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	OMIM: 102771 MGI: 88016 HomoloGene: 2979 GeneCards: AMPD2
Gene location (Human) Chr. Chromosome 1 (human) Band 1p13.3 Start 109,616,104 bp End 109,632,051 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 F2.3|3 46.83 cM Start 107,981,378 bp End 107,993,967 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in anterior pituitary nucleus accumbens pancreatic ductal cell stromal cell of endometrium monocyte putamen caudate nucleus blood spleen prefrontal cortex Top expressed in fossa arcuate nucleus ventromedial nucleus condyle mammillary body motor neuron internal carotid artery external carotid artery lateral hypothalamus paraventricular nucleus of hypothalamus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function hydrolase activity metal ion binding deaminase activity protein binding AMP deaminase activity Cellular component cellular component cytosol Biological process purine ribonucleoside monophosphate biosynthetic process IMP salvage cyclic purine nucleotide metabolic process nucleotide metabolic process purine-containing compound salvage IMP biosynthetic process energy homeostasis AMP metabolic process Sources:Amigo / QuickGO
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_001368809 NM_001289719 NM_001289720 NM_028779 NM_001346665 RefSeq (protein) NP_001244289 NP_001244290 NP_001295099 NP_004028 NP_631895 NP_001355738 NP_001276648 NP_001276649 NP_001333594 NP_083055 Location (UCSC) Chr 1: 109.62 – 109.63 Mb Chr 3: 107.98 – 107.99 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

AMP deaminase 2 is an enzyme that in humans is encoded by the AMPD2 gene.

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.