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P10636 (TAU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 204. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein tau
Alternative name(s):
Neurofibrillary tangle protein
Paired helical filament-tau
Short name=PHF-tau
Gene names
Name:MAPT
Synonyms:MAPTL, MTBT1, TAU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length758 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.42

Subunit structure

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. Ref.25 Ref.28 Ref.31 Ref.38

Subcellular location

Cytoplasmcytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectionaxon. Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. Ref.24

Tissue specificity

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

Developmental stage

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.

Domain

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

Post-translational modification

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. Ref.13 Ref.14 Ref.16 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.33 Ref.34 Ref.37 Ref.41 Ref.42

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.

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%. Ref.37 Ref.41

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.

Involvement in disease

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. Ref.4 Ref.37 Ref.76

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.37 Ref.45 Ref.47 Ref.48 Ref.49 Ref.51 Ref.52 Ref.53 Ref.54 Ref.56 Ref.58 Ref.59 Ref.62 Ref.63 Ref.64 Ref.67 Ref.68 Ref.70 Ref.72 Ref.73 Ref.74 Ref.76 Ref.79 Ref.81

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.37 Ref.55 Ref.60 Ref.61 Ref.66 Ref.69 Ref.76

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. Ref.4 Ref.37 Ref.76

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.37 Ref.57 Ref.65 Ref.71 Ref.76 Ref.77 Ref.78 Ref.80

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. Ref.4 Ref.37 Ref.76

Sequence similarities

Contains 4 Tau/MAP repeats.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAlzheimer disease
Disease mutation
Neurodegeneration
Parkinsonism
   DomainRepeat
   PTMAcetylation
Disulfide bond
Glycation
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

axon cargo transport

Inferred from electronic annotation. Source: Ensembl

axon extension

Inferred from electronic annotation. Source: Ensembl

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

generation of neurons

Non-traceable author statement PubMed 8522593. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from direct assay PubMed 1057175. Source: UniProtKB

mitochondrion transport along microtubule

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular transport

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from direct assay PubMed 1389180. Source: UniProtKB

positive regulation of microtubule polymerization

Inferred from direct assay PubMed 1421571. Source: UniProtKB

regulation of autophagy

Inferred from genetic interaction PubMed 19074461. Source: MGI

regulation of microtubule polymerization

Non-traceable author statement PubMed 1057175. Source: UniProtKB

regulation of microtubule-based movement

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 8642405. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

growth cone

Inferred from direct assay PubMed 8642405. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Traceable author statement Ref.24. Source: ProtInc

nuclear periphery

Inferred from direct assay PubMed 19157893. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 8522593. Source: UniProtKB

tubulin complex

Inferred from direct assay PubMed 8642405. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from physical interaction PubMed 9763511. Source: UniProtKB

apolipoprotein binding

Inferred from physical interaction PubMed 7566652. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 12888622PubMed 20133804PubMed 9736630. Source: UniProtKB

lipoprotein particle binding

Inferred from physical interaction PubMed 7972031. Source: UniProtKB

microtubule binding

Inferred from direct assay PubMed 1918161. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 24113872PubMed 19647741PubMed 17932487PubMed 21985244PubMed 22303461PubMed 24113872PubMed 24165324. Source: IntAct

structural constituent of cytoskeleton

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform Fetal-tau (identifier: P10636-2)

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.
Isoform Tau-A (identifier: P10636-3)

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.
Isoform Tau-B (identifier: P10636-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.
Isoform Tau-C (identifier: P10636-5)

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.
Isoform Tau-D (identifier: P10636-6)

The sequence of this isoform differs from the canonical sequence as follows:
     45-73: Missing.
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
Isoform Tau-E (identifier: P10636-7)

The sequence of this isoform differs from the canonical sequence as follows:
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
Isoform Tau-F (identifier: P10636-8)

Also known as: Tau-4;

The sequence of this isoform differs from the canonical sequence as follows:
     125-375: Missing.
     395-460: Missing.
Isoform Tau-G (identifier: P10636-9)

The sequence of this isoform differs from the canonical sequence as follows:
     502-502: S → SATKQVQRRPPPAGPRSER
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 758757Microtubule-associated protein tau
PRO_0000072739

Regions

Repeat561 – 59131Tau/MAP 1
Repeat592 – 62231Tau/MAP 2
Repeat623 – 65331Tau/MAP 3
Repeat654 – 68532Tau/MAP 4

Sites

Site241Not glycated
Site441Not glycated
Site671Not glycated
Site3811Not glycated
Site3911Not glycated
Site3921Not glycated
Site3941Not glycated
Site4651Not glycated
Site4971Not glycated
Site5071Not glycated
Site5411Not glycated
Site5571Not glycated
Site5711Not glycated
Site5741Not glycated
Site5841Not glycated
Site5911Not glycated
Site6071Not glycated
Site6111Not glycated
Site6151Not glycated
Site6281Not glycated
Site6341Not glycated
Site6381Not glycated
Site6481Not glycated
Site6571Not glycated
Site6601Not glycated
Site6871Not glycated
Site6921Not glycated
Site7001Not glycated
Site7021Not glycated
Site7121Not glycated
Site7551Not glycated

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue181Phosphotyrosine; by FYN Ref.27
Modified residue461Phosphoserine; by PDPK1
Modified residue501Phosphothreonine; by PDPK1
Modified residue2141Phosphoserine; by SGK1 Ref.31
Modified residue3961Phosphoserine; in PHF-tau Ref.16
Modified residue4701Phosphothreonine; by PDPK1 Ref.23
Modified residue4841Deamidated asparagine; in tau and PHF-tau; partial
Modified residue4921Phosphothreonine; by PDPK1
Modified residue4981Phosphothreonine; by PDPK1 Ref.29
Modified residue5141Phosphotyrosine; by TTBK1 Ref.30
Modified residue5151Phosphoserine; by PDPK1 and TTBK1 Ref.30
Modified residue5161Phosphoserine; by PDPK1 and TTBK1 Ref.23 Ref.29 Ref.30 Ref.37
Modified residue5191Phosphoserine; by CK1, PDPK1 and TTBK1 Ref.23 Ref.25 Ref.29 Ref.30 Ref.35 Ref.37 Ref.41
Modified residue5221Phosphothreonine; by CK1 and PDPK1 Ref.25 Ref.29 Ref.37
Modified residue5291Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 Ref.23 Ref.29 Ref.34 Ref.37 Ref.42
Modified residue5311Phosphoserine; by PKA Ref.13 Ref.23 Ref.29 Ref.37
Modified residue5341Phosphothreonine; by PDPK1 Ref.13 Ref.37
Modified residue5481Phosphothreonine; by GSK3-beta and PDPK1 Ref.13 Ref.26 Ref.29
Modified residue5521Phosphoserine; by PDPK1 Ref.13 Ref.23 Ref.29
Modified residue5541Phosphoserine; by PHK Ref.13 Ref.20
Modified residue5791Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK Ref.13 Ref.14 Ref.20 Ref.23 Ref.29 Ref.37 Ref.42
Modified residue5961Deamidated asparagine; in tau and PHF-tau; partial
Modified residue6021Phosphoserine; by PHK Ref.20
Modified residue6061Phosphoserine; by PHK Ref.20
Modified residue6101Phosphoserine; by MARK1; in PHF-tau Ref.14
Modified residue6221Phosphoserine; by MARK1; in PHF-tau Ref.14
Modified residue6411Phosphoserine; by MARK1; in PHF-tau Ref.14
Modified residue6691Phosphoserine; by PHK Ref.20
Modified residue6731Phosphoserine; by MARK1; in PHF-tau Ref.14
Modified residue7131Phosphoserine; by CK1 and PDPK1 Ref.13 Ref.23 Ref.25 Ref.29 Ref.37 Ref.39 Ref.41
Modified residue7171Phosphoserine; alternate Ref.39 Ref.41
Modified residue7201Phosphothreonine
Modified residue7211Phosphoserine; by CK1 and PDPK1 Ref.23 Ref.25 Ref.29 Ref.37 Ref.39 Ref.41
Modified residue7261Phosphoserine Ref.29 Ref.39
Modified residue7331Phosphoserine; by CaMK2 and TTBK1 Ref.30
Modified residue7391Phosphoserine; by PDPK1 and TTBK1 Ref.13 Ref.23 Ref.30 Ref.37
Modified residue7441Phosphothreonine; by TTBK1 Ref.30
Glycosylation871N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation3831N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation4671N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation4801N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation4911N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation5251O-linked (GlcNAc) Ref.41
Glycosylation5421N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation5511N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation5551O-linked (GlcNAc) Ref.41
Glycosylation5761N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation5971N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation5981N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation6641N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation6701N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation6861N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.21
Glycosylation7171O-linked (GlcNAc); alternate Ref.41
Disulfide bond608 ↔ 639 By similarity
Cross-link571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau Ref.13
Cross-link628Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau Ref.13
Cross-link670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau Ref.13

Natural variations

Alternative sequence1 – 4444MAEPR…DAGLK → MLRALQQRKR in isoform Tau-A.
VSP_003175
Alternative sequence45 – 7329Missing in isoform Tau-A, isoform Tau-D and isoform Fetal-tau.
VSP_003176
Alternative sequence74 – 10229Missing in isoform Tau-A, isoform Tau-B, isoform Tau-D, isoform Tau-E and isoform Fetal-tau.
VSP_003177
Alternative sequence103 – 1042Missing in isoform Tau-A.
VSP_003178
Alternative sequence125 – 375251Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau.
VSP_003179
Alternative sequence395 – 46066Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau.
VSP_003180
Alternative sequence5021S → SATKQVQRRPPPAGPRSER in isoform Tau-G.
VSP_026780
Alternative sequence592 – 62231Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C and isoform Fetal-tau.
VSP_003181
Natural variant51R → H in FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro. Ref.70
Corresponds to variant rs63750959 [ dbSNP | Ensembl ].
VAR_019660
Natural variant51R → L in PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau. Ref.71
Corresponds to variant rs63750959 [ dbSNP | Ensembl ].
VAR_019661
Natural variant171T → M. Ref.82
Corresponds to variant rs144611688 [ dbSNP | Ensembl ].
VAR_064622
Natural variant301T → A. Ref.82
VAR_064623
Natural variant2851D → N Risk factor for PSNP1. Ref.45 Ref.57
Corresponds to variant rs62063786 [ dbSNP | Ensembl ].
VAR_010340
Natural variant2891V → A Risk factor for PSNP1. Ref.45 Ref.57
Corresponds to variant rs62063787 [ dbSNP | Ensembl ].
VAR_010341
Natural variant3701R → W.
Corresponds to variant rs17651549 [ dbSNP | Ensembl ].
VAR_056121
Natural variant4411Y → H. Ref.5 Ref.18 Ref.45
Corresponds to variant rs2258689 [ dbSNP | Ensembl ].
VAR_010342
Natural variant4471S → P. Ref.45
Corresponds to variant rs10445337 [ dbSNP | Ensembl ].
VAR_010343
Natural variant5741K → T in PIDB; reduces the ability to promote microtubule assembly by 70%. Ref.60 Ref.61
VAR_010344
Natural variant5831L → V in FTD; less able to promote microtubule assembly than wild-type tau. Ref.74
VAR_019662
Natural variant5891G → V in FTD. Ref.48 Ref.51
VAR_010345
Natural variant5961N → K in FTD; with parkinsonism. Ref.49 Ref.50 Ref.56 Ref.62 Ref.68
VAR_010346
Natural variant5971Missing in FTD. Ref.51
VAR_010347
Natural variant6131N → 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. Ref.64 Ref.72
VAR_019663
Natural variant6131Missing 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. Ref.65 Ref.72 Ref.77 Ref.78
VAR_019664
Natural variant6171V → I. Ref.82
Corresponds to variant rs116733906 [ dbSNP | Ensembl ].
VAR_064624
Natural variant6181P → L in FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments. Ref.47 Ref.48 Ref.49 Ref.51 Ref.53
VAR_010348
Natural variant6181P → S in FTD and CBD; reduction in the ability to promote microtubule assembly. Ref.52 Ref.54 Ref.63 Ref.79
VAR_010349
Natural variant6201G → V in PSNP1. Ref.80
VAR_037439
Natural variant6221S → N in FTD; minimal parkinsonism; very early age of onset. Ref.58
VAR_010350
Natural variant6341K → M in FTD. Ref.81
VAR_037440
Natural variant6371S → F in PIDB; markedly reduced ability of tau to promote microtubule assembly. Ref.69
VAR_019665
Natural variant6541V → M in FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments. Ref.45 Ref.53
VAR_010351
Natural variant6591E → V in FTD. Ref.59
VAR_019666
Natural variant6691S → L in fatal respiratory hypoventilation; unusual apparent autosomal recessive inheritance; reduced binding to microtubules as well as increased fibrillization and aggregation. Ref.75
VAR_019667
Natural variant6861K → I in PIDB; 90% reduction in the rate of microtubule assembly. Ref.66
VAR_019668
Natural variant7061G → R in PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%. Ref.55 Ref.60
VAR_010352
Natural variant7231R → 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. Ref.48 Ref.51 Ref.53 Ref.67 Ref.73 Ref.76
VAR_010353

Experimental info

Mutagenesis5151S → E: No association with plasma membrane.
Mutagenesis5161S → E: No association with plasma membrane.
Mutagenesis5191S → E: No association with plasma membrane.
Mutagenesis5311S → A: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein.
Mutagenesis5481T → A: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
Mutagenesis5481T → E: No association with plasma membrane.
Mutagenesis5521S → A: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
Mutagenesis5521S → E: No association with plasma membrane.
Mutagenesis5791S → A: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
Mutagenesis7131S → E: No association with plasma membrane.
Mutagenesis7211S → E: No association with plasma membrane.
Mutagenesis7261S → E: No association with plasma membrane.
Mutagenesis7301S → E: No association with plasma membrane.
Mutagenesis7391S → E: No association with plasma membrane.
Sequence conflict481L → P in AAU45390. Ref.6
Sequence conflict4141H → L in AAC04277. Ref.5
Sequence conflict5571K → M in AAS17881. Ref.12
Sequence conflict5911K → S in AAS17881. Ref.12
Sequence conflict6171V → Q AA sequence Ref.17
Sequence conflict6221S → K AA sequence Ref.17

Sequences

Sequence LengthMass (Da)Tools
Isoform PNS-tau [UniParc].

Last modified May 31, 2011. Version 5.
Checksum: D46C66CDBCD196E8

FASTA75878,928
        10         20         30         40         50         60 
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 

        70         80         90        100        110        120 
SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG 

       130        140        150        160        170        180 
HVTQEPESGK VVQEGFLREP GPPGLSHQLM SGMPGAPLLP EGPREATRQP SGTGPEDTEG 

       190        200        210        220        230        240 
GRHAPELLKH QLLGDLHQEG PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA 

       250        260        270        280        290        300 
QDGRPPQTAA REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE 

       310        320        330        340        350        360 
FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD LPEPSEKQPA 

       370        380        390        400        410        420 
AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS AKTLKNRPCL SPKHPTPGSS 

       430        440        450        460        470        480 
DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG SSGAKEMKLK GADGKTKIAT PRGAAPPGQK 

       490        500        510        520        530        540 
GQANATRIPA KTPPAPKTPP SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP 

       550        560        570        580        590        600 
KKVAVVRTPP KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD 

       610        620        630        640        650        660 
LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG GGQVEVKSEK 

       670        680        690        700        710        720 
LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK AKTDHGAEIV YKSPVVSGDT 

       730        740        750 
SPRHLSNVSS TGSIDMVDSP QLATLADEVS ASLAKQGL 

« Hide

Isoform Fetal-tau [UniParc].

Checksum: 9B26AEDFF4D2677C
Show »

FASTA35236,760
Isoform Tau-A [UniParc].

Checksum: 4C86C95F53015575
Show »

FASTA31632,944
Isoform Tau-B [UniParc].

Checksum: EA206819FE73B67A
Show »

FASTA38139,720
Isoform Tau-C (Tau-3) [UniParc].

Checksum: A76B304E99E6A978
Show »

FASTA41042,603
Isoform Tau-D [UniParc].

Checksum: F3256B0AB87B348D
Show »

FASTA38340,007
Isoform Tau-E [UniParc].

Checksum: 0D4EABCA15179E7D
Show »

FASTA41242,967
Isoform Tau-F (Tau-4) [UniParc].

Checksum: 835A8706D847A8CC
Show »

FASTA44145,850
Isoform Tau-G [UniParc].

Checksum: 13E913ACD1790C26
Show »

FASTA77680,941

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 bind and stabilize microtubules."
Cho J.H., Johnson G.V.
J. Neurochem. 88:349-358(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-548 BY GSK3B.
[27]"Phosphorylation of tau by fyn: implications for Alzheimer's disease."
Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M., Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.
J. Neurosci. 24:2304-2312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-18 BY FYN.
[28]"Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation."
Babu J.R., Geetha T., Wooten M.W.
J. Neurochem. 94:192-203(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, UBIQUITINATION, PROTEASOMAL DEGRADATION.
[29]"Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease."
Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.
J. Biol. Chem. 280:1790-1796(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-498; SER-516; SER-519; THR-522; THR-529; SER-531; THR-548; SER-552; SER-579; SER-713; SER-721 AND SER-726, DEPHOSPHORYLATION AT THR-498; SER-516; SER-519; THR-522; THR-529; SER-531; THR-548; SER-552; SER-579; SER-713; SER-721 AND SER-726 BY PPP5C.
[30]"Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation."
Sato S., Cerny R.L., Buescher J.L., Ikezu T.
J. Neurochem. 98:1573-1584(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-514; SER-515; SER-516; SER-519; SER-733; SER-739 AND THR-744.
[31]"Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau."
Yang Y.C., Lin C.H., Lee E.H.
Mol. Cell. Biol. 26:8357-8370(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-214 BY SGK1, INTERACTION WITH SGK1.
[32]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis."
Hanger D.P., Byers H.L., Wray S., Leung K.-Y., Saxton M.J., Seereeram A., Reynolds C.H., Ward M.A., Anderton B.H.
J. Biol. Chem. 282:23645-23654(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CSNK1D/CK1.
[34]"Role for DYRK family kinases on regulation of apoptosis."
Yoshida K.
Biochem. Pharmacol. 76:1389-1394(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-529 BY DYRK2.
[35]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease."
Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.X.
Brain 132:1820-1832(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, PHOSPHORYLATION AT SER-516; SER-519; THR-522; THR-529; SER-531; THR-534; SER-579; SER-713; SER-721 AND SER-739, ASSOCIATION WITH ALZHEIMER DISEASE.
[38]"Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease."
Puri R., Suzuki T., Yamakawa K., Ganesh S.
J. Biol. Chem. 284:22657-22663(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPM2A.
[39]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-717; SER-721 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[40]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[41]"Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation."
Smet-Nocca C., Broncel M., Wieruszeski J.M., Tokarski C., Hanoulle X., Leroy A., Landrieu I., Rolando C., Lippens G., Hackenberger C.P.
Mol. Biosyst. 7:1420-1429(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-525; SER-555 AND SER-717, PHOSPHORYLATION AT SER-519; SER-713 SER-717 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY.
[42]"Phosphorylation of microtubule-associated protein tau by AMPK-related kinases."
Yoshida H., Goedert M.
J. Neurochem. 120:165-176(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-529 AND SER-579.
[43]"1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides."
Wintjens R., Wieruszeski J.-M., Drobecq H., Rousselot-Pailley P., Buee L., Lippens G., Landrieu I.
J. Biol. Chem. 276:25150-25156(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 542-554 IN COMPLEX WITH PIN1.
[44]"Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease."
Goedert M., Spillantini M.G.
Biochim. Biophys. Acta 1502:110-121(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[45]"Tau is a candidate gene for chromosome 17 frontotemporal dementia."
Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L., Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D.
Ann. Neurol. 43:815-825(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD MET-654, VARIANTS ASN-285; ALA-289; HIS-441 AND PRO-447.
[46]Erratum
Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L., Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D.
Ann. Neurol. 44:428-428(1998)
[47]"Segregation of a missense mutation in the microtubule-associated protein tau gene with familial frontotemporal dementia and parkinsonism."
Dumanchin C., Camuzat A., Campion D., Verpillat P., Hannequin D., Dubois B., Saugier-Veber P., Martin C., Penet C., Charbonnier F., Agid Y., Frebourg T., Brice A.
Hum. Mol. Genet. 7:1825-1829(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD LEU-618.
[48]"Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17."
Hutton M., Lendon C.L., Rizzu P., Baker M., Froelich S., Houlden H., Pickering-Brown S., Chakraverty S., Isaacs A., Grover A., Hackett J., Adamson J., Lincoln S., Dickson D., Davies P., Petersen R.C., Stevens M., de Graaff E. expand/collapse author list , Wauters E., van Baren J., Hillebrand M., Joosse M., Kwon J.M., Nowotny P., Che L.K., Norton J., Morris J.C., Reed L.A., Trojanowski J., Basun H., Lannfelt L., Neystat M., Fahn S., Dark F., Tannenberg T., Dodd P.R., Hayward N., Kwok J.B.J., Schofield P.R., Andreadis A., Snowden J., Craufurd D., Neary D., Owen F., Oostra B.A., Hardy J., Goate A., van Swieten J., Mann D., Lynch T., Heutink P.
Nature 393:702-705(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FTD VAL-589; LEU-618 AND TRP-723.
[49]"Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17."
Clark L.N., Poorkaj P., Wszolek Z., Geschwind D.H., Nasreddine Z.S., Miller B., Li D., Payami H., Awert F., Markopoulou K., Andreadis A., D'Souza I., Lee V.M.-Y., Reed L., Trojanowski J.Q., Zhukareva V., Bird T., Schellenberg G., Wilhelmsen K.C.
Proc. Natl. Acad. Sci. U.S.A. 95:13103-13107(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FTD LYS-596 AND LEU-618.
[50]"A mutation at codon 279 (N279K) in exon 10 of the Tau gene causes a tauopathy with dementia and supranuclear palsy."
Delisle M.-B., Murrell J.R., Richardson R., Trofatter J.A., Rascol O., Soulages X., Mohr M., Calvas P., Ghetti B.
Acta Neuropathol. 98:62-77(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PPND LYS-596.
[51]"High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands."
Rizzu P., Van Swieten J.C., Joosse M., Hasegawa M., Stevens M., Tibben A., Niermeijer M.F., Hillebrand M., Ravid R., Oostra B.A., Goedert M., van Duijn C.M., Heutink P.
Am. J. Hum. Genet. 64:414-421(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FTD VAL-589; LYS-597 DEL; LEU-618 AND TRP-723.
[52]"FTDP-17: an early-onset phenotype with parkinsonism and epileptic seizures caused by a novel mutation."
Sperfeld A.D., Collatz M.B., Baier H., Palmbach M., Storch A., Schwarz J., Tatsch K., Reske S., Joosse M., Heutink P., Ludolph A.C.
Ann. Neurol. 46:708-715(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD SER-618.
[53]"Accelerated filament formation from tau protein with specific FTDP-17 missense mutations."
Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M., Yen S.H.
FEBS Lett. 447:195-199(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FTD LEU-618; MET-654 AND TRP-723.
[54]"Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau."
Bugiani O., Murrell J.R., Giaccone G., Hasegawa M., Ghigo G., Tabaton M., Morbin M., Primavera A., Carella F., Solaro C., Grisoli M., Savoiardo M., Spillantini M.G., Tagliavini F., Goedert M., Ghetti B.
J. Neuropathol. Exp. Neurol. 58:667-677(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD/CBD SER-618.
[55]"Tau gene mutation G389R causes a tauopathy with abundant pick body-like inclusions and axonal deposits."
Murrell J.R., Spillantini M.G., Zolo P., Guazzelli M., Smith M.J., Hasegawa M., Redi F., Crowther R.A., Pietrini P., Ghetti B., Goedert M.
J. Neuropathol. Exp. Neurol. 58:1207-1226(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PIDB ARG-706.
[56]"A mutation in the microtubule-associated protein tau in pallido-nigro-luysian degeneration."
Yasuda M., Kawamata T., Komure O., Kuno S., D'Souza I., Poorkaj P., Kawai J., Tanimukai S., Yamamoto Y., Hasegawa H., Sasahara M., Hazama F., Schellenberg G.D., Tanaka C.
Neurology 53:864-868(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD LYS-596.
[57]"Mutational analysis of the tau gene in progressive supranuclear palsy."
Higgins J.J., Adler R.L., Loveless J.M.
Neurology 53:1421-1424(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSNP1 ASN-285 AND ALA-289.
[58]"A distinct familial presenile dementia with a novel missense mutation in the tau gene."
Iijima M., Tabira T., Poorkaj P., Schellenberg G.D., Trojanowski J.Q., Lee V.M.-Y., Schmidt M.L., Takahashi K., Nabika T., Matsumoto T., Yamashita Y., Yoshioka S., Ishino H.
NeuroReport 10:497-501(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD ASN-622.
[59]"Frontotemporal dementia with novel tau pathology and a Glu342Val tau mutation."
Lippa C.F., Zhukareva V., Kawarai T., Uryu K., Shafiq M., Nee L.E., Grafman J., Liang Y., St George-Hyslop P.H., Trojanowski J.Q., Lee V.M.-Y.
Ann. Neurol. 48:850-858(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD VAL-659.
[60]"Pick's disease is associated with mutations in the tau gene."
Pickering-Brown S., Baker M., Yen S.-H., Liu W.-K., Hasegawa M., Cairns N., Lantos P.L., Rossor M., Iwatsubo T., Davies Y., Allsop D., Furlong R., Owen F., Hardy J., Mann D., Hutton M.
Ann. Neurol. 48:859-867(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PIDB THR-574 AND ARG-706, CHARACTERIZATION OF VARIANTS PIDB THR-574 AND ARG-706.
[61]"Tau gene mutation K257T causes a tauopathy similar to Pick's disease."
Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R., Xuereb J.H., Crowther R.A., Spillantini M.G.
J. Neuropathol. Exp. Neurol. 59:990-1001(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PIDB THR-574.
[62]"Two brothers with frontotemporal dementia and parkinsonism with an N279K mutation of the tau gene."
Arima K., Kowalska A., Hasegawa M., Mukoyama M., Watanabe R., Kawai M., Takahashi K., Iwatsubo T., Tabira T., Sunohara N.
Neurology 54:1787-1795(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD LYS-596.
[63]"A Japanese patient with frontotemporal dementia and parkinsonism by a tau P301S mutation."
Yasuda M., Yokoyama K., Nakayasu T., Nishimura Y., Matsui M., Yokoyama T., Miyoshi K., Tanaka C.
Neurology 55:1224-1227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD SER-618.
[64]"Familial frontotemporal dementia and parkinsonism with a novel N296H mutation in exon 10 of the tau gene and a widespread tau accumulation in the glial cells."
Iseki E., Matsumura T., Marui W., Hino H., Odawara T., Sugiyama N., Suzuki K., Sawada H., Arai T., Kosaka K.
Acta Neuropathol. 102:285-292(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD HIS-613.
[65]"Familial atypical progressive supranuclear palsy associated with homozygosity for the delN296 mutation in the tau gene."
Pastor P., Pastor E., Carnero C., Vela R., Garcia T., Amer G., Tolosa E., Oliva R.
Ann. Neurol. 49:263-267(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSNP1 ASN-613 DEL.
[66]"Pick's disease associated with the novel Tau gene mutation K369I."
Neumann M., Schulz-Schaeffer W., Crowther R.A., Smith M.J., Spillantini M.G., Goedert M., Kretzschmar H.A.
Ann. Neurol. 50:503-513(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PIDB ILE-686, CHARACTERIZATION OF VARIANT PIDB ILE-686.
[67]"Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3beta identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes."
Connell J.W., Gibb G.M., Betts J.C., Blackstock W.P., Gallo J.-M., Lovestone S., Hutton M., Anderton B.H.
FEBS Lett. 493:40-44(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT FTD TRP-723.
[68]"Clinical and genetic studies of families with the tau N279K mutation (FTDP-17)."
Tsuboi Y., Baker M., Hutton M.L., Uitti R.J., Rascol O., Delisle M.-B., Soulages X., Murrell J.R., Ghetti B., Yasuda M., Komure O., Kuno S., Arima K., Sunohara N., Kobayashi T., Mizuno Y., Wszolek Z.K.
Neurology 59:1791-1793(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD LYS-596.
[69]"A novel tau mutation, S320F, causes a tauopathy with inclusions similar to those in Pick's disease."
Rosso S.M., Van Herpen E., Deelen W., Kamphorst W., Severijnen L.-A., Willemsen R., Ravid R., Niermeijer M.F., Dooijes D., Smith M.J., Goedert M., Heutink P., Van Swieten J.C.
Ann. Neurol. 51:373-376(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PIDB PHE-637, CHARACTERIZATION OF VARIANT PIDB PHE-637.
[70]"Late-onset frontotemporal dementia with a novel exon 1 (Arg5His) tau gene mutation."
Hayashi S., Toyoshima Y., Hasegawa M., Umeda Y., Wakabayashi K., Tokiguchi S., Iwatsubo T., Takahashi H.
Ann. Neurol. 51:525-530(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD HIS-5, CHARACTERIZATION OF VARIANT FTD HIS-5.
[71]"An R5L tau mutation in a subject with a progressive supranuclear palsy phenotype."
Poorkaj P., Muma N.A., Zhukareva V., Cochran E.J., Shannon K.M., Hurtig H., Koller W.C., Bird T.D., Trojanowski J.Q., Lee V.M.-Y., Schellenberg G.D.
Ann. Neurol. 52:511-516(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSNP1 LEU-5, CHARACTERIZATION OF VARIANT PSNP1 LEU-5.
[72]"Functional effects of tau gene mutations deltaN296 and N296H."
Yoshida H., Crowther R.A., Goedert M.
J. Neurochem. 80:548-551(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS FTD ASN-613 DEL AND HIS-613.
[73]"Early-onset, rapidly progressive familial tauopathy with R406W mutation."
Saito Y., Geyer A., Sasaki R., Kuzuhara S., Nanba E., Miyasaka T., Suzuki K., Murayama S.
Neurology 58:811-813(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD TRP-723.
[74]"A novel L266V mutation of the tau gene causes frontotemporal dementia with a unique tau pathology."
Kobayashi T., Ota S., Tanaka K., Ito Y., Hasegawa M., Umeda Y., Motoi Y., Takanashi M., Yasuhara M., Anno M., Mizuno Y., Mori H.
Ann. Neurol. 53:133-137(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD VAL-583, CHARACTERIZATION OF VARIANT FTD VAL-583.
[75]"An English kindred with a novel recessive tauopathy and respiratory failure."
Nicholl D.J., Greenstone M.A., Clarke C.E., Rizzu P., Crooks D., Crowe A., Trojanowski J.Q., Lee V.M.-Y., Heutink P.
Ann. Neurol. 54:682-686(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669, CHARACTERIZATION OF VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669.
[76]"Tau (MAPT) mutation arg406trp presenting clinically with Alzheimer disease does not share a common founder in western Europe."
Rademakers R., Dermaut B., Peeters K., Cruts M., Heutink P., Goate A., Van Broeckhoven C.
Hum. Mutat. 22:409-411(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTDP17/ALZHEIMER DISEASE TRP-723.
[77]"Progressive supranuclear palsy and Parkinson's disease in a family with a new mutation in the tau gene."
Rossi G., Gasparoli E., Pasquali C., Di Fede G., Testa D., Albanese A., Bracco F., Tagliavini F.
Ann. Neurol. 55:448-448(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ATYPICAL PSNP1 ASN-613 DEL.
[78]"Tau gene delN296 mutation, Parkinson's disease, and atypical supranuclear palsy."
Oliva R., Pastor P.
Ann. Neurol. 55:448-449(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSNP1/ATYPICAL PSNP1 ASN-613 DEL.
[79]"Phenotypic heterogeneity within a new family with the MAPT P301S mutation."
Yasuda M., Nakamura Y., Kawamata T., Kaneyuki H., Maeda K., Komure O.
Ann. Neurol. 58:920-928(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD SER-618.
[80]"A new mutation of the tau gene, G303V, in early-onset familial progressive supranuclear palsy."
Ros R., Thobois S., Streichenberger N., Kopp N., Sanchez M.P., Perez M., Hoenicka J., Avila J., Honnorat J., de Yebenes J.G.
Arch. Neurol. 62:1444-1450(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSNP1 VAL-620.
[81]"A novel mutation (K317M) in the MAPT gene causes FTDP and motor neuron disease."
Zarranz J.J., Ferrer I., Lezcano E., Forcadas M.I., Eizaguirre B., Atares B., Puig B., Gomez-Esteban J.C., Fernandez-Maiztegui C., Rouco I., Perez-Concha T., Fernandez M., Rodriguez O., Rodriguez-Martinez A.B., de Pancorbo M.M., Pastor P., Perez-Tur J.
Neurology 64:1578-1585(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTD MET-634.
[82]"A thorough assessment of benign genetic variability in GRN and MAPT."
Guerreiro R.J., Washecka N., Hardy J., Singleton A.
Hum. Mutat. 31:E1126-E1140(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-17; ALA-30 AND ILE-617.
+Additional computationally mapped references.

Web resources

Alzheimer Research Forum

Tau mutations

Protein Spotlight

Vita minima - Issue 68 of March 2006

Wikipedia

Tau protein entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03778 mRNA. Translation: AAA60615.1.
X14474 mRNA. Translation: CAA32636.1.
AF047863 expand/collapse EMBL AC list , AF027491, AF047856, AF047857, AF027492, AF047858, AF027493, AF047859, AF047860, AF047862, AF027494, AF027495, AF027496 Genomic DNA. Translation: AAC04277.1.
AF027491 expand/collapse EMBL AC list , AF027492, AF027493, AF047860, AF047862, AF027495, AF027496, AF047863 Genomic DNA. Translation: AAC04278.1.
AF027491 expand/collapse EMBL AC list , 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.
CCDSCCDS11499.1. [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]
PIRI52232.
QRHUT1. JS0370.
QRHUT2. PN0001.
S26663.
RefSeqNP_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]
UniGeneHs.101174.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00126.
ProteinModelPortalP10636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110308. 61 interactions.
DIPDIP-29753N.
IntActP10636. 32 interactions.
MINTMINT-134394.

Chemistry

ChEMBLCHEMBL1293224.

PTM databases

PhosphoSiteP10636.

Polymorphism databases

DMDM334302961.

Proteomic databases

MaxQBP10636.
PaxDbP10636.
PRIDEP10636.

Protocols and materials databases

DNASU4137.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262410; ENSP00000262410; ENSG00000186868. [P10636-1]
ENST00000334239; ENSP00000334886; ENSG00000186868. [P10636-2]
ENST00000340799; ENSP00000340438; ENSG00000186868. [P10636-7]
ENST00000344290; ENSP00000340820; ENSG00000186868. [P10636-9]
ENST00000347967; ENSP00000302706; ENSG00000186868. [P10636-3]
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]
GeneID4137.
KEGGhsa:4137.
UCSCuc002ijr.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

CTD4137.
GeneCardsGC17P043971.
GeneReviewsMAPT.
HGNCHGNC:6893. MAPT.
HPACAB000151.
MIM157140. gene+phenotype.
172700. phenotype.
260540. phenotype.
600274. phenotype.
601104. phenotype.
neXtProtNX_P10636.
Orphanet275864. 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.
PharmGKBPA238.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148882.
HOVERGENHBG000991.
KOK04380.
OMAMKVKGAD.
OrthoDBEOG738045.
TreeFamTF316358.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP10636.
BgeeP10636.
GenevestigatorP10636.

Family and domain databases

InterProIPR027324. MAP2/MAP4/Tau.
IPR001084. MAP_tubulin-bd_rpt.
IPR002955. Tau.
[Graphical view]
PANTHERPTHR11501. PTHR11501. 1 hit.
PfamPF00418. Tubulin-binding. 4 hits.
[Graphical view]
PRINTSPR01261. TAUPROTEIN.
PROSITEPS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10636.
GeneWikiTau_protein.
GenomeRNAi4137.
NextBio16246.
PMAP-CutDBP10636.
PROP10636.
SOURCESearch...

Entry information

Entry nameTAU_HUMAN
AccessionPrimary (citable) accession number: P10636
Secondary accession number(s): P18518 expand/collapse secondary AC list , Q14799, Q15549, Q15550, Q15551, Q1RMF6, Q53YB1, Q5CZI7, Q5XWF0, Q6QT54, Q9UDJ3, Q9UMH0, Q9UQ96
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 31, 2011
Last modified: July 9, 2014
This is version 204 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM