CNTN2

Contactin 2 (axonal)

Identifiers

CNTN2; AXT; DKFZp781D102; FLJ37193; FLJ42746; MGC157722; TAG-1; TAX; TAX1

External IDs

OMIM: 190197 MGI: 104518 HomoloGene: 3720 GeneCards: CNTN2 Gene

Gene Ontology
Molecular function	• glycoprotein binding • carbohydrate binding • identical protein binding • protein self-association
Cellular component	• plasma membrane • integral to plasma membrane • voltage-gated potassium channel complex • cell surface • axon • anchored to membrane • node of Ranvier • neuronal cell body • myelin sheath • juxtaparanode region of axon • synapse part
Biological process	• microtubule cytoskeleton organization • neuron migration • cell adhesion • cell-matrix adhesion • axon guidance • axonal fasciculation • learning • adult walking behavior • regulation of cell morphogenesis involved in differentiation • positive regulation of protein maturation by peptide bond cleavage • cerebral cortex GABAergic interneuron migration • central nervous system myelination • regulation of axon diameter • neuron projection development • receptor internalization • cellular protein localization • clustering of voltage-gated potassium channels • negative regulation of neuron differentiation • regulation of neuronal synaptic plasticity • regulation of astrocyte differentiation • positive regulation of adenosine receptor signaling pathway • establishment of protein localization to juxtaparanode region of axon
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
205.01 – 205.05 Mb

Chr 1:
134.41 – 134.44 Mb

PubMed search

[1]

[2]

Contactin-2 is a protein that in humans is encoded by the CNTN2 gene.^[1]^[2]^[3]

The protein encoded by this gene is a member of the immunoglobulin superfamily. It is a glycosylphosphatidylinositol (GPI)-anchored neuronal membrane protein that functions as a cell adhesion molecule. It may play a role in the formation of axon connections in the developing nervous system. It may also be involved in glial tumorigenesis and may provide a potential target for therapeutic intervention.^[3]

Interactions

CNTN2 has been shown to interact with CNTNAP2^[4] and NFYB.^[5]

References

^ Tsiotra PC, Karagogeos D, Theodorakis K, Michaelidis TM, Modi WS, Furley AJ, Jessell TM, Papamatheakis J (Mar 1994). "Isolation of the cDNA and chromosomal localization of the gene (TAX1) encoding the human axonal glycoprotein TAG-1". Genomics 18 (3): 562–7. doi:10.1016/S0888-7543(05)80357-X. PMID 8307567.
^ Yoshihara Y, Kawasaki M, Tamada A, Nagata S, Kagamiyama H, Mori K (Mar 1996). "Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily". J Neurobiol 28 (1): 51–69. doi:10.1002/neu.480280106. PMID 8586965.
^ ^a ^b "Entrez Gene: CNTN2 contactin 2 (axonal)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6900.
^ Traka, Maria; Goutebroze Laurence, Denisenko Natalia, Bessa Maria, Nifli Artemisia, Havaki Sophia, Iwakura Yoichiro, Fukamauchi Fumihiko, Watanabe Kazutada, Soliven Betty, Girault Jean-Antoine, Karagogeos Domna (Sep. 2003). "Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers". J. Cell Biol. (United States) 162 (6): 1161–72. doi:10.1083/jcb.200305078. ISSN 0021-9525. PMC 2172849. PMID 12975355. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172849.
^ Pise-Masison, C A; Dittmer J, Clemens K E, Brady J N (Mar. 1997). "Physical and functional interaction between the human T-cell lymphotropic virus type 1 Tax1 protein and the CCAAT binding protein NF-Y". Mol. Cell. Biol. (UNITED STATES) 17 (3): 1236–43. ISSN 0270-7306. PMC 231848. PMID 9032250. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231848.

Walsh FS, Doherty P (1992). "Glycosylphosphatidylinositol anchored recognition molecules that function in axonal fasciculation, growth and guidance in the nervous system.". Cell Biol. Int. Rep. 15 (11): 1151–66. doi:10.1016/0309-1651(91)90061-M. PMID 1838307.
Kuhn TB, Stoeckli ET, Condrau MA, et al. (1991). "Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4).". J. Cell Biol. 115 (4): 1113–26. doi:10.1083/jcb.115.4.1113. PMC 2289947. PMID 1720120. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289947.
Dodd J, Morton SB, Karagogeos D, et al. (1990). "Spatial regulation of axonal glycoprotein expression on subsets of embryonic spinal neurons.". Neuron 1 (2): 105–16. doi:10.1016/0896-6273(88)90194-8. PMID 3272160.
Kenwrick S, Leversha M, Rooke L, et al. (1993). "Localization of the human TAX-1 gene to 1q32.1: a region implicated in microcephaly and Van der Woude syndrome.". Hum. Mol. Genet. 2 (9): 1461–2. doi:10.1093/hmg/2.9.1461. PMID 8242070.
Rader C, Stoeckli ET, Ziegler U, et al. (1993). "Cell-cell adhesion by homophilic interaction of the neuronal recognition molecule axonin-1.". Eur. J. Biochem. 215 (1): 133–41. doi:10.1111/j.1432-1033.1993.tb18015.x. PMID 8344273.
Hasler TH, Rader C, Stoeckli ET, et al. (1993). "cDNA cloning, structural features, and eucaryotic expression of human TAG-1/axonin-1.". Eur. J. Biochem. 211 (1–2): 329–39. doi:10.1111/j.1432-1033.1993.tb19902.x. PMID 8425542.
Kozlov SV, Giger RJ, Hasler T, et al. (1996). "The human TAX1 gene encoding the axon-associated cell adhesion molecule TAG-1/axonin-1: genomic structure and basic promoter". Genomics 30 (2): 141–8. doi:10.1006/geno.1995.9892. PMID 8586412.
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.
Pise-Masison CA, Dittmer J, Clemens KE, Brady JN (1997). "Physical and functional interaction between the human T-cell lymphotropic virus type 1 Tax1 protein and the CCAAT binding protein NF-Y". Mol. Cell. Biol. 17 (3): 1236–43. PMC 231848. PMID 9032250. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231848.
Williams H, Schachner M, Wang B, Kenwrick S (1998). "Radiation hybrid mapping of the genes for tenascin-R (TNR), phosducin (PDC), laminin C1 (LAMC1), and TAX in 1q25-q32". Genomics 46 (1): 165–6. doi:10.1006/geno.1997.4994. PMID 9403076.
Malhotra JD, Tsiotra P, Karagogeos D, Hortsch M (1999). "Cis-activation of L1-mediated ankyrin recruitment by TAG-1 homophilic cell adhesion". J. Biol. Chem. 273 (50): 33354–9. doi:10.1074/jbc.273.50.33354. PMID 9837910.
Freigang J, Proba K, Leder L, et al. (2000). "The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion". Cell 101 (4): 425–33. doi:10.1016/S0092-8674(00)80852-1. PMID 10830169.
Rickman DS, Tyagi R, Zhu XX, et al. (2001). "The gene for the axonal cell adhesion molecule TAX-1 is amplified and aberrantly expressed in malignant gliomas". Cancer Res. 61 (5): 2162–8. PMID 11280781.
Pavlou O, Theodorakis K, Falk J, et al. (2002). "Analysis of interactions of the adhesion molecule TAG-1 and its domains with other immunoglobulin superfamily members". Mol. Cell. Neurosci. 20 (3): 367–81. doi:10.1006/mcne.2002.1105. PMID 12139915.
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.
Traka M, Goutebroze L, Denisenko N, et al. (2003). "Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers". J. Cell Biol. 162 (6): 1161–72. doi:10.1083/jcb.200305078. PMC 2172849. PMID 12975355. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172849.
Nagaraja GM, Kandpal RP (2004). "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins". Biochem. Biophys. Res. Commun. 313 (3): 654–65. doi:10.1016/j.bbrc.2003.12.001. PMID 14697242.

CNTN2

Interactions

References

Further reading