Name | Number of supported studies | Average coverage | |
---|---|---|---|
lung | 18 studies | 33% ± 13% | |
peripheral blood | 15 studies | 29% ± 8% | |
brain | 15 studies | 31% ± 15% | |
eye | 10 studies | 29% ± 11% | |
intestine | 9 studies | 24% ± 12% | |
kidney | 9 studies | 31% ± 6% | |
heart | 6 studies | 24% ± 5% | |
liver | 5 studies | 40% ± 26% | |
pancreas | 4 studies | 47% ± 17% | |
uterus | 4 studies | 38% ± 17% | |
lymph node | 4 studies | 26% ± 10% | |
breast | 4 studies | 26% ± 2% | |
adipose | 4 studies | 19% ± 2% | |
bone marrow | 3 studies | 26% ± 7% | |
placenta | 3 studies | 31% ± 9% | |
prostate | 3 studies | 24% ± 9% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
esophagus | 100% | 5975.59 | 1445 / 1445 | 100% | 41.50 | 183 / 183 |
ovary | 100% | 3434.39 | 180 / 180 | 100% | 43.77 | 430 / 430 |
uterus | 100% | 5522.44 | 170 / 170 | 100% | 38.12 | 459 / 459 |
lung | 100% | 6256.12 | 578 / 578 | 100% | 59.29 | 1154 / 1155 |
kidney | 100% | 5521.39 | 89 / 89 | 100% | 67.42 | 900 / 901 |
breast | 100% | 6033.57 | 459 / 459 | 100% | 47.00 | 1116 / 1118 |
brain | 100% | 4258.93 | 2635 / 2642 | 100% | 72.43 | 705 / 705 |
thymus | 100% | 4772.60 | 653 / 653 | 99% | 48.18 | 601 / 605 |
stomach | 100% | 4234.63 | 359 / 359 | 99% | 56.72 | 284 / 286 |
prostate | 100% | 4383.39 | 244 / 245 | 100% | 40.46 | 500 / 502 |
intestine | 100% | 7130.20 | 966 / 966 | 99% | 55.30 | 522 / 527 |
bladder | 100% | 6325.19 | 21 / 21 | 99% | 45.63 | 497 / 504 |
adrenal gland | 100% | 5317.71 | 258 / 258 | 98% | 31.45 | 225 / 230 |
liver | 100% | 2620.04 | 225 / 226 | 97% | 27.94 | 395 / 406 |
skin | 99% | 4299.41 | 1794 / 1809 | 95% | 41.05 | 447 / 472 |
pancreas | 93% | 2074.44 | 306 / 328 | 99% | 46.00 | 176 / 178 |
blood vessel | 100% | 8249.85 | 1335 / 1335 | 0% | 0 | 0 / 0 |
lymph node | 0% | 0 | 0 / 0 | 100% | 33.29 | 29 / 29 |
muscle | 100% | 7834.04 | 803 / 803 | 0% | 0 | 0 / 0 |
spleen | 100% | 4789.66 | 241 / 241 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 100% | 30.27 | 45 / 45 |
ureter | 0% | 0 | 0 / 0 | 100% | 13.62 | 1 / 1 |
adipose | 100% | 6949.87 | 1203 / 1204 | 0% | 0 | 0 / 0 |
heart | 98% | 6381.83 | 844 / 861 | 0% | 0 | 0 / 0 |
peripheral blood | 86% | 4862.90 | 795 / 929 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 64% | 13.80 | 51 / 80 |
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_0030036 | Biological process | actin cytoskeleton organization |
GO_0051016 | Biological process | barbed-end actin filament capping |
GO_0065003 | Biological process | protein-containing complex assembly |
GO_0008290 | Cellular component | F-actin capping protein complex |
GO_0005903 | Cellular component | brush border |
GO_0030863 | Cellular component | cortical cytoskeleton |
GO_0015629 | Cellular component | actin cytoskeleton |
GO_0070062 | Cellular component | extracellular exosome |
GO_0005829 | Cellular component | cytosol |
GO_0005576 | Cellular component | extracellular region |
GO_0016020 | Cellular component | membrane |
GO_0051015 | Molecular function | actin filament binding |
GO_0005515 | Molecular function | protein binding |
Gene name | CAPZA2 |
Protein name | Capping actin protein of muscle Z-line subunit alpha 2 F-actin-capping protein subunit alpha-2 (CapZ alpha-2) F-actin-capping protein subunit alpha |
Synonyms | hCG_37884 tcag7.31 |
Description | FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. . FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. . FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. . |
Accessions | ENST00000484325.1 ENST00000449080.5 P47755 ENST00000490693.5 C9JUG7 ENST00000361183.8 [P47755-1] ENST00000464223.5 C9JCZ4 A4D0V4 ENST00000426421.5 F8W9N7 F8WED3 C9J7V0 |