378, PubMed:29899447). While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (PubMed:29899447). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner (PubMed:32484300). Plays an important role in mitochondrial fission during mitosis (PubMed:19411255, PubMed:26992161, PubMed:27301544, PubMed:27328748). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (PubMed:17460227, PubMed:26992161, PubMed:27145208, PubMed:27301544, PubMed:27328748). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues (By similarity). Required for formation of endocytic vesicles (PubMed:20688057, PubMed:23792689, PubMed:9570752). Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles (PubMed:17015472, PubMed:23792689). Required for programmed necrosis execution (PubMed:22265414). Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production (PubMed:29478834)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005903 | brush border |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0030672 | synaptic vesicle membrane |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0030742 | GTP-dependent protein binding |
| Molecular Function | GO:0005096 | GTPase activator activity |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0008289 | lipid binding |
| Molecular Function | GO:0008017 | microtubule binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0031267 | small GTPase binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0006897 | endocytosis |
| Biological Process | GO:0060047 | heart contraction |
| Biological Process | GO:0048312 | intracellular distribution of mitochondria |
| Biological Process | GO:0000266 | mitochondrial fission |
| Biological Process | GO:0043653 | mitochondrial fragmentation involved in apoptotic process |
| Biological Process | GO:0090149 | mitochondrial membrane fission |
| Biological Process | GO:0007005 | mitochondrion organization |
| Biological Process | GO:0016559 | peroxisome fission |
| Biological Process | GO:0090141 | positive regulation of mitochondrial fission |
| Biological Process | GO:0090023 | positive regulation of neutrophil chemotaxis |
| Biological Process | GO:0050714 | positive regulation of protein secretion |
| Biological Process | GO:0051259 | protein complex oligomerization |
| Biological Process | GO:0070585 | protein localization to mitochondrion |
| Biological Process | GO:1903578 | regulation of ATP metabolic process |
| Biological Process | GO:1901524 | regulation of mitophagy |
| Biological Process | GO:1900063 | regulation of peroxisome organization |
| Biological Process | GO:0048511 | rhythmic process |
| Cellular Component | GO:0005905 | clathrin-coated pit |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0005741 | mitochondrial outer membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005777 | peroxisome |
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[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.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.