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P10636

- TAU_HUMAN

UniProt

P10636 - TAU_HUMAN

Protein

Microtubule-associated protein tau

Gene

MAPT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 206 (01 Oct 2014)
      Sequence version 5 (31 May 2011)
      Previous versions | rss
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    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. protein binding Source: IntAct
    6. SH3 domain binding Source: UniProtKB
    7. 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

    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. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. cytosol Source: Reactome
    4. growth cone Source: UniProtKB
    5. microtubule Source: UniProtKB-KW
    6. microtubule associated complex Source: ProtInc
    7. nuclear periphery Source: UniProtKB
    8. plasma membrane Source: UniProtKB
    9. tubulin complex Source: UniProtKB

    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)2 Publications
    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)2 Publications
    Cross-linki571 – 571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau2 Publications
    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-tau2 Publications
    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-tau2 Publications
    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); alternate2 Publications
    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

    ArrayExpressiP10636.
    BgeeiP10636.
    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. 61 interactions.
    DIPiDIP-29753N.
    IntActiP10636. 34 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.
    HOVERGENiHBG000991.
    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

    MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT    50
    PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG 100
    TTAEEAGIGD TPSLEDEAAG HVTQEPESGK VVQEGFLREP GPPGLSHQLM 150
    SGMPGAPLLP EGPREATRQP SGTGPEDTEG GRHAPELLKH QLLGDLHQEG 200
    PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA QDGRPPQTAA 250
    REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE 300
    FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD 350
    LPEPSEKQPA AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS 400
    AKTLKNRPCL SPKHPTPGSS DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG 450
    SSGAKEMKLK GADGKTKIAT PRGAAPPGQK GQANATRIPA KTPPAPKTPP 500
    SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP KKVAVVRTPP 550
    KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD 600
    LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG 650
    GGQVEVKSEK LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK 700
    AKTDHGAEIV YKSPVVSGDT SPRHLSNVSS TGSIDMVDSP QLATLADEVS 750
    ASLAKQGL 758
    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

    Alzheimer Research Forum

    Tau 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. 61 interactions.
    DIPi DIP-29753N.
    IntActi P10636. 34 interactions.
    MINTi MINT-134394.

    Chemistry

    ChEMBLi CHEMBL1293224.

    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.
    HOVERGENi HBG000991.
    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

    ArrayExpressi P10636.
    Bgeei P10636.
    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

    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 microtub