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Overview

Uniprot IDP53618
Protein NameCoatomer subunit beta
Gene NameCOPB1
OrganismHomo 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

10 MTAAENVCYT 20 LINVPMDSEP 30 PSEISLKNDL 40 EKGDVKSKTE 50 ALKKVIIMIL 60 NGEKLPGLLM 70 TIIRFVLPLQ 80 DHTIKKLLLV 90 FWEIVPKTTP 100 DGRLLHEMIL 110 VCDAYRKDLQ 120 HPNEFIRGST 130 LRFLCKLKEA 140 ELLEPLMPAI 150 RACLEHRHSY 160 VRRNAVLAIY 170 TIYRNFEHLI 180 PDAPELIHDF 190 LVNEKDASCK 200 RNAFMMLIHA 210 DQDRALDYLS 220 TCIDQVQTFG 230 DILQLVIVEL 240 IYKVCHANPS 250 ERARFIRCIY 260 NLLQSSSPAV 270 KYEAAGTLVT 280 LSSAPTAIKA 290 AAQCYIDLII 300 KESDNNVKLI 310 VLDRLIELKE 320 HPAHERVLQD 330 LVMDILRVLS 340 TPDLEVRKKT 350 LQLALDLVSS 360 RNVEELVIVL 370 KKEVIKTNNV 380 SEHEDTDKYR 390 QLLVRTLHSC 400 SVRFPDMAAN 410 VIPVLMEFLS 420 DNNEAAAADV 430 LEFVREAIQR 440 FDNLRMLIVE 450 KMLEVFHAIK 460 SVKIYRGALW 470 ILGEYCSTKE 480 DIQSVMTEIR 490 RSLGEIPIVE 500 SEIKKEAGEL 510 KPEEEITVGP 520 VQKLVTEMGT 530 YATQSALSSS 540 RPTKKEEDRP 550 PLRGFLLDGD 560 FFVAASLATT 570 LTKIALRYVA 580 LVQEKKKQNS 590 FVAEAMLLMA 600 TILHLGKSSL 610 PKKPITDDDV 620 DRISLCLKVL 630 SECSPLMNDI 640 FNKECRQSLS 650 HMLSAKLEEE 660 KLSQKKESEK 670 RNVTVQPDDP 680 ISFMQLTAKN 690 EMNCKEDQFQ 700 LSLLAAMGNT 710 QRKEAADPLA 720 SKLNKVTQLT 730 GFSDPVYAEA 740 YVHVNQYDIV 750 LDVLVVNQTS 760 DTLQNCTLEL 770 ATLGDLKLVE 780 KPSPLTLAPH 790 DFANIKANVK 800 VASTENGIIF 810 GNIVYDVSGA 820 ASDRNCVVLS 830 DIHIDIMDYI 840 QPATCTDAEF 850 RQMWAEFEWE 860 NKVTVNTNMV 870 DLNDYLQHIL 880 KSTNMKCLTP 890 EKALSGYCGF 900 MAANLYARSI 910 FGEDALANVS 920 IEKPIHQGPD 930 AAVTGHIRIR 940 AKSQGMALSL 950 GDKINLSQKK TSI

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.