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{{Infobox_gene}}
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'''Neurexin-2-alpha''' is a [[protein]] that in humans is encoded by the ''NRXN2'' [[gene]].<ref name="pmid1621094">{{cite journal |vauthors=Ushkaryov YA, Petrenko AG, Geppert M, Sudhof TC | title = Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin | journal = Science | volume = 257 | issue = 5066 | pages = 50–56 |date=Aug 1992 | pmid = 1621094 | pmc =  | doi =10.1126/science.1621094 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NRXN2 neurexin 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9379| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Neurexin 2
| HGNCid = 8009
| Symbol = NRXN2
| AltSymbols =; FLJ40892; KIAA0921
| OMIM = 600566
| ECnumber = 
| Homologene = 86984
| MGIid = 1096362
| GeneAtlas_image1 = PBB_GE_NRXN2_209982_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NRXN2_209983_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005246 |text = calcium channel regulator activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007269 |text = neurotransmitter secretion}} {{GNF_GO|id=GO:0007416 |text = synaptogenesis}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9379
    | Hs_Ensembl = ENSG00000110076
    | Hs_RefseqProtein = NP_055895
    | Hs_RefseqmRNA = NM_015080
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 64130222
    | Hs_GenLoc_end = 64247236
    | Hs_Uniprot = Q9P2S2
    | Mm_EntrezGene = 18190
    | Mm_Ensembl = ENSMUSG00000033768
    | Mm_RefseqmRNA = XM_489806
    | Mm_RefseqProtein = XP_489806
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 6428013
    | Mm_GenLoc_end = 6533217
    | Mm_Uniprot = 
  }}
}}
'''Neurexin 2''', also known as '''NRXN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NRXN2 neurexin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9379| accessdate = }}</ref>


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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 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.<ref name="entrez">{{cite web | title = Entrez Gene: NRXN2 neurexin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9379| accessdate = }}</ref>
| 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" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi=  }}
*{{cite journal  | author=Nakajima D |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones |journal=DNA Res. |volume=9 |issue= 3 |pages= 99–106 |year= 2003 |pmid= 12168954 |doi=10.1093/dnares/9.3.99 |name-list-format=vanc| author2=Okazaki N | author3=Yamakawa H  | display-authors=3  | last4=Kikuno  | first4=R  | last5=Ohara  | first5=O  | last6=Nagase  | first6=T }}
*{{cite journal | author=Ushkaryov YA, Petrenko AG, Geppert M, Südhof TC |title=Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. |journal=Science |volume=257 |issue= 5066 |pages= 50-6 |year= 1992 |pmid= 1621094 |doi=  }}
*{{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  | author=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= 2676-82 |year= 1996 |pmid= 8576240 |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  | author=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 |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=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= 161-72 |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, Böhme B, Karn T, ''et al.'' |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= 9779-84 |year= 1998 |pmid= 9707552 |doi=  }}
*{{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, Silins G, Grimmond S, ''et al.'' |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 }}
*{{cite journal  | author=Nagase T |title=Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro |journal=DNA Res. |volume=6 |issue= 1 |pages= 63–70 |year= 1999 |pmid= 10231032 |doi=10.1093/dnares/6.1.63  |name-list-format=vanc| author2=Ishikawa K  | author3=Suyama M  | display-authors=3  | last4=Kikuno  | first4=R  | last5=Hirosawa  | first5=M  | last6=Miyajima  | first6=N  | last7=Tanaka  | first7=A  | last8=Kotani  | first8=H  | last9=Nomura  | first9=N }}
*{{cite journal  | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 1 |pages= 63-70 |year= 1999 |pmid= 10231032 |doi=  }}
*{{cite journal  | author=Rowen L |title=Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity |journal=Genomics |volume=79 |issue= 4 |pages= 587–597 |year= 2002 |pmid= 11944992 |doi= 10.1006/geno.2002.6734 |name-list-format=vanc| author2=Young J  | author3=Birditt B  | display-authors=3  | last4=Kaur  | first4=Amardeep  | last5=Madan  | first5=Anup  | last6=Philipps  | first6=Dana L.  | last7=Qin  | first7=Shizhen  | last8=Minx  | first8=Patrick  | last9=Wilson  | first9=Richard K. }}
*{{cite journal  | author=Rowen L, Young J, Birditt B, ''et al.'' |title=Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity. |journal=Genomics |volume=79 |issue= 4 |pages= 587-97 |year= 2002 |pmid= 11944992 |doi= 10.1006/geno.2002.6734 }}
*{{cite journal  |vauthors=Tabuchi K, Südhof TC |title=Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing |journal=Genomics |volume=79 |issue= 6 |pages= 849–859 |year= 2002 |pmid= 12036300 |doi= 10.1006/geno.2002.6780 }}
*{{cite journal  | author=Tabuchi K, Südhof TC |title=Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing. |journal=Genomics |volume=79 |issue= 6 |pages= 849-59 |year= 2002 |pmid= 12036300 |doi= 10.1006/geno.2002.6780 }}
*{{cite journal  |vauthors=Nakayama M, Kikuno R, Ohara O |title=Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs |journal=Genome Res. |volume=12 |issue= 11 |pages= 1773–1784 |year= 2003 |pmid= 12421765 |doi= 10.1101/gr.406902 | pmc=187542 }}
*{{cite journal  | author=Nakayama M, Kikuno R, Ohara O |title=Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs. |journal=Genome Res. |volume=12 |issue= 11 |pages= 1773-84 |year= 2003 |pmid= 12421765 |doi= 10.1101/gr.406902 }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–45 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Homma K |title=Alternative splice variants encoding unstable protein domains exist in the human brain |journal=J. Mol. Biol. |volume=343 |issue= 5 |pages= 1207–1220 |year= 2004 |pmid= 15491607 |doi= 10.1016/j.jmb.2004.09.028 |name-list-format=vanc| author2=Kikuno RF  | author3=Nagase T  | display-authors=3  | last4=Ohara  | first4=O  | last5=Nishikawa  | first5=K }}
*{{cite journal  | author=Homma K, Kikuno RF, Nagase T, ''et al.'' |title=Alternative splice variants encoding unstable protein domains exist in the human brain. |journal=J. Mol. Biol. |volume=343 |issue= 5 |pages= 1207-20 |year= 2004 |pmid= 15491607 |doi= 10.1016/j.jmb.2004.09.028 }}
*{{cite journal  | author=Taylor TD |title=Human chromosome 11 DNA sequence and analysis including novel gene identification |journal=Nature |volume=440 |issue= 7083 |pages= 497–500 |year= 2006 |pmid= 16554811 |doi= 10.1038/nature04632 |name-list-format=vanc| author2=Noguchi H  | author3=Totoki Y  | display-authors=3  | last4=Toyoda  | first4=Atsushi  | last5=Kuroki  | first5=Yoko  | last6=Dewar  | first6=Ken  | last7=Lloyd  | first7=Christine  | last8=Itoh  | first8=Takehiko  | last9=Takeda  | first9=Tadayuki }}
*{{cite journal  | author=Taylor TD, Noguchi H, Totoki Y, ''et al.'' |title=Human chromosome 11 DNA sequence and analysis including novel gene identification. |journal=Nature |volume=440 |issue= 7083 |pages= 497-500 |year= 2006 |pmid= 16554811 |doi= 10.1038/nature04632 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 00:52, 18 May 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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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



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