UniProtKB - P10636 (TAU_HUMAN)
Microtubule-associated protein tau
MAPT
Functioni
GO - Molecular functioni
- actin binding Source: ParkinsonsUK-UCL
- apolipoprotein binding Source: BHF-UCL
- chaperone binding Source: ARUK-UCL
- DNA binding Source: ParkinsonsUK-UCL
- double-stranded DNA binding Source: ARUK-UCL
- dynactin binding Source: ParkinsonsUK-UCL
- enzyme binding Source: UniProtKB
- histone-dependent DNA binding Source: ARUK-UCL
- Hsp90 protein binding Source: ARUK-UCL
- identical protein binding Source: CAFA
- lipoprotein particle binding Source: UniProtKB
- microtubule binding Source: UniProtKB
- microtubule lateral binding Source: CAFA
- minor groove of adenine-thymine-rich DNA binding Source: ARUK-UCL
- phosphatidylinositol binding Source: ARUK-UCL
- phosphatidylinositol bisphosphate binding Source: ARUK-UCL
- protein kinase binding Source: ARUK-UCL
- protein-macromolecule adaptor activity Source: ARUK-UCL
- protein phosphatase 2A binding Source: ParkinsonsUK-UCL
- RNA binding Source: ARUK-UCL
- sequence-specific DNA binding Source: ARUK-UCL
- SH3 domain binding Source: UniProtKB
- single-stranded DNA binding Source: ARUK-UCL
GO - Biological processi
- activation of cysteine-type endopeptidase activity involved in apoptotic process Source: ParkinsonsUK-UCL
- amyloid fibril formation Source: CAFA
- astrocyte activation Source: ParkinsonsUK-UCL
- axonal transport Source: ParkinsonsUK-UCL
- axonal transport of mitochondrion Source: ParkinsonsUK-UCL
- axon development Source: ARUK-UCL
- cell-cell signaling Source: ARUK-UCL
- cellular response to brain-derived neurotrophic factor stimulus Source: ARUK-UCL
- cellular response to heat Source: ParkinsonsUK-UCL
- cellular response to nerve growth factor stimulus Source: ARUK-UCL
- cellular response to reactive oxygen species Source: ARUK-UCL
- central nervous system neuron development Source: ARUK-UCL
- cytoplasmic microtubule organization Source: ParkinsonsUK-UCL
- generation of neurons Source: UniProtKB
- internal protein amino acid acetylation Source: ARUK-UCL
- intracellular distribution of mitochondria Source: ParkinsonsUK-UCL
- learning or memory Source: ARUK-UCL
- memory Source: ParkinsonsUK-UCL
- microglial cell activation Source: ParkinsonsUK-UCL
- microtubule cytoskeleton organization Source: UniProtKB
- microtubule polymerization Source: ARUK-UCL
- negative regulation of establishment of protein localization to mitochondrion Source: ParkinsonsUK-UCL
- negative regulation of gene expression Source: ARUK-UCL
- negative regulation of kinase activity Source: ParkinsonsUK-UCL
- negative regulation of mitochondrial fission Source: ParkinsonsUK-UCL
- negative regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
- negative regulation of tubulin deacetylation Source: ARUK-UCL
- neurofibrillary tangle assembly Source: ParkinsonsUK-UCL
- neuron projection development Source: GO_Central
- plus-end-directed organelle transport along microtubule Source: ParkinsonsUK-UCL
- positive regulation of axon extension Source: UniProtKB
- positive regulation of cellular protein localization Source: CAFA
- positive regulation of diacylglycerol kinase activity Source: ParkinsonsUK-UCL
- positive regulation of microtubule polymerization Source: UniProtKB
- positive regulation of neuron death Source: ParkinsonsUK-UCL
- positive regulation of protein localization to synapse Source: ParkinsonsUK-UCL
- positive regulation of superoxide anion generation Source: ParkinsonsUK-UCL
- protein homooligomerization Source: ARUK-UCL
- protein polymerization Source: UniProtKB
- regulation of autophagy Source: MGI
- regulation of calcium-mediated signaling Source: ARUK-UCL
- regulation of cellular response to heat Source: ParkinsonsUK-UCL
- regulation of chromosome organization Source: ARUK-UCL
- regulation of long-term synaptic depression Source: ARUK-UCL
- regulation of microtubule cytoskeleton organization Source: CAFA
- regulation of microtubule polymerization Source: ARUK-UCL
- regulation of microtubule polymerization or depolymerization Source: CAFA
- regulation of mitochondrial fission Source: ParkinsonsUK-UCL
- regulation of response to DNA damage stimulus Source: ParkinsonsUK-UCL
- regulation of synaptic plasticity Source: ARUK-UCL
- response to lead ion Source: ARUK-UCL
- rRNA metabolic process Source: ARUK-UCL
- stress granule assembly Source: ARUK-UCL
- supramolecular fiber organization Source: CAFA
- synapse assembly Source: ARUK-UCL
- synapse organization Source: ParkinsonsUK-UCL
Enzyme and pathway databases
PathwayCommonsi | P10636 |
Reactomei | R-HSA-264870, Caspase-mediated cleavage of cytoskeletal proteins R-HSA-9619483, Activation of AMPK downstream of NMDARs [P10636-8] |
SABIO-RKi | P10636 |
SIGNORi | P10636 |
Names & Taxonomyi
Protein namesi | Recommended name: Microtubule-associated protein tauCuratedAlternative name(s): Neurofibrillary tangle protein Paired helical filament-tau Short name: PHF-tau |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:6893, MAPT |
MIMi | 157140, gene+phenotype |
neXtProti | NX_P10636 |
VEuPathDBi | HostDB:ENSG00000186868.15 |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Cytoplasm and Cytosol
- cytosol 3 Publications
Cytoskeleton
- cytoskeleton 1 Publication
Plasma membrane
- Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
Other locations
Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components (PubMed:10747907). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059).2 Publications
Cytoskeleton
- microtubule Source: UniProtKB-KW
- microtubule cytoskeleton Source: CAFA
- tubulin complex Source: UniProtKB
Cytosol
- cytosol Source: CAFA
Extracellular region or secreted
- extracellular region Source: ARUK-UCL
Mitochondrion
- mitochondrion Source: ARUK-UCL
Nucleus
- nuclear periphery Source: UniProtKB
- nuclear speck Source: HPA
- nucleus Source: ParkinsonsUK-UCL
Plasma Membrane
- axolemma Source: CAFA
- plasma membrane Source: UniProtKB
Other locations
- axon Source: UniProtKB
- axon cytoplasm Source: GOC
- cell body Source: ParkinsonsUK-UCL
- cytoplasm Source: UniProtKB
- cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
- dendrite Source: UniProtKB
- dendritic spine Source: ARUK-UCL
- glial cell projection Source: ARUK-UCL
- growth cone Source: UniProtKB
- main axon Source: ARUK-UCL
- membrane raft Source: ARUK-UCL
- neurofibrillary tangle Source: CAFA
- neuron projection Source: GO_Central
- neuronal cell body Source: ParkinsonsUK-UCL
- somatodendritic compartment Source: ParkinsonsUK-UCL
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule, SecretedPathology & Biotechi
Involvement in diseasei
Frontotemporal dementia (FTD)25 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019660 | 5 | R → H in FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro. 1 PublicationCorresponds to variant dbSNP:rs63750959EnsemblClinVar. | 1 | |
Natural variantiVAR_019662 | 583 | L → V in FTD; less able to promote microtubule assembly than wild-type tau. 1 PublicationCorresponds to variant dbSNP:rs63750349Ensembl. | 1 | |
Natural variantiVAR_010345 | 589 | G → V in FTD. 2 PublicationsCorresponds to variant dbSNP:rs63750376Ensembl. | 1 | |
Natural variantiVAR_084361 | 590 | G → R in FTD; increased aggregation propensity and altered binding affinity towards microtubules and F-actin. 1 PublicationCorresponds to variant dbSNP:rs1247408229Ensembl. | 1 | |
Natural variantiVAR_010346 | 596 | N → K in FTD; with parkinsonism. 5 PublicationsCorresponds to variant dbSNP:rs63750756Ensembl. | 1 | |
Natural variantiVAR_010347 | 597 | Missing in FTD. 1 PublicationCorresponds to variant dbSNP:rs63750688Ensembl. | 1 | |
Natural variantiVAR_019663 | 613 | N → 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. 2 PublicationsCorresponds to variant dbSNP:rs63750416Ensembl. | 1 | |
Natural variantiVAR_010348 | 618 | P → L in FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments. 5 PublicationsCorresponds to variant dbSNP:rs63751273Ensembl. | 1 | |
Natural variantiVAR_010349 | 618 | P → S in FTD and CBD; reduction in the ability to promote microtubule assembly. 4 PublicationsCorresponds to variant dbSNP:rs63751438Ensembl. | 1 | |
Natural variantiVAR_010350 | 622 | S → N in FTD; minimal parkinsonism; very early age of onset. 1 PublicationCorresponds to variant dbSNP:rs63751165Ensembl. | 1 | |
Natural variantiVAR_037440 | 634 | K → M in FTD. 1 PublicationCorresponds to variant dbSNP:rs63750092Ensembl. | 1 | |
Natural variantiVAR_010351 | 654 | V → M in FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments. 2 PublicationsCorresponds to variant dbSNP:rs63750570Ensembl. | 1 | |
Natural variantiVAR_019666 | 659 | E → V in FTD. 1 PublicationCorresponds to variant dbSNP:rs63750711Ensembl. | 1 |
Pick disease of the brain (PIDB)5 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_010344 | 574 | K → T in PIDB; reduces the ability to promote microtubule assembly by 70%. 2 PublicationsCorresponds to variant dbSNP:rs63750129Ensembl. | 1 | |
Natural variantiVAR_019665 | 637 | S → F in PIDB; markedly reduced ability of tau to promote microtubule assembly. 1 PublicationCorresponds to variant dbSNP:rs63750635Ensembl. | 1 | |
Natural variantiVAR_019668 | 686 | K → I in PIDB; 90% reduction in the rate of microtubule assembly. 1 PublicationCorresponds to variant dbSNP:rs63751264Ensembl. | 1 | |
Natural variantiVAR_010352 | 706 | G → R in PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%. 2 PublicationsCorresponds to variant dbSNP:rs63750512Ensembl. | 1 |
Progressive supranuclear palsy 1 (PSNP1)6 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019661 | 5 | R → L in PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau. 1 PublicationCorresponds to variant dbSNP:rs63750959EnsemblClinVar. | 1 | |
Natural variantiVAR_037439 | 620 | G → V in PSNP1. 1 PublicationCorresponds to variant dbSNP:rs63751391Ensembl. | 1 |
Parkinson-dementia syndrome (PARDE)
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 515 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 516 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 519 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 531 | S → A: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein. | 1 | |
Mutagenesisi | 548 | T → A: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein. | 1 | |
Mutagenesisi | 548 | T → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 552 | S → A: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein. | 1 | |
Mutagenesisi | 552 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 579 | S → A: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein. | 1 | |
Mutagenesisi | 713 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 721 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 726 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 730 | S → E: No association with plasma membrane. | 1 | |
Mutagenesisi | 739 | S → E: No association with plasma membrane. | 1 |
Keywords - Diseasei
Alzheimer disease, Disease variant, Neurodegeneration, ParkinsonismOrganism-specific databases
DisGeNETi | 4137 |
MalaCardsi | MAPT |
MIMi | 157140, gene+phenotype 172700, phenotype 260540, phenotype 600274, phenotype 601104, phenotype |
NIAGADSi | ENSG00000186868 |
OpenTargetsi | ENSG00000186868 |
Orphaneti | 275864, Behavioral variant of frontotemporal dementia 240071, Classic progressive supranuclear palsy syndrome 100070, Progressive non-fluent aphasia 240103, Progressive supranuclear palsy-corticobasal syndrome 240085, Progressive supranuclear palsy-parkinsonism syndrome 240112, Progressive supranuclear palsy-progressive non-fluent aphasia syndrome 240094, Progressive supranuclear palsy-pure akinesia with gait freezing syndrome 100069, Semantic dementia |
PharmGKBi | PA238 |
Miscellaneous databases
Pharosi | P10636, Tchem |
Chemistry databases
ChEMBLi | CHEMBL1293224 |
DrugBanki | DB00637, Astemizole DB01248, Docetaxel DB14914, Flortaucipir F-18 DB00448, Lansoprazole DB01229, Paclitaxel |
DrugCentrali | P10636 |
Genetic variation databases
BioMutai | MAPT |
DMDMi | 334302961 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000072739 | 2 – 758 | Microtubule-associated protein tauAdd BLAST | 757 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanine1 Publication | 1 | |
Modified residuei | 18 | Phosphotyrosine; by FYN1 Publication | 1 | |
Modified residuei | 29 | PhosphotyrosineBy similarity | 1 | |
Cross-linki | 44 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 46 | PhosphoserineBy similarity | 1 | |
Modified residuei | 61 | PhosphoserineBy similarity | 1 | |
Modified residuei | 69 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 71 | PhosphothreonineBy similarity | 1 | |
Glycosylationi | 87 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 111 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 214 | Phosphoserine; by SGK11 Publication | 1 | |
Glycosylationi | 383 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 396 | Phosphoserine; in PHF-tau1 Publication | 1 | |
Glycosylationi | 467 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 470 | Phosphothreonine; by PDPK11 Publication | 1 | |
Modified residuei | 472 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 480 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 480 | N6-acetyllysine; alternateBy similarity | 1 | |
Glycosylationi | 480 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 484 | Deamidated asparagine; in tau and PHF-tau; partial1 Publication | 1 | |
Modified residuei | 486 | PhosphothreonineBy similarity | 1 | |
Glycosylationi | 491 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 492 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 498 | Phosphothreonine; by PDPK11 Publication | 1 | |
Modified residuei | 502 | PhosphoserineBy similarity | 1 | |
Modified residuei | 508 | PhosphoserineBy similarity | 1 | |
Modified residuei | 512 | PhosphoserineBy similarity | 1 | |
Modified residuei | 514 | Phosphotyrosine; by TTBK11 Publication | 1 | |
Modified residuei | 515 | Phosphoserine; by PDPK1 and TTBK11 Publication | 1 | |
Modified residuei | 516 | Phosphoserine; by PDPK1 and TTBK14 Publications | 1 | |
Modified residuei | 519 | Phosphoserine; by CK1, PDPK1 and TTBK1Combined sources6 Publications | 1 | |
Modified residuei | 522 | Phosphothreonine; by CK1 and PDPK13 Publications | 1 | |
Glycosylationi | 525 | O-linked (GlcNAc) serine1 Publication | 1 | |
Modified residuei | 529 | Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK15 Publications | 1 | |
Modified residuei | 531 | Phosphoserine; by PKA4 Publications | 1 | |
Modified residuei | 534 | Phosphothreonine; by PDPK12 Publications | 1 | |
Modified residuei | 542 | N6-acetyllysineBy similarity | 1 | |
Glycosylationi | 542 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 548 | Phosphothreonine; by GSK3-beta and PDPK1Combined sources3 Publications | 1 | |
Glycosylationi | 551 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 552 | Phosphoserine; by PDPK1Combined sources3 Publications | 1 | |
Modified residuei | 554 | Phosphoserine; by PHK2 Publications | 1 | |
Glycosylationi | 555 | O-linked (GlcNAc) serine1 Publication | 1 | |
Cross-linki | 571 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau1 Publication | ||
Modified residuei | 576 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 576 | N6-methyllysine; alternateBy similarity | 1 | |
Glycosylationi | 576 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Cross-linki | 576 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 579 | Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1, BRSK2 and PHK8 Publications | 1 | |
Cross-linki | 584 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 596 | Deamidated asparagine; in tau and PHF-tau; partial1 Publication | 1 | |
Glycosylationi | 597 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Modified residuei | 598 | N6-acetyllysine; alternateBy similarity | 1 | |
Glycosylationi | 598 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Cross-linki | 598 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 602 | Phosphoserine; by PHK1 Publication | 1 | |
Modified residuei | 607 | N6-acetyllysineBy similarity | 1 | |
Disulfide bondi | 608 ↔ 639 | By similarity | ||
Modified residuei | 610 | Phosphoserine1 Publication | 1 | |
Modified residuei | 615 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 615 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 622 | Phosphoserine; by PHK2 Publications | 1 | |
Modified residuei | 628 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 628 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 628 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau1 Publication | ||
Modified residuei | 634 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 634 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 638 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 638 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 641 | Phosphoserine1 Publication | 1 | |
Modified residuei | 648 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 648 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 660 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 660 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 664 | N6-acetyllysine; alternateBy similarity | 1 | |
Glycosylationi | 664 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Cross-linki | 664 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 666 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 669 | Phosphoserine; by PHK1 Publication | 1 | |
Glycosylationi | 670 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Cross-linki | 670 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau1 Publication | ||
Modified residuei | 673 | Phosphoserine1 Publication | 1 | |
Modified residuei | 686 | N6-acetyllysine; alternateBy similarity | 1 | |
Glycosylationi | 686 | N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro1 Publication | 1 | |
Cross-linki | 686 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Cross-linki | 692 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 702 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 702 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 711 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 713 | Phosphoserine; by CK1 and PDPK1Combined sources6 Publications | 1 | |
Modified residuei | 717 | Phosphoserine; alternateCombined sources | 1 | |
Glycosylationi | 717 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
Modified residuei | 720 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 721 | Phosphoserine; by CK1 and PDPK1Combined sources5 Publications | 1 | |
Modified residuei | 726 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 733 | Phosphoserine; by CaMK2 and TTBK11 Publication | 1 | |
Modified residuei | 739 | Phosphoserine; by PDPK1 and TTBK14 Publications | 1 | |
Modified residuei | 744 | Phosphothreonine; by TTBK11 Publication | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 24 | Not glycated1 Publication | 1 | |
Sitei | 44 | Not glycated1 Publication | 1 | |
Sitei | 67 | Not glycated1 Publication | 1 | |
Sitei | 381 | Not glycated1 Publication | 1 | |
Sitei | 391 | Not glycated1 Publication | 1 | |
Sitei | 392 | Not glycated1 Publication | 1 | |
Sitei | 394 | Not glycated1 Publication | 1 | |
Sitei | 465 | Not glycated1 Publication | 1 | |
Sitei | 497 | Not glycated1 Publication | 1 | |
Sitei | 507 | Not glycated1 Publication | 1 | |
Sitei | 541 | Not glycated1 Publication | 1 | |
Sitei | 557 | Not glycated1 Publication | 1 | |
Sitei | 571 | Not glycated1 Publication | 1 | |
Sitei | 574 | Not glycated1 Publication | 1 | |
Sitei | 584 | Not glycated1 Publication | 1 | |
Sitei | 591 | Not glycated1 Publication | 1 | |
Sitei | 607 | Not glycated1 Publication | 1 | |
Sitei | 611 | Not glycated1 Publication | 1 | |
Sitei | 615 | Not glycated1 Publication | 1 | |
Sitei | 628 | Not glycated1 Publication | 1 | |
Sitei | 634 | Not glycated1 Publication | 1 | |
Sitei | 638 | Not glycated1 Publication | 1 | |
Sitei | 648 | Not glycated1 Publication | 1 | |
Sitei | 657 | Not glycated1 Publication | 1 | |
Sitei | 660 | Not glycated1 Publication | 1 | |
Sitei | 687 | Not glycated1 Publication | 1 | |
Sitei | 692 | Not glycated1 Publication | 1 | |
Sitei | 700 | Not glycated1 Publication | 1 | |
Sitei | 702 | Not glycated1 Publication | 1 | |
Sitei | 712 | Not glycated1 Publication | 1 | |
Sitei | 755 | Not glycated1 Publication | 1 |
Keywords - PTMi
Acetylation, Disulfide bond, Glycation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P10636 |
jPOSTi | P10636 |
MassIVEi | P10636 |
MaxQBi | P10636 |
PaxDbi | P10636 |
PeptideAtlasi | P10636 |
PRIDEi | P10636 |
ProteomicsDBi | 12705 [P10636-9] 52624 [P10636-1] 52625 [P10636-2] 52626 [P10636-3] 52627 [P10636-4] 52628 [P10636-5] 52629 [P10636-6] 52630 [P10636-7] 52631 [P10636-8] 52632 [P10636-9] |
TopDownProteomicsi | P10636-3 [P10636-3] |
PTM databases
GlyConnecti | 2885, 1 O-Linked glycan (6 sites) |
GlyGeni | P10636, 3 sites |
iPTMneti | P10636 |
MetOSitei | P10636 |
PhosphoSitePlusi | P10636 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSG00000186868, Expressed in parietal lobe and 233 other tissues |
ExpressionAtlasi | P10636, baseline and differential |
Genevisiblei | P10636, HS |
Organism-specific databases
HPAi | ENSG00000186868, Group enriched (brain, skeletal muscle) |
Interactioni
Subunit structurei
Interacts with MARK1, MARK2, MARK3 AND MARK4 (PubMed:23666762).
Interacts with PSMC2 through SQSTM1 (By similarity).
Interacts with SQSTM1 when polyubiquitinated (PubMed:15953362).
Interacts with FKBP4 (By similarity). Binds to CSNK1D (PubMed:14761950).
Interacts with SGK1 (PubMed:16982696).
Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-396 (PubMed:19542233).
Interacts with PIN1 (PubMed:11313338).
Interacts with LRRK2 (PubMed:26014385).
Interacts with LRP1, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (PubMed:32296178).
By similarity8 PublicationsBinary interactionsi
P10636
Isoform Fetal-tau [P10636-2]
With | #Exp. | IntAct |
---|---|---|
FYN [P06241] | 2 | EBI-7796412,EBI-515315 |
LRRK2 [Q5S007] | 3 | EBI-7796412,EBI-5323863 |
SFN [P31947] | 2 | EBI-7796412,EBI-476295 |
YWHAZ [P63104] | 2 | EBI-7796412,EBI-347088 |
Isoform Tau-A [P10636-3]
With | #Exp. | IntAct |
---|---|---|
YWHAZ [P63104] | 9 | EBI-7145070,EBI-347088 |
Isoform Tau-C [P10636-5]
With | #Exp. | IntAct |
---|---|---|
FYN [P06241] | 2 | EBI-21313635,EBI-515315 |
Isoform Tau-D [P10636-6]
Isoform Tau-E [P10636-7]
With | #Exp. | IntAct |
---|---|---|
BIN1 - isoform IIA [O00499-1] | 5 | EBI-6926270,EBI-6926280 |
MAPT - isoform Tau-F [P10636-8]
GO - Molecular functioni
- actin binding Source: ParkinsonsUK-UCL
- apolipoprotein binding Source: BHF-UCL
- chaperone binding Source: ARUK-UCL
- dynactin binding Source: ParkinsonsUK-UCL
- enzyme binding Source: UniProtKB
- Hsp90 protein binding Source: ARUK-UCL
- identical protein binding Source: CAFA
- microtubule binding Source: UniProtKB
- microtubule lateral binding Source: CAFA
- protein kinase binding Source: ARUK-UCL
- protein phosphatase 2A binding Source: ParkinsonsUK-UCL
- SH3 domain binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 110308, 247 interactors |
CORUMi | P10636 |
DIPi | DIP-29753N |
ELMi | P10636 |
IntActi | P10636, 591 interactors |
MINTi | P10636 |
STRINGi | 9606.ENSP00000340820 |
Chemistry databases
BindingDBi | P10636 |
Miscellaneous databases
RNActi | P10636, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P10636 |
SMRi | P10636 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P10636 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 561 – 591 | Tau/MAP 1PROSITE-ProRule annotation1 PublicationAdd BLAST | 31 | |
Repeati | 592 – 622 | Tau/MAP 2PROSITE-ProRule annotation1 PublicationAdd BLAST | 31 | |
Repeati | 623 – 653 | Tau/MAP 3PROSITE-ProRule annotation1 PublicationAdd BLAST | 31 | |
Repeati | 654 – 685 | Tau/MAP 4PROSITE-ProRule annotation1 PublicationAdd BLAST | 32 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 561 – 685 | Microtubule-binding domain1 PublicationAdd BLAST | 125 |
Domaini
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG2418, Eukaryota |
GeneTreei | ENSGT00940000155494 |
HOGENOMi | CLU_021741_2_0_1 |
InParanoidi | P10636 |
OMAi | EPRQEFN |
OrthoDBi | 716848at2759 |
TreeFami | TF316358 |
Family and domain databases
DisProti | DP01100 [P10636-8] |
InterProi | View protein in InterPro IPR001084, MAP_tubulin-bd_rpt IPR002955, Tau |
Pfami | View protein in Pfam PF00418, Tubulin-binding, 4 hits |
PRINTSi | PR01261, TAUPROTEIN |
PROSITEi | View protein in PROSITE PS00229, TAU_MAP_1, 4 hits PS51491, TAU_MAP_2, 4 hits |
s (9+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 9 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 9 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT
60 70 80 90 100
PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG
110 120 130 140 150
TTAEEAGIGD TPSLEDEAAG HVTQEPESGK VVQEGFLREP GPPGLSHQLM
160 170 180 190 200
SGMPGAPLLP EGPREATRQP SGTGPEDTEG GRHAPELLKH QLLGDLHQEG
210 220 230 240 250
PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA QDGRPPQTAA
260 270 280 290 300
REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE
310 320 330 340 350
FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD
360 370 380 390 400
LPEPSEKQPA AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS
410 420 430 440 450
AKTLKNRPCL SPKHPTPGSS DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG
460 470 480 490 500
SSGAKEMKLK GADGKTKIAT PRGAAPPGQK GQANATRIPA KTPPAPKTPP
510 520 530 540 550
SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP KKVAVVRTPP
560 570 580 590 600
KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD
610 620 630 640 650
LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG
660 670 680 690 700
GGQVEVKSEK LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK
710 720 730 740 750
AKTDHGAEIV YKSPVVSGDT SPRHLSNVSS TGSIDMVDSP QLATLADEVS
ASLAKQGL
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.
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.
The sequence of this isoform differs from the canonical sequence as follows:
74-102: Missing.
125-375: Missing.
395-460: Missing.
592-622: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
125-375: Missing.
395-460: Missing.
592-622: Missing.