Search Results
Overview
| Uniprot ID | Q9BR76 |
|---|---|
| Protein Name | Coronin-1B |
| Gene Name | CORO1B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 339 | CEIARFYKLHERKCE |
| 355 | IVMTVPRKSDLFQDD |
| 400 | REAYVPSKQRDLKIS |
| 468 | RALRALVKEQGDRIC |
Function
Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0042802 | identical protein binding |
| Biological Process | GO:0030036 | actin cytoskeleton organization |
| Biological Process | GO:0090135 | actin filament branching |
| Biological Process | GO:0051017 | actin filament bundle assembly |
| Cellular Component | GO:0005884 | actin filament |
| Cellular Component | GO:0031252 | cell leading edge |
| Cellular Component | GO:0071944 | cell periphery |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0030027 | lamellipodium |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0001725 | stress fiber |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0071933 | Arp2/3 complex binding |
| Molecular Function | GO:0045296 | cadherin binding |
| Biological Process | GO:0007015 | actin filament organization |
| Biological Process | GO:0016477 | cell migration |
| Biological Process | GO:0036120 | cellular response to platelet-derived growth factor stimulus |
| Biological Process | GO:0035767 | endothelial cell chemotaxis |
| Biological Process | GO:0034316 | negative regulation of Arp2/3 complex-mediated actin nucleation |
| Biological Process | GO:0071672 | negative regulation of smooth muscle cell chemotaxis |
| Biological Process | GO:2000394 | positive regulation of lamellipodium morphogenesis |
| Biological Process | GO:1902463 | protein localization to cell leading edge |
| Biological Process | GO:0034315 | regulation of Arp2/3 complex-mediated actin nucleation |
| Biological Process | GO:0031529 | ruffle organization |
| Biological Process | GO:0042060 | wound healing |
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] 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.
[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] 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.