Contactin 2

Protein found in humans
CNTN2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2OM5

Identifiers
AliasesCNTN2, AXT, FAME5, TAG-1, TAX, TAX1, contactin 2, transient axonal glycoprotein-1
External IDsOMIM: 190197; MGI: 104518; HomoloGene: 3720; GeneCards: CNTN2; OMA:CNTN2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CNTN2
Genomic location for CNTN2
Band1q32.1Start205,042,937 bp[1]
End205,078,289 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for CNTN2
Genomic location for CNTN2
Band1|1 E4Start132,437,165 bp[2]
End132,470,994 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • inferior ganglion of vagus nerve

  • C1 segment

  • corpus callosum

  • internal globus pallidus

  • subthalamic nucleus

  • pars reticulata

  • ventral tegmental area

  • superior vestibular nucleus

  • external globus pallidus

  • pons
Top expressed in
  • cerebellar cortex

  • superior frontal gyrus

  • primary visual cortex

  • trigeminal ganglion

  • cerebellar vermis

  • ganglionic eminence

  • lobe of cerebellum

  • central gray substance of midbrain

  • deep cerebellar nuclei

  • pontine nuclei
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein self-association
  • identical protein binding
  • carbohydrate binding
  • cell-cell adhesion mediator activity
Cellular component
  • membrane
  • myelin sheath
  • voltage-gated potassium channel complex
  • plasma membrane
  • node of Ranvier
  • synapse
  • integral component of plasma membrane
  • cell surface
  • axon
  • neuronal cell body
  • anchored component of membrane
  • neuron projection
  • juxtaparanode region of axon
  • anchored component of postsynaptic membrane
Biological process
  • clustering of voltage-gated potassium channels
  • negative regulation of neuron differentiation
  • central nervous system myelination
  • receptor internalization
  • neuron migration
  • learning
  • presynaptic membrane organization
  • regulation of astrocyte differentiation
  • regulation of axon diameter
  • cell adhesion
  • positive regulation of protein processing
  • establishment of protein localization to juxtaparanode region of axon
  • positive regulation of adenosine receptor signaling pathway
  • cerebral cortex GABAergic interneuron migration
  • regulation of neuronal synaptic plasticity
  • protein localization to juxtaparanode region of axon
  • regulation of cell morphogenesis involved in differentiation
  • neuron projection development
  • axonal fasciculation
  • microtubule cytoskeleton organization
  • adult walking behavior
  • axon guidance
  • nervous system development
  • homophilic cell adhesion via plasma membrane adhesion molecules
  • dendrite self-avoidance
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6900

21367

Ensembl

ENSG00000184144

ENSMUSG00000053024

UniProt

Q02246

Q61330

RefSeq (mRNA)

NM_005076
NM_001346083

NM_011531
NM_177129

RefSeq (protein)

NP_001333012
NP_005067

NP_796103

Location (UCSC)Chr 1: 205.04 – 205.08 MbChr 1: 132.44 – 132.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Contactin-2 is a protein that in humans is encoded by the CNTN2 gene.[5][6][7]

Function

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.[7]

Interactions

CNTN2 has been shown to interact with CNTNAP2[8] and NFYB.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184144 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000053024 – 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. ^ Tsiotra PC, Karagogeos D, Theodorakis K, Michaelidis TM, Modi WS, Furley AJ, Jessell TM, Papamatheakis J (Dec 1993). "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.
  6. ^ Yoshihara Y, Kawasaki M, Tamada A, Nagata S, Kagamiyama H, Mori K (Sep 1995). "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". Journal of Neurobiology. 28 (1): 51–69. doi:10.1002/neu.480280106. PMID 8586965.
  7. ^ a b "Entrez Gene: CNTN2 contactin 2 (axonal)".
  8. ^ Traka M, Goutebroze L, Denisenko N, Bessa M, Nifli A, Havaki S, Iwakura Y, Fukamauchi F, Watanabe K, Soliven B, Girault JA, Karagogeos D (Sep 2003). "Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers". The Journal of Cell Biology. 162 (6): 1161–72. doi:10.1083/jcb.200305078. PMC 2172849. PMID 12975355.
  9. ^ Pise-Masison CA, Dittmer J, Clemens KE, Brady JN (Mar 1997). "Physical and functional interaction between the human T-cell lymphotropic virus type 1 Tax1 protein and the CCAAT binding protein NF-Y". Molecular and Cellular Biology. 17 (3): 1236–43. doi:10.1128/mcb.17.3.1236. PMC 231848. PMID 9032250.

External links

Further reading

  • Walsh FS, Doherty P (Nov 1991). "Glycosylphosphatidylinositol anchored recognition molecules that function in axonal fasciculation, growth and guidance in the nervous system". Cell Biology International Reports. 15 (11): 1151–66. doi:10.1016/0309-1651(91)90061-M. PMID 1838307.
  • Kuhn TB, Stoeckli ET, Condrau MA, Rathjen FG, Sonderegger P (Nov 1991). "Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)". The Journal of Cell Biology. 115 (4): 1113–26. doi:10.1083/jcb.115.4.1113. PMC 2289947. PMID 1720120.
  • Dodd J, Morton SB, Karagogeos D, Yamamoto M, Jessell TM (Apr 1988). "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. S2CID 36629050.
  • Kenwrick S, Leversha M, Rooke L, Hasler T, Sonderegger P (Sep 1993). "Localization of the human TAX-1 gene to 1q32.1: a region implicated in microcephaly and Van der Woude syndrome" (PDF). Human Molecular Genetics. 2 (9): 1461–2. doi:10.1093/hmg/2.9.1461. PMID 8242070.
  • Rader C, Stoeckli ET, Ziegler U, Osterwalder T, Kunz B, Sonderegger P (Jul 1993). "Cell-cell adhesion by homophilic interaction of the neuronal recognition molecule axonin-1". European Journal of Biochemistry. 215 (1): 133–41. doi:10.1111/j.1432-1033.1993.tb18015.x. PMID 8344273.
  • Hasler TH, Rader C, Stoeckli ET, Zuellig RA, Sonderegger P (Jan 1993). "cDNA cloning, structural features, and eucaryotic expression of human TAG-1/axonin-1". European Journal of Biochemistry. 211 (1–2): 329–39. doi:10.1111/j.1432-1033.1993.tb19902.x. PMID 8425542.
  • Kozlov SV, Giger RJ, Hasler T, Korvatska E, Schorderet DF, Sonderegger P (Nov 1995). "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, Margolis RK, Margolis RU (Jun 1996). "TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM". The Journal of Biological Chemistry. 271 (26): 15716–23. doi:10.1074/jbc.271.26.15716. PMID 8663515.
  • Pise-Masison CA, Dittmer J, Clemens KE, Brady JN (Mar 1997). "Physical and functional interaction between the human T-cell lymphotropic virus type 1 Tax1 protein and the CCAAT binding protein NF-Y". Molecular and Cellular Biology. 17 (3): 1236–43. doi:10.1128/mcb.17.3.1236. PMC 231848. PMID 9032250.
  • Williams H, Schachner M, Wang B, Kenwrick S (Nov 1997). "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 (Dec 1998). "Cis-activation of L1-mediated ankyrin recruitment by TAG-1 homophilic cell adhesion". The Journal of Biological Chemistry. 273 (50): 33354–9. doi:10.1074/jbc.273.50.33354. PMID 9837910.
  • Freigang J, Proba K, Leder L, Diederichs K, Sonderegger P, Welte W (May 2000). "The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion" (PDF). Cell. 101 (4): 425–33. doi:10.1016/S0092-8674(00)80852-1. PMID 10830169. S2CID 15440572. Archived from the original (PDF) on 2018-07-19. Retrieved 2020-09-27.
  • Rickman DS, Tyagi R, Zhu XX, Bobek MP, Song S, Blaivas M, Misek DE, Israel MA, Kurnit DM, Ross DA, Kish PE, Hanash SM (Mar 2001). "The gene for the axonal cell adhesion molecule TAX-1 is amplified and aberrantly expressed in malignant gliomas". Cancer Research. 61 (5): 2162–8. PMID 11280781.
  • Pavlou O, Theodorakis K, Falk J, Kutsche M, Schachner M, Faivre-Sarrailh C, Karagogeos D (Jul 2002). "Analysis of interactions of the adhesion molecule TAG-1 and its domains with other immunoglobulin superfamily members". Molecular and Cellular Neurosciences. 20 (3): 367–81. doi:10.1006/mcne.2002.1105. PMID 12139915. S2CID 714233.
  • Traka M, Goutebroze L, Denisenko N, Bessa M, Nifli A, Havaki S, Iwakura Y, Fukamauchi F, Watanabe K, Soliven B, Girault JA, Karagogeos D (Sep 2003). "Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers". The Journal of Cell Biology. 162 (6): 1161–72. doi:10.1083/jcb.200305078. PMC 2172849. PMID 12975355.
  • Nagaraja GM, Kandpal RP (Jan 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". Biochemical and Biophysical Research Communications. 313 (3): 654–65. doi:10.1016/j.bbrc.2003.12.001. PMID 14697242.


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