| UniProt ID | ABC3G_HUMAN | |
|---|---|---|
| UniProt AC | Q9HC16 | |
| Protein Name | DNA dC->dU-editing enzyme APOBEC-3G | |
| Gene Name | APOBEC3G | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 384 | |
| Subcellular Localization | Cytoplasm. Nucleus. Cytoplasm, P-body. Mainly cytoplasmic. Small amount are found in the nucleus. During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF. | |
| Protein Description | 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.. | |
| Protein Sequence | MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 32 | Phosphorylation | PILSRRNTVWLCYEV CCCCCCCEEEEEEEE | 15.96 | 25159151 | |
| 63 | Ubiquitination | GQVYSELKYHPEMRF CCHHHHHCCCCHHHH | 37.14 | 21890473 | |
| 63 (in isoform 1) | Ubiquitination | - | 37.14 | 21890473 | |
| 181 | Phosphorylation | PWNNLPKYYILLHIM CCCCCCHHHHHHHHH | 8.19 | - | |
| 182 | Phosphorylation | WNNLPKYYILLHIML CCCCCHHHHHHHHHH | 7.39 | - | |
| 218 | Phosphorylation | WVRGRHETYLCYEVE CCCCCCCEEEEEEEE | 18.70 | 21123384 | |
| 219 | Phosphorylation | VRGRHETYLCYEVER CCCCCCEEEEEEEEE | 7.56 | - | |
| 249 | Ubiquitination | LCNQAPHKHGFLEGR CCCCCCCCCCCCCCC | 44.35 | - | |
| 297 | Ubiquitination | SCAQEMAKFISKNKH HHHHHHHHHHHCCCC | 41.75 | 19887642 | |
| 301 | Ubiquitination | EMAKFISKNKHVSLC HHHHHHHCCCCEEEE | 66.26 | 19887642 | |
| 303 | Ubiquitination | AKFISKNKHVSLCIF HHHHHCCCCEEEEEE | 49.47 | 19887642 | |
| 334 | Ubiquitination | TLAEAGAKISIMTYS HHHHHCCEEEEEEHH | 35.75 | 1988764 | |
| 340 | Phosphorylation | AKISIMTYSEFKHCW CEEEEEEHHHCHHHH | 6.71 | 29759185 | |
| 349 | Phosphorylation | EFKHCWDTFVDHQGC HCHHHHHHHCCCCCC | 10.89 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 32 | T | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
| 32 | T | Phosphorylation | Kinase | PKA | - | Uniprot |
| 218 | T | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
| 218 | T | Phosphorylation | Kinase | CAMK2A | P11275 | PSP |
| 218 | T | Phosphorylation | Kinase | PKA | - | Uniprot |
| 218 | T | Phosphorylation | Kinase | CAMK2 | - | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:15581898 |
| - | K | Ubiquitination | E3 ubiquitin ligase | CUL5 | Q93034 | PMID:31253590 |
| - | K | Ubiquitination | E3 ubiquitin ligase | ARIH2 | O95376 | PMID:31253590 |
| - | K | Ubiquitination | E3 ubiquitin ligase | vif | P69720 | PMID:22199232 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ABC3G_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
