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Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)

 TAU_HUMAN               Reviewed;         758 AA.
P10636; P18518; Q14799; Q15549; Q15550; Q15551; Q1RMF6; Q53YB1;
Q5CZI7; Q5XWF0; Q6QT54; Q9UDJ3; Q9UMH0; Q9UQ96;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 5.
30-AUG-2017, entry version 239.
RecName: Full=Microtubule-associated protein tau;
AltName: Full=Neurofibrillary tangle protein;
AltName: Full=Paired helical filament-tau;
Short=PHF-tau;
Name=MAPT; Synonyms=MAPTL, MTBT1, TAU;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FETAL-TAU).
TISSUE=Brain;
PubMed=3131773; DOI=10.1073/pnas.85.11.4051;
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;
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;
PubMed=2516729; DOI=10.1016/0896-6273(89)90050-0;
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),
AND ASSOCIATION WITH ALZHEIMER DISEASE.
TISSUE=Brain;
PubMed=2484340; DOI=10.1016/0896-6273(89)90210-9;
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), ALTERNATIVE SPLICING, AND VARIANT HIS-441.
PubMed=1420178; DOI=10.1021/bi00158a027;
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 GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FETAL-TAU AND TAU-D).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[10]
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, AND DEAMIDATION AT ASN-484 AND
ASN-596.
TISSUE=Brain;
PubMed=1512244;
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).
[11]
PROTEIN SEQUENCE OF 25-44; 529-538; 560-571 AND 671-686, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
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.
[13]
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 IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16443603; DOI=10.1074/jbc.M512786200;
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).
[14]
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, AND
MUTAGENESIS.
PubMed=7706316; DOI=10.1074/jbc.270.13.7679;
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).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 592-622 (ISOFORMS
PNS-TAU/TAU-D/TAU-E/TAU-F).
TISSUE=Brain;
PubMed=2495000; DOI=10.1016/0006-291X(89)92240-7;
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).
[16]
PROTEIN SEQUENCE OF 251-264 AND 379-392, AND PHOSPHORYLATION AT
SER-396.
PubMed=1899488; DOI=10.1126/science.1899488;
Lee V.M., Balin B.J., Otvos L. Jr., Trojanowski J.Q.;
"A68: a major subunit of paired helical filaments and derivatized
forms of normal Tau.";
Science 251:675-678(1991).
[17]
PROTEIN SEQUENCE OF 616-712.
PubMed=1915258;
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).
[18]
IDENTIFICATION (ISOFORM TAU-G), AND VARIANT HIS-441.
PubMed=15365985; DOI=10.1002/humu.20086;
Rademakers R., Cruts M., van Broeckhoven C.;
"The role of tau (MAPT) in frontotemporal dementia and related
tauopathies.";
Hum. Mutat. 24:277-295(2004).
[19]
REVIEW.
PubMed=1713721; DOI=10.1016/0166-2236(91)90105-4;
Goedert M., Crowther R.A., Garner C.C.;
"Molecular characterization of microtubule-associated proteins tau and
MAP2.";
Trends Neurosci. 14:193-199(1991).
[20]
PHOSPHORYLATION AT SER-554; SER-579; SER-602; SER-606 AND SER-669.
PubMed=8999860;
Paudel H.K.;
"The regulatory Ser262 of microtubule-associated protein tau is
phosphorylated by phosphorylase kinase.";
J. Biol. Chem. 272:1777-1785(1997).
[21]
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
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.
PubMed=9326300;
Nacharaju P., Ko L., Yen S.H.;
"Characterization of in vitro glycation sites of tau.";
J. Neurochem. 69:1709-1719(1997).
[22]
PHOSPHORYLATION, AND MUTAGENESIS.
PubMed=9735171; DOI=10.1006/abbi.1998.0813;
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).
[23]
PHOSPHORYLATION AT THR-470; SER-516; SER-519; THR-529; SER-531;
SER-552; SER-579; SER-713; SER-721 AND SER-739, AND MUTAGENESIS.
PubMed=9614189; DOI=10.1091/mbc.9.6.1495;
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).
[24]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=10747907; DOI=10.1074/jbc.M000389200;
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).
[25]
PHOSPHORYLATION AT SER-519; THR-522; SER-713 AND SER-721 BY
CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
PubMed=14761950; DOI=10.1074/jbc.M314116200;
Li G., Yin H., Kuret J.;
"Casein kinase 1 delta phosphorylates tau and disrupts its binding to
microtubules.";
J. Biol. Chem. 279:15938-15945(2004).
[26]
PHOSPHORYLATION AT THR-548 BY GSK3B.
PubMed=14690523;
Cho J.H., Johnson G.V.;
"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.";
J. Neurochem. 88:349-358(2004).
[27]
PHOSPHORYLATION AT TYR-18 BY FYN.
PubMed=14999081; DOI=10.1523/JNEUROSCI.4162-03.2004;
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.;
"Phosphorylation of tau by fyn: implications for Alzheimer's
disease.";
J. Neurosci. 24:2304-2312(2004).
[28]
INTERACTION WITH SQSTM1, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
PubMed=15953362; DOI=10.1111/j.1471-4159.2005.03181.x;
Babu J.R., Geetha T., Wooten M.W.;
"Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal
degradation.";
J. Neurochem. 94:192-203(2005).
[29]
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, AND
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.
PubMed=15546861; DOI=10.1074/jbc.M410775200;
Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.;
"Dephosphorylation of tau by protein phosphatase 5: impairment in
Alzheimer's disease.";
J. Biol. Chem. 280:1790-1796(2005).
[30]
PHOSPHORYLATION AT TYR-514; SER-515; SER-516; SER-519; SER-733;
SER-739 AND THR-744.
PubMed=16923168; DOI=10.1111/j.1471-4159.2006.04059.x;
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).
[31]
PHOSPHORYLATION AT SER-214 BY SGK1, AND INTERACTION WITH SGK1.
PubMed=16982696; DOI=10.1128/MCB.01017-06;
Yang Y.C., Lin C.H., Lee E.H.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite
formation through microtubule depolymerization by SGK1 and by SGK1
phosphorylation of tau.";
Mol. Cell. Biol. 26:8357-8370(2006).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[33]
PHOSPHORYLATION BY CSNK1D/CK1.
PubMed=17562708; DOI=10.1074/jbc.M703269200;
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.;
"Novel phosphorylation sites in tau from Alzheimer brain support a
role for casein kinase 1 in disease pathogenesis.";
J. Biol. Chem. 282:23645-23654(2007).
[34]
PHOSPHORYLATION AT THR-529 BY DYRK2.
PubMed=18599021; DOI=10.1016/j.bcp.2008.05.021;
Yoshida K.;
"Role for DYRK family kinases on regulation of apoptosis.";
Biochem. Pharmacol. 76:1389-1394(2008).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
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).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[37]
GLYCOSYLATION, PHOSPHORYLATION AT SER-516; SER-519; THR-522; THR-529;
SER-531; THR-534; SER-579; SER-713; SER-721 AND SER-739, AND
ASSOCIATION WITH ALZHEIMER DISEASE.
PubMed=19451179; DOI=10.1093/brain/awp099;
Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I.,
Iqbal K., Gong C.X.;
"Reduced O-GlcNAcylation links lower brain glucose metabolism and tau
pathology in Alzheimer's disease.";
Brain 132:1820-1832(2009).
[38]
INTERACTION WITH EPM2A.
PubMed=19542233; DOI=10.1074/jbc.M109.009688;
Puri R., Suzuki T., Yamakawa K., Ganesh S.;
"Hyperphosphorylation and aggregation of Tau in laforin-deficient
mice, an animal model for Lafora disease.";
J. Biol. Chem. 284:22657-22663(2009).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-717; SER-721
AND SER-726, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[41]
GLYCOSYLATION AT SER-525; SER-555 AND SER-717, PHOSPHORYLATION AT
SER-519; SER-713 SER-717 AND SER-721, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=21327254; DOI=10.1039/c0mb00337a;
Smet-Nocca C., Broncel M., Wieruszeski J.M., Tokarski C., Hanoulle X.,
Leroy A., Landrieu I., Rolando C., Lippens G., Hackenberger C.P.;
"Identification of O-GlcNAc sites within peptides of the Tau protein
and their impact on phosphorylation.";
Mol. Biosyst. 7:1420-1429(2011).
[42]
FUNCTION, AND PHOSPHORYLATION AT THR-529 AND SER-579.
PubMed=21985311; DOI=10.1111/j.1471-4159.2011.07523.x;
Yoshida H., Goedert M.;
"Phosphorylation of microtubule-associated protein tau by AMPK-related
kinases.";
J. Neurochem. 120:165-176(2012).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-548; SER-552;
SER-713 AND SER-721, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[44]
PHOSPHORYLATION AT SER-579.
PubMed=23666762; DOI=10.1007/s12017-013-8232-3;
Gu G.J., Lund H., Wu D., Blokzijl A., Classon C., von Euler G.,
Landegren U., Sunnemark D., Kamali-Moghaddam M.;
"Role of individual MARK isoforms in phosphorylation of tau at Ser262
in Alzheimer's disease.";
NeuroMolecular Med. 15:458-469(2013).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[46]
STRUCTURE BY NMR OF 542-554 IN COMPLEX WITH PIN1.
PubMed=11313338; DOI=10.1074/jbc.M010327200;
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).
[47]
REVIEW ON VARIANTS.
PubMed=10899436; DOI=10.1016/S0925-4439(00)00037-5;
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).
[48]
VARIANT FTD MET-654, VARIANTS ASN-285; ALA-289; HIS-441 AND PRO-447,
AND INVOLVEMENT IN FTD.
PubMed=9629852; DOI=10.1002/ana.410430617;
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).
[49]
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).
[50]
VARIANT FTD LEU-618.
PubMed=9736786; DOI=10.1093/hmg/7.11.1825;
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).
[51]
VARIANTS FTD VAL-589; LEU-618 AND TRP-723.
PubMed=9641683; DOI=10.1038/31508;
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).
[52]
VARIANTS FTD LYS-596 AND LEU-618.
PubMed=9789048; DOI=10.1073/pnas.95.22.13103;
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).
[53]
VARIANT PPND LYS-596.
PubMed=10412802; DOI=10.1007/s004010051052;
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).
[54]
VARIANTS FTD VAL-589; LYS-597 DEL; LEU-618 AND TRP-723.
PubMed=9973279; DOI=10.1086/302256;
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).
[55]
VARIANT FTD SER-618.
PubMed=10553987;
DOI=10.1002/1531-8249(199911)46:5<708::AID-ANA5>3.0.CO;2-K;
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).
[56]
VARIANTS FTD LEU-618; MET-654 AND TRP-723.
PubMed=10214944; DOI=10.1016/S0014-5793(99)00294-X;
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).
[57]
VARIANT FTD/CBD SER-618.
PubMed=10374757; DOI=10.1097/00005072-199906000-00011;
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).
[58]
VARIANT PIDB ARG-706.
PubMed=10604746; DOI=10.1097/00005072-199912000-00002;
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).
[59]
VARIANT FTD LYS-596.
PubMed=10489057; DOI=10.1212/WNL.53.4.864;
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).
[60]
VARIANTS PSNP1 ASN-285 AND ALA-289.
PubMed=10534245; DOI=10.1212/WNL.53.7.1421;
Higgins J.J., Adler R.L., Loveless J.M.;
"Mutational analysis of the tau gene in progressive supranuclear
palsy.";
Neurology 53:1421-1424(1999).
[61]
VARIANT FTD ASN-622.
PubMed=10208578; DOI=10.1097/00001756-199902250-00010;
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).
[62]
VARIANT FTD VAL-659.
PubMed=11117541;
DOI=10.1002/1531-8249(200012)48:6<850::AID-ANA5>3.0.CO;2-V;
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).
[63]
VARIANTS PIDB THR-574 AND ARG-706, AND CHARACTERIZATION OF VARIANTS
PIDB THR-574 AND ARG-706.
PubMed=11117542;
DOI=10.1002/1531-8249(200012)48:6<859::AID-ANA6>3.3.CO;2-T;
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).
[64]
VARIANT PIDB THR-574.
PubMed=11089577; DOI=10.1093/jnen/59.11.990;
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).
[65]
VARIANT FTD LYS-596.
PubMed=10802785; DOI=10.1212/WNL.54.9.1787;
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).
[66]
VARIANT FTD SER-618.
PubMed=11071507; DOI=10.1212/WNL.55.8.1224;
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).
[67]
VARIANT FTD HIS-613.
PubMed=11585254;
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).
[68]
VARIANT PSNP1 ASN-613 DEL.
PubMed=11220749;
DOI=10.1002/1531-8249(20010201)49:2<263::AID-ANA50>3.0.CO;2-K;
Pastor P., Pastor E., Carnero C., Vela R., Garcia T., Amer G.,
Tolosa E., Oliva R.;
"Familial atypical progressive supranuclear palsy associated with
homozygosity for the delN296 mutation in the tau gene.";
Ann. Neurol. 49:263-267(2001).
[69]
VARIANT PIDB ILE-686, AND CHARACTERIZATION OF VARIANT PIDB ILE-686.
PubMed=11601501; DOI=10.1002/ana.1223;
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).
[70]
CHARACTERIZATION OF VARIANT FTD TRP-723.
PubMed=11278002; DOI=10.1016/S0014-5793(01)02267-0;
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).
[71]
VARIANT FTD LYS-596.
PubMed=12473774; DOI=10.1212/01.WNL.0000038909.49164.4B;
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).
[72]
VARIANT PIDB PHE-637, AND CHARACTERIZATION OF VARIANT PIDB PHE-637.
PubMed=11891833; DOI=10.1002/ana.10140;
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).
[73]
VARIANT FTD HIS-5, AND CHARACTERIZATION OF VARIANT FTD HIS-5.
PubMed=11921059; DOI=10.1002/ana.10163;
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).
[74]
VARIANT PSNP1 LEU-5, AND CHARACTERIZATION OF VARIANT PSNP1 LEU-5.
PubMed=12325083; DOI=10.1002/ana.10340;
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).
[75]
CHARACTERIZATION OF VARIANTS FTD ASN-613 DEL AND HIS-613.
PubMed=11906000; DOI=10.1046/j.0022-3042.2001.00729.x;
Yoshida H., Crowther R.A., Goedert M.;
"Functional effects of tau gene mutations deltaN296 and N296H.";
J. Neurochem. 80:548-551(2002).
[76]
VARIANT FTD TRP-723.
PubMed=11889249; DOI=10.1212/WNL.58.5.811;
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).
[77]
VARIANT FTD VAL-583, AND CHARACTERIZATION OF VARIANT FTD VAL-583.
PubMed=12509859; DOI=10.1002/ana.10447;
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).
[78]
VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669, AND
CHARACTERIZATION OF VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669.
PubMed=14595660; DOI=10.1002/ana.10747;
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).
[79]
VARIANT FTD/ALZHEIMER DISEASE TRP-723, AND INVOLVEMENT IN ALZHEIMER
DISEASE.
PubMed=14517953; DOI=10.1002/humu.10269;
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).
[80]
VARIANT ATYPICAL PSNP1 ASN-613 DEL.
PubMed=14991829; DOI=10.1002/ana.20006;
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).
[81]
VARIANT PSNP1/ATYPICAL PSNP1 ASN-613 DEL.
PubMed=14991828; DOI=10.1002/ana.20025;
Oliva R., Pastor P.;
"Tau gene delN296 mutation, Parkinson's disease, and atypical
supranuclear palsy.";
Ann. Neurol. 55:448-449(2004).
[82]
VARIANT FTD SER-618.
PubMed=16240366; DOI=10.1002/ana.20668;
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).
[83]
VARIANT PSNP1 VAL-620.
PubMed=16157753; DOI=10.1001/archneur.62.9.1444;
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).
[84]
VARIANT FTD MET-634.
PubMed=15883319; DOI=10.1212/01.WNL.0000160116.65034.12;
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).
[85]
VARIANTS MET-17; ALA-30 AND ILE-617.
PubMed=20020531; DOI=10.1002/humu.21152;
Guerreiro R.J., Washecka N., Hardy J., Singleton A.;
"A thorough assessment of benign genetic variability in GRN and
MAPT.";
Hum. Mutat. 31:E1126-E1140(2010).
[86]
VARIANT FTD/ALZHEIMER DISEASE TRP-723.
PubMed=26086902; DOI=10.1016/j.gene.2015.06.033;
Behnam M., Ghorbani F., Shin J.H., Kim D.S., Jang H., Nouri N.,
Sedghi M., Salehi M., Ansari B., Basiri K.;
"Homozygous MAPT R406W mutation causing FTDP phenotype: A unique
instance of a unique mutation.";
Gene 570:150-152(2015).
-!- 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.
{ECO:0000269|PubMed:21985311}.
-!- SUBUNIT: 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). {ECO:0000250,
ECO:0000269|PubMed:11313338, ECO:0000269|PubMed:14761950,
ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16982696,
ECO:0000269|PubMed:19542233}.
-!- INTERACTION:
P02649:APOE; NbExp=3; IntAct=EBI-366182, EBI-9209835;
P05067:APP; NbExp=9; IntAct=EBI-366182, EBI-77613;
O00499-1:BIN1; NbExp=5; IntAct=EBI-6926270, EBI-6926280;
Q14203:DCTN1; NbExp=8; IntAct=EBI-366233, EBI-724352;
P49841:GSK3B; NbExp=9; IntAct=EBI-366233, EBI-373586;
P08238:HSP90AB1; NbExp=4; IntAct=EBI-366233, EBI-352572;
Q5S007:LRRK2; NbExp=9; IntAct=EBI-366233, EBI-5323863;
Q7KZI7:MARK2; NbExp=2; IntAct=EBI-366233, EBI-516560;
P04156:PRNP; NbExp=2; IntAct=EBI-366182, EBI-977302;
P43004:SLC1A2; NbExp=4; IntAct=EBI-366182, EBI-3440986;
P37840:SNCA; NbExp=3; IntAct=EBI-366233, EBI-985879;
Q9UNE7:STUB1; NbExp=2; IntAct=EBI-366182, EBI-357085;
P63104:YWHAZ; NbExp=9; IntAct=EBI-7145070, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:10747907}. Cell membrane
{ECO:0000269|PubMed:10747907}; Peripheral membrane protein
{ECO:0000269|PubMed:10747907}; Cytoplasmic side
{ECO:0000269|PubMed:10747907}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10747907}. Cell projection, axon
{ECO:0000269|PubMed:10747907}. Note=Mostly found in the axons of
neurons, in the cytosol and in association with plasma membrane
components.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=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;
IsoId=P10636-1; Sequence=Displayed;
Name=Fetal-tau;
IsoId=P10636-2; Sequence=VSP_003176, VSP_003177, VSP_003179,
VSP_003180, VSP_003181;
Name=Tau-A;
IsoId=P10636-3; Sequence=VSP_003175, VSP_003176, VSP_003177,
VSP_003178, VSP_003179, VSP_003180,
VSP_003181;
Name=Tau-B;
IsoId=P10636-4; Sequence=VSP_003177, VSP_003179, VSP_003180,
VSP_003181;
Name=Tau-C; Synonyms=Tau-3;
IsoId=P10636-5; Sequence=VSP_003179, VSP_003180, VSP_003181;
Name=Tau-D;
IsoId=P10636-6; Sequence=VSP_003176, VSP_003177, VSP_003179,
VSP_003180;
Name=Tau-E;
IsoId=P10636-7; Sequence=VSP_003177, VSP_003179, VSP_003180;
Name=Tau-F; Synonyms=Tau-4;
IsoId=P10636-8; Sequence=VSP_003179, VSP_003180;
Name=Tau-G;
IsoId=P10636-9; Sequence=VSP_026780;
Note=No experimental confirmation available.;
-!- 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.
-!- PTM: 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. {ECO:0000269|PubMed:14690523,
ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16982696,
ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254,
ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:7706316,
ECO:0000269|PubMed:8999860, ECO:0000269|PubMed:9614189}.
-!- 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. {ECO:0000250, ECO:0000269|PubMed:15953362,
ECO:0000269|PubMed:16443603}.
-!- PTM: 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%.
{ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189}.
-!- PTM: 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.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:14517953,
ECO:0000269|PubMed:26086902}.
-!- DISEASE: 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. {ECO:0000269|PubMed:10208578,
ECO:0000269|PubMed:10214944, ECO:0000269|PubMed:10374757,
ECO:0000269|PubMed:10489057, ECO:0000269|PubMed:10553987,
ECO:0000269|PubMed:10802785, ECO:0000269|PubMed:11071507,
ECO:0000269|PubMed:11117541, ECO:0000269|PubMed:11278002,
ECO:0000269|PubMed:11585254, ECO:0000269|PubMed:11889249,
ECO:0000269|PubMed:11906000, ECO:0000269|PubMed:11921059,
ECO:0000269|PubMed:12473774, ECO:0000269|PubMed:12509859,
ECO:0000269|PubMed:14517953, ECO:0000269|PubMed:15883319,
ECO:0000269|PubMed:16240366, ECO:0000269|PubMed:26086902,
ECO:0000269|PubMed:9629852, ECO:0000269|PubMed:9641683,
ECO:0000269|PubMed:9736786, ECO:0000269|PubMed:9789048,
ECO:0000269|PubMed:9973279}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:10604746, ECO:0000269|PubMed:11089577,
ECO:0000269|PubMed:11117542, ECO:0000269|PubMed:11601501,
ECO:0000269|PubMed:11891833}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=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: 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.
{ECO:0000269|PubMed:10534245, ECO:0000269|PubMed:11220749,
ECO:0000269|PubMed:12325083, ECO:0000269|PubMed:14991828,
ECO:0000269|PubMed:14991829, ECO:0000269|PubMed:16157753}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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.
-!- WEB RESOURCE: Name=Alzforum; Note=MAPT mutations;
URL="http://www.alzforum.org/mutations/search?genes%255B%255D=348";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Vita minima - Issue 68
of March 2006;
URL="http://web.expasy.org/spotlight/back_issues/068";
-!- WEB RESOURCE: Name=Wikipedia; Note=Tau protein entry;
URL="https://en.wikipedia.org/wiki/Tau_protein";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J03778; AAA60615.1; -; mRNA.
EMBL; X14474; CAA32636.1; -; mRNA.
EMBL; AF047863; AAC04277.1; -; Genomic_DNA.
EMBL; AF027491; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF047856; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF047857; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF027492; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF047858; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF027493; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF047859; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF047860; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF047862; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF027494; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF027495; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF027496; AAC04277.1; JOINED; Genomic_DNA.
EMBL; AF027491; AAC04278.1; -; Genomic_DNA.
EMBL; AF027492; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF027493; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF047860; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF047862; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF027495; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF027496; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF047863; AAC04278.1; JOINED; Genomic_DNA.
EMBL; AF027491; AAC04279.1; -; Genomic_DNA.
EMBL; AF047856; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF047857; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF027492; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF027493; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF047860; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF047862; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF027494; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF027495; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF027496; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF047863; AAC04279.1; JOINED; Genomic_DNA.
EMBL; AF047861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY730549; AAU45390.1; -; mRNA.
EMBL; BT006772; AAP35418.1; -; mRNA.
EMBL; AC004139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000558; AAH00558.1; -; mRNA.
EMBL; BC098281; AAH98281.1; -; mRNA.
EMBL; BC099721; AAH99721.1; -; mRNA.
EMBL; BC101936; AAI01937.1; -; mRNA.
EMBL; BC114504; AAI14505.1; -; mRNA.
EMBL; BC114948; AAI14949.1; -; mRNA.
EMBL; AY526356; AAS17881.1; -; mRNA.
EMBL; M25298; AAA57264.1; -; mRNA.
EMBL; BN000503; CAG26750.1; -; mRNA.
CCDS; CCDS11499.1; -. [P10636-8]
CCDS; CCDS11500.1; -. [P10636-6]
CCDS; CCDS11501.1; -. [P10636-1]
CCDS; CCDS11502.1; -. [P10636-2]
CCDS; CCDS45715.1; -. [P10636-9]
CCDS; CCDS45716.1; -. [P10636-7]
CCDS; CCDS56033.1; -. [P10636-5]
PIR; I52232; I52232.
PIR; JS0370; QRHUT1.
PIR; PN0001; QRHUT2.
PIR; S26663; S26663.
RefSeq; NP_001116538.2; NM_001123066.3. [P10636-9]
RefSeq; NP_001116539.1; NM_001123067.3. [P10636-7]
RefSeq; NP_001190181.1; NM_001203252.1. [P10636-5]
RefSeq; NP_005901.2; NM_005910.5. [P10636-8]
RefSeq; NP_058518.1; NM_016834.4. [P10636-6]
RefSeq; NP_058519.3; NM_016835.4. [P10636-1]
RefSeq; NP_058525.1; NM_016841.4. [P10636-2]
UniGene; Hs.101174; -.
PDB; 1I8H; NMR; -; A=542-554.
PDB; 2MZ7; NMR; -; A=584-629.
PDB; 2ON9; X-ray; 1.51 A; A/B=623-628.
PDB; 3OVL; X-ray; 1.81 A; A=623-628.
PDB; 4E0M; X-ray; 1.75 A; A/B/C/D=622-634.
PDB; 4E0N; X-ray; 1.65 A; A/B/C/D=622-634.
PDB; 4E0O; X-ray; 1.82 A; A/B/C/D=622-634.
PDB; 4FL5; X-ray; 1.90 A; P/Q=527-536.
PDB; 4GLR; X-ray; 1.90 A; A/B=541-557.
PDB; 4NP8; X-ray; 1.51 A; A=623-628.
PDB; 4TQE; X-ray; 1.60 A; A=532-547.
PDB; 4Y32; X-ray; 1.70 A; C/D=528-534.
PDB; 4Y3B; X-ray; 1.80 A; C/D=528-534.
PDB; 4Y5I; X-ray; 1.40 A; F/G=528-534.
PDB; 5DMG; X-ray; 2.50 A; P/X/Z=733-747.
PDB; 5E2V; X-ray; 1.64 A; P=511-528.
PDB; 5E2W; X-ray; 1.50 A; P=511-528.
PDB; 5HF3; X-ray; 1.80 A; B=528-534.
PDB; 5K7N; EM; 1.10 A; Z=623-628.
PDBsum; 1I8H; -.
PDBsum; 2MZ7; -.
PDBsum; 2ON9; -.
PDBsum; 3OVL; -.
PDBsum; 4E0M; -.
PDBsum; 4E0N; -.
PDBsum; 4E0O; -.
PDBsum; 4FL5; -.
PDBsum; 4GLR; -.
PDBsum; 4NP8; -.
PDBsum; 4TQE; -.
PDBsum; 4Y32; -.
PDBsum; 4Y3B; -.
PDBsum; 4Y5I; -.
PDBsum; 5DMG; -.
PDBsum; 5E2V; -.
PDBsum; 5E2W; -.
PDBsum; 5HF3; -.
PDBsum; 5K7N; -.
DisProt; DP01100; -.
ProteinModelPortal; P10636; -.
SMR; P10636; -.
BioGrid; 110308; 114.
DIP; DIP-29753N; -.
ELM; P10636; -.
IntAct; P10636; 52.
MINT; MINT-134394; -.
STRING; 9606.ENSP00000340820; -.
BindingDB; P10636; -.
ChEMBL; CHEMBL1293224; -.
DrugBank; DB01248; Docetaxel.
DrugBank; DB01229; Paclitaxel.
iPTMnet; P10636; -.
PhosphoSitePlus; P10636; -.
BioMuta; MAPT; -.
DMDM; 334302961; -.
MaxQB; P10636; -.
PaxDb; P10636; -.
PeptideAtlas; P10636; -.
PRIDE; P10636; -.
TopDownProteomics; P10636-3; -. [P10636-3]
DNASU; 4137; -.
Ensembl; ENST00000262410; ENSP00000262410; ENSG00000186868. [P10636-1]
Ensembl; ENST00000334239; ENSP00000334886; ENSG00000186868. [P10636-2]
Ensembl; ENST00000340799; ENSP00000340438; ENSG00000186868. [P10636-7]
Ensembl; ENST00000344290; ENSP00000340820; ENSG00000186868. [P10636-9]
Ensembl; ENST00000351559; ENSP00000303214; ENSG00000186868. [P10636-8]
Ensembl; ENST00000415613; ENSP00000410838; ENSG00000186868. [P10636-9]
Ensembl; ENST00000420682; ENSP00000413056; ENSG00000186868. [P10636-7]
Ensembl; ENST00000431008; ENSP00000389250; ENSG00000186868. [P10636-5]
Ensembl; ENST00000446361; ENSP00000408975; ENSG00000186868. [P10636-6]
Ensembl; ENST00000535772; ENSP00000443028; ENSG00000186868. [P10636-5]
Ensembl; ENST00000571987; ENSP00000458742; ENSG00000186868. [P10636-1]
Ensembl; ENST00000574436; ENSP00000460965; ENSG00000186868. [P10636-8]
Ensembl; ENST00000612872; ENSP00000478602; ENSG00000277956. [P10636-7]
Ensembl; ENST00000613360; ENSP00000483784; ENSG00000276155. [P10636-7]
Ensembl; ENST00000620070; ENSP00000484491; ENSG00000277956. [P10636-8]
Ensembl; ENST00000620818; ENSP00000484321; ENSG00000277956. [P10636-5]
Ensembl; ENST00000620981; ENSP00000481769; ENSG00000276155. [P10636-5]
Ensembl; ENST00000621329; ENSP00000477703; ENSG00000276155. [P10636-8]
Ensembl; ENST00000622106; ENSP00000482244; ENSG00000277956. [P10636-6]
Ensembl; ENST00000622728; ENSP00000479142; ENSG00000276155. [P10636-6]
Ensembl; ENST00000626571; ENSP00000486039; ENSG00000276155. [P10636-6]
Ensembl; ENST00000628393; ENSP00000487570; ENSG00000276155. [P10636-2]
Ensembl; ENST00000631447; ENSP00000488373; ENSG00000277956. [P10636-5]
Ensembl; ENST00000632500; ENSP00000487837; ENSG00000277956. [P10636-7]
Ensembl; ENST00000633047; ENSP00000488245; ENSG00000277956. [P10636-2]
Ensembl; ENST00000634049; ENSP00000487819; ENSG00000277956. [P10636-8]
GeneID; 4137; -.
KEGG; hsa:4137; -.
UCSC; uc002ijr.5; human. [P10636-1]
CTD; 4137; -.
DisGeNET; 4137; -.
GeneCards; MAPT; -.
GeneReviews; MAPT; -.
HGNC; HGNC:6893; MAPT.
HPA; CAB000151; -.
HPA; HPA048895; -.
HPA; HPA069524; -.
HPA; HPA069570; -.
MalaCards; MAPT; -.
MIM; 157140; gene+phenotype.
MIM; 172700; phenotype.
MIM; 260540; phenotype.
MIM; 600274; phenotype.
MIM; 601104; phenotype.
neXtProt; NX_P10636; -.
OpenTargets; ENSG00000186868; -.
Orphanet; 275864; Behavioral variant of frontotemporal dementia.
Orphanet; 240071; Classical progressive supranuclear palsy.
Orphanet; 100070; Progressive non-fluent aphasia.
Orphanet; 240103; Progressive supranuclear palsy - corticobasal syndrome.
Orphanet; 240085; Progressive supranuclear palsy - parkinsonism.
Orphanet; 240112; Progressive supranuclear palsy - progressive non fluent aphasia.
Orphanet; 240094; Progressive supranuclear palsy - pure akinesia with gait freezing.
Orphanet; 100069; Semantic dementia.
PharmGKB; PA238; -.
eggNOG; KOG2418; Eukaryota.
eggNOG; ENOG4111J07; LUCA.
GeneTree; ENSGT00530000063491; -.
HOVERGEN; HBG000991; -.
InParanoid; P10636; -.
KO; K04380; -.
OMA; PPEFTFH; -.
OrthoDB; EOG091G0AHK; -.
TreeFam; TF316358; -.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
SABIO-RK; P10636; -.
SIGNOR; P10636; -.
ChiTaRS; MAPT; human.
EvolutionaryTrace; P10636; -.
GeneWiki; Tau_protein; -.
GenomeRNAi; 4137; -.
PMAP-CutDB; P10636; -.
PRO; PR:P10636; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000186868; -.
ExpressionAtlas; P10636; baseline and differential.
Genevisible; P10636; HS.
GO; GO:0030673; C:axolemma; IDA:CAFA.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; NAS:ParkinsonsUK-UCL.
GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:CAFA.
GO; GO:0097418; C:neurofibrillary tangle; IDA:CAFA.
GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0036477; C:somatodendritic compartment; IMP:ParkinsonsUK-UCL.
GO; GO:0045298; C:tubulin complex; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; TAS:ParkinsonsUK-UCL.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; ISS:ParkinsonsUK-UCL.
GO; GO:0034452; F:dynactin binding; TAS:ParkinsonsUK-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0071813; F:lipoprotein particle binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0099609; F:microtubule lateral binding; IMP:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0051721; F:protein phosphatase 2A binding; TAS:ParkinsonsUK-UCL.
GO; GO:0048018; F:receptor agonist activity; IDA:ParkinsonsUK-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:ParkinsonsUK-UCL.
GO; GO:1990000; P:amyloid fibril formation; IMP:CAFA.
GO; GO:0048143; P:astrocyte activation; TAS:ParkinsonsUK-UCL.
GO; GO:0098930; P:axonal transport; TAS:ParkinsonsUK-UCL.
GO; GO:0019896; P:axonal transport of mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:0034605; P:cellular response to heat; TAS:ParkinsonsUK-UCL.
GO; GO:0031122; P:cytoplasmic microtubule organization; TAS:ParkinsonsUK-UCL.
GO; GO:0048699; P:generation of neurons; NAS:UniProtKB.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:ParkinsonsUK-UCL.
GO; GO:0007613; P:memory; IMP:ParkinsonsUK-UCL.
GO; GO:0001774; P:microglial cell activation; TAS:ParkinsonsUK-UCL.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0033673; P:negative regulation of kinase activity; IMP:ParkinsonsUK-UCL.
GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL.
GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
GO; GO:1902988; P:neurofibrillary tangle assembly; NAS:ParkinsonsUK-UCL.
GO; GO:0031175; P:neuron projection development; TAS:ParkinsonsUK-UCL.
GO; GO:0072386; P:plus-end-directed organelle transport along microtubule; TAS:ParkinsonsUK-UCL.
GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
GO; GO:1903829; P:positive regulation of cellular protein localization; IMP:CAFA.
GO; GO:1905689; P:positive regulation of diacylglycerol kinase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IMP:ParkinsonsUK-UCL.
GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:ParkinsonsUK-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:ParkinsonsUK-UCL.
GO; GO:0051259; P:protein oligomerization; TAS:ParkinsonsUK-UCL.
GO; GO:0010506; P:regulation of autophagy; IGI:MGI.
GO; GO:0050848; P:regulation of calcium-mediated signaling; IDA:ParkinsonsUK-UCL.
GO; GO:1900034; P:regulation of cellular response to heat; IMP:ParkinsonsUK-UCL.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:CAFA.
GO; GO:0031113; P:regulation of microtubule polymerization; NAS:UniProtKB.
GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:CAFA.
GO; GO:0090140; P:regulation of mitochondrial fission; IC:ParkinsonsUK-UCL.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:ParkinsonsUK-UCL.
GO; GO:0097435; P:supramolecular fiber organization; IMP:CAFA.
GO; GO:0050808; P:synapse organization; IMP:ParkinsonsUK-UCL.
InterPro; IPR001084; MAP_tubulin-bd_rpt.
InterPro; IPR002955; Tau.
Pfam; PF00418; Tubulin-binding; 4.
PRINTS; PR01261; TAUPROTEIN.
PROSITE; PS00229; TAU_MAP_1; 4.
PROSITE; PS51491; TAU_MAP_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Alzheimer disease;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycation; Glycoprotein; Isopeptide bond; Membrane;
Methylation; Microtubule; Neurodegeneration; Parkinsonism;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1512244}.
CHAIN 2 758 Microtubule-associated protein tau.
/FTId=PRO_0000072739.
REPEAT 561 591 Tau/MAP 1.
REPEAT 592 622 Tau/MAP 2.
REPEAT 623 653 Tau/MAP 3.
REPEAT 654 685 Tau/MAP 4.
SITE 24 24 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 44 44 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 67 67 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 381 381 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 391 391 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 392 392 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 394 394 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 465 465 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 497 497 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 507 507 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 541 541 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 557 557 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 571 571 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 574 574 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 584 584 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 591 591 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 607 607 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 611 611 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 615 615 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 628 628 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 634 634 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 638 638 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 648 648 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 657 657 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 660 660 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 687 687 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 692 692 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 700 700 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 702 702 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 712 712 Not glycated.
{ECO:0000269|PubMed:9326300}.
SITE 755 755 Not glycated.
{ECO:0000269|PubMed:9326300}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:1512244}.
MOD_RES 18 18 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:14999081}.
MOD_RES 29 29 Phosphotyrosine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:P19332}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000250|UniProtKB:P19332}.
MOD_RES 69 69 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 71 71 Phosphothreonine.
{ECO:0000250|UniProtKB:P19332}.
MOD_RES 111 111 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 214 214 Phosphoserine; by SGK1.
{ECO:0000269|PubMed:16982696}.
MOD_RES 396 396 Phosphoserine; in PHF-tau.
{ECO:0000269|PubMed:1899488}.
MOD_RES 470 470 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:9614189}.
MOD_RES 472 472 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 480 480 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 480 480 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 484 484 Deamidated asparagine; in tau and PHF-
tau; partial.
{ECO:0000269|PubMed:1512244}.
MOD_RES 486 486 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 492 492 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 498 498 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:15546861}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 514 514 Phosphotyrosine; by TTBK1.
{ECO:0000269|PubMed:16923168}.
MOD_RES 515 515 Phosphoserine; by PDPK1 and TTBK1.
{ECO:0000269|PubMed:16923168}.
MOD_RES 516 516 Phosphoserine; by PDPK1 and TTBK1.
{ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16923168,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:9614189}.
MOD_RES 519 519 Phosphoserine; by CK1, PDPK1 and TTBK1.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:14761950,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16923168,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:21327254,
ECO:0000269|PubMed:9614189}.
MOD_RES 522 522 Phosphothreonine; by CK1 and PDPK1.
{ECO:0000269|PubMed:14761950,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:19451179}.
MOD_RES 529 529 Phosphothreonine; by BRSK1, BRSK2, DYRK2
and PDPK1. {ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:18599021,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:21985311,
ECO:0000269|PubMed:23666762,
ECO:0000269|PubMed:9614189}.
MOD_RES 531 531 Phosphoserine; by PKA.
{ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:9614189}.
MOD_RES 534 534 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:19451179}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 548 548 Phosphothreonine; by GSK3-beta and PDPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14690523,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603}.
MOD_RES 552 552 Phosphoserine; by PDPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:9614189}.
MOD_RES 554 554 Phosphoserine; by PHK.
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:8999860}.
MOD_RES 576 576 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 576 576 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 579 579 Phosphoserine; by MARK1, MARK4, BRSK1,
BRSK2 and PHK.
{ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:21985311,
ECO:0000269|PubMed:7706316,
ECO:0000269|PubMed:8999860,
ECO:0000269|PubMed:9614189}.
MOD_RES 596 596 Deamidated asparagine; in tau and PHF-
tau; partial.
{ECO:0000269|PubMed:1512244}.
MOD_RES 598 598 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 602 602 Phosphoserine; by PHK.
{ECO:0000269|PubMed:8999860}.
MOD_RES 606 606 Phosphoserine; by PHK.
{ECO:0000269|PubMed:8999860}.
MOD_RES 607 607 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 610 610 Phosphoserine; by MARK1; in PHF-tau.
{ECO:0000269|PubMed:7706316}.
MOD_RES 615 615 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 622 622 Phosphoserine; by MARK1; in PHF-tau.
{ECO:0000269|PubMed:7706316}.
MOD_RES 628 628 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 628 628 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 634 634 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 638 638 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 641 641 Phosphoserine; by MARK1; in PHF-tau.
{ECO:0000269|PubMed:7706316}.
MOD_RES 648 648 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 660 660 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 664 664 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 666 666 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 669 669 Phosphoserine; by PHK.
{ECO:0000269|PubMed:8999860}.
MOD_RES 673 673 Phosphoserine; by MARK1; in PHF-tau.
{ECO:0000269|PubMed:7706316}.
MOD_RES 686 686 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 702 702 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 711 711 Phosphotyrosine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 713 713 Phosphoserine; by CK1 and PDPK1.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14761950,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:21327254,
ECO:0000269|PubMed:9614189}.
MOD_RES 717 717 Phosphoserine; alternate.
{ECO:0000244|PubMed:19690332}.
MOD_RES 720 720 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 721 721 Phosphoserine; by CK1 and PDPK1.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14761950,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:21327254,
ECO:0000269|PubMed:9614189}.
MOD_RES 726 726 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:15546861}.
MOD_RES 733 733 Phosphoserine; by CaMK2 and TTBK1.
{ECO:0000269|PubMed:16923168}.
MOD_RES 739 739 Phosphoserine; by PDPK1 and TTBK1.
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:16923168,
ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:9614189}.
MOD_RES 744 744 Phosphothreonine; by TTBK1.
{ECO:0000269|PubMed:16923168}.
CARBOHYD 87 87 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 383 383 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 467 467 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 480 480 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 491 491 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 525 525 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:21327254}.
CARBOHYD 542 542 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 551 551 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 555 555 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:21327254}.
CARBOHYD 576 576 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 597 597 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 598 598 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 664 664 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 670 670 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 686 686 N-linked (Glc) (glycation) lysine; in
PHF-tau; in vitro.
{ECO:0000269|PubMed:19451179}.
CARBOHYD 717 717 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:21327254}.
DISULFID 608 639 {ECO:0000250}.
CROSSLNK 44 44 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 571 571 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin); in
PHF-tau. {ECO:0000269|PubMed:16443603}.
CROSSLNK 576 576 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 584 584 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 598 598 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 615 615 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 628 628 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin); in
PHF-tau. {ECO:0000269|PubMed:16443603}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 638 638 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 648 648 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 660 660 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 664 664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin); in
PHF-tau. {ECO:0000269|PubMed:16443603}.
CROSSLNK 686 686 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 692 692 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 702 702 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
VAR_SEQ 1 44 MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDA
GLK -> MLRALQQRKR (in isoform Tau-A).
{ECO:0000303|PubMed:2516729}.
/FTId=VSP_003175.
VAR_SEQ 45 73 Missing (in isoform Tau-A, isoform Tau-D
and isoform Fetal-tau).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2498079,
ECO:0000303|PubMed:2516729,
ECO:0000303|PubMed:3131773,
ECO:0000303|Ref.7}.
/FTId=VSP_003176.
VAR_SEQ 74 102 Missing (in isoform Tau-A, isoform Tau-B,
isoform Tau-D, isoform Tau-E and isoform
Fetal-tau). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2484340,
ECO:0000303|PubMed:2498079,
ECO:0000303|PubMed:2516729,
ECO:0000303|PubMed:3131773,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_003177.
VAR_SEQ 103 104 Missing (in isoform Tau-A).
{ECO:0000303|PubMed:2516729}.
/FTId=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). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2484340,
ECO:0000303|PubMed:2498079,
ECO:0000303|PubMed:2516729,
ECO:0000303|PubMed:3131773,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=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). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2484340,
ECO:0000303|PubMed:2498079,
ECO:0000303|PubMed:2516729,
ECO:0000303|PubMed:3131773,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_003180.
VAR_SEQ 502 502 S -> SATKQVQRRPPPAGPRSER (in isoform Tau-
G). {ECO:0000305}.
/FTId=VSP_026780.
VAR_SEQ 592 622 Missing (in isoform Tau-A, isoform Tau-B,
isoform Tau-C and isoform Fetal-tau).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2484340,
ECO:0000303|PubMed:2516729,
ECO:0000303|PubMed:3131773,
ECO:0000303|Ref.7}.
/FTId=VSP_003181.
VARIANT 5 5 R -> H (in FTD; reduces the ability of
tau to promote microtubule assembly and
promotes fibril formation in vitro;
dbSNP:rs63750959).
{ECO:0000269|PubMed:11921059}.
/FTId=VAR_019660.
VARIANT 5 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;
dbSNP:rs63750959).
{ECO:0000269|PubMed:12325083}.
/FTId=VAR_019661.
VARIANT 17 17 T -> M (in dbSNP:rs144611688).
{ECO:0000269|PubMed:20020531}.
/FTId=VAR_064622.
VARIANT 30 30 T -> A (in dbSNP:rs748728879).
{ECO:0000269|PubMed:20020531}.
/FTId=VAR_064623.
VARIANT 285 285 D -> N (risk factor for PSNP1;
dbSNP:rs62063786).
{ECO:0000269|PubMed:10534245,
ECO:0000269|PubMed:9629852}.
/FTId=VAR_010340.
VARIANT 289 289 V -> A (risk factor for PSNP1;
dbSNP:rs62063787).
{ECO:0000269|PubMed:10534245,
ECO:0000269|PubMed:9629852}.
/FTId=VAR_010341.
VARIANT 370 370 R -> W (in dbSNP:rs17651549).
/FTId=VAR_056121.
VARIANT 441 441 Y -> H (in dbSNP:rs2258689).
{ECO:0000269|PubMed:1420178,
ECO:0000269|PubMed:15365985,
ECO:0000269|PubMed:9629852}.
/FTId=VAR_010342.
VARIANT 447 447 S -> P (in dbSNP:rs10445337).
{ECO:0000269|PubMed:9629852}.
/FTId=VAR_010343.
VARIANT 574 574 K -> T (in PIDB; reduces the ability to
promote microtubule assembly by 70%;
dbSNP:rs63750129).
{ECO:0000269|PubMed:11089577,
ECO:0000269|PubMed:11117542}.
/FTId=VAR_010344.
VARIANT 583 583 L -> V (in FTD; less able to promote
microtubule assembly than wild-type tau;
dbSNP:rs63750349).
{ECO:0000269|PubMed:12509859}.
/FTId=VAR_019662.
VARIANT 589 589 G -> V (in FTD; dbSNP:rs63750376).
{ECO:0000269|PubMed:9641683,
ECO:0000269|PubMed:9973279}.
/FTId=VAR_010345.
VARIANT 596 596 N -> K (in FTD; with parkinsonism;
dbSNP:rs63750756).
{ECO:0000269|PubMed:10412802,
ECO:0000269|PubMed:10489057,
ECO:0000269|PubMed:10802785,
ECO:0000269|PubMed:12473774,
ECO:0000269|PubMed:9789048}.
/FTId=VAR_010346.
VARIANT 597 597 Missing (in FTD).
{ECO:0000269|PubMed:9973279}.
/FTId=VAR_010347.
VARIANT 613 613 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;
dbSNP:rs63750416).
{ECO:0000269|PubMed:11585254,
ECO:0000269|PubMed:11906000}.
/FTId=VAR_019663.
VARIANT 613 613 Missing (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).
{ECO:0000269|PubMed:11220749,
ECO:0000269|PubMed:11906000,
ECO:0000269|PubMed:14991828,
ECO:0000269|PubMed:14991829}.
/FTId=VAR_019664.
VARIANT 617 617 V -> I (in dbSNP:rs116733906).
{ECO:0000269|PubMed:20020531}.
/FTId=VAR_064624.
VARIANT 618 618 P -> L (in FTD; most common mutation;
reduction in the ability to promote
microtubule assembly; accelerates
aggregation of tau into filaments;
dbSNP:rs63751273).
{ECO:0000269|PubMed:10214944,
ECO:0000269|PubMed:9641683,
ECO:0000269|PubMed:9736786,
ECO:0000269|PubMed:9789048,
ECO:0000269|PubMed:9973279}.
/FTId=VAR_010348.
VARIANT 618 618 P -> S (in FTD and CBD; reduction in the
ability to promote microtubule assembly;
dbSNP:rs63751438).
{ECO:0000269|PubMed:10374757,
ECO:0000269|PubMed:10553987,
ECO:0000269|PubMed:11071507,
ECO:0000269|PubMed:16240366}.
/FTId=VAR_010349.
VARIANT 620 620 G -> V (in PSNP1; dbSNP:rs63751391).
{ECO:0000269|PubMed:16157753}.
/FTId=VAR_037439.
VARIANT 622 622 S -> N (in FTD; minimal parkinsonism;
very early age of onset;
dbSNP:rs63751165).
{ECO:0000269|PubMed:10208578}.
/FTId=VAR_010350.
VARIANT 634 634 K -> M (in FTD; dbSNP:rs63750092).
{ECO:0000269|PubMed:15883319}.
/FTId=VAR_037440.
VARIANT 637 637 S -> F (in PIDB; markedly reduced ability
of tau to promote microtubule assembly;
dbSNP:rs63750635).
{ECO:0000269|PubMed:11891833}.
/FTId=VAR_019665.
VARIANT 654 654 V -> M (in FTD; ultrastructural and
biochemical characteristics
indistinguishable from Alzheimer disease;
accelerates aggregation of tau into
filaments; dbSNP:rs63750570).
{ECO:0000269|PubMed:10214944,
ECO:0000269|PubMed:9629852}.
/FTId=VAR_010351.
VARIANT 659 659 E -> V (in FTD; dbSNP:rs63750711).
{ECO:0000269|PubMed:11117541}.
/FTId=VAR_019666.
VARIANT 669 669 S -> L (in fatal respiratory
hypoventilation; unusual apparent
autosomal recessive inheritance; reduced
binding to microtubules as well as
increased fibrillization and aggregation;
dbSNP:rs63750425).
{ECO:0000269|PubMed:14595660}.
/FTId=VAR_019667.
VARIANT 686 686 K -> I (in PIDB; 90% reduction in the
rate of microtubule assembly;
dbSNP:rs63751264).
{ECO:0000269|PubMed:11601501}.
/FTId=VAR_019668.
VARIANT 706 706 G -> R (in PIDB; in vitro the mutation
reduces the ability of tau to promote
microtubule assembly by 25 to 30%;
dbSNP:rs63750512).
{ECO:0000269|PubMed:10604746,
ECO:0000269|PubMed:11117542}.
/FTId=VAR_010352.
VARIANT 723 723 R -> 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; dbSNP:rs63750424).
{ECO:0000269|PubMed:10214944,
ECO:0000269|PubMed:11278002,
ECO:0000269|PubMed:11889249,
ECO:0000269|PubMed:14517953,
ECO:0000269|PubMed:26086902,
ECO:0000269|PubMed:9641683,
ECO:0000269|PubMed:9973279}.
/FTId=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).
{ECO:0000305}.
CONFLICT 414 414 H -> L (in Ref. 5; AAC04277).
{ECO:0000305}.
CONFLICT 557 557 K -> M (in Ref. 12; AAS17881).
{ECO:0000305}.
CONFLICT 591 591 K -> S (in Ref. 12; AAS17881).
{ECO:0000305}.
CONFLICT 617 617 V -> Q (in Ref. 17; AA sequence).
{ECO:0000305}.
CONFLICT 622 622 S -> K (in Ref. 17; AA sequence).
{ECO:0000305}.
HELIX 596 599 {ECO:0000244|PDB:2MZ7}.
HELIX 603 605 {ECO:0000244|PDB:2MZ7}.
STRAND 607 610 {ECO:0000244|PDB:2MZ7}.
HELIX 613 615 {ECO:0000244|PDB:2MZ7}.
TURN 620 622 {ECO:0000244|PDB:2MZ7}.
STRAND 625 627 {ECO:0000244|PDB:4E0N}.
SEQUENCE 758 AA; 78928 MW; D46C66CDBCD196E8 CRC64;
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG
SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG
HVTQEPESGK VVQEGFLREP GPPGLSHQLM SGMPGAPLLP EGPREATRQP SGTGPEDTEG
GRHAPELLKH QLLGDLHQEG PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA
QDGRPPQTAA REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE
FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD LPEPSEKQPA
AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS AKTLKNRPCL SPKHPTPGSS
DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG SSGAKEMKLK GADGKTKIAT PRGAAPPGQK
GQANATRIPA KTPPAPKTPP SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP
KKVAVVRTPP KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD
LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG GGQVEVKSEK
LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK AKTDHGAEIV YKSPVVSGDT
SPRHLSNVSS TGSIDMVDSP QLATLADEVS ASLAKQGL


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