Tissue | GTEx Coverage  | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
|---|---|---|---|---|---|---|
| breast | 100% | 3642.15 | 459 / 459 | 100% | 133.91 | 1118 / 1118 |
| esophagus | 100% | 2489.58 | 1445 / 1445 | 100% | 78.74 | 183 / 183 |
| lung | 100% | 4039.32 | 578 / 578 | 100% | 130.70 | 1155 / 1155 |
| pancreas | 100% | 4123.52 | 328 / 328 | 100% | 104.81 | 178 / 178 |
| prostate | 100% | 3721.98 | 245 / 245 | 100% | 163.16 | 502 / 502 |
| ovary | 100% | 3332.07 | 180 / 180 | 100% | 71.05 | 429 / 430 |
| thymus | 100% | 4367.17 | 653 / 653 | 100% | 126.73 | 603 / 605 |
| stomach | 100% | 2822.67 | 359 / 359 | 100% | 86.63 | 285 / 286 |
| intestine | 100% | 3000.47 | 966 / 966 | 100% | 91.66 | 525 / 527 |
| brain | 99% | 2912.77 | 2626 / 2642 | 100% | 100.58 | 705 / 705 |
| uterus | 100% | 3707.43 | 170 / 170 | 99% | 79.60 | 456 / 459 |
| bladder | 100% | 3061.52 | 21 / 21 | 99% | 88.33 | 500 / 504 |
| liver | 100% | 2024.82 | 226 / 226 | 99% | 65.76 | 402 / 406 |
| kidney | 100% | 2391.96 | 89 / 89 | 99% | 83.47 | 890 / 901 |
| adrenal gland | 100% | 4358.47 | 258 / 258 | 98% | 137.24 | 225 / 230 |
| skin | 100% | 3190.83 | 1807 / 1809 | 96% | 95.09 | 452 / 472 |
| adipose | 100% | 3487.43 | 1204 / 1204 | 0% | 0 | 0 / 0 |
| blood vessel | 100% | 5136.43 | 1335 / 1335 | 0% | 0 | 0 / 0 |
| lymph node | 0% | 0 | 0 / 0 | 100% | 50.63 | 29 / 29 |
| spleen | 100% | 3346.37 | 241 / 241 | 0% | 0 | 0 / 0 |
| tonsil | 0% | 0 | 0 / 0 | 100% | 61.76 | 45 / 45 |
| ureter | 0% | 0 | 0 / 0 | 100% | 42.41 | 1 / 1 |
| muscle | 100% | 2050.44 | 801 / 803 | 0% | 0 | 0 / 0 |
| heart | 98% | 2493.36 | 845 / 861 | 0% | 0 | 0 / 0 |
| eye | 0% | 0 | 0 / 0 | 66% | 29.29 | 53 / 80 |
| peripheral blood | 57% | 1078.99 | 534 / 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_0030968 | Biological process | endoplasmic reticulum unfolded protein response |
| GO_1904153 | Biological process | negative regulation of retrograde protein transport, ER to cytosol |
| GO_0030970 | Biological process | retrograde protein transport, ER to cytosol |
| GO_0036503 | Biological process | ERAD pathway |
| GO_0005788 | Cellular component | endoplasmic reticulum lumen |
| GO_0044322 | Cellular component | endoplasmic reticulum quality control compartment |
| GO_0005515 | Molecular function | protein binding |
| GO_0051082 | Molecular function | unfolded protein binding |
| Gene name | ERLEC1 |
| Protein name | Endoplasmic reticulum lectin 1 (ER lectin) (Erlectin) (XTP3-transactivated gene B protein) Endoplasmic reticulum lectin 1 Endoplasmic reticulum lectin |
| Synonyms | UNQ1878/PRO4321 C2orf30 XTP3TPB |
| Description | FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. .; FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. . |
| Accessions | ENST00000692745.1 A0A8I5KU57 ENST00000690836.1 A0A8I5KSC7 ENST00000688147.1 ENST00000688464.1 A0A8I5KVG1 A0A8I5KVT1 A0A8I5KQC1 ENST00000687552.1 ENST00000689106.1 ENST00000689291.1 A0A8I5KTD9 A0A8I5KTC7 ENST00000689943.1 A0A8I5KY03 A0A8I5KYX4 ENST00000692971.1 ENST00000684875.1 ENST00000405123.7 [Q96DZ1-3] ENST00000685400.1 A0A8I5KUG7 A0A8I5KWA3 ENST00000693696.1 A0A8I5KWJ1 ENST00000185150.9 [Q96DZ1-1] ENST00000686424.1 ENST00000689496.1 ENST00000692786.1 A0A8I5KYU6 A0A8I5KV23 A0A8I5KU16 A0A8I5KTW2 ENST00000691939.1 ENST00000690740.1 ENST00000690280.1 A0A8I5KXM1 A0A8I5KXV7 A0A8I5KRL2 ENST00000691217.1 ENST00000692350.1 A0A8I5KS40 ENST00000378239.5 [Q96DZ1-2] A0A8I5KR40 ENST00000687723.1 A0A8I5KUW0 ENST00000688274.1 ENST00000691853.1 ENST00000691171.1 ENST00000689100.1 A0A8I5KXY6 Q96DZ1 |
