Search Results
Overview
| Uniprot ID | Q9UHD8 |
|---|---|
| Protein Name | Septin-9 |
| Gene Name | SEPTIN9 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 141 | RAEVLGHKTPEPAPR |
| 156 | RTEITIVKPQESAHR |
| 186 | PATDAAPKRVEIQMP |
| 262 | TPRDAGLKQAPASRN |
| 28 | DSSGPALKRSFEVEE |
| 3 | *****MKKSYSGGTR |
| 326 | FKSKISRKSVQPTSE |
| 343 | IPKTIEIKSITHDIE |
| 352 | ITHDIEEKGVRMKLT |
| 62 | TVASSTQKFQDLGVK |
| 69 | KFQDLGVKNSEPSAR |
| 99 | RVELSGPKAAEPVSR |
Function
Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). 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:0005929 | cilium |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0045171 | intercellular bridge |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0015630 | microtubule cytoskeleton |
| Cellular Component | GO:0097730 | non-motile cilium |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0031105 | septin complex |
| Cellular Component | GO:0005940 | septin ring |
| Cellular Component | GO:0001725 | stress fiber |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Biological Process | GO:0007010 | cytoskeleton organization |
| Biological Process | GO:0061640 | cytoskeleton-dependent cytokinesis |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:1902857 | positive regulation of non-motile cilium assembly |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[5] 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.
[6] 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.
[7] 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.
[8] 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.