ABC3F_HUMAN - dbPTM
ABC3F_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABC3F_HUMAN
UniProt AC Q8IUX4
Protein Name DNA dC->dU-editing enzyme APOBEC-3F
Gene Name APOBEC3F
Organism Homo sapiens (Human).
Sequence Length 373
Subcellular Localization Cytoplasm. Cytoplasm, P-body.
Protein Description DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits 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 hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation..
Protein Sequence MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRSLSQEGASVEIMGYKDFKYCWENFVYNDDEPFKPWKGLKYNFLFLDSKLQEILE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
32PhosphorylationPILSRRNTVWLCYEV
CCCCCCCEEEEEEEE
15.9625159151
136MethylationDYRRALCRLSQAGAR
HHHHHHHHHHHCCCE
37.92-
138PhosphorylationRRALCRLSQAGARVK
HHHHHHHHHCCCEEE
9.9122210691
161PhosphorylationYCWENFVYSEGQPFM
HHHHHEEEECCCCCC
9.2522210691
162PhosphorylationCWENFVYSEGQPFMP
HHHHEEEECCCCCCC
29.9222210691
171PhosphorylationGQPFMPWYKFDDNYA
CCCCCCCEECCCCHH
8.9122210691
177PhosphorylationWYKFDDNYAFLHRTL
CEECCCCHHHHHHHH
13.01-
216PhosphorylationKAYGRNESWLCFTME
HHHCCCCCEEEEEEE
28.97-
295PhosphorylationAEFLARHSNVNLTIF
HHHHHHCCCCEEEEE
36.6030108239
300PhosphorylationRHSNVNLTIFTARLY
HCCCCEEEEEEEEEH
14.6130108239
307PhosphorylationTIFTARLYYFWDTDY
EEEEEEEHHEECCCH
7.3424043423
308PhosphorylationIFTARLYYFWDTDYQ
EEEEEEHHEECCCHH
11.6424043423
312PhosphorylationRLYYFWDTDYQEGLR
EEHHEECCCHHHHHH
27.4824043423
314PhosphorylationYYFWDTDYQEGLRSL
HHEECCCHHHHHHHH
15.5724043423
352AcetylationYNDDEPFKPWKGLKY
CCCCCCCCCCCCCEE
61.7626051181

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligasevifP69720
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABC3F_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 ABC3F_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VIF_HV1B1vifphysical
19109396
VIF_HV1BRvifphysical
19109396
VIF_HV1H2vifphysical
19109396
VIF_HV1B1vifphysical
18619467
VIF_HV1BRvifphysical
18619467
VIF_HV1H2vifphysical
18619467
VIF_HV1B1vifphysical
19088851
VIF_HV1BRvifphysical
19088851
VIF_HV1H2vifphysical
19088851
VIF_HV1B1vifphysical
20592083
VIF_HV1BRvifphysical
20592083
VIF_HV1H2vifphysical
20592083
VIF_HV1B1vifphysical
19535447
VIF_HV1BRvifphysical
19535447
VIF_HV1H2vifphysical
19535447

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABC3F_HUMAN

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Related Literatures of Post-Translational Modification

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