Name | Number of supported studies | Average coverage | |
|---|---|---|---|
| peripheral blood | 20 studies | 64% ± 15% | |
| lung | 18 studies | 66% ± 19% | |
| intestine | 13 studies | 51% ± 27% | |
| kidney | 9 studies | 61% ± 20% | |
| eye | 9 studies | 51% ± 20% | |
| brain | 9 studies | 38% ± 14% | |
| bone marrow | 6 studies | 48% ± 22% | |
| lymph node | 6 studies | 70% ± 14% | |
| liver | 6 studies | 50% ± 23% | |
| pancreas | 5 studies | 66% ± 24% | |
| uterus | 5 studies | 69% ± 24% | |
| prostate | 4 studies | 61% ± 25% | |
| breast | 4 studies | 76% ± 6% | |
| placenta | 3 studies | 64% ± 30% | |
| heart | 3 studies | 31% ± 15% | |
| adrenal gland | 3 studies | 55% ± 21% | |
| esophagus | 3 studies | 63% ± 30% | |
| skin | 3 studies | 56% ± 23% | |
| thymus | 3 studies | 73% ± 29% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
|---|---|---|---|---|---|---|
| bladder | 100% | 5521.52 | 21 / 21 | 100% | 144.75 | 504 / 504 |
| brain | 100% | 5960.18 | 2642 / 2642 | 100% | 135.07 | 705 / 705 |
| esophagus | 100% | 5710.29 | 1445 / 1445 | 100% | 130.25 | 183 / 183 |
| lung | 100% | 5638.83 | 578 / 578 | 100% | 142.69 | 1155 / 1155 |
| ovary | 100% | 6831.16 | 180 / 180 | 100% | 164.09 | 430 / 430 |
| prostate | 100% | 5609.76 | 245 / 245 | 100% | 120.27 | 502 / 502 |
| uterus | 100% | 6641.14 | 170 / 170 | 100% | 179.13 | 459 / 459 |
| thymus | 100% | 5296.51 | 653 / 653 | 100% | 141.93 | 604 / 605 |
| breast | 100% | 5931.82 | 459 / 459 | 100% | 155.14 | 1116 / 1118 |
| stomach | 100% | 4182.86 | 359 / 359 | 100% | 104.64 | 285 / 286 |
| intestine | 100% | 5408.52 | 966 / 966 | 100% | 104.31 | 525 / 527 |
| skin | 100% | 5916.79 | 1809 / 1809 | 100% | 98.56 | 470 / 472 |
| kidney | 100% | 5214.03 | 89 / 89 | 99% | 96.83 | 895 / 901 |
| liver | 100% | 2113.04 | 226 / 226 | 99% | 74.54 | 403 / 406 |
| adrenal gland | 100% | 5358.34 | 258 / 258 | 99% | 94.31 | 228 / 230 |
| pancreas | 99% | 2750.40 | 326 / 328 | 99% | 112.59 | 177 / 178 |
| adipose | 100% | 5715.89 | 1204 / 1204 | 0% | 0 | 0 / 0 |
| blood vessel | 100% | 6252.79 | 1335 / 1335 | 0% | 0 | 0 / 0 |
| lymph node | 0% | 0 | 0 / 0 | 100% | 145.81 | 29 / 29 |
| spleen | 100% | 5001.13 | 241 / 241 | 0% | 0 | 0 / 0 |
| tonsil | 0% | 0 | 0 / 0 | 100% | 139.71 | 45 / 45 |
| ureter | 0% | 0 | 0 / 0 | 100% | 93.71 | 1 / 1 |
| muscle | 99% | 2846.87 | 798 / 803 | 0% | 0 | 0 / 0 |
| heart | 99% | 3271.18 | 853 / 861 | 0% | 0 | 0 / 0 |
| eye | 0% | 0 | 0 / 0 | 99% | 71.57 | 79 / 80 |
| peripheral blood | 98% | 4986.10 | 910 / 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_0032436 | Biological process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| GO_0016925 | Biological process | protein sumoylation |
| GO_0005654 | Cellular component | nucleoplasm |
| GO_0016605 | Cellular component | PML body |
| GO_0005634 | Cellular component | nucleus |
| GO_0031386 | Molecular function | protein tag activity |
| GO_0031625 | Molecular function | ubiquitin protein ligase binding |
| GO_0005515 | Molecular function | protein binding |
| GO_0044389 | Molecular function | ubiquitin-like protein ligase binding |
| GO_0003723 | Molecular function | RNA binding |
| Gene name | SUMO2 |
| Protein name | Small ubiquitin-related modifier 2 (SUMO-2) (HSMT3) (SMT3 homolog 2) (SUMO-3) (Sentrin-2) (Ubiquitin-like protein SMT3B) (Smt3B) Small ubiquitin like modifier 2 |
| Synonyms | SMT3H2 SMT3B |
| Description | FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451 . This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins . Plays a role in the regulation of sumoylation status of SETX . . |
| Accessions | J3KRH1 ENST00000420826.7 [P61956-1] ENST00000578238.2 P61956 ENST00000314523.7 [P61956-2] |