NRXN2: Difference between revisions

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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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 [[alternative splicing|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 [[protein isoforms|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.<ref name="entrez" />
| summary_text = [[Neurexin]]s 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 [[alternative splicing|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 [[protein isoforms|isoforms]]. The alpha-neurexins contain epidermal growth factor-like ([[EGF-like]]) sequences and [[laminin G domain]]s, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins.<ref name="entrez" />
}}
}}


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*{{cite journal  |vauthors=Ichtchenko K, Nguyen T, Südhof TC |title=Structures, alternative splicing, and neurexin binding of multiple neuroligins |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2676–2682 |year= 1996 |pmid= 8576240 |doi=10.1074/jbc.271.5.2676  }}
*{{cite journal  |vauthors=Ichtchenko K, Nguyen T, Südhof TC |title=Structures, alternative splicing, and neurexin binding of multiple neuroligins |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2676–2682 |year= 1996 |pmid= 8576240 |doi=10.1074/jbc.271.5.2676  }}
*{{cite journal  |vauthors=Hata Y, Butz S, Südhof TC |title=CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins |journal=J. Neurosci. |volume=16 |issue= 8 |pages= 2488–94 |year= 1996 |pmid= 8786425 |doi=  }}
*{{cite journal  |vauthors=Hata Y, Butz S, Südhof TC |title=CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins |journal=J. Neurosci. |volume=16 |issue= 8 |pages= 2488–94 |year= 1996 |pmid= 8786425 |doi=  }}
*{{cite journal |vauthors=Kurschner C, Mermelstein PG, Holden WT, Surmeier DJ |title=CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins |journal=Mol. Cell. Neurosci. |volume=11 |issue= 3 |pages= 161–172 |year= 1998 |pmid= 9647694 |doi= 10.1006/mcne.1998.0679 }}
*{{cite journal |authorlink4=D. James Surmeier |vauthors=Kurschner C, Mermelstein PG, Holden WT, Surmeier DJ |title=CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins |journal=Mol. Cell. Neurosci. |volume=11 |issue= 3 |pages= 161–172 |year= 1998 |pmid= 9647694 |doi= 10.1006/mcne.1998.0679 }}
*{{cite journal  | author=Hock B |title=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 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 17 |pages= 9779–9784 |year= 1998 |pmid= 9707552 |doi=10.1073/pnas.95.17.9779  | pmc=21413  |name-list-format=vanc| author2=Böhme B  | author3=Karn T  | display-authors=3  | last4=Yamamoto  | first4=T  | last5=Kaibuchi  | first5=K  | last6=Holtrich  | first6=U  | last7=Holland  | first7=S  | last8=Pawson  | first8=T  | last9=Rübsamen-Waigmann  | first9=H  }}
*{{cite journal  | author=Hock B |title=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 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 17 |pages= 9779–9784 |year= 1998 |pmid= 9707552 |doi=10.1073/pnas.95.17.9779  | pmc=21413  |name-list-format=vanc| author2=Böhme B  | author3=Karn T  | display-authors=3  | last4=Yamamoto  | first4=T  | last5=Kaibuchi  | first5=K  | last6=Holtrich  | first6=U  | last7=Holland  | first7=S  | last8=Pawson  | first8=T  | last9=Rübsamen-Waigmann  | first9=H  }}
*{{cite journal  | author=Bergman L |title=A 500-kb sequence-ready cosmid contig and transcript map of the MEN1 region on 11q13 |journal=Genomics |volume=55 |issue= 1 |pages= 49–56 |year= 1999 |pmid= 9888998 |doi= 10.1006/geno.1998.5625  |name-list-format=vanc| author2=Silins G  | author3=Grimmond S  | display-authors=3  | last4=Hummerich  | first4=H  | last5=Stewart  | first5=C  | last6=Little  | first6=P  | last7=Hayward  | first7=N }}
*{{cite journal  | author=Bergman L |title=A 500-kb sequence-ready cosmid contig and transcript map of the MEN1 region on 11q13 |journal=Genomics |volume=55 |issue= 1 |pages= 49–56 |year= 1999 |pmid= 9888998 |doi= 10.1006/geno.1998.5625  |name-list-format=vanc| author2=Silins G  | author3=Grimmond S  | display-authors=3  | last4=Hummerich  | first4=H  | last5=Stewart  | first5=C  | last6=Little  | first6=P  | last7=Hayward  | first7=N }}

Latest revision as of 00:52, 18 May 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Neurexin-2-alpha is a protein that in humans is encoded by the NRXN2 gene.[1][2]

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.[2]

References

  1. Ushkaryov YA, Petrenko AG, Geppert M, Sudhof TC (Aug 1992). "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin". Science. 257 (5066): 50–56. doi:10.1126/science.1621094. PMID 1621094.
  2. 2.0 2.1 "Entrez Gene: NRXN2 neurexin 2".

Further reading