AMP deaminase 2

Adenosine monophosphate deaminase 2
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4NO3​, 4NO5​
Identifiers
Symbols	AMPD2 ; PCH9; SPG63
External IDs	OMIM: 102771 MGI: 88016 HomoloGene: 2979 ChEMBL: 2997 GeneCards: AMPD2 Gene
EC number	3.5.4.6
Gene ontology Molecular function • AMP deaminase activity • protein binding • metal ion binding Cellular component • cellular_component • cytosol Biological process • purine nucleobase metabolic process • IMP biosynthetic process • IMP salvage • purine-containing compound salvage • small molecule metabolic process • AMP metabolic process • ATP metabolic process • GTP metabolic process • cyclic purine nucleotide metabolic process • nucleobase-containing small molecule metabolic process • energy homeostasis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	271	109674
Ensembl	ENSG00000116337	ENSMUSG00000027889
UniProt	Q01433	Q9DBT5
RefSeq (mRNA)	NM_001257360	NM_001289719
RefSeq (protein)	NP_001244289	NP_001276648
Location (UCSC)	Chr 1: 109.62 – 109.63 Mb	Chr 3: 108.07 – 108.09 Mb
PubMed search

AMP deaminase 2 is an enzyme that in humans is encoded by the AMPD2 gene.^[1][2]

References

1. Mahnke-Zizelman DK, Sabina RL (Nov 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". J Biol Chem 267 (29): 20866–77. PMID 1400401.
2. "Entrez Gene: AMPD2 adenosine monophosphate deaminase 2 (isoform L)".

Further reading

• Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL (1992). "Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA.". J. Biol. Chem. 267 (31): 22407–13. PMID 1429593.
• Van den Bergh F, Sabina RL (1996). "Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L". Biochem. J. 312 ( Pt 2) (Pt 2): 401–10. PMC 1136276. PMID 8526848.
• Mahnke-Zizelman DK, van den Bergh F, Bausch-Jurken MT; et al. (1996). "Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters". Biochim. Biophys. Acta 1308 (2): 122–32. doi:10.1016/0167-4781(96)00089-9. PMID 8764830.
• Haas AL, Sabina RL (2003). "N-terminal extensions of the human AMPD2 polypeptide influence ATP regulation of isoform L". Biochem. Biophys. Res. Commun. 305 (2): 421–7. doi:10.1016/S0006-291X(03)00787-3. PMID 12745092.
• Beausoleil SA, Villén J, Gerber SA; et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.