APOBEC3G
entrez
60489
canonical
uniprot
Q9HC16
canonical
ensembl
ENSG00000239713
resolver
ensp
ENSP00000385057
resolver
ensp
ENSP00000690192
resolver
genesymbol
APOBEC3G
resolver
hgnc
HGNC:17357
resolver
uniprot
B2RDR9
resolver
uniprot
Q45F02
resolver
uniprot
Q5TF77
resolver
uniprot
Q7Z2N1
resolver
uniprot
Q7Z2N4
resolver
uniprot
Q9H9H8
resolver
uniprot_entry
ABC3G_HUMAN
resolver
uniprot_sec
B2RDR9
resolver
uniprot_sec
Q45F02
resolver
uniprot_sec
Q5TF77
resolver
uniprot_sec
Q7Z2N1
resolver
uniprot_sec
Q7Z2N4
resolver
uniprot_sec
Q9H9H8
resolver
activity_regulation
ACTIVITY REGULATION: (Microbial infection) Antiviral activity is neutralized by the HIV-1 virion infectivity factor (Vif), that prevents its incorporation into progeny virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome (PubMed:21835787, PubMed:22190037, PubMed:36754086, PubMed:37419875). Can also be neutralized by simian immunodeficiency virus sooty mangabey monkey virus (SIV-sm) and chimpanzee immunodeficiency virus (SIV-cpz) Vif (PubMed:21835787). {ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:36754086, ECO:0000269|PubMed:37419875}.
uniprot
proteins
amino_acid_sequence
MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN
uniprot
proteins
ec_number
3.5.4.38
uniprot
proteins
function
FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms (PubMed:12808465, PubMed:16527742, PubMed:17121840, PubMed:18288108, PubMed:18849968, PubMed:19153609, PubMed:21123384, PubMed:22791714, PubMed:25542899). Exhibits potent antiviral activity against Vif-deficient HIV-1 (PubMed:12167863, PubMed:12859895, PubMed:14557625, PubMed:20219927, PubMed:21835787, PubMed:22807680, PubMed:22915799, PubMed:23097438, PubMed:23152537, PubMed:31397674). 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 (PubMed:12808465, PubMed:12808466, PubMed:12809610, PubMed:12970355, PubMed:14528300, PubMed:22807680). 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 (PubMed:12808465, PubMed:12808466, PubMed:12809610, PubMed:12970355, PubMed:14528300). Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (PubMed:12808465, PubMed:12809610, PubMed:12970355, PubMed:14528300). 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) (PubMed:15031497, PubMed:16378963, PubMed:18448976, PubMed:19458006, PubMed:20335265). May inhibit the mobility of LTR and non-LTR retrotransposons (PubMed:16527742). {ECO:0000269|PubMed:12167863, ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12809610, ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:14528300, ECO:0000269|PubMed:14557625, ECO:0000269|PubMed:15031497, ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:17121840, ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609, ECO:0000269|PubMed:19458006, ECO:0000269|PubMed:20219927, ECO:0000269|PubMed:20335265, ECO:0000269|PubMed:21123384, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22791714, ECO:0000269|PubMed:22807680, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:23152537, ECO:0000269|PubMed:25542899, ECO:0000269|PubMed:31397674, ECO:0000303|PubMed:18448976}.
uniprot
proteins
mass_dalton
46408
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="E->A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259."; /evidence="ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885"; MUTAGEN 67; /note="E->A: No effect on cytidine deaminase and antiviral activity."; /evidence="ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885"; MUTAGEN 67; /note="E->Q: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885"; MUTAGEN 74; /note="F->W: Remains sensitive to HIV-1 Vif and able to bind Vif."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 80; /note="L->D: Remains sensitive to HIV-1 Vif and able to bind Vif."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 81; /note="H->A: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466"; MUTAGEN 85; /note="E->Q: Does not decrease cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808466"; MUTAGEN 86; /note="Y->A: Remains sensitive to HIV-1 Vif and able to bind Vif."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 97; /note="C->A: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466"; MUTAGEN 100; /note="C->A,S: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355"; MUTAGEN 107; /note="F->K: Remains sensitive to HIV-1 Vif and able to bind Vif."; /evidence="ECO:0000269|PubMed:23001005"; MUTAGEN 128; /note="D->K: Resistant to HIV-1 Vif with complete loss of Vif-induced ubiquitination and degradation and Vif binding."; /evidence="ECO:0000269|PubMed:15054139, ECO:0000269|PubMed:23001005, ECO:0000269|PubMed:37419875"; MUTAGEN 210; /note="P->A,G: Nearly abolished catalytic efficiency of cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 213; /note="R->A: Slightly reduces enzyme activity."; /evidence="ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18849968"; MUTAGEN 213; /note="R->E: Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18849968"; MUTAGEN 215; /note="R->A,E: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18849968"; MUTAGEN 217; /note="E->K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247."; /evidence="ECO:0000269|PubMed:21123384"; MUTAGEN 218; /note="T->A: Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity."; /evidence="ECO:0000269|PubMed:21659520"; MUTAGEN 218; /note="T->E: Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity."; /evidence="ECO:0000269|PubMed:21659520"; MUTAGEN 221; /note="C->S: Does not decrease cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808466"; MUTAGEN 244; /note="N->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18849968"; MUTAGEN 245; /note="Q->A: Nearly abolished cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 247; /note="P->K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217."; /evidence="ECO:0000269|PubMed:21123384"; MUTAGEN 248; /note="H->A: Improved catalytic efficiency of cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 250; /note="H->A: Improved catalytic efficiency of cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 256; /note="R->A: Strongly reduced cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 257; /note="H->A: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466"; MUTAGEN 259; /note="E->A: Loss of cytidine deaminase activity and significant decrease in antiviral activity."; /evidence="ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885, ECO:0000269|PubMed:18288108"; MUTAGEN 259; /note="E->A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67."; /evidence="ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885, ECO:0000269|PubMed:18288108"; MUTAGEN 259; /note="E->Q: Decreases cytidine deaminase activity and antiviral activity."; /evidence="ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:17020885, ECO:0000269|PubMed:18288108"; MUTAGEN 264; /note="D->A: Nearly abolished cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 268; /note="F->A: Strongly reduced cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 285; /note="W->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:18849968"; MUTAGEN 288; /note="C->A: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466"; MUTAGEN 291; /note="C->A,S: Decreases cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:12970355"; MUTAGEN 297..303; /note="KFISKNK->RFISRNR: In 4KR mutant; decreased ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif; when associated with R-334."; /evidence="ECO:0000269|PubMed:19887642, ECO:0000269|PubMed:37419875"; MUTAGEN 313; /note="R->A,E: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18288108"; MUTAGEN 315; /note="Y->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:18849968"; MUTAGEN 320; /note="R->A: Slightly reduces enzyme activity."; /evidence="ECO:0000269|PubMed:18288108"; MUTAGEN 320; /note="R->E: Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:18288108"; MUTAGEN 323; /note="E->Q: Does not decrease cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:12808466"; MUTAGEN 334; /note="K->R: In 4KR mutant; decreased ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif; when associated with R-297--R-303."; /evidence="ECO:0000269|PubMed:19887642"; MUTAGEN 370; /note="D->A: Reduced catalytic efficiency of cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 374; /note="R->A: Reduced cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 376; /note="R->A: Strongly reduced cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899"; MUTAGEN 380; /note="Q->A: Strongly reduced cytidine deaminase activity."; /evidence="ECO:0000269|PubMed:25542899
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Following infection by HIV-1, ubiquitinated by a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, leading to its degradation (PubMed:14528300, PubMed:14528301, PubMed:19887642, PubMed:22190037, PubMed:23300442, PubMed:31253590, PubMed:36754086, PubMed:37419875). Deubiquitinated by USP49; leading to stabilization (PubMed:31397674). {ECO:0000269|PubMed:14528300, ECO:0000269|PubMed:14528301, ECO:0000269|PubMed:19887642, ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:23300442, ECO:0000269|PubMed:31253590, ECO:0000269|PubMed:31397674, ECO:0000269|PubMed:36754086, ECO:0000269|PubMed:37419875}.; PTM: Phosphorylation at Thr-32 reduces its binding to HIV-1 Vif and subsequent ubiquitination and degradation thus promoting its antiviral activity. {ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:21659520}.
uniprot
proteins
protein_family
Cytidine and deoxycytidylate deaminase family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
11863358
uniprot
proteins
pubmed
12167863
uniprot
proteins
pubmed
12683974
uniprot
proteins
pubmed
12808465
uniprot
proteins
pubmed
12808466
uniprot
proteins
pubmed
12809610
uniprot
proteins
pubmed
12859895
uniprot
proteins
pubmed
12970355
uniprot
proteins
pubmed
14527406
uniprot
proteins
pubmed
14528300
uniprot
proteins
pubmed
14528301
uniprot
proteins
pubmed
14557052
uniprot
proteins
pubmed
14557625
uniprot
proteins
pubmed
14565218
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15031497
uniprot
proteins
pubmed
15054139
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16378963
uniprot
proteins
pubmed
16418394
uniprot
proteins
pubmed
16527742
uniprot
proteins
pubmed
16699599
uniprot
proteins
pubmed
17020885
uniprot
proteins
pubmed
17121840
uniprot
proteins
pubmed
18288108
uniprot
proteins
pubmed
18304004
uniprot
proteins
pubmed
18448976
uniprot
proteins
pubmed
18667511
uniprot
proteins
pubmed
18836454
uniprot
proteins
pubmed
18842592
uniprot
proteins
pubmed
18849968
uniprot
proteins
pubmed
19008196
uniprot
proteins
pubmed
19153609
uniprot
proteins
pubmed
19458006
uniprot
proteins
pubmed
19887642
uniprot
proteins
pubmed
20219927
uniprot
proteins
pubmed
20308164
uniprot
proteins
pubmed
20335265
uniprot
proteins
pubmed
20510315
uniprot
proteins
pubmed
21123384
uniprot
proteins
pubmed
21239176
uniprot
proteins
pubmed
21489586
uniprot
proteins
pubmed
21659520
uniprot
proteins
pubmed
21835787
uniprot
proteins
pubmed
22001110
uniprot
proteins
pubmed
22181350
uniprot
proteins
pubmed
22190037
uniprot
proteins
pubmed
22301159
uniprot
proteins
pubmed
22546055
uniprot
proteins
pubmed
22787460
uniprot
proteins
pubmed
22791714
uniprot
proteins
pubmed
22807680
uniprot
proteins
pubmed
22912627
uniprot
proteins
pubmed
22915799
uniprot
proteins
pubmed
23001005
uniprot
proteins
pubmed
23097438
uniprot
proteins
pubmed
23152537
uniprot
proteins
pubmed
23300442
uniprot
proteins
pubmed
23318957
uniprot
proteins
pubmed
25542899
uniprot
proteins
pubmed
31253590
uniprot
proteins
pubmed
31397674
uniprot
proteins
pubmed
31792451
uniprot
proteins
pubmed
36754086
uniprot
proteins
pubmed
37419875
uniprot
proteins
sequence_length
384
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21659520, ECO:0000269|PubMed:21835787}. Nucleus {ECO:0000269|PubMed:18667511}. Cytoplasm, P-body {ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:22915799}. Note=Mainly cytoplasmic (PubMed:16527742, PubMed:16699599, PubMed:21835787). Small amount are found in the nucleus (PubMed:18667511). During HIV-1 infection, virion-encapsidated in absence of HIV-1 Vif (PubMed:12859895). {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21835787}.
uniprot
proteins