Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Mapt. (This text reflects annotations as of Tuesday, May 21, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of January 19, 2011. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Mapt
  • participates in the following biological processes:
    • regulation of microtubule-based movement ^[4]
  • performs the following molecular functions:
    • microtubule binding ^[4]
  • is located in the following cellular components:
    • axon ^{[1, 2, 5]}
    • cilium axoneme ^[9]
    • cytoplasm ^[3]
    • microtubule ^[5]
    • nucleus ^[3]
• The gene product of Mapt has been shown to bind to the gene products of Ppp3ca, Ywhaz. ^{[13, 14, 16]} Researchers have inferred, based on physical interactions, that the gene product of Mapt
  • performs the following molecular functions:
    • protein kinase binding ^[11]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Mapt
  • participates in the following biological processes:
    • axon extension ^{[7, 10]}
    • microtubule cytoskeleton organization ^[8]
    • mitochondrion transport along microtubule ^[10]
    • negative regulation of intracellular transport ^[10]
    • neuron migration ^[6]
    • positive regulation of axon extension ^{[3, 10]}
• Researchers have inferred, based on genetic interactions, that the gene product of Mapt
  • participates in the following biological processes:
    • adult walking behavior based on interactions with Npc1 ^[12]
    • axon cargo transport based on interactions with App ^[15]
    • axonogenesis based on interactions with Map1b ^[7]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Mapt:
  • participates in the following biological processes:
    • apoptotic process
    • microtubule cytoskeleton organization
    • positive regulation of axon extension
    • positive regulation of microtubule polymerization
    • regulation of autophagy
    • response to nutrient
    • response to organic substance
  • performs the following molecular functions:
    • apolipoprotein binding
    • enzyme binding
    • lipoprotein particle binding
    • microtubule binding
    • protein domain specific binding
    • protein kinase binding
    • SH3 domain binding
  • is located in the following cellular components:
    • axon
    • axonal growth cone
    • growth cone
    • neuron projection
    • nuclear periphery
    • plasma membrane
    • tubulin complex

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Summary text based on GO annotations supported by structural data

• Mapt encodes a protein or proteins that contain the following InterPro domains: Microtubule associated protein MAP2/MAP4/Tau, Tau and MAP proteins tubulin-binding repeat, Tau protein, indicating that the gene product:
  • performs the following molecular functions:
    • tubulin binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Mapt indicates that it:
  • is located in the following cellular components:
    • cell projection
    • cytoskeleton
    • membrane

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References

1. Bretin S et al. (2005) Differential expression of CRMP1, CRMP2A, CRMP2B, and CRMP5 in axons or dendrites of distinct neurons in the mouse brain. J Comp Neurol, 486:1-17. (PubMed:15834957)
2. Brion JP et al. (1988) Dendritic and axonal distribution of the microtubule-associated proteins MAP2 and tau in the cerebellum of the nervous mutant mouse. Brain Res Dev Brain Res, 44:221-32. (PubMed:3147150)
3. de Barreda EG et al. (2010) Tau deficiency leads to the upregulation of BAF-57, a protein involved in neuron-specific gene repression. FEBS Lett, 584:2265-70. (PubMed:20338169)
4. Dixit R et al. (2008) Differential regulation of dynein and kinesin motor proteins by tau. Science, 319:1086-9. (PubMed:18202255)
5. Fukami S et al. (2002) Abeta-degrading endopeptidase, neprilysin, in mouse brain: synaptic and axonal localization inversely correlating with Abeta pathology. Neurosci Res, 43:39-56. (PubMed:12074840)
6. Fuster-Matanzo A et al. (2009) Function of tau protein in adult newborn neurons. FEBS Lett, 583:3063-8. (PubMed:19695252)
7. Gonzalez-Billault C et al. (2002) Participation of structural microtubule-associated proteins (MAPs) in the development of neuronal polarity. J Neurosci Res, 67:713-9. (PubMed:11891784)
8. Harada A et al. (1994) Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature, 369:488-91. (PubMed:8202139)
9. Hoover AN et al. (2008) C2cd3 is required for cilia formation and Hedgehog signaling in mouse. Development, 135:4049-58. (PubMed:19004860)
10. Jimenez-Mateos EM et al. (2006) Role of MAP1B in axonal retrograde transport of mitochondria. Biochem J, 397:53-9. (PubMed:16536727)
11. Li D et al. (2010) Direct association of Sprouty-related protein with an EVH1 domain (SPRED) 1 or SPRED2 with DYRK1A modifies substrate/kinase interactions. J Biol Chem, 285:35374-85. (PubMed:20736167)
12. Pacheco CD et al. (2009) Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis. Hum Mol Genet, 18:956-65. (PubMed:19074461)
13. Sadik G et al. (2009) Phosphorylation of tau at Ser214 mediates its interaction with 14-3-3 protein: implications for the mechanism of tau aggregation. J Neurochem, 108:33-43. (PubMed:19014373)
14. Vega IE et al. (2008) A novel calcium-binding protein is associated with tau proteins in tauopathy. J Neurochem, 106:96-106. (PubMed:18346207)
15. Vossel KA et al. (2010) Tau reduction prevents Abeta-induced defects in axonal transport. Science, 330:198. (PubMed:20829454)
16. Yu DY et al. (2008) Tau binds both subunits of calcineurin, and binding is impaired by calmodulin. Biochim Biophys Acta, 1783:2255-61. (PubMed:18639592)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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