XPNPEP2
| X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound | |||||||||||
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| Identifiers | |||||||||||
| Symbols | XPNPEP2 ; | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 37766 | ||||||||||
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| RNA expression pattern | |||||||||||
| File:PBB GE XPNPEP2 216910 at tn.png | |||||||||||
| File:PBB GE XPNPEP2 206484 s at tn.png | |||||||||||
| More reference expression data | |||||||||||
| Orthologs | |||||||||||
| Template:GNF Ortholog box | |||||||||||
| Species | Human | Mouse | |||||||||
| Entrez | n/a | n/a | |||||||||
| Ensembl | n/a | n/a | |||||||||
| UniProt | n/a | n/a | |||||||||
| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
| PubMed search | n/a | n/a | |||||||||
X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound, also known as XPNPEP2, is a human gene.[1]
Aminopeptidase P is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. Structurally, the enzyme is a member of the 'pita bread fold' family and occurs in mammalian tissues in both soluble and GPI-anchored membrane-bound forms. A membrane-bound and soluble form of this enzyme have been identified as products of two separate genes.[1]
References
Further reading
- Vanhoof G, De Meester I, Goossens F; et al. (1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P.". Biochem. Pharmacol. 44 (3): 479–87. PMID 1510698.
- Venema RC, Ju H, Zou R; et al. (1997). "Cloning and tissue distribution of human membrane-bound aminopeptidase P.". Biochim. Biophys. Acta. 1354 (1): 45–8. PMID 9375790.
- Sprinkle TJ, Stone AA, Venema RC; et al. (1999). "Assignment of the membrane-bound human aminopeptidase P gene (XPNPEP2) to chromosome Xq25". Genomics. 50 (1): 114–6. doi:10.1006/geno.1998.5302. PMID 9628831.
- Cottrell GS, Hyde RJ, Hooper NM, Turner AJ (1998). "The cloning and functional expression of human pancreatic aminopeptidase P.". Biochem. Soc. Trans. 26 (3): S248. PMID 9765967.
- Dias Neto E, Correa RG, Verjovski-Almeida S; et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. PMID 10737800.
- Prueitt RL, Ross JL, Zinn AR (2000). "Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene". Cytogenet. Cell Genet. 89 (1–2): 44–50. PMID 10894934.
- 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. PMID 12477932.
- Fu GK, Wang JT, Yang J; et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
- Suzuki Y, Yamashita R, Shirota M; et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMID 15342556.
- 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. PMID 15489334.
- Ross MT, Grafham DV, Coffey AJ; et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. doi:10.1038/nature03440. PMID 15772651.
- Molinaro G, Duan QL, Chagnon M; et al. (2007). "Kinin-dependent hypersensitivity reactions in hemodialysis: metabolic and genetic factors". Kidney Int. 70 (10): 1823–31. doi:10.1038/sj.ki.5001873. PMID 17003818.
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