MGI:Tnr

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0005102	receptor binding	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR002181 InterPro:IPR014716 InterPro:IPR014715	F	From MGI
	GO:0005178	integrin binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:Q05546	F	From MGI
	GO:0005576	extracellular region	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0964	C	From MGI
	GO:0005578	proteinaceous extracellular matrix	MGI:MGI:3836851 PMID:19141078^[1]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005578	proteinaceous extracellular matrix	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:Q05546	C	From MGI
	GO:0005578	proteinaceous extracellular matrix	MGI:MGI:67553 PMID:7530142^[2]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92752	C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92752	C	From MGI
	GO:0007155	cell adhesion	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0130	P	From MGI
	GO:0007158	neuron cell-cell adhesion	MGI:MGI:3629017 PMID:15034584^[3]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0007162	negative regulation of cell adhesion	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:Q05546	P	From MGI
	GO:0007165	signal transduction	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR002181 InterPro:IPR014716 InterPro:IPR014715	P	From MGI
	GO:0008306	associative learning	MGI:MGI:3605565 PMID:12882316^[4]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0009986	cell surface	MGI:MGI:2181238 PMID:12056833^[5]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0010977	negative regulation of neuron projection development	MGI:MGI:1101253 PMID:9405406^[6]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0022029	telencephalon cell migration	MGI:MGI:3629017 PMID:15034584^[3]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0022408	negative regulation of cell-cell adhesion	MGI:MGI:3629017 PMID:15034584^[3]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0022408	negative regulation of cell-cell adhesion	MGI:MGI:3655167 PMID:16831557^[7]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0030198	extracellular matrix organization	MGI:MGI:1337730 PMID:10341229^[8]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0030198	extracellular matrix organization	MGI:MGI:1927381 PMID:11077416^[9]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0030198	extracellular matrix organization	MGI:MGI:3652670 PMID:16870730^[10]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0030517	negative regulation of axon extension	MGI:MGI:3655167 PMID:16831557^[7]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0035641	locomotory exploration behavior	MGI:MGI:3529716 PMID:14529817^[11]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0045121	membrane raft	MGI:MGI:2181238 PMID:12056833^[5]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0046625	sphingolipid binding	MGI:MGI:2181238 PMID:12056833^[5]	TAS: Traceable Author Statement		F	From MGI
	GO:0048692	negative regulation of axon extension involved in regeneration	MGI:MGI:3652670 PMID:16870730^[10]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0050804	regulation of synaptic transmission	MGI:MGI:2677542 PMID:11377840^[12]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0050805	negative regulation of synaptic transmission	MGI:MGI:3039956 PMID:15033179^[13]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0050808	synapse organization	MGI:MGI:3608232 PMID:16262627^[14]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0050885	neuromuscular process controlling balance	MGI:MGI:3605565 PMID:12882316^[4]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0051968	positive regulation of synaptic transmission, glutamatergic	MGI:MGI:3762112 PMID:11161481^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0051971	positive regulation of transmission of nerve impulse	MGI:MGI:1337730 PMID:10341229^[8]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0060291	long-term synaptic potentiation	MGI:MGI:3712708 PMID:17537973^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0060291	long-term synaptic potentiation	MGI:MGI:3762112 PMID:11161481^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154583	P	From MGI
	GO:0072534	perineuronal net	MGI:MGI:1337730 PMID:10341229^[8]	IDA: Inferred from Direct Assay		C	From MGI
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Bekku Y et al. (2009) Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS. J Neurochem 108: 1266-76 PubMed GONUTS page
↑ Schachner M et al. (1994) The perplexing multifunctionality of janusin, a tenascin-related molecule. Perspect Dev Neurobiol 2: 33-41 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Saghatelyan A et al. (2004) Tenascin-R mediates activity-dependent recruitment of neuroblasts in the adult mouse forebrain. Nat Neurosci 7: 347-56 PubMed GONUTS page
↑ ^4.0 ^4.1 Montag-Sallaz M & Montag D (2003) Severe cognitive and motor coordination deficits in tenascin-R-deficient mice. Genes Brain Behav 2: 20-31 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Kappler J et al. (2002) Tenascins are associated with lipid rafts isolated from mouse brain. Biochem Biophys Res Commun 294: 742-7 PubMed GONUTS page
↑ Xiao ZC et al. (1997) Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan. J Biol Chem 272: 32092-101 PubMed GONUTS page
↑ ^7.0 ^7.1 Pesheva P et al. (2006) Early coevolution of adhesive but not antiadhesive tenascin-R ligand-receptor pairs in vertebrates: a phylogenetic study. Mol Cell Neurosci 32: 366-86 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Weber P et al. (1999) Mice deficient for tenascin-R display alterations of the extracellular matrix and decreased axonal conduction velocities in the CNS. J Neurosci 19: 4245-62 PubMed GONUTS page
↑ Brückner G et al. (2000) Postnatal development of perineuronal nets in wild-type mice and in a mutant deficient in tenascin-R. J Comp Neurol 428: 616-29 PubMed GONUTS page
↑ ^10.0 ^10.1 Apostolova I et al. (2006) Tenascin-R restricts posttraumatic remodeling of motoneuron innervation and functional recovery after spinal cord injury in adult mice. J Neurosci 26: 7849-59 PubMed GONUTS page
↑ Freitag S et al. (2003) Behavioral alterations in mice deficient for the extracellular matrix glycoprotein tenascin-R. Behav Brain Res 145: 189-207 PubMed GONUTS page
↑ Bukalo O et al. (2001) Modification of extracellular matrix by enzymatic removal of chondroitin sulfate and by lack of tenascin-R differentially affects several forms of synaptic plasticity in the hippocampus. Neuroscience 104: 359-69 PubMed GONUTS page
↑ Gurevicius K et al. (2004) Enhanced cortical and hippocampal neuronal excitability in mice deficient in the extracellular matrix glycoprotein tenascin-R. Mol Cell Neurosci 25: 515-23 PubMed GONUTS page
↑ Syková E et al. (2005) Reduced extracellular space in the brain of tenascin-R- and HNK-1-sulphotransferase deficient mice. Eur J Neurosci 22: 1873-80 PubMed GONUTS page
↑ ^15.0 ^15.1 Saghatelyan AK et al. (2001) Reduced perisomatic inhibition, increased excitatory transmission, and impaired long-term potentiation in mice deficient for the extracellular matrix glycoprotein tenascin-R. Mol Cell Neurosci 17: 226-40 PubMed GONUTS page
↑ Bukalo O et al. (2007) Hippocampal metaplasticity induced by deficiency in the extracellular matrix glycoprotein tenascin-R. J Neurosci 27: 6019-28 PubMed GONUTS page

[PMID:19141078-0] Bekku Y et al. (2009) Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS. J Neurochem 108: 1266-76 PubMed GONUTS page

[PMID:7530142-1] Schachner M et al. (1994) The perplexing multifunctionality of janusin, a tenascin-related molecule. Perspect Dev Neurobiol 2: 33-41 PubMed GONUTS page

[PMID:15034584-2] 3.0 ^3.1 ^3.2 Saghatelyan A et al. (2004) Tenascin-R mediates activity-dependent recruitment of neuroblasts in the adult mouse forebrain. Nat Neurosci 7: 347-56 PubMed GONUTS page

[PMID:12882316-3] 4.0 ^4.1 Montag-Sallaz M & Montag D (2003) Severe cognitive and motor coordination deficits in tenascin-R-deficient mice. Genes Brain Behav 2: 20-31 PubMed GONUTS page

[PMID:12056833-4] 5.0 ^5.1 ^5.2 Kappler J et al. (2002) Tenascins are associated with lipid rafts isolated from mouse brain. Biochem Biophys Res Commun 294: 742-7 PubMed GONUTS page

[PMID:9405406-5] Xiao ZC et al. (1997) Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan. J Biol Chem 272: 32092-101 PubMed GONUTS page

[PMID:16831557-6] 7.0 ^7.1 Pesheva P et al. (2006) Early coevolution of adhesive but not antiadhesive tenascin-R ligand-receptor pairs in vertebrates: a phylogenetic study. Mol Cell Neurosci 32: 366-86 PubMed GONUTS page

[PMID:10341229-7] 8.0 ^8.1 ^8.2 Weber P et al. (1999) Mice deficient for tenascin-R display alterations of the extracellular matrix and decreased axonal conduction velocities in the CNS. J Neurosci 19: 4245-62 PubMed GONUTS page

[PMID:11077416-8] Brückner G et al. (2000) Postnatal development of perineuronal nets in wild-type mice and in a mutant deficient in tenascin-R. J Comp Neurol 428: 616-29 PubMed GONUTS page

[PMID:16870730-9] 10.0 ^10.1 Apostolova I et al. (2006) Tenascin-R restricts posttraumatic remodeling of motoneuron innervation and functional recovery after spinal cord injury in adult mice. J Neurosci 26: 7849-59 PubMed GONUTS page

[PMID:14529817-10] Freitag S et al. (2003) Behavioral alterations in mice deficient for the extracellular matrix glycoprotein tenascin-R. Behav Brain Res 145: 189-207 PubMed GONUTS page

[PMID:11377840-11] Bukalo O et al. (2001) Modification of extracellular matrix by enzymatic removal of chondroitin sulfate and by lack of tenascin-R differentially affects several forms of synaptic plasticity in the hippocampus. Neuroscience 104: 359-69 PubMed GONUTS page

[PMID:15033179-12] Gurevicius K et al. (2004) Enhanced cortical and hippocampal neuronal excitability in mice deficient in the extracellular matrix glycoprotein tenascin-R. Mol Cell Neurosci 25: 515-23 PubMed GONUTS page

[PMID:16262627-13] Syková E et al. (2005) Reduced extracellular space in the brain of tenascin-R- and HNK-1-sulphotransferase deficient mice. Eur J Neurosci 22: 1873-80 PubMed GONUTS page

[PMID:11161481-14] 15.0 ^15.1 Saghatelyan AK et al. (2001) Reduced perisomatic inhibition, increased excitatory transmission, and impaired long-term potentiation in mice deficient for the extracellular matrix glycoprotein tenascin-R. Mol Cell Neurosci 17: 226-40 PubMed GONUTS page

[PMID:17537973-15] Bukalo O et al. (2007) Hippocampal metaplasticity induced by deficiency in the extracellular matrix glycoprotein tenascin-R. J Neurosci 27: 6019-28 PubMed GONUTS page

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Tnr ( synonyms: J1-tenascin, janusin, restrictin, TN-R )
Protein Name(s)	tenascin R,
External Links
MGI	MGI:99516

MGI:Tnr

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