Search Results
Overview
| Uniprot ID | Q01082 |
|---|---|
| Protein Name | Spectrin beta chain, non-erythrocytic 1 |
| Gene Name | SPTBN1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1021 | DLQKEAEKLESEHPD |
| 1120 | NYEEDYQKMRDMGEM |
| 1210 | GAEAAIKKQEDFMTT |
| 124 | DKALQFLKEQRVHLE |
| 1249 | NSDRIQEKVDSIDDR |
| 1354 | TEAVVKEKLTGLHKM |
| 1360 | EKLTGLHKMWEVLES |
| 1420 | TSVNILLKKQQMLEN |
| 1421 | SVNILLKKQQMLENQ |
| 1451 | QALSQEGKSTDEVDS |
| 1478 | LEPLNERKHNLLASK |
| 1526 | TVQLLIKKNQTLQKE |
| 1622 | MMSEEKAKDEQSAVS |
| 1632 | QSAVSMLKKHQILEQ |
| 1633 | SAVSMLKKHQILEQA |
| 1653 | ETVHQLSKTSRALVA |
| 1678 | MRQSKVDKLYAGLKD |
| 1684 | DKLYAGLKDLAEERR |
| 173 | TEDNKEKKSAKDALL |
| 1809 | AASYELHKFYHDAKE |
| 1815 | HKFYHDAKEIFGRIQ |
| 1827 | RIQDKHKKLPEELGR |
| 1878 | QAAYAGDKADDIQKR |
| 1913 | RLVDTGDKFRFFSMV |
| 1981 | GKSLLARKHYASEEI |
| 1991 | ASEEIKEKLLQLTEK |
| 1998 | KLLQLTEKRKEMIDK |
| 2064 | KRHEAFEKSAATWDE |
| 2177 | PTSDRKAKTALPAQS |
| 2238 | NQEMGFYKDAKTAAS |
| 224 | PDLIDFDKLKKSNAH |
| 2241 | MGFYKDAKTAASGIP |
| 2269 | CEVALDYKKKKHVFK |
| 227 | IDFDKLKKSNAHYNL |
| 2270 | EVALDYKKKKHVFKL |
| 2344 | TSESSPGKREKDKEK |
| 2362 | KRFSLFGKKK***** |
| 2363 | RFSLFGKKK****** |
| 288 | KALAVEGKRIGKVLD |
| 292 | VEGKRIGKVLDNAIE |
| 379 | KMRANNQKVYMPREG |
| 419 | NELIRQEKLEQLARR |
| 463 | AVEAATKKHEAIETD |
| 497 | AENYHDIKRITARKD |
| 62 | VQKKTFTKWVNSHLA |
| 659 | GWIREKEKILSSDDY |
| 668 | LSSDDYGKDLTSVMR |
| 784 | YSTQSLVKKHKDVAE |
| 842 | AELTRLRKQALQDTL |
| 976 | SWIREKTKVIESTQD |
| 997 | GVMALQRKLTGMERD |
Function
Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030673 | axolemma |
| Cellular Component | GO:0030054 | cell junction |
| Cellular Component | GO:0042995 | cell projection |
| Cellular Component | GO:0030864 | cortical actin cytoskeleton |
| Cellular Component | GO:0032437 | cuticular plate |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0031430 | M band |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0014069 | postsynaptic density |
| Cellular Component | GO:0008091 | spectrin |
| Cellular Component | GO:0014731 | spectrin-associated cytoskeleton |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0030506 | ankyrin binding |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0051020 | GTPase binding |
| Molecular Function | GO:0005543 | phospholipid binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Biological Process | GO:0030036 | actin cytoskeleton organization |
| Biological Process | GO:0051693 | actin filament capping |
| Biological Process | GO:0007417 | central nervous system development |
| Biological Process | GO:0021556 | central nervous system formation |
| Biological Process | GO:0043001 | Golgi to plasma membrane protein transport |
| Biological Process | GO:0071709 | membrane assembly |
| Biological Process | GO:0000281 | mitotic cytokinesis |
| Biological Process | GO:0007009 | plasma membrane organization |
| Biological Process | GO:0032743 | positive regulation of interleukin-2 production |
| Biological Process | GO:1903078 | positive regulation of protein localization to plasma membrane |
| Biological Process | GO:0072659 | protein localization to plasma membrane |
| Biological Process | GO:1903076 | regulation of protein localization to plasma membrane |
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] 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.
[3] 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.
[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] 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.
[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.