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DNPEP

From Wikipedia, the free encyclopedia
DNPEP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDNPEP, ASPEP, DAP, aspartyl aminopeptidase
External IDsOMIM: 611367; MGI: 1278328; HomoloGene: 6110; GeneCards: DNPEP; OMA:DNPEP - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001110831
NM_016878

RefSeq (protein)

NP_001104301
NP_058574

Location (UCSC)Chr 2: 219.37 – 219.4 MbChr 1: 75.28 – 75.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Function

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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

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123992Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026209Ensembl, 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. ^ a b "Entrez Gene: DNPEP aspartyl aminopeptidase".

Further reading

[edit]
  • 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.
[edit]
  • 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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