Name | Number of supported studies | Average coverage | |
---|---|---|---|
peripheral blood | 21 studies | 65% ± 14% | |
lung | 19 studies | 70% ± 18% | |
brain | 19 studies | 52% ± 19% | |
intestine | 15 studies | 55% ± 28% | |
eye | 11 studies | 53% ± 23% | |
kidney | 9 studies | 69% ± 18% | |
lymph node | 7 studies | 71% ± 20% | |
bone marrow | 6 studies | 51% ± 26% | |
uterus | 6 studies | 75% ± 28% | |
liver | 6 studies | 63% ± 16% | |
pancreas | 5 studies | 83% ± 20% | |
prostate | 5 studies | 71% ± 31% | |
placenta | 4 studies | 79% ± 25% | |
heart | 4 studies | 34% ± 17% | |
adipose | 4 studies | 44% ± 19% | |
breast | 4 studies | 87% ± 3% | |
ovary | 3 studies | 68% ± 32% | |
adrenal gland | 3 studies | 73% ± 12% | |
esophagus | 3 studies | 61% ± 24% | |
skin | 3 studies | 73% ± 13% | |
stomach | 3 studies | 55% ± 24% | |
thymus | 3 studies | 76% ± 26% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
ovary | 100% | 118033.16 | 180 / 180 | 100% | 1570.99 | 430 / 430 |
prostate | 100% | 51607.27 | 245 / 245 | 100% | 1829.90 | 502 / 502 |
stomach | 100% | 50655.10 | 359 / 359 | 100% | 1585.50 | 286 / 286 |
esophagus | 100% | 47805.52 | 1444 / 1445 | 100% | 2018.72 | 183 / 183 |
breast | 100% | 59465.40 | 459 / 459 | 100% | 2192.39 | 1117 / 1118 |
intestine | 100% | 47907.06 | 966 / 966 | 100% | 1736.56 | 526 / 527 |
lung | 100% | 65810.03 | 577 / 578 | 100% | 1679.78 | 1152 / 1155 |
uterus | 100% | 70094.75 | 170 / 170 | 100% | 1616.43 | 457 / 459 |
skin | 100% | 60485.39 | 1808 / 1809 | 100% | 2754.22 | 470 / 472 |
bladder | 100% | 66041.14 | 21 / 21 | 99% | 1719.06 | 501 / 504 |
thymus | 100% | 58047.61 | 653 / 653 | 99% | 1417.62 | 600 / 605 |
brain | 99% | 58068.36 | 2620 / 2642 | 100% | 1245.32 | 705 / 705 |
pancreas | 100% | 48793.75 | 327 / 328 | 99% | 1195.00 | 177 / 178 |
adrenal gland | 100% | 83797.47 | 258 / 258 | 98% | 2008.48 | 225 / 230 |
kidney | 100% | 50924.88 | 89 / 89 | 97% | 1095.89 | 876 / 901 |
liver | 94% | 26123.85 | 213 / 226 | 97% | 1055.15 | 393 / 406 |
adipose | 100% | 61717.61 | 1204 / 1204 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 100% | 2295.92 | 80 / 80 |
lymph node | 0% | 0 | 0 / 0 | 100% | 1903.79 | 29 / 29 |
muscle | 100% | 95662.61 | 803 / 803 | 0% | 0 | 0 / 0 |
spleen | 100% | 42038.13 | 241 / 241 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 100% | 1378.57 | 45 / 45 |
ureter | 0% | 0 | 0 / 0 | 100% | 799.81 | 1 / 1 |
blood vessel | 100% | 62853.43 | 1334 / 1335 | 0% | 0 | 0 / 0 |
heart | 97% | 61339.90 | 834 / 861 | 0% | 0 | 0 / 0 |
peripheral blood | 63% | 44062.69 | 584 / 929 | 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_0030511 | Biological process | positive regulation of transforming growth factor beta receptor signaling pathway |
GO_0006986 | Biological process | response to unfolded protein |
GO_0032435 | Biological process | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
GO_0034605 | Biological process | cellular response to heat |
GO_0061077 | Biological process | chaperone-mediated protein folding |
GO_0032880 | Biological process | regulation of protein localization |
GO_0071353 | Biological process | cellular response to interleukin-4 |
GO_1901799 | Biological process | negative regulation of proteasomal protein catabolic process |
GO_2000010 | Biological process | positive regulation of protein localization to cell surface |
GO_0001890 | Biological process | placenta development |
GO_0031396 | Biological process | regulation of protein ubiquitination |
GO_0051131 | Biological process | chaperone-mediated protein complex assembly |
GO_0006457 | Biological process | protein folding |
GO_0097435 | Biological process | supramolecular fiber organization |
GO_0007004 | Biological process | telomere maintenance via telomerase |
GO_0045597 | Biological process | positive regulation of cell differentiation |
GO_0043066 | Biological process | negative regulation of apoptotic process |
GO_1905323 | Biological process | telomerase holoenzyme complex assembly |
GO_0050821 | Biological process | protein stabilization |
GO_0045429 | Biological process | positive regulation of nitric oxide biosynthetic process |
GO_0019062 | Biological process | virion attachment to host cell |
GO_0032516 | Biological process | positive regulation of phosphoprotein phosphatase activity |
GO_0051726 | Biological process | regulation of cell cycle |
GO_0005576 | Cellular component | extracellular region |
GO_0005886 | Cellular component | plasma membrane |
GO_0048471 | Cellular component | perinuclear region of cytoplasm |
GO_0016020 | Cellular component | membrane |
GO_0005739 | Cellular component | mitochondrion |
GO_0070062 | Cellular component | extracellular exosome |
GO_0032991 | Cellular component | protein-containing complex |
GO_0005654 | Cellular component | nucleoplasm |
GO_0043025 | Cellular component | neuronal cell body |
GO_0034774 | Cellular component | secretory granule lumen |
GO_0120293 | Cellular component | dynein axonemal particle |
GO_0009986 | Cellular component | cell surface |
GO_0101031 | Cellular component | protein folding chaperone complex |
GO_1904813 | Cellular component | ficolin-1-rich granule lumen |
GO_0005829 | Cellular component | cytosol |
GO_0044294 | Cellular component | dendritic growth cone |
GO_0008180 | Cellular component | COP9 signalosome |
GO_0044295 | Cellular component | axonal growth cone |
GO_0005737 | Cellular component | cytoplasm |
GO_0034751 | Cellular component | aryl hydrocarbon receptor complex |
GO_1990565 | Cellular component | HSP90-CDC37 chaperone complex |
GO_0042470 | Cellular component | melanosome |
GO_0005634 | Cellular component | nucleus |
GO_0042803 | Molecular function | protein homodimerization activity |
GO_0030911 | Molecular function | TPR domain binding |
GO_0141069 | Molecular function | receptor ligand inhibitor activity |
GO_0070182 | Molecular function | DNA polymerase binding |
GO_0019887 | Molecular function | protein kinase regulator activity |
GO_0044183 | Molecular function | protein folding chaperone |
GO_0042277 | Molecular function | peptide binding |
GO_0019900 | Molecular function | kinase binding |
GO_0045296 | Molecular function | cadherin binding |
GO_0031072 | Molecular function | heat shock protein binding |
GO_0019901 | Molecular function | protein kinase binding |
GO_0031625 | Molecular function | ubiquitin protein ligase binding |
GO_0042802 | Molecular function | identical protein binding |
GO_0051082 | Molecular function | unfolded protein binding |
GO_0043008 | Molecular function | ATP-dependent protein binding |
GO_0030235 | Molecular function | nitric-oxide synthase regulator activity |
GO_0140662 | Molecular function | ATP-dependent protein folding chaperone |
GO_0005524 | Molecular function | ATP binding |
GO_0003723 | Molecular function | RNA binding |
GO_0048156 | Molecular function | tau protein binding |
GO_0023026 | Molecular function | MHC class II protein complex binding |
GO_0046983 | Molecular function | protein dimerization activity |
GO_0097718 | Molecular function | disordered domain specific binding |
GO_0005515 | Molecular function | protein binding |
GO_1990226 | Molecular function | histone methyltransferase binding |
GO_0016887 | Molecular function | ATP hydrolysis activity |
GO_0003725 | Molecular function | double-stranded RNA binding |
GO_0042826 | Molecular function | histone deacetylase binding |
Gene name | HSP90AB1 |
Protein name | Heat shock protein HSP 90-beta Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) |
Synonyms | HSP90B HSPC2 HSPCB |
Description | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function . Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle . Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression . Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation . Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery . Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription . Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 . .; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes . Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). . |
Accessions | ENST00000620073.4 ENST00000353801.7 P08238 ENST00000371646.10 ENST00000371554.2 Q6PK50 |