Search Results
Overview
| Uniprot ID | P68363 |
|---|---|
| Protein Name | Tubulin alpha-1B chain |
| Gene Name | TUBA1B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 112 | RGHYTIGKEIIDLVL |
| 163 | RLSVDYGKKSKLEFS |
| 280 | APVISAEKAYHEQLS |
| 304 | EPANQMVKCDPRHGK |
| 311 | KCDPRHGKYMACCLL |
| 326 | YRGDVVPKDVNAAIA |
| 336 | NAAIATIKTKRSIQF |
| 338 | AIATIKTKRSIQFVD |
| 370 | VPGGDLAKVQRAVCM |
| 394 | AWARLDHKFDLMYAK |
| 401 | KFDLMYAKRAFVHWY |
| 60 | FSETGAGKHVPRAVF |
| 96 | PEQLITGKEDAANNY |
Function
Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:38305685, PubMed:34996871, PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005929 | cilium |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005881 | cytoplasmic microtubule |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0015630 | microtubule cytoskeleton |
| Molecular Function | GO:0003725 | double-stranded RNA binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Molecular Function | GO:0005198 | structural molecule activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0030705 | cytoskeleton-dependent intracellular transport |
| Biological Process | GO:0000226 | microtubule cytoskeleton organization |
| Biological Process | GO:0007017 | microtubule-based process |
| Biological Process | GO:0000278 | mitotic cell cycle |
| Biological Process | GO:0030182 | neuron differentiation |
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] 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.
[3] 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.
[4] 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.
[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.