AMP deaminase 2

AMPD2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAMPD2, PCH9, SPG63, adenosine monophosphate deaminase 2
External IDsMGI: 88016 HomoloGene: 2979 GeneCards: AMPD2
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1p13.3Start109,616,104 bp[1]
End109,632,051 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

271

109674

Ensembl

ENSG00000116337

ENSMUSG00000027889

UniProt

Q01433

Q9DBT5

RefSeq (mRNA)

NM_001289719
NM_001289720
NM_028779
NM_001346665

RefSeq (protein)

NP_001276648
NP_001276649
NP_001333594
NP_083055

Location (UCSC)Chr 1: 109.62 – 109.63 MbChr 3: 108.07 – 108.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. 1 2 3 GRCh38: Ensembl release 89: ENSG00000116337 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027889 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. 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. doi:10.1002/ijc.31903. PMID 30267407.

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.


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