DNPEP

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

DNPEP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDNPEP, ASPEP, DAP, aspartyl aminopeptidase
External IDsOMIM: 611367 MGI: 1278328 HomoloGene: 6110 GeneCards: DNPEP
Gene location (Human)
Chr.Chromosome 2 (human)[1]
Band2q35Start219,373,527 bp[1]
End219,400,022 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

23549

13437

Ensembl

ENSG00000123992

ENSMUSG00000026209

UniProt

Q9ULA0

Q9Z2W0

RefSeq (mRNA)

NM_001110831
NM_016878

RefSeq (protein)

NP_001104301
NP_058574

Location (UCSC)Chr 2: 219.37 – 219.4 MbChr 1: 75.31 – 75.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 general metabolism of intracellular proteins.[6]

Model organisms

Model organisms have been used in the study of DNPEP function. A conditional knockout mouse line called Dnpeptm1e(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[7] Male and female animals underwent a standardized phenotypic screen[8] to determine the effects of deletion.[9][10][11][12] Additional screens performed: In-depth immunological phenotyping.[13]

See also
  •  Biology portal

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".
  7. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
  8. "International Mouse Phenotyping Consortium".
  9. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  10. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  11. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
  12. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  13. "Infection and Immunity Immunophenotyping (3i) Consortium".

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. 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.
  • 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)


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