NFASC

Neurofascin homolog (chicken)
Identifiers
Symbols	NFASC ; DKFZp686P2250; FLJ46866; KIAA0756; NF; NRCAML
External IDs	Template:OMIM5 Template:MGI HomoloGene: 24945
Gene ontology Molecular function Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE NFASC 213438 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

Neurofascin homolog (chicken), also known as NFASC, is a human gene.

Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM; MIM 308840) involved in axon subcellular targeting and synapse formation during neural development (Ango et al., 2004).[supplied by OMIM]

Further reading

• Hortsch M (1996). "The L1 family of neural cell adhesion molecules: old proteins performing new tricks". Neuron. 17 (4): 587–93. PMID 8893017.
• 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. PMID 12168954.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Volkmer H, Hassel B, Wolff JM; et al. (1992). "Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily". J. Cell Biol. 118 (1): 149–61. PMID 1377696.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Burmeister M, Ren Q, Makris GJ; et al. (1996). "Genes for the neuronal immunoglobulin domain cell adhesion molecules neurofascin and Nr-CAM map to mouse chromosomes 1 and 12 and homologous human chromosomes". Mamm. Genome. 7 (7): 558–9. PMID 8672144.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tuvia S, Garver TD, Bennett V (1998). "The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation". Proc. Natl. Acad. Sci. U.S.A. 94 (24): 12957–62. PMID 9371782.CS1 maint: Multiple names: authors list (link)
• Ren Q, Bennett V (1998). "Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules". J. Neurochem. 70 (5): 1839–49. PMID 9572267.
• Zhang X, Davis JQ, Carpenter S, Bennett V (1998). "Structural requirements for association of neurofascin with ankyrin". J. Biol. Chem. 273 (46): 30785–94. PMID 9804856.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Koroll M, Rathjen FG, Volkmer H (2001). "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity". J. Biol. Chem. 276 (14): 10646–54. doi:10.1074/jbc.M010647200. PMID 11152476.CS1 maint: Multiple names: authors list (link)
• Ratcliffe CF, Westenbroek RE, Curtis R, Catterall WA (2001). "Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain". J. Cell Biol. 154 (2): 427–34. PMID 11470829.CS1 maint: Multiple names: authors list (link)
• Jenkins SM, Kizhatil K, Kramarcy NR; et al. (2002). "FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons". J. Cell. Sci. 114 (Pt 21): 3823–35. PMID 11719549.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jenkins SM, Bennett V (2002). "Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments". J. Cell Biol. 155 (5): 739–46. doi:10.1083/jcb.200109026. PMID 11724816.
• Charles P, Tait S, Faivre-Sarrailh C; et al. (2002). "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction". Curr. Biol. 12 (3): 217–20. PMID 11839274.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kizhatil K, Wu YX, Sen A, Bennett V (2002). "A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin". J. Neurosci. 22 (18): 7948–58. PMID 12223548.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gollan L, Salomon D, Salzer JL, Peles E (2004). "Caspr regulates the processing of contactin and inhibits its binding to neurofascin". J. Cell Biol. 163 (6): 1213–8. doi:10.1083/jcb.200309147. PMID 14676309.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ango F, di Cristo G, Higashiyama H; et al. (2004). "Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment". Cell. 119 (2): 257–72. doi:10.1016/j.cell.2004.10.004. PMID 15479642.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)