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P10636

- TAU_HUMAN

UniProt

P10636 - TAU_HUMAN

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Protein

Microtubule-associated protein tau

Gene

MAPT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. 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. 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei24 – 241Not glycated
Sitei44 – 441Not glycated
Sitei67 – 671Not glycated
Sitei381 – 3811Not glycated
Sitei391 – 3911Not glycated
Sitei392 – 3921Not glycated
Sitei394 – 3941Not glycated
Sitei465 – 4651Not glycated
Sitei497 – 4971Not glycated
Sitei507 – 5071Not glycated
Sitei541 – 5411Not glycated
Sitei557 – 5571Not glycated
Sitei571 – 5711Not glycated
Sitei574 – 5741Not glycated
Sitei584 – 5841Not glycated
Sitei591 – 5911Not glycated
Sitei607 – 6071Not glycated
Sitei611 – 6111Not glycated
Sitei615 – 6151Not glycated
Sitei628 – 6281Not glycated
Sitei634 – 6341Not glycated
Sitei638 – 6381Not glycated
Sitei648 – 6481Not glycated
Sitei657 – 6571Not glycated
Sitei660 – 6601Not glycated
Sitei687 – 6871Not glycated
Sitei692 – 6921Not glycated
Sitei700 – 7001Not glycated
Sitei702 – 7021Not glycated
Sitei712 – 7121Not glycated
Sitei755 – 7551Not glycated

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. enzyme binding Source: UniProtKB
  3. lipoprotein particle binding Source: UniProtKB
  4. microtubule binding Source: UniProtKB
  5. SH3 domain binding Source: UniProtKB
  6. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. adult walking behavior Source: Ensembl
  2. apoptotic process Source: Reactome
  3. axon cargo transport Source: Ensembl
  4. axon extension Source: Ensembl
  5. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  6. generation of neurons Source: UniProtKB
  7. microtubule cytoskeleton organization Source: UniProtKB
  8. mitochondrion transport along microtubule Source: Ensembl
  9. negative regulation of intracellular transport Source: Ensembl
  10. neuron migration Source: Ensembl
  11. positive regulation of axon extension Source: UniProtKB
  12. positive regulation of microtubule polymerization Source: UniProtKB
  13. regulation of autophagy Source: MGI
  14. regulation of microtubule-based movement Source: Ensembl
  15. regulation of microtubule polymerization Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein tau
Alternative name(s):
Neurofibrillary tangle protein
Paired helical filament-tau
Short name:
PHF-tau
Gene namesi
Name:MAPT
Synonyms:MAPTL, MTBT1, TAU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6893. MAPT.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell projectionaxon 1 Publication
Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. axoneme Source: Ensembl
  3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  4. cytosol Source: Reactome
  5. growth cone Source: UniProtKB
  6. microtubule Source: UniProtKB-KW
  7. microtubule associated complex Source: ProtInc
  8. nuclear periphery Source: UniProtKB
  9. plasma membrane Source: UniProtKB
  10. tubulin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Frontotemporal dementia (FTD) [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.19 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → H in FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro. 1 Publication
Corresponds to variant rs63750959 [ dbSNP | Ensembl ].
VAR_019660
Natural varianti583 – 5831L → V in FTD; less able to promote microtubule assembly than wild-type tau. 1 Publication
VAR_019662
Natural varianti589 – 5891G → V in FTD. 2 Publications
VAR_010345
Natural varianti596 – 5961N → K in FTD; with parkinsonism. 5 Publications
VAR_010346
Natural varianti597 – 5971Missing in FTD. 1 Publication
VAR_010347
Natural varianti613 – 6131N → H in FTD; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level. 1 Publication
VAR_019663
Natural varianti618 – 6181P → L in FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments. 5 Publications
VAR_010348
Natural varianti618 – 6181P → S in FTD and CBD; reduction in the ability to promote microtubule assembly. 4 Publications
VAR_010349
Natural varianti622 – 6221S → N in FTD; minimal parkinsonism; very early age of onset. 1 Publication
VAR_010350
Natural varianti634 – 6341K → M in FTD. 1 Publication
VAR_037440
Natural varianti654 – 6541V → M in FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments. 2 Publications
VAR_010351
Natural varianti659 – 6591E → V in FTD. 1 Publication
VAR_019666
Natural varianti723 – 7231R → W in FTD/Alzheimer disease; accelerates aggregation of tau into filaments; reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms. 5 Publications
VAR_010353
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.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti574 – 5741K → T in PIDB; reduces the ability to promote microtubule assembly by 70%. 2 Publications
VAR_010344
Natural varianti637 – 6371S → F in PIDB; markedly reduced ability of tau to promote microtubule assembly. 1 Publication
VAR_019665
Natural varianti686 – 6861K → I in PIDB; 90% reduction in the rate of microtubule assembly. 1 Publication
VAR_019668
Natural varianti706 – 7061G → R in PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%. 2 Publications
VAR_010352
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.
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-613.6 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → L in PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau. 1 Publication
Corresponds to variant rs63750959 [ dbSNP | Ensembl ].
VAR_019661
Natural varianti285 – 2851D → N Risk factor for PSNP1. 2 Publications
Corresponds to variant rs62063786 [ dbSNP | Ensembl ].
VAR_010340
Natural varianti289 – 2891V → A Risk factor for PSNP1. 2 Publications
Corresponds to variant rs62063787 [ dbSNP | Ensembl ].
VAR_010341
Natural varianti613 – 6131Missing in PSNP1/atypical PSNP1; heterozygosity may be a risk factor for both a PSNP1-like syndrome and Parkinson disease; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level. 3 Publications
VAR_019664
Natural varianti620 – 6201G → V in PSNP1. 1 Publication
VAR_037439
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 mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi515 – 5151S → E: No association with plasma membrane.
Mutagenesisi516 – 5161S → E: No association with plasma membrane.
Mutagenesisi519 – 5191S → E: No association with plasma membrane.
Mutagenesisi531 – 5311S → A: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein.
Mutagenesisi548 – 5481T → A: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
Mutagenesisi548 – 5481T → E: No association with plasma membrane.
Mutagenesisi552 – 5521S → A: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
Mutagenesisi552 – 5521S → E: No association with plasma membrane.
Mutagenesisi579 – 5791S → A: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
Mutagenesisi713 – 7131S → E: No association with plasma membrane.
Mutagenesisi721 – 7211S → E: No association with plasma membrane.
Mutagenesisi726 – 7261S → E: No association with plasma membrane.
Mutagenesisi730 – 7301S → E: No association with plasma membrane.
Mutagenesisi739 – 7391S → E: No association with plasma membrane.

Keywords - Diseasei

Alzheimer disease, Disease mutation, Neurodegeneration, Parkinsonism

Organism-specific databases

MIMi157140. gene+phenotype.
172700. phenotype.
260540. phenotype.
600274. phenotype.
601104. phenotype.
Orphaneti275864. Behavioral variant of frontotemporal dementia.
240071. Classical progressive supranuclear palsy.
100070. Progressive non-fluent aphasia.
240103. Progressive supranuclear palsy - corticobasal syndrome.
240085. Progressive supranuclear palsy - parkinsonism.
240112. Progressive supranuclear palsy - progressive non fluent aphasia.
240094. Progressive supranuclear palsy - pure akinesia with gait freezing.
100069. Semantic dementia.
PharmGKBiPA238.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 758757Microtubule-associated protein tauPRO_0000072739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei18 – 181Phosphotyrosine; by FYN1 Publication
Modified residuei46 – 461Phosphoserine; by PDPK1
Modified residuei50 – 501Phosphothreonine; by PDPK1
Glycosylationi87 – 871N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei214 – 2141Phosphoserine; by SGK11 Publication
Glycosylationi383 – 3831N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei396 – 3961Phosphoserine; in PHF-tau1 Publication
Glycosylationi467 – 4671N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei470 – 4701Phosphothreonine; by PDPK11 Publication
Glycosylationi480 – 4801N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei484 – 4841Deamidated asparagine; in tau and PHF-tau; partial
Glycosylationi491 – 4911N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei492 – 4921Phosphothreonine; by PDPK1
Modified residuei498 – 4981Phosphothreonine; by PDPK11 Publication
Modified residuei514 – 5141Phosphotyrosine; by TTBK11 Publication
Modified residuei515 – 5151Phosphoserine; by PDPK1 and TTBK11 Publication
Modified residuei516 – 5161Phosphoserine; by PDPK1 and TTBK14 Publications
Modified residuei519 – 5191Phosphoserine; by CK1, PDPK1 and TTBK17 Publications
Modified residuei522 – 5221Phosphothreonine; by CK1 and PDPK13 Publications
Glycosylationi525 – 5251O-linked (GlcNAc)1 Publication
Modified residuei529 – 5291Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK15 Publications
Modified residuei531 – 5311Phosphoserine; by PKA4 Publications
Modified residuei534 – 5341Phosphothreonine; by PDPK12 Publications
Glycosylationi542 – 5421N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei548 – 5481Phosphothreonine; by GSK3-beta and PDPK13 Publications
Glycosylationi551 – 5511N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei552 – 5521Phosphoserine; by PDPK13 Publications
Modified residuei554 – 5541Phosphoserine; by PHK2 Publications
Glycosylationi555 – 5551O-linked (GlcNAc)1 Publication
Cross-linki571 – 571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau1 Publication
Glycosylationi576 – 5761N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei579 – 5791Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK7 Publications
Modified residuei596 – 5961Deamidated asparagine; in tau and PHF-tau; partial
Glycosylationi597 – 5971N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Glycosylationi598 – 5981N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei602 – 6021Phosphoserine; by PHK1 Publication
Modified residuei606 – 6061Phosphoserine; by PHK1 Publication
Disulfide bondi608 ↔ 639By similarity
Modified residuei610 – 6101Phosphoserine; by MARK1; in PHF-tau1 Publication
Modified residuei622 – 6221Phosphoserine; by MARK1; in PHF-tau1 Publication
Cross-linki628 – 628Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau1 Publication
Modified residuei641 – 6411Phosphoserine; by MARK1; in PHF-tau1 Publication
Glycosylationi664 – 6641N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei669 – 6691Phosphoserine; by PHK1 Publication
Glycosylationi670 – 6701N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Cross-linki670 – 670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau1 Publication
Modified residuei673 – 6731Phosphoserine; by MARK1; in PHF-tau1 Publication
Glycosylationi686 – 6861N-linked (Glc) (glycation); in PHF-tau; in vitro1 Publication
Modified residuei713 – 7131Phosphoserine; by CK1 and PDPK17 Publications
Modified residuei717 – 7171Phosphoserine; alternate2 Publications
Glycosylationi717 – 7171O-linked (GlcNAc); alternate1 Publication
Modified residuei720 – 7201Phosphothreonine
Modified residuei721 – 7211Phosphoserine; by CK1 and PDPK16 Publications
Modified residuei726 – 7261Phosphoserine2 Publications
Modified residuei733 – 7331Phosphoserine; by CaMK2 and TTBK11 Publication
Modified residuei739 – 7391Phosphoserine; by PDPK1 and TTBK14 Publications
Modified residuei744 – 7441Phosphothreonine; by TTBK11 Publication

Post-translational modificationi

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 or MARK2), causing detachment from microtubules, and their disassembly. 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. 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.12 Publications
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.By similarity2 Publications
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%.7 Publications
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.

Keywords - PTMi

Acetylation, Disulfide bond, Glycation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10636.
PaxDbiP10636.
PRIDEiP10636.

PTM databases

PhosphoSiteiP10636.

Miscellaneous databases

PMAP-CutDBP10636.

Expressioni

Tissue specificityi

Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

Developmental stagei

Four-repeat (type II) TAU/MAPT is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) TAU/MAPT is found in both adult and fetal brain.

Gene expression databases

BgeeiP10636.
ExpressionAtlasiP10636. baseline and differential.
GenevestigatoriP10636.

Organism-specific databases

HPAiCAB000151.

Interactioni

Subunit structurei

Interacts with PSMC2 through SQSTM1 By similarity. Interacts with SQSTM1 when polyubiquitinated. Interacts with FKBP4 By similarity. Binds to CSNK1D. Interacts with SGK1. Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-396.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APOEP026493EBI-366182,EBI-9209835
APPP050679EBI-366182,EBI-77613
BIN1O00499-15EBI-6926270,EBI-6926280
DCTN1Q142038EBI-366233,EBI-724352
GSK3BP498419EBI-366233,EBI-373586
HSP90AB1P082384EBI-366233,EBI-352572
LRRK2Q5S0079EBI-366233,EBI-5323863
PRNPP041562EBI-366182,EBI-977302
SLC1A2P430044EBI-366182,EBI-3440986
SNCAP378403EBI-366233,EBI-985879
STUB1Q9UNE72EBI-366182,EBI-357085
YWHAZP631049EBI-7145070,EBI-347088

Protein-protein interaction databases

BioGridi110308. 72 interactions.
DIPiDIP-29753N.
IntActiP10636. 35 interactions.
MINTiMINT-134394.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I8HNMR-A542-554[»]
2ON9X-ray1.51A/B623-628[»]
3OVLX-ray1.81A623-628[»]
4FL5X-ray1.90P/Q527-536[»]
4GLRX-ray1.90A/B541-557[»]
4NP8X-ray1.51A623-628[»]
DisProtiDP00126.
ProteinModelPortaliP10636.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati561 – 59131Tau/MAP 1Add
BLAST
Repeati592 – 62231Tau/MAP 2Add
BLAST
Repeati623 – 65331Tau/MAP 3Add
BLAST
Repeati654 – 68532Tau/MAP 4Add
BLAST

Domaini

The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.

Sequence similaritiesi

Contains 4 Tau/MAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG148882.
GeneTreeiENSGT00530000063491.
HOVERGENiHBG000991.
InParanoidiP10636.
KOiK04380.
OMAiMKVKGAD.
OrthoDBiEOG738045.
TreeFamiTF316358.

Family and domain databases

InterProiIPR027324. MAP2/MAP4/Tau.
IPR001084. MAP_tubulin-bd_rpt.
IPR002955. Tau.
[Graphical view]
PANTHERiPTHR11501. PTHR11501. 1 hit.
PfamiPF00418. Tubulin-binding. 4 hits.
[Graphical view]
PRINTSiPR01261. TAUPROTEIN.
PROSITEiPS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 9 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist. Isoforms differ from each other by the presence or absence of up to 5 of the 15 exons. One of these optional exons contains the additional tau/MAP repeat.

Isoform PNS-tau (identifier: P10636-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT
60 70 80 90 100
PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG
110 120 130 140 150
TTAEEAGIGD TPSLEDEAAG HVTQEPESGK VVQEGFLREP GPPGLSHQLM
160 170 180 190 200
SGMPGAPLLP EGPREATRQP SGTGPEDTEG GRHAPELLKH QLLGDLHQEG
210 220 230 240 250
PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA QDGRPPQTAA
260 270 280 290 300
REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE
310 320 330 340 350
FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD
360 370 380 390 400
LPEPSEKQPA AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS
410 420 430 440 450
AKTLKNRPCL SPKHPTPGSS DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG
460 470 480 490 500
SSGAKEMKLK GADGKTKIAT PRGAAPPGQK GQANATRIPA KTPPAPKTPP
510 520 530 540 550
SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP KKVAVVRTPP
560 570 580 590 600
KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD
610 620 630 640 650
LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG
660 670 680 690 700
GGQVEVKSEK LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK
710 720 730 740 750
AKTDHGAEIV YKSPVVSGDT SPRHLSNVSS TGSIDMVDSP QLATLADEVS

ASLAKQGL
Length:758
Mass (Da):78,928
Last modified:May 31, 2011 - v5
Checksum:iD46C66CDBCD196E8
GO
Isoform Fetal-tau (identifier: P10636-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-73: Missing.
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Show »
Length:352
Mass (Da):36,760
Checksum:i9B26AEDFF4D2677C
GO
Isoform Tau-A (identifier: P10636-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLK → MLRALQQRKR
     45-73: Missing.
     74-102: Missing.
     103-104: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Show »
Length:316
Mass (Da):32,944
Checksum:i4C86C95F53015575
GO
Isoform Tau-B (identifier: P10636-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Show »
Length:381
Mass (Da):39,720
Checksum:iEA206819FE73B67A
GO
Isoform Tau-C (identifier: P10636-5) [UniParc]FASTAAdd to Basket

Also known as: Tau-3

The sequence of this isoform differs from the canonical sequence as follows:
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Show »
Length:410
Mass (Da):42,603
Checksum:iA76B304E99E6A978
GO
Isoform Tau-D (identifier: P10636-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-73: Missing.
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.

Show »
Length:383
Mass (Da):40,007
Checksum:iF3256B0AB87B348D
GO
Isoform Tau-E (identifier: P10636-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.

Show »
Length:412
Mass (Da):42,967
Checksum:i0D4EABCA15179E7D
GO
Isoform Tau-F (identifier: P10636-8) [UniParc]FASTAAdd to Basket

Also known as: Tau-4

The sequence of this isoform differs from the canonical sequence as follows:
     125-375: Missing.
     395-460: Missing.

Show »
Length:441
Mass (Da):45,850
Checksum:i835A8706D847A8CC
GO
Isoform Tau-G (identifier: P10636-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     502-502: S → SATKQVQRRPPPAGPRSER

Note: No experimental confirmation available.

Show »
Length:776
Mass (Da):80,941
Checksum:i13E913ACD1790C26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481L → P in AAU45390. 1 PublicationCurated
Sequence conflicti414 – 4141H → L in AAC04277. (PubMed:1420178)Curated
Sequence conflicti557 – 5571K → M in AAS17881. 1 PublicationCurated
Sequence conflicti591 – 5911K → S in AAS17881. 1 PublicationCurated
Sequence conflicti617 – 6171V → Q AA sequence (PubMed:1915258)Curated
Sequence conflicti622 – 6221S → K AA sequence (PubMed:1915258)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → H in FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro. 1 Publication
Corresponds to variant rs63750959 [ dbSNP | Ensembl ].
VAR_019660
Natural varianti5 – 51R → L in PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau. 1 Publication
Corresponds to variant rs63750959 [ dbSNP | Ensembl ].
VAR_019661
Natural varianti17 – 171T → M.1 Publication
Corresponds to variant rs144611688 [ dbSNP | Ensembl ].
VAR_064622
Natural varianti30 – 301T → A.1 Publication
VAR_064623
Natural varianti285 – 2851D → N Risk factor for PSNP1. 2 Publications
Corresponds to variant rs62063786 [ dbSNP | Ensembl ].
VAR_010340
Natural varianti289 – 2891V → A Risk factor for PSNP1. 2 Publications
Corresponds to variant rs62063787 [ dbSNP | Ensembl ].
VAR_010341
Natural varianti370 – 3701R → W.
Corresponds to variant rs17651549 [ dbSNP | Ensembl ].
VAR_056121
Natural varianti441 – 4411Y → H.3 Publications
Corresponds to variant rs2258689 [ dbSNP | Ensembl ].
VAR_010342
Natural varianti447 – 4471S → P.1 Publication
Corresponds to variant rs10445337 [ dbSNP | Ensembl ].
VAR_010343
Natural varianti574 – 5741K → T in PIDB; reduces the ability to promote microtubule assembly by 70%. 2 Publications
VAR_010344
Natural varianti583 – 5831L → V in FTD; less able to promote microtubule assembly than wild-type tau. 1 Publication
VAR_019662
Natural varianti589 – 5891G → V in FTD. 2 Publications
VAR_010345
Natural varianti596 – 5961N → K in FTD; with parkinsonism. 5 Publications
VAR_010346
Natural varianti597 – 5971Missing in FTD. 1 Publication
VAR_010347
Natural varianti613 – 6131N → H in FTD; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level. 1 Publication
VAR_019663
Natural varianti613 – 6131Missing in PSNP1/atypical PSNP1; heterozygosity may be a risk factor for both a PSNP1-like syndrome and Parkinson disease; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level. 3 Publications
VAR_019664
Natural varianti617 – 6171V → I.1 Publication
Corresponds to variant rs116733906 [ dbSNP | Ensembl ].
VAR_064624
Natural varianti618 – 6181P → L in FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments. 5 Publications
VAR_010348
Natural varianti618 – 6181P → S in FTD and CBD; reduction in the ability to promote microtubule assembly. 4 Publications
VAR_010349
Natural varianti620 – 6201G → V in PSNP1. 1 Publication
VAR_037439
Natural varianti622 – 6221S → N in FTD; minimal parkinsonism; very early age of onset. 1 Publication
VAR_010350
Natural varianti634 – 6341K → M in FTD. 1 Publication
VAR_037440
Natural varianti637 – 6371S → F in PIDB; markedly reduced ability of tau to promote microtubule assembly. 1 Publication
VAR_019665
Natural varianti654 – 6541V → M in FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments. 2 Publications
VAR_010351
Natural varianti659 – 6591E → V in FTD. 1 Publication
VAR_019666
Natural varianti669 – 6691S → L in fatal respiratory hypoventilation; unusual apparent autosomal recessive inheritance; reduced binding to microtubules as well as increased fibrillization and aggregation. 1 Publication
VAR_019667
Natural varianti686 – 6861K → I in PIDB; 90% reduction in the rate of microtubule assembly. 1 Publication
VAR_019668
Natural varianti706 – 7061G → R in PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%. 2 Publications
VAR_010352
Natural varianti723 – 7231R → W in FTD/Alzheimer disease; accelerates aggregation of tau into filaments; reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms. 5 Publications
VAR_010353

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444MAEPR…DAGLK → MLRALQQRKR in isoform Tau-A. 1 PublicationVSP_003175Add
BLAST
Alternative sequencei45 – 7329Missing in isoform Tau-A, isoform Tau-D and isoform Fetal-tau. 5 PublicationsVSP_003176Add
BLAST
Alternative sequencei74 – 10229Missing in isoform Tau-A, isoform Tau-B, isoform Tau-D, isoform Tau-E and isoform Fetal-tau. 7 PublicationsVSP_003177Add
BLAST
Alternative sequencei103 – 1042Missing in isoform Tau-A. 1 PublicationVSP_003178
Alternative sequencei125 – 375251Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau. 7 PublicationsVSP_003179Add
BLAST
Alternative sequencei395 – 46066Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau. 7 PublicationsVSP_003180Add
BLAST
Alternative sequencei502 – 5021S → SATKQVQRRPPPAGPRSER in isoform Tau-G. CuratedVSP_026780
Alternative sequencei592 – 62231Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C and isoform Fetal-tau. 5 PublicationsVSP_003181Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03778 mRNA. Translation: AAA60615.1.
X14474 mRNA. Translation: CAA32636.1.
AF047863
, AF027491, AF047856, AF047857, AF027492, AF047858, AF027493, AF047859, AF047860, AF047862, AF027494, AF027495, AF027496 Genomic DNA. Translation: AAC04277.1.
AF027491
, AF027492, AF027493, AF047860, AF047862, AF027495, AF027496, AF047863 Genomic DNA. Translation: AAC04278.1.
AF027491
, AF047856, AF047857, AF027492, AF027493, AF047860, AF047862, AF027494, AF027495, AF027496, AF047863 Genomic DNA. Translation: AAC04279.1.
AF047861 Genomic DNA. No translation available.
AY730549 mRNA. Translation: AAU45390.1.
BT006772 mRNA. Translation: AAP35418.1.
AC004139 Genomic DNA. No translation available.
AC010792 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
AC217779 Genomic DNA. No translation available.
BC000558 mRNA. Translation: AAH00558.1.
BC098281 mRNA. Translation: AAH98281.1.
BC099721 mRNA. Translation: AAH99721.1.
BC101936 mRNA. Translation: AAI01937.1.
BC114504 mRNA. Translation: AAI14505.1.
BC114948 mRNA. Translation: AAI14949.1.
AY526356 mRNA. Translation: AAS17881.1.
M25298 mRNA. Translation: AAA57264.1.
BN000503 mRNA. Translation: CAG26750.1.
CCDSiCCDS11499.1. [P10636-8]
CCDS11500.1. [P10636-6]
CCDS11501.1. [P10636-1]
CCDS11502.1. [P10636-2]
CCDS45715.1. [P10636-9]
CCDS45716.1. [P10636-7]
CCDS56033.1. [P10636-5]
PIRiI52232.
JS0370. QRHUT1.
PN0001. QRHUT2.
S26663.
RefSeqiNP_001116538.2. NM_001123066.3. [P10636-9]
NP_001116539.1. NM_001123067.3. [P10636-7]
NP_001190181.1. NM_001203252.1. [P10636-5]
NP_005901.2. NM_005910.5. [P10636-8]
NP_058518.1. NM_016834.4. [P10636-6]
NP_058519.3. NM_016835.4. [P10636-1]
NP_058525.1. NM_016841.4. [P10636-2]
XP_006725337.1. XM_006725274.1. [P10636-6]
XP_006725338.1. XM_006725275.1. [P10636-2]
UniGeneiHs.101174.

Genome annotation databases

EnsembliENST00000262410; ENSP00000262410; ENSG00000186868. [P10636-1]
ENST00000334239; ENSP00000334886; ENSG00000186868. [P10636-2]
ENST00000340799; ENSP00000340438; ENSG00000186868. [P10636-7]
ENST00000344290; ENSP00000340820; ENSG00000186868. [P10636-9]
ENST00000351559; ENSP00000303214; ENSG00000186868. [P10636-8]
ENST00000415613; ENSP00000410838; ENSG00000186868. [P10636-9]
ENST00000420682; ENSP00000413056; ENSG00000186868. [P10636-7]
ENST00000431008; ENSP00000389250; ENSG00000186868. [P10636-5]
ENST00000446361; ENSP00000408975; ENSG00000186868. [P10636-6]
ENST00000535772; ENSP00000443028; ENSG00000186868. [P10636-5]
ENST00000571987; ENSP00000458742; ENSG00000186868. [P10636-1]
ENST00000574436; ENSP00000460965; ENSG00000186868. [P10636-8]
GeneIDi4137.
KEGGihsa:4137.
UCSCiuc002ijr.4. human. [P10636-1]
uc002ijs.4. human. [P10636-8]
uc002ijt.4. human. [P10636-6]
uc002iju.4. human. [P10636-2]
uc002ijx.4. human. [P10636-7]
uc010dau.3. human. [P10636-9]
uc021tyv.1. human. [P10636-5]
uc021tyw.1. human. [P10636-4]

Polymorphism databases

DMDMi334302961.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Alzforum

MAPT mutations

Protein Spotlight

Vita minima - Issue 68 of March 2006

Wikipedia

Tau protein entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03778 mRNA. Translation: AAA60615.1 .
X14474 mRNA. Translation: CAA32636.1 .
AF047863
, AF027491 , AF047856 , AF047857 , AF027492 , AF047858 , AF027493 , AF047859 , AF047860 , AF047862 , AF027494 , AF027495 , AF027496 Genomic DNA. Translation: AAC04277.1 .
AF027491
, AF027492 , AF027493 , AF047860 , AF047862 , AF027495 , AF027496 , AF047863 Genomic DNA. Translation: AAC04278.1 .
AF027491
, AF047856 , AF047857 , AF027492 , AF027493 , AF047860 , AF047862 , AF027494 , AF027495 , AF027496 , AF047863 Genomic DNA. Translation: AAC04279.1 .
AF047861 Genomic DNA. No translation available.
AY730549 mRNA. Translation: AAU45390.1 .
BT006772 mRNA. Translation: AAP35418.1 .
AC004139 Genomic DNA. No translation available.
AC010792 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
AC217779 Genomic DNA. No translation available.
BC000558 mRNA. Translation: AAH00558.1 .
BC098281 mRNA. Translation: AAH98281.1 .
BC099721 mRNA. Translation: AAH99721.1 .
BC101936 mRNA. Translation: AAI01937.1 .
BC114504 mRNA. Translation: AAI14505.1 .
BC114948 mRNA. Translation: AAI14949.1 .
AY526356 mRNA. Translation: AAS17881.1 .
M25298 mRNA. Translation: AAA57264.1 .
BN000503 mRNA. Translation: CAG26750.1 .
CCDSi CCDS11499.1. [P10636-8 ]
CCDS11500.1. [P10636-6 ]
CCDS11501.1. [P10636-1 ]
CCDS11502.1. [P10636-2 ]
CCDS45715.1. [P10636-9 ]
CCDS45716.1. [P10636-7 ]
CCDS56033.1. [P10636-5 ]
PIRi I52232.
JS0370. QRHUT1.
PN0001. QRHUT2.
S26663.
RefSeqi NP_001116538.2. NM_001123066.3. [P10636-9 ]
NP_001116539.1. NM_001123067.3. [P10636-7 ]
NP_001190181.1. NM_001203252.1. [P10636-5 ]
NP_005901.2. NM_005910.5. [P10636-8 ]
NP_058518.1. NM_016834.4. [P10636-6 ]
NP_058519.3. NM_016835.4. [P10636-1 ]
NP_058525.1. NM_016841.4. [P10636-2 ]
XP_006725337.1. XM_006725274.1. [P10636-6 ]
XP_006725338.1. XM_006725275.1. [P10636-2 ]
UniGenei Hs.101174.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I8H NMR - A 542-554 [» ]
2ON9 X-ray 1.51 A/B 623-628 [» ]
3OVL X-ray 1.81 A 623-628 [» ]
4FL5 X-ray 1.90 P/Q 527-536 [» ]
4GLR X-ray 1.90 A/B 541-557 [» ]
4NP8 X-ray 1.51 A 623-628 [» ]
DisProti DP00126.
ProteinModelPortali P10636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110308. 72 interactions.
DIPi DIP-29753N.
IntActi P10636. 35 interactions.
MINTi MINT-134394.

Chemistry

ChEMBLi CHEMBL1293224.
DrugBanki DB01248. Docetaxel.
DB01229. Paclitaxel.

PTM databases

PhosphoSitei P10636.

Polymorphism databases

DMDMi 334302961.

Proteomic databases

MaxQBi P10636.
PaxDbi P10636.
PRIDEi P10636.

Protocols and materials databases

DNASUi 4137.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262410 ; ENSP00000262410 ; ENSG00000186868 . [P10636-1 ]
ENST00000334239 ; ENSP00000334886 ; ENSG00000186868 . [P10636-2 ]
ENST00000340799 ; ENSP00000340438 ; ENSG00000186868 . [P10636-7 ]
ENST00000344290 ; ENSP00000340820 ; ENSG00000186868 . [P10636-9 ]
ENST00000351559 ; ENSP00000303214 ; ENSG00000186868 . [P10636-8 ]
ENST00000415613 ; ENSP00000410838 ; ENSG00000186868 . [P10636-9 ]
ENST00000420682 ; ENSP00000413056 ; ENSG00000186868 . [P10636-7 ]
ENST00000431008 ; ENSP00000389250 ; ENSG00000186868 . [P10636-5 ]
ENST00000446361 ; ENSP00000408975 ; ENSG00000186868 . [P10636-6 ]
ENST00000535772 ; ENSP00000443028 ; ENSG00000186868 . [P10636-5 ]
ENST00000571987 ; ENSP00000458742 ; ENSG00000186868 . [P10636-1 ]
ENST00000574436 ; ENSP00000460965 ; ENSG00000186868 . [P10636-8 ]
GeneIDi 4137.
KEGGi hsa:4137.
UCSCi uc002ijr.4. human. [P10636-1 ]
uc002ijs.4. human. [P10636-8 ]
uc002ijt.4. human. [P10636-6 ]
uc002iju.4. human. [P10636-2 ]
uc002ijx.4. human. [P10636-7 ]
uc010dau.3. human. [P10636-9 ]
uc021tyv.1. human. [P10636-5 ]
uc021tyw.1. human. [P10636-4 ]

Organism-specific databases

CTDi 4137.
GeneCardsi GC17P043971.
GeneReviewsi MAPT.
HGNCi HGNC:6893. MAPT.
HPAi CAB000151.
MIMi 157140. gene+phenotype.
172700. phenotype.
260540. phenotype.
600274. phenotype.
601104. phenotype.
neXtProti NX_P10636.
Orphaneti 275864. Behavioral variant of frontotemporal dementia.
240071. Classical progressive supranuclear palsy.
100070. Progressive non-fluent aphasia.
240103. Progressive supranuclear palsy - corticobasal syndrome.
240085. Progressive supranuclear palsy - parkinsonism.
240112. Progressive supranuclear palsy - progressive non fluent aphasia.
240094. Progressive supranuclear palsy - pure akinesia with gait freezing.
100069. Semantic dementia.
PharmGKBi PA238.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG148882.
GeneTreei ENSGT00530000063491.
HOVERGENi HBG000991.
InParanoidi P10636.
KOi K04380.
OMAi MKVKGAD.
OrthoDBi EOG738045.
TreeFami TF316358.

Enzyme and pathway databases

Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.

Miscellaneous databases

EvolutionaryTracei P10636.
GeneWikii Tau_protein.
GenomeRNAii 4137.
NextBioi 16246.
PMAP-CutDB P10636.
PROi P10636.
SOURCEi Search...

Gene expression databases

Bgeei P10636.
ExpressionAtlasi P10636. baseline and differential.
Genevestigatori P10636.

Family and domain databases

InterProi IPR027324. MAP2/MAP4/Tau.
IPR001084. MAP_tubulin-bd_rpt.
IPR002955. Tau.
[Graphical view ]
PANTHERi PTHR11501. PTHR11501. 1 hit.
Pfami PF00418. Tubulin-binding. 4 hits.
[Graphical view ]
PRINTSi PR01261. TAUPROTEIN.
PROSITEi PS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau."
    Goedert M., Wischik C., Crowther R., Walker J., Klug A.
    Proc. Natl. Acad. Sci. U.S.A. 85:4051-4055(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FETAL-TAU).
    Tissue: Brain.
  2. "Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain."
    Goedert M., Spillantini M.G., Potier M.-C., Ulrich J., Crowther R.A.
    EMBO J. 8:393-399(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-D).
    Tissue: Brain.
  3. "The microtubule binding domain of tau protein."
    Lee G., Neve R.L., Kosik K.S.
    Neuron 2:1615-1624(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A AND FETAL-TAU).
    Tissue: Fetal brain.
  4. "Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease."
    Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A.
    Neuron 3:519-526(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B; TAU-C; TAU-E AND TAU-F), ASSOCIATION WITH ALZHEIMER DISEASE.
    Tissue: Brain.
  5. "Structure and novel exons of the human tau gene."
    Andreadis A., Brown W.M., Kosik K.S.
    Biochemistry 31:10626-10633(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PNS-TAU; FETAL-TAU AND TAU-F), ALTERNATIVE SPLICING, VARIANT HIS-441.
  6. "Cloning of tau-related genes."
    Chun J., Kwon T., Lee E.-J., Hyun S.-H., Kang S.S.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-E).
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FETAL-TAU).
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FETAL-TAU AND TAU-D).
    Tissue: Brain.
  10. "Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain."
    Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K., Ihara Y.
    J. Biol. Chem. 267:17047-17054(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-73; 103-381; 468-497; 508-571; 577-583; 592-607; 616-634; 639-657; 661-664; 671-700 AND 703-758, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    Tissue: Brain.
  11. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 25-44; 529-538; 560-571 AND 671-686, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  12. "Molecular interactions of recombinant neural protein tau with recombinant and native PrP proteins in vitro."
    Han J., Zhang J., Dong X.-P.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 466-740 (ISOFORMS TAU-A/TAU-B/TAU-C/FETAL-TAU).
  13. "Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation."
    Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.
    J. Biol. Chem. 281:10825-10838(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 543-551; 560-574; 576-584 AND 623-634, PHOSPHORYLATION AT SER-531; THR-534; THR-548; SER-552; SER-554; SER-579; SER-713 AND SER-739, UBIQUITINATION AT LYS-571; LYS-628 AND LYS-670, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262."
    Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., Meyer H.E., Mandelkow E.-M., Mandelkow E.
    J. Biol. Chem. 270:7679-7688(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 577-584; 608-611; 616-628; 639-648 AND 671-686, PHOSPHORYLATION AT SER-579; SER-610; SER-622; SER-641 AND SER-673, MUTAGENESIS.
  15. "A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments."
    Mori H., Hamada Y., Kawaguchi M., Honda T., Kondo J., Ihara Y.
    Biochem. Biophys. Res. Commun. 159:1221-1226(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 592-622 (ISOFORMS PNS-TAU/TAU-D/TAU-E/TAU-F).
    Tissue: Brain.
  16. "A68: a major subunit of paired helical filaments and derivatized forms of normal Tau."
    Lee V.M., Balin B.J., Otvos L. Jr., Trojanowski J.Q.
    Science 251:675-678(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 251-264 AND 379-392, PHOSPHORYLATION AT SER-396.
  17. "Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease."
    Jakes R., Novak M., Davison M., Wischik C.M.
    EMBO J. 10:2725-2729(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 616-712.
  18. "The role of tau (MAPT) in frontotemporal dementia and related tauopathies."
    Rademakers R., Cruts M., van Broeckhoven C.
    Hum. Mutat. 24:277-295(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM TAU-G), VARIANT HIS-441.
  19. "Molecular characterization of microtubule-associated proteins tau and MAP2."
    Goedert M., Crowther R.A., Garner C.C.
    Trends Neurosci. 14:193-199(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase."
    Paudel H.K.
    J. Biol. Chem. 272:1777-1785(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-554; SER-579; SER-602; SER-606 AND SER-669.
  21. "Characterization of in vitro glycation sites of tau."
    Nacharaju P., Ko L., Yen S.H.
    J. Neurochem. 69:1709-1719(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-87; LYS-383; LYS-467; LYS-480; LYS-491; LYS-542; LYS-551; LYS-576; LYS-597; LYS-598; LYS-664; LYS-670 AND LYS-686, LACK OF GLYCATION AT LYS-24; LYS-44; LYS-67; LYS-381; LYS-391; LYS-392; LYS-394; LYS-465; LYS-497; LYS-507; LYS-541; LYS-557; LYS-571; LYS-574; LYS-584; LYS-591; LYS-607; LYS-611; LYS-615; LYS-628; LYS-634; LYS-638; LYS-648; LYS-657; LYS-660; LYS-687; LYS-692; LYS-700; LYS-702; LYS-712 AND LYS-755.
  22. "Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules."
    Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., Iqbal K.
    Arch. Biochem. Biophys. 357:299-309(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS.
  23. "The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease."
    Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., Trinczek B., Biernat J., Godemann R., Mandelkow E.-M., Mandelkow E.
    Mol. Biol. Cell 9:1495-1512(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-470; SER-516; SER-519; THR-529; SER-531; SER-552; SER-579; SER-713; SER-721 AND SER-739, MUTAGENESIS.
  24. "Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments."
    Maas T., Eidenmueller J., Brandt R.
    J. Biol. Chem. 275:15733-15740(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  25. "Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules."
    Li G., Yin H., Kuret J.
    J. Biol. Chem. 279:15938-15945(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-519; THR-522; SER-713 AND SER-721 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
  26. "Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to