Name | Number of supported studies | Average coverage | |
---|---|---|---|
hepatocyte | 6 studies | 82% ± 20% | |
epithelial cell of proximal tubule | 5 studies | 30% ± 13% | |
cholangiocyte | 3 studies | 46% ± 19% | |
endothelial cell | 3 studies | 35% ± 12% |
Name | Number of supported studies | Average coverage | |
---|---|---|---|
liver | 4 studies | 45% ± 15% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
liver | 100% | 58832.07 | 226 / 226 | 94% | 441.52 | 382 / 406 |
kidney | 100% | 4553.73 | 89 / 89 | 25% | 6.49 | 223 / 901 |
prostate | 88% | 8.78 | 216 / 245 | 2% | 0.03 | 9 / 502 |
ovary | 87% | 7.74 | 156 / 180 | 0% | 0 | 0 / 430 |
uterus | 85% | 10.58 | 145 / 170 | 1% | 0.05 | 6 / 459 |
pancreas | 73% | 5.75 | 240 / 328 | 7% | 0.12 | 13 / 178 |
brain | 75% | 7.25 | 1985 / 2642 | 0% | 0.00 | 1 / 705 |
lung | 73% | 10.31 | 421 / 578 | 1% | 0.04 | 15 / 1155 |
bladder | 62% | 3.00 | 13 / 21 | 1% | 0.02 | 4 / 504 |
spleen | 61% | 89.00 | 148 / 241 | 0% | 0 | 0 / 0 |
intestine | 60% | 5.08 | 581 / 966 | 0% | 0.87 | 2 / 527 |
adrenal gland | 60% | 5.39 | 155 / 258 | 0% | 0 | 0 / 230 |
peripheral blood | 57% | 17.65 | 530 / 929 | 0% | 0 | 0 / 0 |
stomach | 56% | 3.81 | 202 / 359 | 1% | 0.01 | 2 / 286 |
esophagus | 47% | 3.79 | 685 / 1445 | 2% | 0.05 | 4 / 183 |
blood vessel | 47% | 3.54 | 623 / 1335 | 0% | 0 | 0 / 0 |
thymus | 45% | 3.35 | 293 / 653 | 0% | 0.00 | 1 / 605 |
skin | 43% | 4.16 | 769 / 1809 | 1% | 0.03 | 3 / 472 |
breast | 40% | 5.43 | 183 / 459 | 0% | 0.05 | 4 / 1118 |
adipose | 39% | 10.28 | 474 / 1204 | 0% | 0 | 0 / 0 |
heart | 37% | 5.26 | 317 / 861 | 0% | 0 | 0 / 0 |
muscle | 36% | 2.22 | 286 / 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 |
eye | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 80 |
gingiva | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
lymph node | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 29 |
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 |
tonsil | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 45 |
ureter | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 1 |
GO_0008285 | Biological process | negative regulation of cell population proliferation |
GO_0046716 | Biological process | muscle cell cellular homeostasis |
GO_0043536 | Biological process | positive regulation of blood vessel endothelial cell migration |
GO_0051918 | Biological process | negative regulation of fibrinolysis |
GO_0022617 | Biological process | extracellular matrix disassembly |
GO_0051702 | Biological process | biological process involved in interaction with symbiont |
GO_0007596 | Biological process | blood coagulation |
GO_0042246 | Biological process | tissue regeneration |
GO_0042730 | Biological process | fibrinolysis |
GO_0051919 | Biological process | positive regulation of fibrinolysis |
GO_0060707 | Biological process | trophoblast giant cell differentiation |
GO_0048771 | Biological process | tissue remodeling |
GO_0060716 | Biological process | labyrinthine layer blood vessel development |
GO_0006508 | Biological process | proteolysis |
GO_0045445 | Biological process | myoblast differentiation |
GO_0099183 | Biological process | trans-synaptic signaling by BDNF, modulating synaptic transmission |
GO_0071674 | Biological process | mononuclear cell migration |
GO_2000048 | Biological process | negative regulation of cell-cell adhesion mediated by cadherin |
GO_0010812 | Biological process | negative regulation of cell-substrate adhesion |
GO_0005615 | Cellular component | extracellular space |
GO_0098978 | Cellular component | glutamatergic synapse |
GO_0009897 | Cellular component | external side of plasma membrane |
GO_0005576 | Cellular component | extracellular region |
GO_0098685 | Cellular component | Schaffer collateral - CA1 synapse |
GO_0005886 | Cellular component | plasma membrane |
GO_0070062 | Cellular component | extracellular exosome |
GO_0062023 | Cellular component | collagen-containing extracellular matrix |
GO_0009986 | Cellular component | cell surface |
GO_0072562 | Cellular component | blood microparticle |
GO_0031093 | Cellular component | platelet alpha granule lumen |
GO_0019899 | Molecular function | enzyme binding |
GO_0004175 | Molecular function | endopeptidase activity |
GO_0019904 | Molecular function | protein domain specific binding |
GO_0019900 | Molecular function | kinase binding |
GO_0005102 | Molecular function | signaling receptor binding |
GO_0034185 | Molecular function | apolipoprotein binding |
GO_0002020 | Molecular function | protease binding |
GO_1990405 | Molecular function | protein antigen binding |
GO_0008236 | Molecular function | serine-type peptidase activity |
GO_0051087 | Molecular function | protein-folding chaperone binding |
GO_0005515 | Molecular function | protein binding |
GO_0004252 | Molecular function | serine-type endopeptidase activity |
Gene name | PLG |
Protein name | Plasminogen (EC 3.4.21.7) Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B] |
Synonyms | hCG_2029799 |
Description | FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. .; FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. .; FUNCTION: (Microbial infection) ENO/enoloase from parasite P.falciparum (strain NF54) interacts with PLG present in the mosquito blood meal to promote the invasion of the mosquito midgut by the parasite ookinete . The catalytic active form, plasmin, is essential for the invasion of the mosquito midgut . .; FUNCTION: (Microbial infection) Binds to OspC on the surface of B.burgdorferi cells, possibly conferring an extracellular protease activity on the bacteria that allows it to traverse host tissue. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. . |
Accessions | A0A9L9PXP2 Q5TEH5 ENST00000366924.6 ENST00000297289.9 A0A9L9PYG2 A6PVI2 ENST00000706906.1 ENST00000418964.2 ENST00000308192.14 A0A9L9PY04 Q9UMI2 A0A0F7G8J1 P00747 ENST00000494325.2 |