Tag | Content |
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CPLM ID | CPLM-022916 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA dC->dU-editing enzyme APOBEC-3B |
Protein Synonyms/Alias | A3B; Phorbolin-1-related protein; Phorbolin-2/3 |
Gene Name | APOBEC3B |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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320 | YDYDPLYKEALQMLR | ubiquitination | [1] |
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Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. 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 against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T- cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. |
Sequence Annotation | DOMAIN 66 100 CMP/dCMP deaminase zinc-binding 1. DOMAIN 253 289 CMP/dCMP deaminase zinc-binding 2. ACT_SITE 255 255 Proton donor (Potential). METAL 66 66 Zinc (By similarity). METAL 97 97 Zinc (By similarity). METAL 100 100 Zinc (By similarity). METAL 253 253 Zinc (By similarity). METAL 284 284 Zinc (By similarity). METAL 289 289 Zinc (By similarity). |
Keyword | Alternative splicing; Antiviral defense; Complete proteome; Hydrolase; Immunity; Innate immunity; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; RNA-binding; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 382 AA |
Protein Sequence | MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGQVY 60 FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC VAKLAEFLSE HPNVTLTISA 120 ARLYYYWERD YRRALCRLSQ AGARVTIMDY EEFAYCWENF VYNEGQQFMP WYKFDENYAF 180 LHRTLKEILR YLMDPDTFTF NFNNDPLVLR RRQTYLCYEV ERLDNGTWVL MDQHMGFLCN 240 EAKNLLCGFY GRHAELRFLD LVPSLQLDPA QIYRVTWFIS WSPCFSWGCA GEVRAFLQEN 300 THVRLRIFAA RIYDYDPLYK EALQMLRDAG AQVSIMTYDE FEYCWDTFVY RQGCPFQPWD 360 GLEEHSQALS GRLRAILQNQ GN 382 |
Gene Ontology | GO:0005634; C:nucleus; IDA:UniProtKB. GO:0047844; F:deoxycytidine deaminase activity; IMP:UniProtKB. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0051607; P:defense response to virus; IDA:UniProtKB. GO:0045087; P:innate immune response; IEA:UniProtKB-KW. GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. |
Interpro | |
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