DNPEP

Aspartyl aminopeptidase
Identifiers
Symbols	DNPEP; ASPEP; DAP
External IDs	OMIM: 611367 MGI: 1278328 HomoloGene: 6110 GeneCards: DNPEP Gene
EC number	3.4.11.21
Gene Ontology Molecular function • aminopeptidase activity • protein binding • peptidase activity • metallopeptidase activity • zinc ion binding • metal ion binding Cellular component • cytoplasm Biological process • proteolysis • peptide metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23549	13437
Ensembl	ENSG00000123992	ENSMUSG00000026209
UniProt	Q9ULA0	Q3TVK3
RefSeq (mRNA)	NM_012100	NM_016878
RefSeq (protein)	NP_036232	NP_058574
Location (UCSC)	Chr 2: 220.24 – 220.59 Mb	Chr 1: 75.3 – 75.31 Mb
PubMed search	[1]	[2]

Aspartyl aminopeptidase is an enzyme that in humans is encoded by the DNPEP gene.^[1][2]

The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins.^[2]

References

1. ^ Wilk S, Wilk E, Magnusson RP (Aug 1998). "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase". J Biol Chem 273 (26): 15961–70. doi:10.1074/jbc.273.26.15961. PMID 9632644. 
2. ^ ^{a b} "Entrez Gene: DNPEP aspartyl aminopeptidase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23549. 

Further reading

• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Prieto I, Hermoso F, Gasparo M, et al. (2004). "Angiotensinase activities in the kidney of renovascular hypertensive rats.". Peptides 24 (5): 755–60. doi:10.1016/S0196-9781(03)00121-9. PMID 12895663. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Wilk S, Wilk E, Magnusson RP (2002). "Identification of histidine residues important in the catalysis and structure of aspartyl aminopeptidase.". Arch. Biochem. Biophys. 407 (2): 176–83. doi:10.1016/S0003-9861(02)00494-0. PMID 12413488. 

External Links

• The MEROPS online database for peptidases and their inhibitors: M18.002