APOBEC2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2NYT

Identifiers

Aliases

APOBEC2, ARCD1, ARP1, apolipoprotein B mRNA editing enzyme catalytic subunit 2

External IDs

MGI: 1343178 HomoloGene: 4941 GeneCards: APOBEC2

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


10930


11811

Ensembl


ENSG00000124701


ENSMUSG00000040694

UniProt


Q9Y235


Q9WV35

RefSeq (mRNA)


NM_006789


NM_009694

RefSeq (protein)


NP_006780.1


NP_033824.1

Location (UCSC)

Chr 6: 41.05 – 41.06 Mb

Chr 17: 48.42 – 48.43 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Probable C->U-editing enzyme APOBEC-2 is a protein that in humans is encoded by the APOBEC2 gene.^[3]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Liao W, Hong SH, Chan BH, Rudolph FB, Clark SC, Chan L (Aug 1999). "APOBEC-2, a cardiac- and skeletal muscle-specific member of the cytidine deaminase supergene family". Biochem Biophys Res Commun. 260 (2): 398–404. doi:10.1006/bbrc.1999.0925. PMID 10403781.
↑ "Entrez Gene: APOBEC2 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2".

Wedekind JE, Dance GS, Sowden MP, Smith HC (2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.". Trends Genet. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
Lau PP, Zhu HJ, Baldini A, et al. (1994). "Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene". Proc. Natl. Acad. Sci. U.S.A. 91 (18): 8522–6. doi:10.1073/pnas.91.18.8522. PMC 44638. PMID 8078915.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Oka K, Kobayashi K, Sullivan M, et al. (1997). "Tissue-specific inhibition of apolipoprotein B mRNA editing in the liver by adenovirus-mediated transfer of a dominant negative mutant APOBEC-1 leads to increased low density lipoprotein in mice". J. Biol. Chem. 272 (3): 1456–60. doi:10.1074/jbc.272.3.1456. PMID 8999814.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Anant S, Mukhopadhyay D, Sankaranand V, et al. (2001). "ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing". Am. J. Physiol., Cell Physiol. 281 (6): C1904–16. PMID 11698249.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Prochnow C, Bransteitter R, Klein MG, et al. (2007). "The APOBEC-2 crystal structure and functional implications for the deaminase AID". Nature. 445 (7126): 447–51. doi:10.1038/nature05492. PMID 17187054.

PDB gallery

2nyt: The APOBEC2 Crystal Structure and Functional Implications for AID

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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APOBEC2

References

Further reading