COPB1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006886Biological processintracellular protein transport
GO_0006891Biological processintra-Golgi vesicle-mediated transport
GO_0006888Biological processendoplasmic reticulum to Golgi vesicle-mediated transport
GO_0030667Cellular componentsecretory granule membrane
GO_0030126Cellular componentCOPI vesicle coat
GO_0005886Cellular componentplasma membrane
GO_0016020Cellular componentmembrane
GO_0005789Cellular componentendoplasmic reticulum membrane
GO_0005794Cellular componentGolgi apparatus
GO_0000139Cellular componentGolgi membrane
GO_0005829Cellular componentcytosol
GO_0070821Cellular componenttertiary granule membrane
GO_0005793Cellular componentendoplasmic reticulum-Golgi intermediate compartment
GO_0101003Cellular componentficolin-1-rich granule membrane
GO_0030133Cellular componenttransport vesicle
GO_0043231Cellular componentintracellular membrane-bounded organelle
GO_0005798Cellular componentGolgi-associated vesicle
GO_0005198Molecular functionstructural molecule activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameCOPB1
Protein nameCoatomer subunit beta (Beta-coat protein) (Beta-COP)
COPI coat complex subunit beta 1
SynonymsCOPB
MSTP026
DescriptionFUNCTION: 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. .

AccessionsE9PKQ1
E9PP63
ENST00000534771.1
E9PP73
ENST00000249923.7
ENST00000529866.5
P53618
ENST00000439561.7
ENST00000534234.5