Search Results
Overview
| Uniprot ID | P09493 |
|---|---|
| Protein Name | Tropomyosin alpha-1 chain |
| Gene Name | TPM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 112 | RLATALQKLEEAEKA |
| 118 | QKLEEAEKAADESER |
| 161 | IAEDADRKYEEVARK |
| 168 | KYEEVARKLVIIESD |
| 205 | KTVTNNLKSLEAQAE |
| 213 | SLEAQAEKYSQKEDR |
| 248 | FAERSVTKLEKSIDD |
| 264 | EDELYAQKLKYKAIS |
Function
Binds to actin filaments in muscle and non-muscle cells (PubMed:23170982). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:23170982). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005884 | actin filament |
| Cellular Component | GO:0032059 | bleb |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005862 | muscle thin filament tropomyosin |
| Cellular Component | GO:0032587 | ruffle membrane |
| Cellular Component | GO:0030017 | sarcomere |
| Cellular Component | GO:0001725 | stress fiber |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0008092 | cytoskeletal protein binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Molecular Function | GO:0008307 | structural constituent of muscle |
| Biological Process | GO:0007015 | actin filament organization |
| Biological Process | GO:0060048 | cardiac muscle contraction |
| Biological Process | GO:0034614 | cellular response to reactive oxygen species |
| Biological Process | GO:0007010 | cytoskeleton organization |
| Biological Process | GO:0030049 | muscle filament sliding |
| Biological Process | GO:0030336 | negative regulation of cell migration |
| Biological Process | GO:1904753 | negative regulation of vascular associated smooth muscle cell migration |
| Biological Process | GO:1904706 | negative regulation of vascular associated smooth muscle cell proliferation |
| Biological Process | GO:0045785 | positive regulation of cell adhesion |
| Biological Process | GO:0003065 | positive regulation of heart rate by epinephrine |
| Biological Process | GO:0051496 | positive regulation of stress fiber assembly |
| Biological Process | GO:0008360 | regulation of cell shape |
| Biological Process | GO:0008016 | regulation of heart contraction |
| Biological Process | GO:0006937 | regulation of muscle contraction |
| Biological Process | GO:0031529 | ruffle organization |
| Biological Process | GO:0045214 | sarcomere organization |
| Biological Process | GO:0055010 | ventricular cardiac muscle tissue morphogenesis |
| Biological Process | GO:0042060 | wound healing |
Reference
[1] 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.
[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.