MAPT
entrez
4137
canonical
uniprot
P10636
canonical
ensembl
ENSG00000186868
resolver
ensembl
ENSG00000276155
resolver
ensembl
ENSG00000277956
resolver
ensp
ENSP00000262410
resolver
ensp
ENSP00000303214
resolver
ensp
ENSP00000334886
resolver
ensp
ENSP00000340820
resolver
ensp
ENSP00000389250
resolver
ensp
ENSP00000408975
resolver
ensp
ENSP00000410838
resolver
ensp
ENSP00000413056
resolver
ensp
ENSP00000443028
resolver
ensp
ENSP00000458742
resolver
ensp
ENSP00000554836
resolver
ensp
ENSP00000554837
resolver
ensp
ENSP00000554838
resolver
ensp
ENSP00000554840
resolver
ensp
ENSP00000554841
resolver
ensp
ENSP00000554842
resolver
ensp
ENSP00000554843
resolver
ensp
ENSP00000554846
resolver
ensp
ENSP00000642170
resolver
ensp
ENSP00000642171
resolver
ensp
ENSP00000642174
resolver
enst
ENST00000262410
resolver
enst
ENST00000344290
resolver
enst
ENST00000884784
resolver
genesymbol
MAPT
resolver
genesymbol_syn
MAPTL
resolver
genesymbol_syn
MTBT1
resolver
genesymbol_syn
TAU
resolver
hgnc
HGNC:6893
resolver
uniprot
A0A7I2PJZ2
resolver
uniprot
A0A7I2PLE3
resolver
uniprot
B3KTM0
resolver
uniprot
P18518
resolver
uniprot
Q14799
resolver
uniprot
Q15549
resolver
uniprot
Q15550
resolver
uniprot
Q15551
resolver
uniprot
Q1RMF6
resolver
uniprot
Q53YB1
resolver
uniprot
Q5CZI7
resolver
uniprot
Q5XWF0
resolver
uniprot
Q6QT54
resolver
uniprot
Q9UDJ3
resolver
uniprot
Q9UMH0
resolver
uniprot
Q9UQ96
resolver
uniprot_entry
A0A7I2PJZ2_HUMAN
resolver
uniprot_entry
A0A7I2PLE3_HUMAN
resolver
uniprot_entry
B3KTM0_HUMAN
resolver
uniprot_entry
TAU_HUMAN
resolver
uniprot_sec
P18518
resolver
uniprot_sec
Q14799
resolver
uniprot_sec
Q15549
resolver
uniprot_sec
Q15550
resolver
uniprot_sec
Q15551
resolver
uniprot_sec
Q1RMF6
resolver
uniprot_sec
Q53YB1
resolver
uniprot_sec
Q5CZI7
resolver
uniprot_sec
Q5XWF0
resolver
uniprot_sec
Q6QT54
resolver
uniprot_sec
Q9UDJ3
resolver
uniprot_sec
Q9UMH0
resolver
uniprot_sec
Q9UQ96
resolver
amino_acid_sequence
MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
uniprot
proteins
disease_involvement
DISEASE: Note=In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). O-GlcNAcylation is greatly reduced in Alzheimer disease brain cerebral cortex leading to an increase in TAU/MAPT phosphorylations. {ECO:0000269|PubMed:14517953, ECO:0000269|PubMed:26086902}.; DISEASE: Frontotemporal dementia 1 (FTD1) [MIM:600274]: A form of dementia characterized by pathologic finding of frontotemporal lobar degeneration, presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. {ECO:0000269|PubMed:10208578, ECO:0000269|PubMed:10214944, ECO:0000269|PubMed:10374757, ECO:0000269|PubMed:10489057, ECO:0000269|PubMed:10553987, ECO:0000269|PubMed:10802785, ECO:0000269|PubMed:11071507, ECO:0000269|PubMed:11117541, ECO:0000269|PubMed:11278002, ECO:0000269|PubMed:11585254, ECO:0000269|PubMed:11889249, ECO:0000269|PubMed:11906000, ECO:0000269|PubMed:11921059, ECO:0000269|PubMed:12473774, ECO:0000269|PubMed:12509859, ECO:0000269|PubMed:14517953, ECO:0000269|PubMed:15883319, ECO:0000269|PubMed:16240366, ECO:0000269|PubMed:26086902, ECO:0000269|PubMed:32961270, ECO:0000269|PubMed:9629852, ECO:0000269|PubMed:9641683, ECO:0000269|PubMed:9736786, ECO:0000269|PubMed:9789048, ECO:0000269|PubMed:9973279}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pick disease of the brain (PIDB) [MIM:172700]: A rare form of dementia pathologically defined by severe atrophy, neuronal loss and gliosis. It is characterized by the occurrence of tau-positive inclusions, swollen neurons (Pick cells) and argentophilic neuronal inclusions known as Pick bodies that disproportionally affect the frontal and temporal cortical regions. Clinical features include aphasia, apraxia, confusion, anomia, memory loss and personality deterioration. {ECO:0000269|PubMed:10604746, ECO:0000269|PubMed:11089577, ECO:0000269|PubMed:11117542, ECO:0000269|PubMed:11601501, ECO:0000269|PubMed:11891833}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease.; DISEASE: Progressive supranuclear palsy 1 (PSNP1) [MIM:601104]: Characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613. {ECO:0000269|PubMed:10534245, ECO:0000269|PubMed:11220749, ECO:0000269|PubMed:12325083, ECO:0000269|PubMed:14991828, ECO:0000269|PubMed:14991829, ECO:0000269|PubMed:16157753}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Parkinson-dementia syndrome (PARDE) [MIM:260540]: A syndrome characterized by parkinsonism, tremor, rigidity, dementia, ophthalmoparesis and pyramidal signs. Neurofibrillary degeneration occurs in the hippocampus, basal ganglia and brainstem nuclei. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:32961270}.
uniprot
proteins
mass_dalton
78928
uniprot
proteins
mutagenesis
MUTAGEN 515; /note="S->E: No association with plasma membrane."; MUTAGEN 516; /note="S->E: No association with plasma membrane."; MUTAGEN 519; /note="S->E: No association with plasma membrane."; MUTAGEN 531; /note="S->A: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein."; MUTAGEN 548; /note="T->A: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein."; MUTAGEN 548; /note="T->E: No association with plasma membrane."; MUTAGEN 552; /note="S->A: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein."; MUTAGEN 552; /note="S->E: No association with plasma membrane."; MUTAGEN 579; /note="S->A: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein."; MUTAGEN 713; /note="S->E: No association with plasma membrane."; MUTAGEN 721; /note="S->E: No association with plasma membrane."; MUTAGEN 726; /note="S->E: No association with plasma membrane."; MUTAGEN 730; /note="S->E: No association with plasma membrane."; MUTAGEN 739; /note="S->E: No association with plasma membrane.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3 or MARK4), causing detachment from microtubules, and their disassembly (PubMed:23666762, PubMed:7706316). Phosphorylation decreases with age. Phosphorylation within tau/MAP's repeat domain or in flanking regions seems to reduce tau/MAP's interaction with, respectively, microtubules or plasma membrane components (PubMed:7706316). Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis. Phosphorylation at Ser-548 by GSK3B reduces ability to bind and stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons. There is a reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces glycosylation by a factor of 2 and 4 respectively. Phosphorylation on Ser-721 is reduced by about 41.5% by GlcNAcylation on Ser-717. Dephosphorylated at several serine and threonine residues by the serine/threonine phosphatase PPP5C. {ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16982696, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860, ECO:0000269|PubMed:9614189}.; PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur. {ECO:0000250, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16443603}.; PTM: O-glycosylated. O-GlcNAcylation content is around 8.2%. There is reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces O-GlcNAcylation by a factor of 2 and 4 respectively. O-GlcNAcylation on Ser-717 decreases the phosphorylation on Ser-721 by about 41.5%. {ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189}.; PTM: Glycation of PHF-tau, but not normal brain TAU/MAPT. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD.
uniprot
proteins
pubmed
10208578
uniprot
proteins
pubmed
10214944
uniprot
proteins
pubmed
10374757
uniprot
proteins
pubmed
10412802
uniprot
proteins
pubmed
10489057
uniprot
proteins
pubmed
10534245
uniprot
proteins
pubmed
10553987
uniprot
proteins
pubmed
10604746
uniprot
proteins
pubmed
10747907
uniprot
proteins
pubmed
10802785
uniprot
proteins
pubmed
10899436
uniprot
proteins
pubmed
11071507
uniprot
proteins
pubmed
11089577
uniprot
proteins
pubmed
11117541
uniprot
proteins
pubmed
11117542
uniprot
proteins
pubmed
11220749
uniprot
proteins
pubmed
11278002
uniprot
proteins
pubmed
11313338
uniprot
proteins
pubmed
11585254
uniprot
proteins
pubmed
11601501
uniprot
proteins
pubmed
11889249
uniprot
proteins
pubmed
11891833
uniprot
proteins
pubmed
11906000
uniprot
proteins
pubmed
11921059
uniprot
proteins
pubmed
12325083
uniprot
proteins
pubmed
12473774
uniprot
proteins
pubmed
12509859
uniprot
proteins
pubmed
1420178
uniprot
proteins
pubmed
14517953
uniprot
proteins
pubmed
14595660
uniprot
proteins
pubmed
14690523
uniprot
proteins
pubmed
14761950
uniprot
proteins
pubmed
14991828
uniprot
proteins
pubmed
14991829
uniprot
proteins
pubmed
14999081
uniprot
proteins
pubmed
1512244
uniprot
proteins
pubmed
15365985
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15546861
uniprot
proteins
pubmed
15883319
uniprot
proteins
pubmed
15953362
uniprot
proteins
pubmed
16157753
uniprot
proteins
pubmed
16240366
uniprot
proteins
pubmed
16443603
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16923168
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
16982696
uniprot
proteins
pubmed
1713721
uniprot
proteins
pubmed
17562708
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18599021
uniprot
proteins
pubmed
1899488
uniprot
proteins
pubmed
1915258
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19451179
uniprot
proteins
pubmed
19542233
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20020531
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21327254
uniprot
proteins
pubmed
21985311
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23666762
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2484340
uniprot
proteins
pubmed
2495000
uniprot
proteins
pubmed
2498079
uniprot
proteins
pubmed
2516729
uniprot
proteins
pubmed
26014385
uniprot
proteins
pubmed
26086902
uniprot
proteins
pubmed
3131773
uniprot
proteins
pubmed
32272059
uniprot
proteins
pubmed
32296178
uniprot
proteins
pubmed
32961270
uniprot
proteins
pubmed
7706316
uniprot
proteins
pubmed
8999860
uniprot
proteins
pubmed
9326300
uniprot
proteins
pubmed
9614189
uniprot
proteins
pubmed
9629852
uniprot
proteins
pubmed
9641683
uniprot
proteins
pubmed
9735171
uniprot
proteins
pubmed
9736786
uniprot
proteins
pubmed
9789048
uniprot
proteins
pubmed
9973279
uniprot
proteins
sequence_length
758
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10747907, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:26014385}. Cell membrane {ECO:0000269|PubMed:10747907}; Peripheral membrane protein {ECO:0000269|PubMed:10747907}; Cytoplasmic side {ECO:0000269|PubMed:10747907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10747907}. Cell projection, axon {ECO:0000269|PubMed:10747907}. Cell projection, dendrite {ECO:0000269|PubMed:23666762}. Secreted {ECO:0000269|PubMed:32272059}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components (PubMed:10747907). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:10747907, ECO:0000269|PubMed:32272059}.
uniprot
proteins