APOBEC2

APOBEC2
Available structures
PDB	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	OMIM: 604797 MGI: 1343178 HomoloGene: 4941 GeneCards: APOBEC2
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
	biceps brachii; ; triceps brachii muscle; ; thoracic diaphragm; ; vastus lateralis muscle; ; deltoid muscle; ; gastrocnemius muscle; ; tibialis anterior muscle; ; right ventricle; ; left ventricle; ; body of tongue;
	Top expressed in
	quadriceps femoris muscle; ; zone of skin; ; esophagus; ; skeletal muscle tissue; ; heart; ; lip; ; epithelium of urethra; ; ejaculatory duct; ; seminal vesicula; ; proximal tubule;
	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
	10930
	11811
	ENSG00000124701
	ENSMUSG00000040694
	Q9Y235
	Q9WV35
	NM_006789
	NM_009694
	NP_006780
	NP_033824
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 14, 2022

Probable C->U-editing enzyme APOBEC-2 is a protein that in humans is encoded by the APOBEC2 gene.^[5]^[6]

Related Research Articles

Activation-induced cytidine deaminase, also known as AICDA, AID and single-stranded DNA cytosine deaminase, is a 24 kDa enzyme which in humans is encoded by the AICDA gene. It creates mutations in DNA by deamination of cytosine base, which turns it into uracil. In other words, it changes a C:G base pair into a U:G mismatch. The cell's DNA replication machinery recognizes the U as a T, and hence C:G is converted to a T:A base pair. During germinal center development of B lymphocytes, AID also generates other types of mutations, such as C:G to A:T. The mechanism by which these other mutations are created is not well understood. It is a member of the APOBEC family.

Apolipoprotein B (ApoB) is a protein that in humans is encoded by the APOB gene.

APOBEC3G is a human enzyme encoded by the APOBEC3G gene that belongs to the APOBEC superfamily of proteins. This family of proteins has been suggested to play an important role in innate anti-viral immunity. APOBEC3G belongs to the family of cytidine deaminases that catalyze the deamination of cytidine to uridine in the single stranded DNA substrate. The C-terminal domain of A3G renders catalytic activity, several NMR and crystal structures explain the substrate specificity and catalytic activity.

Missense mRNA is a messenger RNA bearing one or more mutated codons that yield polypeptides with an amino acid sequence different from the wild-type or naturally occurring polypeptide. Missense mRNA molecules are created when template DNA strands or the mRNA strands themselves undergo a missense mutation in which a protein coding sequence is mutated and an altered amino acid sequence is coded for.

Apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1 also known as C->U-editing enzyme APOBEC-1 is a protein that in humans is encoded by the APOBEC1 gene.

Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene.

DNA dC->dU-editing enzyme APOBEC-3F is a protein that in humans is encoded by the APOBEC3F gene.

CUGBP, Elav-like family member 2, also known as Etr-3 is a protein that in humans is encoded by the CELF2 gene.

APOBEC1 complementation factor is a protein that in humans is encoded by the A1CF gene.

DNA dC->dU-editing enzyme APOBEC-3C is a protein that in humans is encoded by the APOBEC3C gene.

Aquaporin-8 is a protein that in humans is encoded by the AQP8 gene.

<span class="mw-page-title-main">APOBEC3A</span>

Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A, also known as APOBEC3A, or A3A is a gene of the APOBEC3 family found in humans, non-human primates, and some other mammals. It is a single-domain DNA cytidine deaminase with antiviral effects. While other members of the family such as APOBEC3G are believed to act by editing ssDNA by removing an amino group from cytosine in DNA, introducing a cytosine to uracil change which can ultimately lead to a cytosine to thymine mutation, one study suggests that APOBEC3A can inhibit parvoviruses by another mechanism. The cellular function of APOBEC3A is likely to be the destruction of foreign DNA through extensive deamination of cytosine.Stenglein MD, Burns MB, Li M, Lengyel J, Harris RS. "APOBEC3 proteins mediate the clearance of foreign DNA from human cells". Nature Structural & Molecular Biology. 17 (2): 222–9. doi:10.1038/nsmb.1744. PMC 2921484. PMID 20062055.

Probable DNA dC->dU-editing enzyme APOBEC-3B is a protein that in humans is encoded by the APOBEC3B gene.

Probable DNA dC->dU-editing enzyme APOBEC-3D is a protein that in humans is encoded by the APOBEC3D gene.

Uridine-cytidine kinase-like 1 is an enzyme that in humans is encoded by the UCKL1 gene.

<span class="mw-page-title-main">APOBEC</span> Enzyme involved in messenger RNA editing

APOBEC is a family of evolutionarily conserved cytidine deaminases.

DNA dC->dU-editing enzyme APOBEC-3H, also known as Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3H or APOBEC-related protein 10, is a protein that in humans is encoded by the APOBEC3H gene.

C->U-editing enzyme APOBEC-4, also known as Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4, is a protein that in humans is encoded by the APOBEC4 gene. It is primarily expressed in testis and found in mammals, chicken, but not fishes.

In molecular biology, kataegis describes a pattern of localized hypermutations identified in some cancer genomes, in which a large number of highly patterned basepair mutations occur in a small region of DNA. The mutational clusters are usually several hundred basepairs long, alternating between a long range of C→T substitutional pattern and a long range of G→A substitutional pattern. This suggests that kataegis is carried out on only one of the two template strands of DNA during replication. Compared to other cancer-related mutations, such as chromothripsis, kataegis is more commonly seen; it is not an accumulative process but likely happens during one cycle of replication.

Nina Papavasiliou is an immunologist and Helmholtz Professor in the Division of Immune Diversity at the German Cancer Research Center in Heidelberg, Germany. She is also an Adjunct Professor at the Rockefeller University, where she was previously Associate Professor and head of the Laboratory of Lymphocyte Biology. She is best known for her work in the fields of DNA and RNA editing.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000124701 - Ensembl, May 2017
1 2 3 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. 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. 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. 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. S2CID 4394772.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000124701 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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. 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 Coenzyme 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)

APOBEC2

Contents

Related Research Articles

References

External links

Further reading