Search Results
Overview
| Uniprot ID | P53618 |
|---|---|
| Protein Name | Coatomer subunit beta |
| Gene Name | COPB1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 309 | LDRLIELKEHPAHER |
| 535 | SSSRPTKKEEDRPPL |
| 575 | YVALVQEKKKQNSFV |
| 576 | VALVQEKKKQNSFVA |
| 703 | AMGNTQRKEAADPLA |
| 712 | AADPLASKLNKVTQL |
Function
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030126 | COPI vesicle coat |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0005793 | endoplasmic reticulum-Golgi intermediate compartment |
| Cellular Component | GO:0101003 | ficolin-1-rich granule membrane |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0000139 | Golgi membrane |
| Cellular Component | GO:0005798 | Golgi-associated vesicle |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0030667 | secretory granule membrane |
| Cellular Component | GO:0070821 | tertiary granule membrane |
| Cellular Component | GO:0030133 | transport vesicle |
| Molecular Function | GO:0005198 | structural molecule activity |
| Biological Process | GO:0006888 | endoplasmic reticulum to Golgi vesicle-mediated transport |
| Biological Process | GO:0006891 | intra-Golgi vesicle-mediated transport |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:0006890 | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
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] 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] 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.