Tau protein

MAPT
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1I8H, 4GLR, 2ON9, 3OVL, 4E0M, 4E0N, 4E0O, 4FL5, 4NP8, 2MZ7, 4TQE, 4Y5I, 4Y32, 5DMG, 4Y3B, 5HF3, 5E2W, 5E2V
Identifiers
Aliases	MAPT, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND, PPP1R103, TAU, microtubule associated protein tau, Tau proteins, tau-40
External IDs	OMIM: 157140 MGI: 97180 HomoloGene: 74962 GeneCards: MAPT
Gene location (Human)
Chr.	Chromosome 17 (human)
End	46,028,334 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	104,332,090 bp
RNA expression pattern
	Top expressed in
	superior frontal gyrus; ; prefrontal cortex; ; Brodmann area 9; ; hypothalamus; ; hippocampus proper; ; temporal lobe; ; amygdala; ; putamen; ; corpus callosum; ; caudate nucleus;
	Top expressed in
	ventromedial nucleus; ; mammillary body; ; lateral hypothalamus; ; temporal lobe; ; entorhinal cortex; ; lateral geniculate nucleus; ; superior colliculus; ; amygdala; ; visual cortex; ; dorsal tegmental nucleus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	apolipoprotein binding; SH3 domain binding; tubulin binding; protein binding; lipoprotein particle binding; enzyme binding; DNA binding; actin binding; microtubule binding; dynactin binding; receptor ligand activity; protein phosphatase 2A binding; Hsp90 protein binding; minor groove of adenine-thymine-rich DNA binding; double-stranded DNA binding; single-stranded DNA binding; RNA binding; protein kinase binding; protein-macromolecule adaptor activity; phosphatidylinositol binding; identical protein binding; protein homodimerization activity; sequence-specific DNA binding; chaperone binding; histone-dependent DNA binding; microtubule lateral binding; phosphatidylinositol bisphosphate binding;
Cellular component	cytoplasm; cell body; cell projection; nuclear periphery; growth cone; neurofibrillary tangle; plasma membrane; tubulin complex; dendrite; cytoplasmic ribonucleoprotein granule; cytoskeleton; nucleus; cytosol; microtubule; microtubule associated complex; membrane; nuclear speck; axon; somatodendritic compartment; neuronal cell body; axon cytoplasm; extracellular region; intracellular anatomical structure; mitochondrion; microtubule cytoskeleton; axolemma; neuron projection; dendritic spine; main axon; membrane raft; glial cell projection;
Biological process	generation of neurons; regulation of autophagy; regulation of microtubule polymerization; positive regulation of microtubule polymerization; positive regulation of axon extension; microtubule cytoskeleton organization; microglial cell activation; activation of cysteine-type endopeptidase activity involved in apoptotic process; signal transduction; memory; negative regulation of mitochondrial membrane potential; axonal transport of mitochondrion; cytoplasmic microtubule organization; neuron projection development; positive regulation of superoxide anion generation; negative regulation of kinase activity; cellular response to heat; astrocyte activation; intracellular distribution of mitochondria; synapse organization; regulation of calcium-mediated signaling; protein complex oligomerization; plus-end-directed organelle transport along microtubule; regulation of mitochondrial fission; negative regulation of mitochondrial fission; axonal transport; regulation of cellular response to heat; positive regulation of neuron death; positive regulation of protein localization to synapse; neurofibrillary tangle assembly; negative regulation of establishment of protein localization to mitochondrion; positive regulation of diacylglycerol kinase activity; regulation of response to DNA damage stimulus; internal protein amino acid acetylation; cell-cell signaling; response to lead ion; regulation of signaling receptor activity; negative regulation of gene expression; rRNA metabolic process; central nervous system neuron development; regulation of microtubule polymerization or depolymerization; regulation of chromosome organization; stress granule assembly; cellular response to reactive oxygen species; microtubule polymerization; regulation of synaptic plasticity; axon development; regulation of microtubule cytoskeleton organization; supramolecular fiber organization; regulation of long-term synaptic depression; positive regulation of protein localization; negative regulation of tubulin deacetylation; amyloid fibril formation; cellular response to nerve growth factor stimulus; cellular response to brain-derived neurotrophic factor stimulus;
	Sources:Amigo / QuickGO
Orthologs
	4137
	17762
	ENSG00000186868; ENSG00000276155; ENSG00000277956
	ENSMUSG00000018411
	P10636
	P10637
NM_001123066; NM_001123067; NM_001203251; NM_001203252; NM_005910;
	NM_016834; NM_016835; NM_016841; NM_001377265; NM_001377266; NM_001377267; NM_001377268
	NM_001038609; NM_010838; NM_001285454; NM_001285455; NM_001285456
NP_001116538; NP_001116539; NP_001190180; NP_001190181; NP_005901;
	NP_058518; NP_058519; NP_058525; NP_001364194; NP_001364195; NP_001364196; NP_001364197
NP_001033698; NP_001272383; NP_001272384; NP_001272385; NP_034968;
	NP_001390904; NP_001390905; NP_001390906; NP_001390907; NP_001390908; NP_001390909; NP_001390910; NP_001390911; NP_001390912; NP_001390913; NP_001390916; NP_001390919; NP_001390921; NP_001390923; NP_001390925; NP_001390927; NP_001390928; NP_001390931; NP_001390933; NP_001390934; NP_001390935; NP_001390939; NP_001390940; NP_001390941; NP_001390943; NP_001390944; NP_001390945
	Wikidata
View/Edit Human	View/Edit Mouse

The tau proteins (abbreviated from tubulin associated unit) are a group of six highly soluble protein isoforms produced by alternative splicing from the gene MAPT (microtubule-associated protein tau). They have roles primarily in maintaining the stability of microtubules in axons and are abundant in the neurons of the central nervous system (CNS), where the cerebral cortex has the highest abundance. They are less common elsewhere but are also expressed at very low levels in CNS astrocytes and oligodendrocytes.

Pathologies and dementias of the nervous system such as Alzheimer's disease and Parkinson's disease are associated with tau proteins that have become hyperphosphorylated insoluble aggregates called neurofibrillary tangles. The tau proteins were identified in 1975 as heat-stable proteins essential for microtubule assembly, and since then they have been characterized as intrinsically disordered proteins.

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