Search Results
Overview
| Uniprot ID | O95721 |
|---|---|
| Protein Name | Synaptosomal-associated protein 29 |
| Gene Name | SNAP29 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 154 | KEAISTSKEQEAKYQ |
| 169 | ASHPNLRKLDDTDPV |
| 191 | MSTDAYPKNPHLRAY |
| 201 | HLRAYHQKIDSNLDE |
Function
SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0031629 | synaptic vesicle fusion to presynaptic active zone membrane |
| Cellular Component | GO:0005776 | autophagosome |
| Cellular Component | GO:0000421 | autophagosome membrane |
| Cellular Component | GO:0035577 | azurophil granule membrane |
| Cellular Component | GO:0020018 | ciliary pocket membrane |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0000139 | Golgi membrane |
| Cellular Component | GO:0005765 | lysosomal membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0098793 | presynapse |
| Cellular Component | GO:0031201 | SNARE complex |
| Molecular Function | GO:0005484 | SNAP receptor activity |
| Molecular Function | GO:0019905 | syntaxin binding |
| Biological Process | GO:0097352 | autophagosome maturation |
| Biological Process | GO:0016240 | autophagosome membrane docking |
| Biological Process | GO:0009267 | cellular response to starvation |
| Biological Process | GO:0060271 | cilium assembly |
| Biological Process | GO:0006887 | exocytosis |
| Biological Process | GO:0016236 | macroautophagy |
| Biological Process | GO:0061025 | membrane fusion |
| Biological Process | GO:0015031 | protein transport |
| Biological Process | GO:0016082 | synaptic vesicle priming |
| Biological Process | GO:0006906 | vesicle fusion |
| Biological Process | GO:0006903 | vesicle targeting |
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] 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.