Search Results
Overview
| Uniprot ID | Q15019 |
|---|---|
| Protein Name | Septin-2 |
| Gene Name | SEPTIN2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 174 | FMKAIHNKVNIVPVI |
| 190 | KADTLTLKERERLKK |
| 3 | *****MSKQQPTQFI |
| 310 | RLKRGGRKVENEDMN |
Function
Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Cellular Component | GO:0005930 | axoneme |
| Cellular Component | GO:0032153 | cell division site |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0060170 | ciliary membrane |
| Cellular Component | GO:0005929 | cilium |
| Cellular Component | GO:0032154 | cleavage furrow |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0045171 | intercellular bridge |
| Cellular Component | GO:0000776 | kinetochore |
| Cellular Component | GO:0015630 | microtubule cytoskeleton |
| Cellular Component | GO:0030496 | midbody |
| Cellular Component | GO:0097730 | non-motile cilium |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032391 | photoreceptor connecting cilium |
| Cellular Component | GO:0031105 | septin complex |
| Cellular Component | GO:0005940 | septin ring |
| Cellular Component | GO:0097227 | sperm annulus |
| Cellular Component | GO:0005819 | spindle |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0030234 | enzyme regulator activity |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Biological Process | GO:0030154 | cell differentiation |
| Biological Process | GO:0060271 | cilium assembly |
| Biological Process | GO:0007010 | cytoskeleton organization |
| Biological Process | GO:0061640 | cytoskeleton-dependent cytokinesis |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:0007224 | smoothened signaling pathway |
| Biological Process | GO:0007283 | spermatogenesis |
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] 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.
[4] 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.
[5] 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.