DNPEP

DNPEP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4DYO
Identifiers
Aliases	DNPEP , ASPEP, DAP, aspartyl aminopeptidase
External IDs	OMIM: 611367 MGI: 1278328 HomoloGene: 6110 GeneCards: DNPEP
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2q35 Start 219,372,043 bp [1] End 219,400,022 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 C4 Start 75,284,540 bp [2] End 75,294,634 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in canal of the cervix gastric mucosa left uterine tube upper lobe of left lung skin of abdomen gastrocnemius muscle right lung body of stomach right coronary artery sperm Top expressed in intestinal villus internal carotid artery external carotid artery aortic valve ascending aorta endocardial cushion Paneth cell atrium seminiferous tubule superior cervical ganglion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity zinc ion binding aminopeptidase activity protein binding hydrolase activity metallopeptidase activity metal ion binding metalloaminopeptidase activity identical protein binding Cellular component blood microparticle nucleus cytosol cytoplasm extracellular region Biological process proteolysis peptide metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23549 13437 Ensembl ENSG00000123992 ENSMUSG00000026209 UniProt Q9ULA0 Q9Z2W0 RefSeq (mRNA) NM_012100 NM_001319116 NM_001319117 NM_001319118 NM_001319119 NM_001319120 NM_001319121 NM_001319122 NM_001110831 NM_016878 RefSeq (protein) NP_001306045 NP_001306046 NP_001306047 NP_001306048 NP_001306049 NP_001306050 NP_001306051 NP_036232 NP_001306050.1 NP_001306051.1 NP_001104301 NP_058574 Location (UCSC) Chr 2: 219.37 – 219.4 Mb Chr 1: 75.28 – 75.29 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Aspartyl aminopeptidase is an enzyme that in humans is encoded by the DNPEP gene. ^{[5] [6]}

Function

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 the general metabolism of intracellular proteins. ^[6]

See also

•   Biologyportal

References

1. GRCh38: Ensembl release 89: ENSG00000123992 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026209 - 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. Wilk S, Wilk E, Magnusson RP (Jun 1998). "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase". The Journal of Biological Chemistry. 273 (26): 15961–70. doi: 10.1074/jbc.273.26.15961 . PMID   9632644.
6. "Entrez Gene: DNPEP aspartyl aminopeptidase".

Further reading

• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Prieto I, Hermoso F, de Gasparo M, Vargas F, Alba F, Segarra AB, Banegas I, Ramírez M (May 2003). "Angiotensinase activities in the kidney of renovascular hypertensive rats". Peptides. 24 (5): 755–60. CiteSeerX   10.1.1.379.1582 . doi:10.1016/S0196-9781(03)00121-9. PMID   12895663. S2CID   16379232.
• Wilk S, Wilk E, Magnusson RP (Nov 2002). "Identification of histidine residues important in the catalysis and structure of aspartyl aminopeptidase". Archives of Biochemistry and Biophysics. 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
• PDBe-KB provides an overview of all the structure information available in the PDB for Human Aspartyl aminopeptidase (DNPEP)