[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FETAL-TAU). TISSUE=Brain; DOI=10.1073/pnas.85.11.4051; PubMed=3131773 [NCBI, ExPASy, EBI, Israel, Japan] Goedert M., Wischik C., Crowther R., Walker J., Klug A.; "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."; Proc. Natl. Acad. Sci. U.S.A. 85:4051-4055(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-D). TISSUE=Brain; PubMed=2498079 [NCBI, ExPASy, EBI, Israel, Japan] Goedert M., Spillantini M.G., Potier M.-C., Ulrich J., Crowther R.A.; "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."; EMBO J. 8:393-399(1989).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A AND FETAL-TAU). TISSUE=Fetal brain; DOI=10.1016/0896-6273(89)90050-0; PubMed=2516729 [NCBI, ExPASy, EBI, Israel, Japan] Lee G., Neve R.L., Kosik K.S.; "The microtubule binding domain of tau protein."; Neuron 2:1615-1624(1989).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B; TAU-C; TAU-E AND TAU-F). TISSUE=Brain; DOI=10.1016/0896-6273(89)90210-9; PubMed=2484340 [NCBI, ExPASy, EBI, Israel, Japan] Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A.; "Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease."; Neuron 3:519-526(1989).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PNS-TAU; FETAL-TAU AND TAU-F), AND ALTERNATIVE SPLICING. DOI=10.1021/bi00158a027; PubMed=1420178 [NCBI, ExPASy, EBI, Israel, Japan] Andreadis A., Brown W.M., Kosik K.S.; "Structure and novel exons of the human tau gene."; Biochemistry 31:10626-10633(1992).
[6]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-E). Chun J., Kwon T., Lee E.-J., Hyun S.-H., Kang S.S.; "Cloning of tau-related genes."; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FETAL-TAU). 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.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FETAL-TAU AND TAU-D). TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[9]	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. TISSUE=Brain; PubMed=1512244 [NCBI, ExPASy, EBI, Israel, Japan] Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K., Ihara Y.; "Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain."; J. Biol. Chem. 267:17047-17054(1992).
[10]	PROTEIN SEQUENCE OF 25-44; 529-538; 560-571 AND 671-686, AND MASS SPECTROMETRY. TISSUE=Fetal brain cortex; Lubec G., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[11]	NUCLEOTIDE SEQUENCE [MRNA] OF 466-740 (ISOFORMS TAU-A/TAU-B/TAU-C/FETAL-TAU). Han J., Zhang J., Dong X.-P.; "Molecular interactions of recombinant neural protein tau with recombinant and native PrP proteins in vitro."; Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[12]	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, AND MASS SPECTROMETRY. DOI=10.1074/jbc.M512786200; PubMed=16443603 [NCBI, ExPASy, EBI, Israel, Japan] Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.; "Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation."; J. Biol. Chem. 281:10825-10838(2006).
[13]	PROTEIN SEQUENCE OF 577-584; 608-611; 616-628; 639-648 AND 671-686, PHOSPHORYLATION, AND MUTAGENESIS. DOI=10.1074/jbc.270.13.7679; PubMed=7706316 [NCBI, ExPASy, EBI, Israel, Japan] Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., Meyer H.E., Mandelkow E.-M., Mandelkow E.; "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."; J. Biol. Chem. 270:7679-7688(1995).
[14]	NUCLEOTIDE SEQUENCE [MRNA] OF 592-622 (ISOFORMS PNS-TAU/TAU-D/TAU-E/TAU-F). TISSUE=Brain; DOI=10.1016/0006-291X(89)92240-7; PubMed=2495000 [NCBI, ExPASy, EBI, Israel, Japan] Mori H., Hamada Y., Kawaguchi M., Honda T., Kondo J., Ihara Y.; "A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments."; Biochem. Biophys. Res. Commun. 159:1221-1226(1989).
[15]	PROTEIN SEQUENCE OF 616-712. PubMed=1915258 [NCBI, ExPASy, EBI, Israel, Japan] Jakes R., Novak M., Davison M., Wischik C.M.; "Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease."; EMBO J. 10:2725-2729(1991).
[16]	IDENTIFICATION (ISOFORM TAU-G). DOI=10.1002/humu.20086; PubMed=15365985 [NCBI, ExPASy, EBI, Israel, Japan] Rademakers R., Cruts M., van Broeckhoven C.; "The role of tau (MAPT) in frontotemporal dementia and related tauopathies."; Hum. Mutat. 24:277-295(2004).
[17]	REVIEW. DOI=10.1016/0166-2236(91)90105-4; PubMed=1713721 [NCBI, ExPASy, EBI, Israel, Japan] Goedert M., Crowther R.A., Garner C.C.; "Molecular characterization of microtubule-associated proteins tau and MAP2."; Trends Neurosci. 14:193-199(1991).
[18]	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, AND ABSENCE 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. PubMed=9326300 [NCBI, ExPASy, EBI, Israel, Japan] Nacharaju P., Ko L., Yen S.H.; "Characterization of in vitro glycation sites of tau."; J. Neurochem. 69:1709-1719(1997).
[19]	PHOSPHORYLATION, AND MUTAGENESIS. DOI=10.1006/abbi.1998.0813; PubMed=9735171 [NCBI, ExPASy, EBI, Israel, Japan] Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., Iqbal K.; "Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules."; Arch. Biochem. Biophys. 357:299-309(1998).
[20]	PHOSPHORYLATION, AND MUTAGENESIS. PubMed=9614189 [NCBI, ExPASy, EBI, Israel, Japan] Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., Trinczek B., Biernat J., Godemann R., Mandelkow E.-M., Mandelkow E.; "The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease."; Mol. Biol. Cell 9:1495-1512(1998).
[21]	SUBCELLULAR LOCATION, AND PHOSPHORYLATION. DOI=10.1074/jbc.M000389200; PubMed=10747907 [NCBI, ExPASy, EBI, Israel, Japan] Maas T., Eidenmueller J., Brandt R.; "Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments."; J. Biol. Chem. 275:15733-15740(2000).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[23]	INTERACTION WITH SQSTM1, UBIQUITINATION, AND PROTEASOMAL DEGRADATION. DOI=10.1111/j.1471-4159.2005.03181.x; PubMed=15953362 [NCBI, ExPASy, EBI, Israel, Japan] Babu J.R., Geetha T., Wooten M.W.; "Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation."; J. Neurochem. 94:192-203(2005).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-548; SER-673; SER-713; THR-720 AND SER-721, AND MASS SPECTROMETRY. TISSUE=Brain cortex; DOI=10.1021/pr0498436; PubMed=15822905 [NCBI, ExPASy, EBI, Israel, Japan] DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A.; "Phosphoproteomic analysis of synaptosomes from human cerebral cortex."; J. Proteome Res. 4:306-315(2005).
[25]	PHOSPHORYLATION AT TYR-514; SER-515; SER-516; SER-519; SER-733; SER-739 AND THR-744. DOI=10.1111/j.1471-4159.2006.04059.x; PubMed=16923168 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Cerny R.L., Buescher J.L., Ikezu T.; "Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation."; J. Neurochem. 98:1573-1584(2006).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-548 AND SER-552, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[27]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-529; THR-534 AND SER-721, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[28]	STRUCTURE BY NMR OF 542-554 IN COMPLEX WITH PIN1. DOI=10.1074/jbc.M010327200; PubMed=11313338 [NCBI, ExPASy, EBI, Israel, Japan] Wintjens R., Wieruszeski J.-M., Drobecq H., Rousselot-Pailley P., Buee L., Lippens G., Landrieu I.; "1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides."; J. Biol. Chem. 276:25150-25156(2001).
[29]	REVIEW ON VARIANTS. DOI=10.1016/S0925-4439(00)00037-5; PubMed=10899436 [NCBI, ExPASy, EBI, Israel, Japan] Goedert M., Spillantini M.G.; "Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease."; Biochim. Biophys. Acta 1502:110-121(2000).
[30]	VARIANT FTDP17 MET-654, AND VARIANTS ASN-285; ALA-289; TYR-441 AND PRO-447. DOI=10.1002/ana.410430617; PubMed=9629852 [NCBI, ExPASy, EBI, Israel, Japan] Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L., Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D.; "Tau is a candidate gene for chromosome 17 frontotemporal dementia."; Ann. Neurol. 43:815-825(1998).
[31]	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).
[32]	VARIANT FTDP17 LEU-618. DOI=10.1093/hmg/7.11.1825; PubMed=9736786 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Segregation of a missense mutation in the microtubule-associated protein tau gene with familial frontotemporal dementia and parkinsonism."; Hum. Mol. Genet. 7:1825-1829(1998).
[33]	VARIANTS FTDP17 VAL-589; LEU-618 AND TRP-723. DOI=10.1038/31508; PubMed=9641683 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17."; Nature 393:702-705(1998).
[34]	VARIANT PPND LYS-596, AND VARIANT FTDP17 LEU-618. DOI=10.1073/pnas.95.22.13103; PubMed=9789048 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17."; Proc. Natl. Acad. Sci. U.S.A. 95:13103-13107(1998).
[35]	VARIANT PPND LYS-596. DOI=10.1007/s004010051052; PubMed=10412802 [NCBI, ExPASy, EBI, Israel, Japan] Delisle M.-B., Murrell J.R., Richardson R., Trofatter J.A., Rascol O., Soulages X., Mohr M., Calvas P., Ghetti B.; "A mutation at codon 279 (N279K) in exon 10 of the Tau gene causes a tauopathy with dementia and supranuclear palsy."; Acta Neuropathol. 98:62-77(1999).
[36]	VARIANTS FTDP17 VAL-589; LYS-597 DEL; LEU-618 AND TRP-723. DOI=10.1086/302256; PubMed=9973279 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands."; Am. J. Hum. Genet. 64:414-421(1999).
[37]	VARIANT FTDP17 SER-618. DOI=10.1002/1531-8249(199911)46:5<708::AID-ANA5>3.0.CO;2-K; PubMed=10553987 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "FTDP-17: an early-onset phenotype with parkinsonism and epileptic seizures caused by a novel mutation."; Ann. Neurol. 46:708-715(1999).
[38]	VARIANTS FTDP17 LEU-618; MET-654 AND TRP-723. DOI=10.1016/S0014-5793(99)00294-X; PubMed=10214944 [NCBI, ExPASy, EBI, Israel, Japan] Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M., Yen S.H.; "Accelerated filament formation from tau protein with specific FTDP-17 missense mutations."; FEBS Lett. 447:195-199(1999).
[39]	VARIANT FTDP17/CBD SER-618. PubMed=10374757 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau."; J. Neuropathol. Exp. Neurol. 58:667-677(1999).
[40]	VARIANT DEMENTIA ARG-706. PubMed=10604746 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Tau gene mutation G389R causes a tauopathy with abundant pick body-like inclusions and axonal deposits."; J. Neuropathol. Exp. Neurol. 58:1207-1226(1999).
[41]	VARIANT PPND LYS-596. PubMed=10489057 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A mutation in the microtubule-associated protein tau in pallido-nigro-luysian degeneration."; Neurology 53:864-868(1999).
[42]	VARIANTS PSP ASN-285 AND ALA-289. PubMed=10534245 [NCBI, ExPASy, EBI, Israel, Japan] Higgins J.J., Adler R.L., Loveless J.M.; "Mutational analysis of the tau gene in progressive supranuclear palsy."; Neurology 53:1421-1424(1999).
[43]	VARIANT FTDP17 ASN-622. PubMed=10208578 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A distinct familial presenile dementia with a novel missense mutation in the tau gene."; NeuroReport 10:497-501(1999).
[44]	VARIANT FTDP17 VAL-659. DOI=10.1002/1531-8249(200012)48:6<850::AID-ANA5>3.3.CO;2-M; PubMed=11117541 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Frontotemporal dementia with novel tau pathology and a Glu342Val tau mutation."; Ann. Neurol. 48:850-858(2000).
[45]	VARIANTS DEMENTIA THR-574 AND ARG-706, AND CHARACTERIZATION OF VARIANTS DEMENTIA THR-574 AND ARG-706. DOI=10.1002/1531-8249(200012)48:6<859::AID-ANA6>3.3.CO;2-T; PubMed=11117542 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Pick's disease is associated with mutations in the tau gene."; Ann. Neurol. 48:859-867(2000).
[46]	VARIANT DEMENTIA THR-574. PubMed=11089577 [NCBI, ExPASy, EBI, Israel, Japan] Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R., Xuereb J.H., Crowther R.A., Spillantini M.G.; "Tau gene mutation K257T causes a tauopathy similar to Pick's disease."; J. Neuropathol. Exp. Neurol. 59:990-1001(2000).
[47]	VARIANT PPND LYS-596. PubMed=10802785 [NCBI, ExPASy, EBI, Israel, Japan] Arima K., Kowalska A., Hasegawa M., Mukoyama M., Watanabe R., Kawai M., Takahashi K., Iwatsubo T., Tabira T., Sunohara N.; "Two brothers with frontotemporal dementia and parkinsonism with an N279K mutation of the tau gene."; Neurology 54:1787-1795(2000).
[48]	VARIANT FTDP17 SER-618. PubMed=11071507 [NCBI, ExPASy, EBI, Israel, Japan] Yasuda M., Yokoyama K., Nakayasu T., Nishimura Y., Matsui M., Yokoyama T., Miyoshi K., Tanaka C.; "A Japanese patient with frontotemporal dementia and parkinsonism by a tau P301S mutation."; Neurology 55:1224-1227(2000).
[49]	VARIANT FTPD17 HIS-613. PubMed=11585254 [NCBI, ExPASy, EBI, Israel, Japan] Iseki E., Matsumura T., Marui W., Hino H., Odawara T., Sugiyama N., Suzuki K., Sawada H., Arai T., Kosaka K.; "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."; Acta Neuropathol. 102:285-292(2001).
[50]	VARIANT PSP ASN-613 DEL. DOI=10.1002/1531-8249(20010201)49:2<263::AID-ANA50>3.0.CO;2-K; PubMed=11220749 [NCBI, ExPASy, EBI, Israel, Japan] Pastor P., Pastor E., Carnero C., Vela R., Garcia T., Amer G., Tolosa E., Oliva R.; "Familial atypical progressive supranuclear palsy associated with homozigosity for the delN296 mutation in the tau gene."; Ann. Neurol. 49:263-267(2001).
[51]	VARIANT PICK DISEASE ILE-686, AND CHARACTERIZATION OF VARIANT PICK DISEASE ILE-686. DOI=10.1002/ana.1223; PubMed=11601501 [NCBI, ExPASy, EBI, Israel, Japan] Neumann M., Schulz-Schaeffer W., Crowther R.A., Smith M.J., Spillantini M.G., Goedert M., Kretzschmar H.A.; "Pick's disease associated with the novel Tau gene mutation K369I."; Ann. Neurol. 50:503-513(2001).
[52]	CHARACTERIZATION OF VARIANT FTDP17 TRP-723. DOI=10.1016/S0014-5793(01)02267-0; PubMed=11278002 [NCBI, ExPASy, EBI, Israel, Japan] Connell J.W., Gibb G.M., Betts J.C., Blackstock W.P., Gallo J.-M., Lovestone S., Hutton M., Anderton B.H.; "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."; FEBS Lett. 493:40-44(2001).
[53]	VARIANT PPND LYS-596. PubMed=12473774 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Clinical and genetic studies of families with the tau N279K mutation (FTDP-17)."; Neurology 59:1791-1793(2002).
[54]	VARIANT PICK DISEASE PHE-637, AND CHARACTERIZATION OF VARIANT PICK DISEASE PHE-637. DOI=10.1002/ana.10140; PubMed=11891833 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A novel tau mutation, S320F, causes a tauopathy with inclusions similar to those in Pick's disease."; Ann. Neurol. 51:373-376(2002).
[55]	VARIANT FTDP17 HIS-5, AND CHARACTERIZATION OF VARIANT FTDP17 HIS-5. DOI=10.1002/ana.10163; PubMed=11921059 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi S., Toyoshima Y., Hasegawa M., Umeda Y., Wakabayashi K., Tokiguchi S., Iwatsubo T., Takahashi H.; "Late-onset frontotemporal dementia with a novel exon 1 (Arg5His) tau gene mutation."; Ann. Neurol. 51:525-530(2002).
[56]	VARIANT PSP LEU-5, AND CHARACTERIZATION OF VARIANT PSP LEU-5. DOI=10.1002/ana.10340; PubMed=12325083 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "An R5L tau mutation in a subject with a progressive supranuclear palsy phenotype."; Ann. Neurol. 52:511-516(2002).
[57]	CHARACTERIZATION OF VARIANTS FTDP17 ASN-613 DEL AND HIS-613. DOI=10.1046/j.0022-3042.2001.00729.x; PubMed=11906000 [NCBI, ExPASy, EBI, Israel, Japan] Yoshida H., Crowther R.A., Goedert M.; "Functional effects of tau gene mutations deltaN296 and N296H."; J. Neurochem. 80:548-551(2002).
[58]	VARIANT FTDP17 TRP-723. PubMed=11889249 [NCBI, ExPASy, EBI, Israel, Japan] Saito Y., Geyer A., Sasaki R., Kuzuhara S., Nanba E., Miyasaka T., Suzuki K., Murayama S.; "Early-onset, rapidly progressive familial tauopathy with R406W mutation."; Neurology 58:811-813(2002).
[59]	VARIANT FTDP17 VAL-583, AND CHARACTERIZATION OF VARIANT FTDP17 VAL-583. DOI=10.1002/ana.10447; PubMed=12509859 [NCBI, ExPASy, EBI, Israel, Japan] Kobayashi T., Ota S., Tanaka K., Ito Y., Hasegawa M., Umeda Y., Motoi Y., Takanashi M., Yasuhara M., Anno M., Mizuno Y., Mori H.; "A novel L266V mutation of the tau gene causes frontotemporal dementia with a unique tau pathology."; Ann. Neurol. 53:133-137(2003).
[60]	VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669, AND CHARACTERIZATION OF VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669. DOI=10.1002/ana.10747; PubMed=14595660 [NCBI, ExPASy, EBI, Israel, Japan] Nicholl D.J., Greenstone M.A., Clarke C.E., Rizzu P., Crooks D., Crowe A., Trojanowski J.Q., Lee V.M.-Y., Heutink P.; "An English kindred with a novel recessive tauopathy and respiratory failure."; Ann. Neurol. 54:682-686(2003).
[61]	VARIANT FTDP17/ALZHEIMER DISEASE TRP-723. DOI=10.1002/humu.10269; PubMed=14517953 [NCBI, ExPASy, EBI, Israel, Japan] Rademakers R., Dermaut B., Peeters K., Cruts M., Heutink P., Goate A., Van Broeckhoven C.; "Tau (MAPT) mutation arg406trp presenting clinically with Alzheimer disease does not share a common founder in western Europe."; Hum. Mutat. 22:409-411(2003).
[62]	VARIANT ATYPICAL PSP ASN-613 DEL. DOI=10.1002/ana.20006; PubMed=14991829 [NCBI, ExPASy, EBI, Israel, Japan] Rossi G., Gasparoli E., Pasquali C., Di Fede G., Testa D., Albanese A., Bracco F., Tagliavini F.; "Progressive supranuclear palsy and Parkinson's disease in a family with a new mutation in the tau gene."; Ann. Neurol. 55:448-448(2004).
[63]	VARIANT PSP/ATYPICAL PSP ASN-613 DEL. DOI=10.1002/ana.20025; PubMed=14991828 [NCBI, ExPASy, EBI, Israel, Japan] Oliva R., Pastor P.; "Tau gene delN296 mutation, Parkinson's disease, and atypical supranuclear palsy."; Ann. Neurol. 55:448-449(2004).
[64]	VARIANT FTDP17 SER-618. DOI=10.1002/ana.20668; PubMed=16240366 [NCBI, ExPASy, EBI, Israel, Japan] Yasuda M., Nakamura Y., Kawamata T., Kaneyuki H., Maeda K., Komure O.; "Phenotypic heterogeneity within a new family with the MAPT P301S mutation."; Ann. Neurol. 58:920-928(2005).
[65]	VARIANT PSP VAL-620. DOI=10.1001/archneur.62.9.1444; PubMed=16157753 [NCBI, ExPASy, EBI, Israel, Japan] Ros R., Thobois S., Streichenberger N., Kopp N., Sanchez M.P., Perez M., Hoenicka J., Avila J., Honnorat J., de Yebenes J.G.; "A new mutation of the tau gene, G303V, in early-onset familial progressive supranuclear palsy."; Arch. Neurol. 62:1444-1450(2005).
[66]	VARIANT FTDP17 MET-634. DOI=10.1212/01.WNL.0000160116.65034.12; PubMed=15883319 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A novel mutation (K317M) in the MAPT gene causes FTDP and motor neuron disease."; Neurology 64:1578-1585(2005).

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 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.
SUBUNIT: Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated.
INTERACTION:
Self; NbExp=1; IntAct=EBI-366182, EBI-366182;
P05067:APP; NbExp=4; IntAct=EBI-366182, EBI-77613;
P05067:APP; NbExp=1; IntAct=EBI-366233, EBI-77613;
P49840:GSK3A; NbExp=1; IntAct=EBI-366182, EBI-1044067;
Q9UNE7:STUB1; NbExp=2; IntAct=EBI-366182, EBI-357085;
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, axon. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.

ALTERNATIVE PRODUCTS: 9 named isoforms [FASTA] produced by alternative splicing. 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.

Name	PNS-tau
Isoform ID	P10636-1
This is the isoform sequence displayed in this entry.

Name	Fetal-tau
Isoform ID	P10636-2
Features which should be applied to build the isoform sequence: VSP_003176, VSP_003177, VSP_003179, VSP_003180, VSP_003181.

Name	Tau-A
Isoform ID	P10636-3
Features which should be applied to build the isoform sequence: VSP_003175, VSP_003176, VSP_003177, VSP_003178, VSP_003179, VSP_003180, VSP_003181.

Name	Tau-B
Isoform ID	P10636-4
Features which should be applied to build the isoform sequence: VSP_003177, VSP_003179, VSP_003180, VSP_003181.

Name	Tau-C
Synonyms	Tau-3
Isoform ID	P10636-5
Features which should be applied to build the isoform sequence: VSP_003179, VSP_003180, VSP_003181.

Name	Tau-D
Isoform ID	P10636-6
Features which should be applied to build the isoform sequence: VSP_003176, VSP_003177, VSP_003179, VSP_003180.

Name	Tau-E
Isoform ID	P10636-7
Features which should be applied to build the isoform sequence: VSP_003177, VSP_003179, VSP_003180.

Name	Tau-F
Synonyms	Tau-4
Isoform ID	P10636-8
Features which should be applied to build the isoform sequence: VSP_003179, VSP_003180.

Name	Tau-G
Isoform ID	P10636-9
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_026780.

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 is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau 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.
PTM: Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK: CDC2, CDK5, GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in PHF-tau), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) in Alzheimer diseased brains. Phosphorylation decreases with age. Phosphorylation within tau's repeat domain or in flanking regions seems to reduce tau'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.
PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur.
PTM: Glycation of PHF-tau, but not normal brain tau. 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.
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).
DISEASE: Defects in MAPT are a cause of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274, 172700]; also called frontotemporal dementia (FTD) or historically termed Pick complex. This form of frontotemporal dementia is characterized by 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.
DISEASE: Defects in MAPT are a cause of pallido-ponto-nigral degeneration (PPND) [MIM:168610]. The clinical features include ocular motility abnormalities, dystonia and urinary incontinence, besides progressive parkinsonism and dementia.
DISEASE: Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease.
DISEASE: Defects in MAPT are a cause of progressive supranuclear palsy (PSP) [MIM:601104, 260540]; also known as Steele-Richardson-Olszewski syndrome. PSP is 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.
DISEASE: Defects in MAPT may be a cause of hereditary dysphasic disinhibition dementia (HDDD) [MIM:607485]. HDDD is a frontotemporal dementia characterized by progressive cognitive deficits with memory loss and personality changes, severe dysphasic disturbances leading to mutism, and hyperphagia.
SIMILARITY: Contains 4 Tau/MAP repeats.
WEB RESOURCE: Name=Alzheimer Research Forum; Note=Tau mutations; URL="http://www.alzforum.org/res/com/mut/tau/default.asp";.
WEB RESOURCE: Name=Protein Spotlight; Note=Vita minima - Issue 68 of March 2006; URL="http://www.expasy.org/spotlight/back_issues/sptlt068.shtml";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=MAPT";.
WEB RESOURCE: Name=Wikipedia; Note=Tau protein entry; URL="http://en.wikipedia.org/wiki/Tau_protein";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J03778; AAA60615.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X14474; CAA32636.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047863; AAC04277.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027491; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047856; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047857; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027492; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047858; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027493; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047859; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047860; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047862; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027494; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027495; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027496; AAC04277.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027491; AAC04278.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027492; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027493; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047860; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047862; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027495; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027496; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047863; AAC04278.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027491; AAC04279.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047856; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047857; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027492; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027493; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047860; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047862; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027494; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027495; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF027496; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047863; AAC04279.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047861; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AY730549; AAU45390.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006772; AAP35418.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000558; AAH00558.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC098281; AAH98281.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099721; AAH99721.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101936; AAI01937.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114504; AAI14505.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114948; AAI14949.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY526356; AAS17881.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M25298; AAA57264.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BN000503; CAG26750.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00025499; -.
IPI00026836; -.
IPI00217976; -.
IPI00220171; -.
IPI00220173; -.
IPI00220174; -.
IPI00220175; -.
IPI00293683; -.
IPI00747283; -.

PIR

I52232; I52232.
JS0370; QRHUT1.
PN0001; QRHUT2.
S26663; S26663.

RefSeq

NP_001116538.1; -.
NP_001116539.1; -.
NP_005901.2; -.
NP_058518.1; -.
NP_058519.2; -.
NP_058525.1; -.

UniGene

Hs.101174

3D structure databases

PDB

1I8H; NMR; -; A=542-554.

[ExPASy / RCSB / EBI]

1I8H; -.

DP00126; -.

Protein-protein interaction databases

IntAct

P10636; 6.

PTM databases

PhosphoSite

P10636; -.

Enzyme and pathway databases

Pathway_Interaction_DB

lysophospholipid_pathway; LPA receptor mediated events.
reelinpathway; Reelin signaling pathway.
p38gammadeltapathway; Signaling mediated by p38-gamma and p38-delta.

Reactome

REACT_578; Apoptosis.

Organism-specific databases

GC17P041327; -.

HIX0013906; -.

HGNC:6893; MAPT.

CAB000151; -.

157140; gene+phenotype. [NCBI / EBI]
172700; phenotype. [NCBI / EBI]
260540; phenotype. [NCBI / EBI]
600274; phenotype. [NCBI / EBI]
601104; phenotype. [NCBI / EBI]
607485; phenotype. [NCBI / EBI]

Orphanet

36385; Fronto-temporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17).
282; Frontotemporal dementia.
33540; Parkinson's disease dementia, familial.
2883; Pick disease of brain.
683; Supranuclear palsy, progressive.

PharmGKB

PA238; -.

Gene expression databases

ArrayExpress

P10636; -.

Bgee

P10636; -.

GermOnline

ENSG00000186868; Homo sapiens.

Ontologies

GO:0030424;	Cellular component: axon (inferred from direct assay from UniProtKB).
GO:0005829;	Cellular component: cytosol (traceable author statement from ProtInc).
GO:0030426;	Cellular component: growth cone (inferred from direct assay from UniProtKB).
GO:0005874;	Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
GO:0005875;	Cellular component: microtubule associated complex (traceable author statement from ProtInc).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0045298;	Cellular component: tubulin complex (inferred from direct assay from UniProtKB).
GO:0034187;	Molecular function: apolipoprotein E binding (inferred from physical interaction from UniProtKB).
GO:0019899;	Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0008034;	Molecular function: lipoprotein binding (inferred from physical interaction from UniProtKB).
GO:0008017;	Molecular function: microtubule binding (inferred from direct assay from UniProtKB).
GO:0017124;	Molecular function: SH3 domain binding (inferred from physical interaction from UniProtKB).
GO:0005200;	Molecular function: structural constituent of cytoskeleton (traceable author statement from ProtInc).
GO:0000226;	Biological process: microtubule cytoskeleton organization (inferred from direct assay from UniProtKB).
GO:0007026;	Biological process: negative regulation of microtubule depolymerization (inferred from electronic annotation from InterPro).
GO:0045773;	Biological process: positive regulation of axon extension (inferred from direct assay from UniProtKB).
GO:0031116;	Biological process: positive regulation of microtubule polymerization (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR015562; Map_tau.
IPR002955; Tau_protein.
IPR001084; Tau_tubulin-bd.
Graphical view of domain structure.

PANTHER

PTHR11501:SF4; Map_tau; 1.

Pfam

PF00418; Tubulin-binding; 4.
Pfam graphical view of domain structure.

PRINTS

PR01261; TAUPROTEIN.

PROSITE

PS00229; TAU_MAP; 4.

Proteomic databases

PRIDE

P10636; -.

Genome annotation databases

Ensembl

ENSG00000186868; Homo sapiens. [Contig view]

GeneID

4137; -.

KEGG

hsa:4137; -.

Phylogenomic databases

HOVERGEN

P10636; -.

Other

16246; -.

P10636; -.

MAPT; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Alternative splicing; Alzheimer disease; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Disulfide bond; Glycation; Glycoprotein; Isopeptide bond; Membrane; Microtubule; Parkinsonism; Phosphoprotein; Polymorphism; Repeat; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 758`	`757`	`Microtubule-associated protein tau.`	`PRO_0000072739`
`REPEAT`	`561 591`	`31`	`Tau/MAP motif 1.`
`REPEAT`	`592 622`	`31`	`Tau/MAP motif 2.`
`REPEAT`	`623 653`	`31`	`Tau/MAP motif 3.`
`REPEAT`	`654 685`	`32`	`Tau/MAP motif 4.`
`SITE`	`24 24`	`1`	`Not glycated.`
`SITE`	`44 44`	`1`	`Not glycated.`
`SITE`	`67 67`	`1`	`Not glycated.`
`SITE`	`381 381`	`1`	`Not glycated.`
`SITE`	`391 391`	`1`	`Not glycated.`
`SITE`	`392 392`	`1`	`Not glycated.`
`SITE`	`394 394`	`1`	`Not glycated.`
`SITE`	`465 465`	`1`	`Not glycated.`
`SITE`	`497 497`	`1`	`Not glycated.`
`SITE`	`507 507`	`1`	`Not glycated.`
`SITE`	`541 541`	`1`	`Not glycated.`
`SITE`	`557 557`	`1`	`Not glycated.`
`SITE`	`571 571`	`1`	`Not glycated.`
`SITE`	`574 574`	`1`	`Not glycated.`
`SITE`	`584 584`	`1`	`Not glycated.`
`SITE`	`591 591`	`1`	`Not glycated.`
`SITE`	`607 607`	`1`	`Not glycated.`
`SITE`	`611 611`	`1`	`Not glycated.`
`SITE`	`615 615`	`1`	`Not glycated.`
`SITE`	`628 628`	`1`	`Not glycated.`
`SITE`	`634 634`	`1`	`Not glycated.`
`SITE`	`638 638`	`1`	`Not glycated.`
`SITE`	`648 648`	`1`	`Not glycated.`
`SITE`	`657 657`	`1`	`Not glycated.`
`SITE`	`660 660`	`1`	`Not glycated.`
`SITE`	`687 687`	`1`	`Not glycated.`
`SITE`	`692 692`	`1`	`Not glycated.`
`SITE`	`700 700`	`1`	`Not glycated.`
`SITE`	`702 702`	`1`	`Not glycated.`
`SITE`	`712 712`	`1`	`Not glycated.`
`SITE`	`755 755`	`1`	`Not glycated.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`46 46`		`Phosphoserine; by PDPK.`
`MOD_RES`	`50 50`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`111 111`		`Phosphothreonine (By similarity).`
`MOD_RES`	`470 470`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`484 484`		`Deamidated asparagine; in tau and PHF-tau; partial.`
`MOD_RES`	`492 492`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`498 498`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`514 514`		`Phosphotyrosine; by TTBK1.`
`MOD_RES`	`515 515`		`Phosphoserine; by PDPK and TTBK1.`
`MOD_RES`	`516 516`		`Phosphoserine; by PDPK and TTBK1.`
`MOD_RES`	`519 519`		`Phosphoserine; by PDPK and TTBK1.`
`MOD_RES`	`522 522`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`529 529`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`531 531`		`Phosphoserine; by PKA.`
`MOD_RES`	`534 534`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`548 548`		`Phosphothreonine; by PDPK.`
`MOD_RES`	`552 552`		`Phosphoserine; by PDPK.`
`MOD_RES`	`554 554`		`Phosphoserine; in PHF-tau.`
`MOD_RES`	`579 579`		`Phosphoserine; by MARK1.`
`MOD_RES`	`596 596`		`Deamidated asparagine; in tau and PHF-tau; partial.`
`MOD_RES`	`610 610`		`Phosphoserine; by MARK1; in PHF-tau.`
`MOD_RES`	`622 622`		`Phosphoserine; by MARK1; in PHF-tau.`
`MOD_RES`	`641 641`		`Phosphoserine; by MARK1; in PHF-tau.`
`MOD_RES`	`673 673`		`Phosphoserine; by MARK1; in PHF-tau.`
`MOD_RES`	`713 713`		`Phosphoserine; by PDPK.`
`MOD_RES`	`717 717`		`Phosphoserine (By similarity).`
`MOD_RES`	`720 720`		`Phosphothreonine.`
`MOD_RES`	`721 721`		`Phosphoserine; by PDPK.`
`MOD_RES`	`726 726`		`Phosphoserine (By similarity).`
`MOD_RES`	`729 729`		`Phosphoserine (By similarity).`
`MOD_RES`	`731 731`		`Phosphothreonine (By similarity).`
`MOD_RES`	`733 733`		`Phosphoserine; by CaMK2 and TTBK1.`
`MOD_RES`	`739 739`		`Phosphoserine; by PDPK and TTBK1.`
`MOD_RES`	`744 744`		`Phosphothreonine; by TTBK1.`
`CARBOHYD`	`87 87`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`383 383`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`467 467`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`480 480`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`491 491`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`542 542`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`551 551`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`576 576`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`597 597`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`598 598`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`664 664`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`670 670`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`CARBOHYD`	`686 686`		`N-linked (Glc) (glycation); in PHF-tau; in vitro.`
`DISULFID`	`608 639`		`By similarity.`
`CROSSLNK`	`571 571`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau.`
`CROSSLNK`	`628 628`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau.`
`CROSSLNK`	`670 670`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau.`
`VAR_SEQ`	`1 44`		`MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDT` `DAGLK -> MLRALQQRKR (in isoform Tau-A).`	`VSP_003175`
`VAR_SEQ`	`45 73`		`Missing (in isoform Tau-A, isoform Tau-D and isoform Fetal-tau).`	`VSP_003176`
`VAR_SEQ`	`74 102`		`Missing (in isoform Tau-A, isoform Tau-B, isoform Tau-D, isoform Tau-E and isoform Fetal-tau).`	`VSP_003177`
`VAR_SEQ`	`103 104`		`Missing (in isoform Tau-A).`	`VSP_003178`
`VAR_SEQ`	`125 375`		`Missing (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`
`VAR_SEQ`	`395 460`		`Missing (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`
`VAR_SEQ`	`502 502`		`S -> SATKQVQRRPPPAGPRSER (in isoform Tau-G).`	`VSP_026780`
`VAR_SEQ`	`592 622`		`Missing (in isoform Tau-A, isoform Tau-B, isoform Tau-C and isoform Fetal-tau).`	`VSP_003181`
`VARIANT`	`5 5`	`1`	`R -> H (in FTDP17; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro).`	`VAR_019660`
`VARIANT`	`5 5`	`1`	`R -> L (in PSP; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau).`	`VAR_019661`
`VARIANT`	`285 285`	`1`	`D -> N (risk factor for progressive supranuclear palsy).`	`VAR_010340`
`VARIANT`	`289 289`	`1`	`V -> A (risk factor for progressive supranuclear palsy).`	`VAR_010341`
`VARIANT`	`370 370`	`1`	`R -> W (in dbSNP:rs17651549 [NCBI]).`	`VAR_056121`
`VARIANT`	`441 441`	`1`	`H -> Y.`	`VAR_010342`
`VARIANT`	`447 447`	`1`	`S -> P.`	`VAR_010343`
`VARIANT`	`574 574`	`1`	`K -> T (in dementia; a dementia resembling Pick disease; reduces the ability to promote microtubule assembly by 70%).`	`VAR_010344`
`VARIANT`	`583 583`	`1`	`L -> V (in FTDP17; less able to promote microtubule assembly than wild-type tau).`	`VAR_019662`
`VARIANT`	`589 589`	`1`	`G -> V (in FTDP17).`	`VAR_010345`
`VARIANT`	`596 596`	`1`	`N -> K (in PPND).`	`VAR_010346`
`VARIANT`	`597 597`	`1`	`Missing (in FTDP17).`	`VAR_010347`
`VARIANT`	`613 613`	`1`	`N -> H (in FTDP17; 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).`	`VAR_019663`
`VARIANT`	`613 613`	`1`	`Missing (in PSP/atypical PSP; heterozygosity may be a risk factor for both a PSP-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).`	`VAR_019664`
`VARIANT`	`618 618`	`1`	`P -> L (in FTDP17; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments).`	`VAR_010348`
`VARIANT`	`618 618`	`1`	`P -> S (in FTDP17 and CBD; reduction in the ability to promote microtubule assembly).`	`VAR_010349`
`VARIANT`	`620 620`	`1`	`G -> V (in PSP).`	`VAR_037439`
`VARIANT`	`622 622`	`1`	`S -> N (in FTDP17; minimal parkinsonism; very early age of onset).`	`VAR_010350`
`VARIANT`	`634 634`	`1`	`K -> M (in FTDP17).`	`VAR_037440`
`VARIANT`	`637 637`	`1`	`S -> F (in Pick disease; markedly reduced ability of tau to promote microtubule assembly).`	`VAR_019665`
`VARIANT`	`654 654`	`1`	`V -> M (in FTDP17; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments).`	`VAR_010351`
`VARIANT`	`659 659`	`1`	`E -> V (in FTDP17).`	`VAR_019666`
`VARIANT`	`669 669`	`1`	`S -> L (in fatal respiratory hypoventilation; unusual apparent autosomal recessive inheritance; reduced binding to microtubules as well as increased fibrillization and aggregation).`	`VAR_019667`
`VARIANT`	`686 686`	`1`	`K -> I (in Pick disease; 90% reduction in the rate of microtubule assembly).`	`VAR_019668`
`VARIANT`	`706 706`	`1`	`G -> R (in dementia; a dementia resembling Pick disease; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%).`	`VAR_010352`
`VARIANT`	`723 723`	`1`	`R -> W (in FTDP17/Alzheimer disease; accelerates aggregation of tau into filaments; reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms).`	`VAR_010353`
`MUTAGEN`	`515 515`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`516 516`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`519 519`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`531 531`		`S->A: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein.`
`MUTAGEN`	`548 548`		`T->A: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein.`
`MUTAGEN`	`548 548`		`T->E: No association with plasma membrane.`
`MUTAGEN`	`552 552`		`S->A: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.`
`MUTAGEN`	`552 552`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`579 579`		`S->A: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.`
`MUTAGEN`	`713 713`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`721 721`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`726 726`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`730 730`		`S->E: No association with plasma membrane.`
`MUTAGEN`	`739 739`		`S->E: No association with plasma membrane.`
`CONFLICT`	`48 48`		`L -> P (in Ref. 6; AAU45390).`
`CONFLICT`	`557 557`		`K -> M (in Ref. 11; AAS17881).`
`CONFLICT`	`591 591`		`K -> S (in Ref. 11; AAS17881).`
`CONFLICT`	`617 617`		`V -> Q (in Ref. 15; AA sequence).`
`CONFLICT`	`622 622`		`S -> K (in Ref. 15; AA sequence).`

Sequence information

Length: 758 AA [This is the length of the unprocessed precursor]

Molecular weight: 78878 Da [This is the MW of the unprocessed precursor]

CRC64: ED2ADF89E1C4E445 [This is a checksum on the sequence]

        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 SPKLPTPGSS 

       430        440        450        460        470        480 
DPLIQPSSPA VCPEPPSSPK HVSSVTSRTG 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

P10636 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools