Biology:P2RX5
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Short description: Protein-coding gene in the species Homo sapiens
![]() Generic protein structure example |
P2X purinoceptor 5 is a protein that in humans is encoded by the P2RX5 gene.[1][2]
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Several characteristic motifs of ATP-gated channels are present in its primary structure, but, unlike other members of the purinoceptors family, this receptor has only a single transmembrane domain. Four transcript variants encoding distinct isoforms have been identified for this gene.[2]
See also
- P2X receptor
References
- ↑ "Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system". FEBS Lett 418 (1–2): 195–9. Jan 1998. doi:10.1016/S0014-5793(97)01380-X. PMID 9414125.
- ↑ 2.0 2.1 "Entrez Gene: P2RX5 purinergic receptor P2X, ligand-gated ion channel, 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5026.
Further reading
- North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
- "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion". Genome Res. 10 (2): 165–73. 2000. doi:10.1101/gr.10.2.165. PMID 10673275.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. 2004. doi:10.1038/nbt810. PMID 12665801.
- "Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes". J. Invest. Dermatol. 120 (6): 1007–15. 2003. doi:10.1046/j.1523-1747.2003.12261.x. PMID 12787128.
- "Expression of purinergic receptors in non-melanoma skin cancers and their functional roles in A431 cells". J. Invest. Dermatol. 121 (2): 315–27. 2003. doi:10.1046/j.1523-1747.2003.12379.x. PMID 12880424.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "A frameshift polymorphism in P2X5 elicits an allogeneic cytotoxic T lymphocyte response associated with remission of chronic myeloid leukemia". J. Clin. Invest. 115 (12): 3506–16. 2006. doi:10.1172/JCI24832. PMID 16322791.
- "Purinoceptor expression on keratinocytes reflects their function on the epidermis during chronic venous insufficiency". Arch. Dermatol. Res. 298 (6): 301–7. 2007. doi:10.1007/s00403-006-0693-x. PMID 16967306.
- "P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate". J. Biol. Chem. 281 (51): 39561–72. 2007. doi:10.1074/jbc.M606113200. PMID 17001079.
External links
- P2RX5+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
![]() | Original source: https://en.wikipedia.org/wiki/P2RX5.
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