| Tbio | Coatomer subunit beta |
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.
This gene encodes a protein subunit of the coatomer complex associated with non-clathrin coated vesicles. The coatomer complex, also known as the coat protein complex 1, forms in the cytoplasm and is recruited to the Golgi by activated guanosine triphosphatases. Once at the Golgi membrane, the coatomer complex may assist in the movement of protein and lipid components back to the endoplasmic reticulum. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jan 2009]
This gene encodes a protein subunit of the coatomer complex associated with non-clathrin coated vesicles. The coatomer complex, also known as the coat protein complex 1, forms in the cytoplasm and is recruited to the Golgi by activated guanosine triphosphatases. Once at the Golgi membrane, the coatomer complex may assist in the movement of protein and lipid components back to the endoplasmic reticulum. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jan 2009]
Comments
Property Summary
| NCBI Gene PubMed Count | 45 |
| Grant Count | 5 |
| R01 Count | 1 |
| Funding | $1,728,894 |
| PubMed Score | 82.57 |
| PubTator Score | 33.09 |
| Disease | log2 FC | p |
|---|---|---|
| Multiple myeloma | 1.669 | 0.000 |
| psoriasis | 1.200 | 0.000 |
| osteosarcoma | 1.192 | 0.001 |
| glioblastoma | 1.300 | 0.003 |
| juvenile dermatomyositis | 1.149 | 0.000 |
| acute quadriplegic myopathy | 1.034 | 0.000 |
| diabetes mellitus | -1.100 | 0.004 |
| ovarian cancer | 2.100 | 0.001 |
| dermatomyositis | 1.100 | 0.003 |
| PMID | Text |
|---|---|
| 23559827 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 21543478 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 21543478 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 21543478 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 20622010 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 19149577 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 19149577 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 18725938 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 18725938 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| 15202998 | HIV-1 Nef utilizes beta-COP in CD28 downregulation |
| More... |
MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQ 1 - 70 DHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAI 71 - 140 RACLEHRHSYVRRNAVLAIYTIYRNFEHLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLS 141 - 210 TCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKA 211 - 280 AAQCYIDLIIKESDNNVKLIVLDRLIELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSS 281 - 350 RNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDNNEAAAADV 351 - 420 LEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEIRRSLGEIPIVE 421 - 490 SEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATT 491 - 560 LTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDI 561 - 630 FNKECRQSLSHMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNT 631 - 700 QRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVE 701 - 770 KPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEF 771 - 840 RQMWAEFEWENKVTVNTNMVDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVS 841 - 910 IEKPIHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSI 911 - 953 //
| PMID | Year | Title |
|---|---|---|
| 25944712 | 2015 | N-terminome analysis of the human mitochondrial proteome. |
| 25208829 | 2014 | Genome-wide association study of vitamin D levels in children: replication in the Western Australian Pregnancy Cohort (Raine) study. |
| 25036637 | 2014 | A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. |
| 24806965 | 2014 | TMEM115 is an integral membrane protein of the Golgi complex involved in retrograde transport. |
| 24275569 | 2014 | An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. |
| 22555292 | 2012 | LINC complex alterations in DMD and EDMD/CMT fibroblasts. |
| 22223895 | 2012 | Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-?-acetylation features. |
| 21269460 | 2011 | Initial characterization of the human central proteome. |
| 20551905 | 2010 | A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane. |
| 20362547 | 2010 | Enhancement of TREK1 channel surface expression by protein-protein interaction with beta-COP. |
| More... |
