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APOBEC2
Identifiers
Aliases	APOBEC2, ARCD1, ARP1, apolipoprotein B mRNA editing enzyme catalytic subunit 2
External IDs	OMIM: 604797; MGI: 1343178; GeneCards: APOBEC2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2NYT
Enzyme activity
Gene location (Human)
Chr.	Chromosome 6 (human)
End	41,064,891 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	48,739,958 bp
RNA expression pattern
	Top expressed in
	Skeletal muscle tissue of rectus abdominis; ; biceps brachii; ; triceps brachii muscle; ; Skeletal muscle tissue of biceps brachii; ; muscle of thigh; ; glutes; ; thoracic diaphragm; ; vastus lateralis muscle; ; deltoid muscle; ; apex of heart;
	Top expressed in
	quadriceps femoris muscle; ; muscle of thigh; ; zone of skin; ; esophagus; ; skeletal muscle tissue; ; heart; ; lip; ; epithelium of urethra; ; ejaculatory duct; ; epithelium of male urethra;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; zinc ion binding; catalytic activity; hydrolase activity; metal ion binding; RNA binding; cytidine deaminase activity; identical protein binding;
Cellular component	nucleus; cytoplasm;
Biological process	DNA demethylation; mRNA processing; mRNA modification; cytidine deamination; cytidine to uridine editing;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	10930
	11811
	ENSG00000124701
	ENSMUSG00000040694
	Q9Y235
	Q9WV35
	NM_006789
	NM_009694
	NP_006780
	NP_033824
	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.^[5]^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000124701 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000040694 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1999BBRC..260..398L. doi:10.1006/bbrc.1999.0925. PMID 10403781.
^ "Entrez Gene: APOBEC2 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2".

External links

Human APOBEC2 genome location and APOBEC2 gene details page in the UCSC Genome Browser.

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. Bibcode:1994PNAS...91.8522L. 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. doi:10.1152/ajpcell.2001.281.6.C1904. PMID 11698249. S2CID 7343760.
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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2003Natur.425..805M. 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. Bibcode:2007Natur.445..447P. doi:10.1038/nature05492. PMID 17187054. S2CID 4394772.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000124701 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000040694 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10403781-5] 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. Bibcode:1999BBRC..260..398L. doi:10.1006/bbrc.1999.0925. PMID 10403781.

[entrez-6] "Entrez Gene: APOBEC2 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2".

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v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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APOBEC2

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