NRXN2

Protein-coding gene in the species Homo sapiens
NRXN2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4NXR

Identifiers
AliasesNRXN2, neurexin 2
External IDsOMIM: 600566; MGI: 1096362; HomoloGene: 86984; GeneCards: NRXN2; OMA:NRXN2 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for NRXN2
Genomic location for NRXN2
Band11q13.1Start64,606,174 bp[1]
End64,723,197 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for NRXN2
Genomic location for NRXN2
Band19 A|19Start6,468,761 bp[2]
End6,594,199 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right hemisphere of cerebellum

  • prefrontal cortex

  • right frontal lobe

  • amygdala

  • cingulate gyrus

  • anterior cingulate cortex

  • Brodmann area 9

  • ganglionic eminence

  • paraflocculus of cerebellum

  • cerebellar vermis
Top expressed in
  • cerebellum

  • cerebellar cortex

  • olfactory bulb

  • primary visual cortex

  • superior frontal gyrus

  • hypothalamus

  • striatum of neuraxis

  • dentate gyrus of hippocampal formation granule cell

  • hippocampus proper

  • layer of retina
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • neuroligin family protein binding
  • transmembrane signaling receptor activity
  • cell adhesion molecule binding
  • calcium channel regulator activity
  • metal ion binding
Cellular component
  • integral component of membrane
  • membrane
  • plasma membrane
  • presynapse
  • protein-containing complex
Biological process
  • neuron cell-cell adhesion
  • cell adhesion
  • signal transduction
  • gephyrin clustering involved in postsynaptic density assembly
  • postsynaptic density protein 95 clustering
  • vocalization behavior
  • vocal learning
  • neuroligin clustering involved in postsynaptic membrane assembly
  • adult behavior
  • postsynaptic membrane assembly
  • social behavior
  • synapse assembly
  • neurotransmitter secretion
  • chemical synaptic transmission
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9379

18190

Ensembl

ENSG00000110076

ENSMUSG00000033768

UniProt

P58401
Q9P2S2

E9Q7X7

RefSeq (mRNA)
NM_015080
NM_138732
NM_138734
NM_001376262
NM_001376263

NM_001376265
NM_001376266
NM_001376267
NM_001400681
NM_001400682

NM_001205234
NM_001205235
NM_020253
NM_001369363

RefSeq (protein)
NP_055895
NP_620060
NP_620063
NP_001363191
NP_001363192

NP_001363194
NP_001363195
NP_001363196
NP_055895.1
NP_620060.1

NP_001192163
NP_001192164
NP_064649
NP_001356292

Location (UCSC)Chr 11: 64.61 – 64.72 MbChr 19: 6.47 – 6.59 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Neurexin-2-alpha is a protein that in humans is encoded by the NRXN2 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110076 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033768 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. Bibcode:1992Sci...257...50U. doi:10.1126/science.1621094. PMID 1621094.
  6. ^ a b "Entrez Gene: NRXN2 neurexin 2".

Further reading

  • Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
  • Ichtchenko K, Nguyen T, Südhof TC (1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". J. Biol. Chem. 271 (5): 2676–2682. doi:10.1074/jbc.271.5.2676. PMID 8576240.
  • 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. doi:10.1523/JNEUROSCI.16-08-02488.1996. PMC 6578772. PMID 8786425.
  • Kurschner C, Mermelstein PG, Holden WT, Surmeier DJ (1998). "CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins". Mol. Cell. Neurosci. 11 (3): 161–172. doi:10.1006/mcne.1998.0679. PMID 9647694. S2CID 36534759.
  • 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): 9779–9784. Bibcode:1998PNAS...95.9779H. doi:10.1073/pnas.95.17.9779. PMC 21413. PMID 9707552.
  • Bergman L, Silins G, Grimmond S, et al. (1999). "A 500-kb sequence-ready cosmid contig and transcript map of the MEN1 region on 11q13". Genomics. 55 (1): 49–56. doi:10.1006/geno.1998.5625. PMID 9888998.
  • Nagase T, Ishikawa K, Suyama M, et al. (1999). "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". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
  • 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): 587–597. doi:10.1006/geno.2002.6734. PMID 11944992.
  • Tabuchi K, Südhof TC (2002). "Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing". Genomics. 79 (6): 849–859. doi:10.1006/geno.2002.6780. PMID 12036300.
  • Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Res. 12 (11): 1773–1784. doi:10.1101/gr.406902. PMC 187542. PMID 12421765.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
  • Homma K, Kikuno RF, Nagase T, et al. (2004). "Alternative splice variants encoding unstable protein domains exist in the human brain". J. Mol. Biol. 343 (5): 1207–1220. doi:10.1016/j.jmb.2004.09.028. PMID 15491607.
  • Taylor TD, Noguchi H, Totoki Y, et al. (2006). "Human chromosome 11 DNA sequence and analysis including novel gene identification". Nature. 440 (7083): 497–500. Bibcode:2006Natur.440..497T. doi:10.1038/nature04632. PMID 16554811.


  • v
  • t
  • e