Search Results
Overview
| Uniprot ID | P60709 |
|---|---|
| Protein Name | Actin, cytoplasmic 1 |
| Gene Name | ACTB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 113 | TEAPLNPKANREKMT |
| 215 | IVRDIKEKLCYVALD |
| 291 | KCDVDIRKDLYANTV |
| 315 | GIADRMQKEITALAP |
| 326 | ALAPSTMKIKIIAPP |
| 328 | APSTMKIKIIAPPER |
| 50 | VMVGMGQKDSYVGDE |
| 61 | VGDEAQSKRGILTLK |
| 68 | KRGILTLKYPIEHGI |
Function
Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0030071 | regulation of mitotic metaphase/anaphase transition |
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Cellular Component | GO:0005884 | actin filament |
| Cellular Component | GO:0005912 | adherens junction |
| Cellular Component | GO:0043296 | apical junction complex |
| Cellular Component | GO:0030424 | axon |
| Cellular Component | GO:0072562 | blood microparticle |
| Cellular Component | GO:0005903 | brush border |
| Cellular Component | GO:0044305 | calyx of Held |
| Cellular Component | GO:0005911 | cell-cell junction |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0030863 | cortical cytoskeleton |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0036464 | cytoplasmic ribonucleoprotein granule |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0097433 | dense body |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0000776 | kinetochore |
| Cellular Component | GO:0030027 | lamellipodium |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0035267 | NuA4 histone acetyltransferase complex |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0098871 | postsynaptic actin cytoskeleton |
| Cellular Component | GO:0098793 | presynapse |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0098685 | Schaffer collateral - CA1 synapse |
| Cellular Component | GO:0045202 | synapse |
| Cellular Component | GO:0070160 | tight junction |
| Cellular Component | GO:0031982 | vesicle |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0019894 | kinesin binding |
| Molecular Function | GO:0050998 | nitric-oxide synthase binding |
| Molecular Function | GO:0030235 | nitric-oxide synthase regulator activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Molecular Function | GO:0098973 | structural constituent of postsynaptic actin cytoskeleton |
| Molecular Function | GO:0030957 | Tat protein binding |
| Molecular Function | GO:0048156 | tau protein binding |
| Molecular Function | GO:0141108 | transporter regulator activity |
| Biological Process | GO:0034333 | adherens junction assembly |
| Biological Process | GO:0045176 | apical protein localization |
| Biological Process | GO:0007409 | axonogenesis |
| Biological Process | GO:0048870 | cell motility |
| Biological Process | GO:0072749 | cellular response to cytochalasin B |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0007010 | cytoskeleton organization |
| Biological Process | GO:0007163 | establishment or maintenance of cell polarity |
| Biological Process | GO:0035633 | maintenance of blood-brain barrier |
| Biological Process | GO:0007020 | microtubule nucleation |
| Biological Process | GO:0001738 | morphogenesis of a polarized epithelium |
| Biological Process | GO:0045596 | negative regulation of cell differentiation |
| Biological Process | GO:0070527 | platelet aggregation |
| Biological Process | GO:0045597 | positive regulation of cell differentiation |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:2000781 | positive regulation of double-strand break repair |
| Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0045663 | positive regulation of myoblast differentiation |
| Biological Process | GO:0051623 | positive regulation of norepinephrine uptake |
| Biological Process | GO:1902459 | positive regulation of stem cell population maintenance |
| Biological Process | GO:0045582 | positive regulation of T cell differentiation |
| Biological Process | GO:0071896 | protein localization to adherens junction |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:2000779 | regulation of double-strand break repair |
| Biological Process | GO:0070316 | regulation of G0 to G1 transition |
| Biological Process | GO:2000045 | regulation of G1/S transition of mitotic cell cycle |
| Biological Process | GO:0051621 | regulation of norepinephrine uptake |
| Biological Process | GO:2000819 | regulation of nucleotide-excision repair |
| Biological Process | GO:1903076 | regulation of protein localization to plasma membrane |
| Biological Process | GO:1900242 | regulation of synaptic vesicle endocytosis |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0150111 | regulation of transepithelial transport |
| Biological Process | GO:0021762 | substantia nigra development |
Reference
[1] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[2] 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.
[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[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] 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.
[6] 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.