Name | Number of supported studies | Average coverage | |
---|---|---|---|
brain | 16 studies | 35% ± 19% | |
lung | 11 studies | 23% ± 6% | |
peripheral blood | 8 studies | 24% ± 9% | |
bone marrow | 4 studies | 22% ± 8% | |
heart | 4 studies | 19% ± 2% | |
liver | 4 studies | 30% ± 16% | |
intestine | 4 studies | 22% ± 7% | |
adipose | 4 studies | 33% ± 16% | |
pancreas | 3 studies | 47% ± 26% | |
placenta | 3 studies | 21% ± 7% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
breast | 100% | 10870.47 | 459 / 459 | 100% | 229.74 | 1118 / 1118 |
esophagus | 100% | 8667.34 | 1445 / 1445 | 100% | 135.80 | 183 / 183 |
lung | 100% | 12007.99 | 578 / 578 | 100% | 142.43 | 1155 / 1155 |
ovary | 100% | 11065.09 | 180 / 180 | 100% | 110.85 | 430 / 430 |
skin | 100% | 14369.58 | 1809 / 1809 | 100% | 190.22 | 472 / 472 |
stomach | 100% | 8273.66 | 359 / 359 | 100% | 123.00 | 286 / 286 |
intestine | 100% | 10038.07 | 966 / 966 | 100% | 116.04 | 526 / 527 |
prostate | 100% | 9720.87 | 245 / 245 | 100% | 146.60 | 501 / 502 |
bladder | 100% | 9574.05 | 21 / 21 | 100% | 119.76 | 502 / 504 |
brain | 100% | 9214.65 | 2631 / 2642 | 100% | 123.90 | 705 / 705 |
pancreas | 100% | 6720.81 | 328 / 328 | 99% | 108.60 | 177 / 178 |
thymus | 100% | 10938.37 | 653 / 653 | 99% | 115.46 | 600 / 605 |
uterus | 100% | 10908.31 | 170 / 170 | 99% | 116.65 | 455 / 459 |
kidney | 100% | 7059.09 | 89 / 89 | 98% | 101.33 | 887 / 901 |
liver | 100% | 6165.00 | 225 / 226 | 98% | 98.26 | 396 / 406 |
adrenal gland | 100% | 10070.54 | 258 / 258 | 94% | 88.78 | 217 / 230 |
adipose | 100% | 11618.78 | 1204 / 1204 | 0% | 0 | 0 / 0 |
blood vessel | 100% | 12015.40 | 1335 / 1335 | 0% | 0 | 0 / 0 |
lymph node | 0% | 0 | 0 / 0 | 100% | 96.18 | 29 / 29 |
muscle | 100% | 8315.20 | 803 / 803 | 0% | 0 | 0 / 0 |
spleen | 100% | 10378.75 | 241 / 241 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 100% | 97.66 | 45 / 45 |
ureter | 0% | 0 | 0 / 0 | 100% | 25.05 | 1 / 1 |
eye | 0% | 0 | 0 / 0 | 99% | 99.02 | 79 / 80 |
peripheral blood | 99% | 10125.71 | 916 / 929 | 0% | 0 | 0 / 0 |
heart | 98% | 7892.31 | 842 / 861 | 0% | 0 | 0 / 0 |
abdomen | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
bone marrow | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
diaphragm | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
gingiva | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasal cavity | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasopharynx | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nose | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
placenta | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
spinal column | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
GO_0006890 | Biological process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
GO_0007165 | Biological process | signal transduction |
GO_0006886 | Biological process | intracellular protein transport |
GO_0030157 | Biological process | pancreatic juice secretion |
GO_0006891 | Biological process | intra-Golgi vesicle-mediated transport |
GO_0006888 | Biological process | endoplasmic reticulum to Golgi vesicle-mediated transport |
GO_0005615 | Cellular component | extracellular space |
GO_0030126 | Cellular component | COPI vesicle coat |
GO_0016020 | Cellular component | membrane |
GO_0005789 | Cellular component | endoplasmic reticulum membrane |
GO_0070062 | Cellular component | extracellular exosome |
GO_0000139 | Cellular component | Golgi membrane |
GO_0005829 | Cellular component | cytosol |
GO_0030426 | Cellular component | growth cone |
GO_0005737 | Cellular component | cytoplasm |
GO_0030133 | Cellular component | transport vesicle |
GO_0005179 | Molecular function | hormone activity |
GO_0005198 | Molecular function | structural molecule activity |
GO_0005515 | Molecular function | protein binding |
Gene name | COPA |
Protein name | Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (HEP-COP) (HEPCOP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin] Coatomer subunit alpha COPI coat complex subunit alpha |
Synonyms | |
Description | 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 (By similarity). .; FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor. 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. . 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. . 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. . 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. . 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. . 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. . |
Accessions | ENST00000368069.7 [P53621-2] P53621 ENST00000650154.1 ENST00000647899.1 A0A3B3IS23 A0A3B3ITV3 ENST00000647683.1 A0A3B3IS84 ENST00000649676.1 A0A3B3ITX2 A0A3B3IU78 A0A3B3IU89 A0A3B3ISK1 ENST00000648280.1 ENST00000648805.1 A0A3B3IU84 ENST00000649963.1 A0A3B3IT15 ENST00000648501.1 ENST00000241704.8 [P53621-1] A0A3B3ISC6 ENST00000649787.1 ENST00000649231.1 ENST00000647799.1 A0A3B3ITI7 |