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; OMA:AMPD2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p13.3 Start 109,616,104 bp [1] End 109,632,051 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3 F2.3|3 46.83 cM Start 107,981,378 bp [2] End 107,993,967 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in anterior pituitary granulocyte nucleus accumbens pancreatic ductal cell stromal cell of endometrium right frontal lobe monocyte putamen caudate nucleus blood Top expressed in fossa arcuate nucleus ventromedial nucleus condyle mammillary body motor neuron internal carotid artery Rostral migratory stream external carotid artery lateral 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

AMP deaminase 2 is an enzyme that in humans is encoded by the AMPD2 gene. ^{[5] [6]}

High AMPD2 expression levels correlate with poor patient outcome and a proliferative tumor phenotype in undifferentiated pleomorphic sarcoma (UPS). ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000116337 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027889 – 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.
5. 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. doi: 10.1016/S0021-9258(19)36768-7 . PMID   1400401.
6. "Entrez Gene: AMPD2 adenosine monophosphate deaminase 2 (isoform L)".
7. Orth MF, Gerke JS, Knösel T, Altendorf-Hofmann A, Musa J, Alba-Rubio R, et al. (September 2018). "Functional genomics identifies AMPD2 as a new prognostic marker for undifferentiated pleomorphic sarcoma". International Journal of Cancer. 144 (4): 859–867. doi: 10.1002/ijc.31903 . PMID   30267407.

External links

• Human AMPD2 genome location and AMPD2 gene details page in the UCSC Genome Browser .

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. doi: 10.1016/S0021-9258(18)41686-9 . 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. S2CID   14294292.
• 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. S2CID   7827573.