AMP deaminase 2

AMPD2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4NO3, 4NO5
Identifiers
Aliases	AMPD2, PCH9, SPG63, adenosine monophosphate deaminase 2
External IDs	MGI: 88016 HomoloGene: 2979 GeneCards: AMPD2
Gene ontology Molecular function • hydrolase activity • metal ion binding • deaminase activity • protein binding • AMP deaminase activity Cellular component • cytosol • cellular component Biological process • purine ribonucleoside monophosphate biosynthetic process • GTP metabolic process • ATP metabolic process • IMP salvage • cyclic purine nucleotide metabolic process • nucleotide metabolic process • AMP metabolic process • purine-containing compound salvage • energy homeostasis • IMP biosynthetic process • cholesterol homeostasis • glomerular visceral epithelial cell development 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_001257361 NM_001308170 NM_004037 NM_139156 NM_203404	NM_001289719 NM_001289720 NM_028779
RefSeq (protein)	NP_001244289.1 NP_001244290.1 NP_001295099.1 NP_004028.3 NP_631895.1 NP_981949.1 NP_001244289.1 NP_004028.3	NP_001276648.1 NP_001276649.1 NP_083055.1
Location (UCSC)	Chr 1: 109.62 – 109.63 Mb	Chr 3: 108.07 – 108.09 Mb
PubMed search	[1]	[2]
Wikidata

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AMP deaminase 2 is an enzyme that in humans is encoded by the AMPD2 gene.^[3][4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "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): 401–10. doi:10.1042/bj3120401. 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.