Neurocan

Identifiers

NCAN; CSPG3; FLJ44681

External IDs

OMIM: 600826 MGI: 104694 HomoloGene: 3229 GeneCards: NCAN Gene

Gene Ontology
Molecular function	• binding • calcium ion binding • sugar binding • hyaluronic acid binding
Cellular component	• extracellular region
Biological process	• cell adhesion • axon guidance • regulation of synapse structural plasticity
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
19.32 – 19.36 Mb

Chr 8:
72.62 – 72.64 Mb

PubMed search

[1]

[2]

Neurocan core protein is a protein that in humans is encoded by the NCAN gene.^[1]^[2]

Neurocan is a chondroitin sulfate proteoglycan consisting of neurocan and chondroitin sulfate. It is thought to be involved in the modulation of cell adhesion and migration.^[2]

References

^ Rauch U, Karthikeyan L, Maurel P, Margolis RU, Margolis RK (Oct 1992). "Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain". J Biol Chem 267 (27): 19536–47. PMID 1326557.
^ ^a ^b "Entrez Gene: NCAN neurocan". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1463.

Rauch U, Grimpe B, Kulbe G, et al. (1996). "Structure and chromosomal localization of the mouse neurocan gene.". Genomics 28 (3): 405–10. doi:10.1006/geno.1995.1168. PMID 7490074.
Friedlander DR, Milev P, Karthikeyan L, et al. (1994). "The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and inhibits neuronal adhesion and neurite outgrowth.". J. Cell Biol. 125 (3): 669–80. doi:10.1083/jcb.125.3.669. PMC 2119998. PMID 7513709. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2119998.
Milev P, Maurel P, Häring M, et al. (1996). "TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM.". J. Biol. Chem. 271 (26): 15716–23. doi:10.1074/jbc.271.26.15716. PMID 8663515.
Retzler C, Göhring W, Rauch U (1996). "Analysis of neurocan structures interacting with the neural cell adhesion molecule N-CAM.". J. Biol. Chem. 271 (44): 27304–10. doi:10.1074/jbc.271.44.27304. PMID 8910306.
Rauch U, Clement A, Retzler C, et al. (1997). "Mapping of a defined neurocan binding site to distinct domains of tenascin-C.". J. Biol. Chem. 272 (43): 26905–12. doi:10.1074/jbc.272.43.26905. PMID 9341124.
Milev P, Chiba A, Häring M, et al. (1998). "High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule.". J. Biol. Chem. 273 (12): 6998–7005. doi:10.1074/jbc.273.12.6998. PMID 9507007.
Prange CK, Pennacchio LA, Lieuallen K, et al. (1998). "Characterization of the human neurocan gene, CSPG3.". Gene 221 (2): 199–205. doi:10.1016/S0378-1119(98)00455-7. PMID 9795216.
Oleszewski M, Gutwein P, von der Lieth W, et al. (2000). "Characterization of the L1-neurocan-binding site. Implications for L1-L1 homophilic binding.". J. Biol. Chem. 275 (44): 34478–85. doi:10.1074/jbc.M004147200. PMID 10934197.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310948.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.

Protein: lectins

Animal

C-type lectins	Asialoglycoprotein receptor · KLRD1 · Collectin (Mannan-binding lectin) · Mannose receptor · proteochondroitin sulfate (Aggrecan, Versican, Brevican, Neurocan)

Other	Calnexin · Calreticulin · CD22 · CD33 · Galectin · Myelin-associated glycoprotein · N-Acetylglucosamine receptor · Selectin · Sialoadhesin

Plant

Abrin · Ricin · Mitogens (Concanavalin A, Phytohaemagglutinin, Pokeweed mitogen) · Legume lectin · BanLec

Protein, glycoconjugate: glycoproteins and glycopeptides

Mucoproteins

Mucin	CD43 · CD164 · MUC1 · MUC2 · MUC3A · MUC3B · MUC4 · MUC5AC · MUC5B · MUC6 · MUC7 · MUC8 · MUC12 · MUC13 · MUC15 · MUC16 · MUC17 · MUC19 · MUC20

Other	Haptoglobin · Intrinsic factor · Orosomucoid · Peptidoglycan · Phytohaemagglutinin · Ovomucin

Proteoglycans

CS/DS	Decorin · Biglycan · Versican

HS/CS	Testican · Perlecan

CS	Chondroitin sulfate proteoglycans: Aggrecan · Neurocan · Brevican · CD44 · CSPG4 · CSPG5 · Platelet factor 4 · Structural maintenance of chromosomes 3

KS	Fibromodulin · Lumican · Keratocan

HS	Syndecan 1

Other

Activin and inhibin · ADAM · Alpha 1-antichymotrypsin · Apolipoprotein H · CD70 · Asialoglycoprotein · Avidin · B-cell activating factor · 4-1BB ligand · Cholesterylester transfer protein · Clusterin · Colony-stimulating factor · Hemopexin · Lactoferrin · Membrane glycoproteins · Myelin protein zero · Osteonectin · Protein C · Protein S · Serum amyloid P component · Sialoglycoprotein (CD43, Glycophorin, Glycophorin C) · Thrombopoietin · Thyroglobulin · Thyroxine-binding proteins · Transcortin · Tumor necrosis factor-alpha · Uteroglobin · Vitronectin

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

biochemical families: prot · nucl · carb (glpr, alco, glys) · lipd (fata/i, phld, strd, gllp, eico) · amac/i · ncbs/i · ttpy/i

Neurocan

References

Further reading