Name | Number of supported studies | Average coverage | |
---|---|---|---|
peripheral blood | 18 studies | 42% ± 12% | |
lung | 17 studies | 31% ± 10% | |
intestine | 10 studies | 25% ± 9% | |
kidney | 7 studies | 28% ± 9% | |
brain | 5 studies | 28% ± 7% | |
liver | 5 studies | 26% ± 8% | |
pancreas | 4 studies | 40% ± 18% | |
placenta | 4 studies | 24% ± 7% | |
bone marrow | 4 studies | 30% ± 12% | |
uterus | 4 studies | 34% ± 12% | |
lymph node | 4 studies | 37% ± 6% | |
breast | 4 studies | 30% ± 5% | |
prostate | 3 studies | 27% ± 8% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
esophagus | 100% | 8243.49 | 1445 / 1445 | 100% | 211.37 | 183 / 183 |
ovary | 100% | 7106.32 | 180 / 180 | 100% | 179.81 | 430 / 430 |
skin | 100% | 10007.65 | 1809 / 1809 | 100% | 330.20 | 472 / 472 |
intestine | 100% | 8340.28 | 966 / 966 | 99% | 226.13 | 524 / 527 |
stomach | 100% | 6374.50 | 359 / 359 | 99% | 222.62 | 284 / 286 |
prostate | 100% | 8023.41 | 245 / 245 | 99% | 224.84 | 497 / 502 |
brain | 99% | 5354.32 | 2619 / 2642 | 100% | 168.45 | 704 / 705 |
thymus | 100% | 7435.98 | 652 / 653 | 99% | 144.27 | 598 / 605 |
kidney | 100% | 8233.52 | 89 / 89 | 99% | 158.04 | 889 / 901 |
lung | 100% | 11122.54 | 578 / 578 | 99% | 178.40 | 1139 / 1155 |
breast | 100% | 9733.44 | 459 / 459 | 98% | 186.31 | 1101 / 1118 |
bladder | 100% | 8268.95 | 21 / 21 | 98% | 204.18 | 494 / 504 |
uterus | 100% | 8775.43 | 170 / 170 | 98% | 166.42 | 449 / 459 |
pancreas | 99% | 4526.30 | 324 / 328 | 99% | 181.31 | 176 / 178 |
adrenal gland | 100% | 7253.64 | 258 / 258 | 96% | 200.04 | 221 / 230 |
liver | 100% | 4237.85 | 225 / 226 | 96% | 113.39 | 390 / 406 |
adipose | 100% | 10811.69 | 1204 / 1204 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 100% | 408.32 | 80 / 80 |
lymph node | 0% | 0 | 0 / 0 | 100% | 248.30 | 29 / 29 |
spleen | 100% | 9233.08 | 241 / 241 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 100% | 158.91 | 45 / 45 |
ureter | 0% | 0 | 0 / 0 | 100% | 122.79 | 1 / 1 |
blood vessel | 100% | 10377.39 | 1334 / 1335 | 0% | 0 | 0 / 0 |
peripheral blood | 100% | 11117.64 | 925 / 929 | 0% | 0 | 0 / 0 |
heart | 98% | 4564.02 | 847 / 861 | 0% | 0 | 0 / 0 |
muscle | 97% | 3391.16 | 779 / 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 |
placenta | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
spinal column | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
GO_0007266 | Biological process | Rho protein signal transduction |
GO_0032880 | Biological process | regulation of protein localization |
GO_0071526 | Biological process | semaphorin-plexin signaling pathway |
GO_0098693 | Biological process | regulation of synaptic vesicle cycle |
GO_0043066 | Biological process | negative regulation of apoptotic process |
GO_0035023 | Biological process | regulation of Rho protein signal transduction |
GO_0001772 | Cellular component | immunological synapse |
GO_0070062 | Cellular component | extracellular exosome |
GO_0005856 | Cellular component | cytoskeleton |
GO_0005829 | Cellular component | cytosol |
GO_0098685 | Cellular component | Schaffer collateral - CA1 synapse |
GO_0016020 | Cellular component | membrane |
GO_0005634 | Cellular component | nucleus |
GO_0005094 | Molecular function | Rho GDP-dissociation inhibitor activity |
GO_0005515 | Molecular function | protein binding |
GO_0005096 | Molecular function | GTPase activator activity |
Gene name | ARHGDIA |
Protein name | Rho GDP-dissociation inhibitor 1 (Rho GDI 1) (Rho-GDI alpha) Rho GDP-dissociation inhibitor 1 (Rho-GDI alpha) |
Synonyms | GDIA1 HEL-S-47e |
Description | FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. . |
Accessions | ENST00000584461.5 ENST00000581876.5 ENST00000580033.5 J3KTF8 ENST00000580685.5 [P52565-1] J3KS60 ENST00000400721.8 [P52565-2] J3QQX2 ENST00000541078.6 [P52565-1] A0A0S2Z3D9 ENST00000578351.1 ENST00000579121.5 P52565 J3KRY1 ENST00000269321.12 [P52565-1] V9HWE8 J3KRE2 ENST00000583868.5 |