NRXN3

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Neurexin 3
Identifiers
Symbols NRXN3 ; KIAA0743
External IDs Template:OMIM5 Template:MGI HomoloGene88711
RNA expression pattern
File:PBB GE NRXN3 205795 at tn.png
File:PBB GE NRXN3 215021 s at tn.png
File:PBB GE NRXN3 215020 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

Neurexin 3, also known as NRXN3, is a human gene.[1]

Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two, NRXN1 and NRXN3, are among the largest known human genes. Three of the genes (NRXN1-3) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain epidermal growth factor-like (EGF-like) sequences and laminin G domains, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins.[1]

References

  1. 1.0 1.1 "Entrez Gene: NRXN3 neurexin 3".

Further reading

  • Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
  • Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Heilig R, Eckenberg R, Petit JL; et al. (2003). "The DNA sequence and analysis of human chromosome 14". Nature. 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121.
  • 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.
  • Occhi G, Rampazzo A, Beffagna G, Antonio Danieli G (2002). "Identification and characterization of heart-specific splicing of human neurexin 3 mRNA (NRXN3)". Biochem. Biophys. Res. Commun. 298 (1): 151–5. PMID 12379233.
  • Tabuchi K, Südhof TC (2002). "Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing". Genomics. 79 (6): 849–59. doi:10.1006/geno.2002.6780. PMID 12036300.
  • Rowen L, Young J, Birditt B; et al. (2002). "Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity". Genomics. 79 (4): 587–97. doi:10.1006/geno.2002.6734. PMID 11944992.
  • Nagase T, Ishikawa K, Suyama M; et al. (1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86. PMID 9872452.
  • Hock B, Böhme B, Karn T; et al. (1998). "PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 9779–84. PMID 9707552.
  • Nagase T, Ishikawa K, Miyajima N; et al. (1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–9. PMID 9628581.
  • Hata Y, Butz S, Südhof TC (1996). "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins". J. Neurosci. 16 (8): 2488–94. PMID 8786425.
  • Ichtchenko K, Nguyen T, Südhof TC (1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". J. Biol. Chem. 271 (5): 2676–82. PMID 8576240.
  • Ushkaryov YA, Petrenko AG, Geppert M, Südhof TC (1992). "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin". Science. 257 (5066): 50–6. PMID 1621094.

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