Name | Number of supported studies | Average coverage | |
---|---|---|---|
peripheral blood | 12 studies | 23% ± 5% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
thymus | 99% | 415.17 | 647 / 653 | 95% | 14.16 | 577 / 605 |
ovary | 100% | 986.09 | 180 / 180 | 93% | 11.53 | 400 / 430 |
lung | 100% | 623.12 | 576 / 578 | 92% | 12.98 | 1060 / 1155 |
uterus | 100% | 610.58 | 170 / 170 | 89% | 13.94 | 409 / 459 |
bladder | 100% | 596.57 | 21 / 21 | 88% | 16.99 | 444 / 504 |
breast | 96% | 379.19 | 442 / 459 | 84% | 9.25 | 942 / 1118 |
kidney | 93% | 286.00 | 83 / 89 | 84% | 12.99 | 758 / 901 |
esophagus | 95% | 262.40 | 1368 / 1445 | 75% | 8.06 | 138 / 183 |
adrenal gland | 100% | 637.00 | 257 / 258 | 66% | 4.91 | 152 / 230 |
prostate | 100% | 627.56 | 245 / 245 | 58% | 3.72 | 293 / 502 |
stomach | 89% | 244.47 | 320 / 359 | 69% | 6.88 | 197 / 286 |
intestine | 99% | 482.34 | 958 / 966 | 59% | 5.01 | 310 / 527 |
skin | 67% | 185.04 | 1221 / 1809 | 83% | 15.80 | 394 / 472 |
pancreas | 29% | 48.36 | 94 / 328 | 90% | 9.76 | 160 / 178 |
lymph node | 0% | 0 | 0 / 0 | 100% | 51.97 | 29 / 29 |
peripheral blood | 100% | 2901.33 | 929 / 929 | 0% | 0 | 0 / 0 |
spleen | 100% | 2202.67 | 241 / 241 | 0% | 0 | 0 / 0 |
ureter | 0% | 0 | 0 / 0 | 100% | 3.10 | 1 / 1 |
adipose | 98% | 370.45 | 1180 / 1204 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 98% | 25.35 | 44 / 45 |
brain | 51% | 97.24 | 1337 / 2642 | 46% | 4.11 | 324 / 705 |
liver | 60% | 101.17 | 136 / 226 | 35% | 2.85 | 144 / 406 |
blood vessel | 85% | 233.81 | 1138 / 1335 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 84% | 7.73 | 67 / 80 |
heart | 72% | 140.67 | 622 / 861 | 0% | 0 | 0 / 0 |
muscle | 6% | 8.13 | 49 / 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_0045869 | Biological process | negative regulation of single stranded viral RNA replication via double stranded DNA intermediate |
GO_0045071 | Biological process | negative regulation of viral genome replication |
GO_0016553 | Biological process | base conversion or substitution editing |
GO_0045087 | Biological process | innate immune response |
GO_0051607 | Biological process | defense response to virus |
GO_0070383 | Biological process | DNA cytosine deamination |
GO_0009972 | Biological process | cytidine deamination |
GO_0010526 | Biological process | retrotransposon silencing |
GO_0016554 | Biological process | cytidine to uridine editing |
GO_0048525 | Biological process | negative regulation of viral process |
GO_0002230 | Biological process | positive regulation of defense response to virus by host |
GO_0030895 | Cellular component | apolipoprotein B mRNA editing enzyme complex |
GO_0000932 | Cellular component | P-body |
GO_0005829 | Cellular component | cytosol |
GO_0005737 | Cellular component | cytoplasm |
GO_1990904 | Cellular component | ribonucleoprotein complex |
GO_0005634 | Cellular component | nucleus |
GO_0008829 | Molecular function | dCTP deaminase activity |
GO_0042802 | Molecular function | identical protein binding |
GO_0004126 | Molecular function | cytidine deaminase activity |
GO_0008270 | Molecular function | zinc ion binding |
GO_0003723 | Molecular function | RNA binding |
GO_0005515 | Molecular function | protein binding |
Gene name | APOBEC3G |
Protein name | Apolipoprotein B mRNA editing enzyme DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.-) (Deoxycytidine deaminase) DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.38) (APOBEC-related cytidine deaminase) (APOBEC-related protein) (ARCD) (APOBEC-related protein 9) (ARP-9) (CEM-15) (CEM15) (Deoxycytidine deaminase) (A3G) |
Synonyms | MDS019 |
Description | FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against Vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons. . FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. . FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. . |
Accessions | F2YHL6 Q9HC16 ENST00000407997.4 [Q9HC16-1] M4VSD8 B2LYL6 |