Name | Number of supported studies | Average coverage | |
---|---|---|---|
endothelial cell | 52 studies | 63% ± 22% | |
pericyte | 39 studies | 59% ± 22% | |
fibroblast | 32 studies | 51% ± 25% | |
smooth muscle cell | 31 studies | 49% ± 19% | |
macrophage | 30 studies | 46% ± 15% | |
endothelial cell of lymphatic vessel | 17 studies | 42% ± 13% | |
capillary endothelial cell | 17 studies | 68% ± 18% | |
endothelial cell of artery | 16 studies | 72% ± 20% | |
microglial cell | 16 studies | 51% ± 22% | |
vein endothelial cell | 15 studies | 62% ± 18% | |
endothelial cell of vascular tree | 14 studies | 60% ± 18% | |
myofibroblast cell | 12 studies | 56% ± 22% | |
mast cell | 9 studies | 41% ± 14% | |
myeloid cell | 9 studies | 40% ± 18% | |
connective tissue cell | 8 studies | 61% ± 23% | |
hepatocyte | 6 studies | 62% ± 24% | |
endothelial cell of sinusoid | 5 studies | 42% ± 19% | |
retina horizontal cell | 5 studies | 49% ± 17% | |
adventitial cell | 5 studies | 48% ± 12% | |
cardiac muscle cell | 5 studies | 22% ± 3% | |
mononuclear phagocyte | 4 studies | 22% ± 6% | |
T cell | 4 studies | 26% ± 9% | |
glomerular endothelial cell | 4 studies | 71% ± 7% | |
leukocyte | 4 studies | 36% ± 25% | |
chondrocyte | 4 studies | 45% ± 15% | |
lymphocyte | 4 studies | 18% ± 3% | |
tissue-resident macrophage | 3 studies | 41% ± 18% | |
conventional dendritic cell | 3 studies | 24% ± 3% | |
dendritic cell | 3 studies | 37% ± 7% | |
muscle cell | 3 studies | 74% ± 12% | |
myoepithelial cell | 3 studies | 47% ± 11% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
breast | 100% | 73907.02 | 458 / 459 | 96% | 383.02 | 1071 / 1118 |
lung | 100% | 412496.54 | 578 / 578 | 86% | 383.56 | 995 / 1155 |
prostate | 95% | 76429.20 | 233 / 245 | 91% | 313.70 | 457 / 502 |
thymus | 99% | 54065.45 | 647 / 653 | 85% | 212.23 | 517 / 605 |
liver | 91% | 85820.28 | 206 / 226 | 92% | 952.45 | 375 / 406 |
kidney | 97% | 73130.80 | 86 / 89 | 83% | 535.43 | 750 / 901 |
esophagus | 92% | 52302.29 | 1323 / 1445 | 78% | 231.21 | 142 / 183 |
bladder | 100% | 113545.43 | 21 / 21 | 65% | 172.79 | 330 / 504 |
intestine | 97% | 44450.07 | 937 / 966 | 68% | 168.36 | 357 / 527 |
adrenal gland | 82% | 26845.86 | 211 / 258 | 77% | 222.13 | 176 / 230 |
stomach | 82% | 33859.04 | 296 / 359 | 74% | 255.59 | 213 / 286 |
uterus | 98% | 66906.56 | 167 / 170 | 48% | 209.11 | 221 / 459 |
skin | 33% | 7824.99 | 600 / 1809 | 94% | 980.96 | 443 / 472 |
brain | 27% | 5848.65 | 724 / 2642 | 98% | 405.06 | 690 / 705 |
ovary | 55% | 20215.12 | 99 / 180 | 62% | 114.68 | 265 / 430 |
pancreas | 21% | 4255.12 | 69 / 328 | 93% | 324.62 | 166 / 178 |
adipose | 100% | 96111.99 | 1204 / 1204 | 0% | 0 | 0 / 0 |
blood vessel | 100% | 164837.77 | 1335 / 1335 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 99% | 1011.84 | 79 / 80 |
spleen | 97% | 43777.64 | 234 / 241 | 0% | 0 | 0 / 0 |
heart | 97% | 41632.90 | 834 / 861 | 0% | 0 | 0 / 0 |
lymph node | 0% | 0 | 0 / 0 | 55% | 84.12 | 16 / 29 |
tonsil | 0% | 0 | 0 / 0 | 44% | 73.23 | 20 / 45 |
muscle | 32% | 6900.95 | 257 / 803 | 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 |
peripheral blood | 0% | 0 | 0 / 929 | 0% | 0 | 0 / 0 |
placenta | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
spinal column | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
ureter | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 1 |
GO_0007584 | Biological process | response to nutrient |
GO_0001869 | Biological process | negative regulation of complement activation, lectin pathway |
GO_0006953 | Biological process | acute-phase response |
GO_0001553 | Biological process | luteinization |
GO_0010037 | Biological process | response to carbon dioxide |
GO_1990402 | Biological process | embryonic liver development |
GO_0051384 | Biological process | response to glucocorticoid |
GO_0034695 | Biological process | response to prostaglandin E |
GO_0048863 | Biological process | stem cell differentiation |
GO_0002438 | Biological process | acute inflammatory response to antigenic stimulus |
GO_0005615 | Cellular component | extracellular space |
GO_0005576 | Cellular component | extracellular region |
GO_0070062 | Cellular component | extracellular exosome |
GO_0062023 | Cellular component | collagen-containing extracellular matrix |
GO_0072562 | Cellular component | blood microparticle |
GO_0031093 | Cellular component | platelet alpha granule lumen |
GO_0019899 | Molecular function | enzyme binding |
GO_0043120 | Molecular function | tumor necrosis factor binding |
GO_0019966 | Molecular function | interleukin-1 binding |
GO_0004866 | Molecular function | endopeptidase inhibitor activity |
GO_0004867 | Molecular function | serine-type endopeptidase inhibitor activity |
GO_0042802 | Molecular function | identical protein binding |
GO_0005102 | Molecular function | signaling receptor binding |
GO_0048403 | Molecular function | brain-derived neurotrophic factor binding |
GO_0002020 | Molecular function | protease binding |
GO_0048306 | Molecular function | calcium-dependent protein binding |
GO_0019838 | Molecular function | growth factor binding |
GO_0048406 | Molecular function | nerve growth factor binding |
GO_0019959 | Molecular function | interleukin-8 binding |
GO_0005515 | Molecular function | protein binding |
Gene name | A2M |
Protein name | Alternative protein A2M Alpha-2-macroglobulin (Alpha-2-M) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5) Alpha-2-macroglobulin |
Synonyms | CPAMD5 FWP007 |
Description | FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. |
Accessions | L0R6B6 F5H1E8 ENST00000404455.2 H0YFH1 ENST00000546069.1 P01023 ENST00000318602.12 F8W7L3 ENST00000539638.5 Q9BQ22 |