TAU_HUMAN
ID TAU_HUMAN Reviewed; 758 AA.
AC P10636; P18518; Q14799; Q15549; Q15550; Q15551; Q1RMF6; Q53YB1; Q5CZI7;
AC Q5XWF0; Q6QT54; Q9UDJ3; Q9UMH0; Q9UQ96;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 5.
DT 03-AUG-2022, entry version 276.
DE RecName: Full=Microtubule-associated protein tau {ECO:0000305};
DE AltName: Full=Neurofibrillary tangle protein;
DE AltName: Full=Paired helical filament-tau;
DE Short=PHF-tau;
GN Name=MAPT {ECO:0000312|HGNC:HGNC:6893}; Synonyms=MAPTL, MTBT1, TAU;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FETAL-TAU).
RC TISSUE=Brain;
RX PubMed=3131773; DOI=10.1073/pnas.85.11.4051;
RA Goedert M., Wischik C., Crowther R., Walker J., Klug A.;
RT "Cloning and sequencing of the cDNA encoding a core protein of the paired
RT helical filament of Alzheimer disease: identification as the microtubule-
RT associated protein tau.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4051-4055(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-D).
RC TISSUE=Brain;
RX PubMed=2498079; DOI=10.1002/j.1460-2075.1989.tb03390.x;
RA Goedert M., Spillantini M.G., Potier M.-C., Ulrich J., Crowther R.A.;
RT "Cloning and sequencing of the cDNA encoding an isoform of microtubule-
RT associated protein tau containing four tandem repeats: differential
RT expression of tau protein mRNAs in human brain.";
RL EMBO J. 8:393-399(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A AND FETAL-TAU).
RC TISSUE=Fetal brain;
RX PubMed=2516729; DOI=10.1016/0896-6273(89)90050-0;
RA Lee G., Neve R.L., Kosik K.S.;
RT "The microtubule binding domain of tau protein.";
RL Neuron 2:1615-1624(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B; TAU-C; TAU-E AND TAU-F), AND
RP ASSOCIATION WITH ALZHEIMER DISEASE.
RC TISSUE=Brain;
RX PubMed=2484340; DOI=10.1016/0896-6273(89)90210-9;
RA Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A.;
RT "Multiple isoforms of human microtubule-associated protein tau: sequences
RT and localization in neurofibrillary tangles of Alzheimer's disease.";
RL Neuron 3:519-526(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PNS-TAU; FETAL-TAU AND TAU-F),
RP ALTERNATIVE SPLICING, AND VARIANT HIS-441.
RX PubMed=1420178; DOI=10.1021/bi00158a027;
RA Andreadis A., Brown W.M., Kosik K.S.;
RT "Structure and novel exons of the human tau gene.";
RL Biochemistry 31:10626-10633(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-E).
RA Chun J., Kwon T., Lee E.-J., Hyun S.-H., Kang S.S.;
RT "Cloning of tau-related genes.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FETAL-TAU).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FETAL-TAU AND TAU-D).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-73; 103-381; 468-497; 508-571; 577-583; 592-607;
RP 616-634; 639-657; 661-664; 671-700 AND 703-758, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND DEAMIDATION AT ASN-484 AND ASN-596.
RC TISSUE=Brain;
RX PubMed=1512244; DOI=10.1016/s0021-9258(18)41890-x;
RA Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K.,
RA Ihara Y.;
RT "Protein sequence and mass spectrometric analyses of tau in the Alzheimer's
RT disease brain.";
RL J. Biol. Chem. 267:17047-17054(1992).
RN [11]
RP PROTEIN SEQUENCE OF 25-44; 529-538; 560-571 AND 671-686, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 466-740 (ISOFORMS
RP TAU-A/TAU-B/TAU-C/FETAL-TAU).
RA Han J., Zhang J., Dong X.-P.;
RT "Molecular interactions of recombinant neural protein tau with recombinant
RT and native PrP proteins in vitro.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP PROTEIN SEQUENCE OF 543-551; 560-574; 576-584 AND 623-634, PHOSPHORYLATION
RP AT SER-531; THR-534; THR-548; SER-552; SER-554; SER-579; SER-713 AND
RP SER-739, UBIQUITINATION AT LYS-571; LYS-628 AND LYS-670, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.m512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6
RT ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [14]
RP PROTEIN SEQUENCE OF 577-584; 608-611; 616-628; 639-648 AND 671-686,
RP PHOSPHORYLATION AT SER-579; SER-610; SER-622; SER-641 AND SER-673,
RP MUTAGENESIS, AND DOMAIN.
RX PubMed=7706316; DOI=10.1074/jbc.270.13.7679;
RA Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G.,
RA Meyer H.E., Mandelkow E.-M., Mandelkow E.;
RT "Microtubule-associated protein/microtubule affinity-regulating kinase
RT (p110mark). A novel protein kinase that regulates tau-microtubule
RT interactions and dynamic instability by phosphorylation at the Alzheimer-
RT specific site serine 262.";
RL J. Biol. Chem. 270:7679-7688(1995).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 592-622 (ISOFORMS PNS-TAU/TAU-D/TAU-E/TAU-F).
RC TISSUE=Brain;
RX PubMed=2495000; DOI=10.1016/0006-291x(89)92240-7;
RA Mori H., Hamada Y., Kawaguchi M., Honda T., Kondo J., Ihara Y.;
RT "A distinct form of tau is selectively incorporated into Alzheimer's paired
RT helical filaments.";
RL Biochem. Biophys. Res. Commun. 159:1221-1226(1989).
RN [16]
RP PROTEIN SEQUENCE OF 251-264 AND 379-392, AND PHOSPHORYLATION AT SER-396.
RX PubMed=1899488; DOI=10.1126/science.1899488;
RA Lee V.M., Balin B.J., Otvos L. Jr., Trojanowski J.Q.;
RT "A68: a major subunit of paired helical filaments and derivatized forms of
RT normal Tau.";
RL Science 251:675-678(1991).
RN [17]
RP PROTEIN SEQUENCE OF 616-712.
RX PubMed=1915258; DOI=10.1002/j.1460-2075.1991.tb07820.x;
RA Jakes R., Novak M., Davison M., Wischik C.M.;
RT "Identification of 3- and 4-repeat tau isoforms within the PHF in
RT Alzheimer's disease.";
RL EMBO J. 10:2725-2729(1991).
RN [18]
RP IDENTIFICATION (ISOFORM TAU-G), AND VARIANT HIS-441.
RX PubMed=15365985; DOI=10.1002/humu.20086;
RA Rademakers R., Cruts M., van Broeckhoven C.;
RT "The role of tau (MAPT) in frontotemporal dementia and related
RT tauopathies.";
RL Hum. Mutat. 24:277-295(2004).
RN [19]
RP REVIEW.
RX PubMed=1713721; DOI=10.1016/0166-2236(91)90105-4;
RA Goedert M., Crowther R.A., Garner C.C.;
RT "Molecular characterization of microtubule-associated proteins tau and
RT MAP2.";
RL Trends Neurosci. 14:193-199(1991).
RN [20]
RP PHOSPHORYLATION AT SER-554; SER-579; SER-602; SER-622 AND SER-669.
RX PubMed=8999860; DOI=10.1016/s0021-9258(19)67481-8;
RA Paudel H.K.;
RT "The regulatory Ser262 of microtubule-associated protein tau is
RT phosphorylated by phosphorylase kinase.";
RL J. Biol. Chem. 272:1777-1785(1997).
RN [21]
RP GLYCATION AT LYS-87; LYS-383; LYS-467; LYS-480; LYS-491; LYS-542; LYS-551;
RP LYS-576; LYS-597; LYS-598; LYS-664; LYS-670 AND LYS-686, AND LACK OF
RP GLYCATION AT LYS-24; LYS-44; LYS-67; LYS-381; LYS-391; LYS-392; LYS-394;
RP LYS-465; LYS-497; LYS-507; LYS-541; LYS-557; LYS-571; LYS-574; LYS-584;
RP LYS-591; LYS-607; LYS-611; LYS-615; LYS-628; LYS-634; LYS-638; LYS-648;
RP LYS-657; LYS-660; LYS-687; LYS-692; LYS-700; LYS-702; LYS-712 AND LYS-755.
RX PubMed=9326300; DOI=10.1046/j.1471-4159.1997.69041709.x;
RA Nacharaju P., Ko L., Yen S.H.;
RT "Characterization of in vitro glycation sites of tau.";
RL J. Neurochem. 69:1709-1719(1997).
RN [22]
RP PHOSPHORYLATION, AND MUTAGENESIS.
RX PubMed=9735171; DOI=10.1006/abbi.1998.0813;
RA Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., Iqbal K.;
RT "Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal
RT inhibition of its binding to microtubules.";
RL Arch. Biochem. Biophys. 357:299-309(1998).
RN [23]
RP PHOSPHORYLATION AT THR-470; SER-516; SER-519; THR-529; SER-531; SER-552;
RP SER-579; SER-713; SER-721 AND SER-739, AND MUTAGENESIS.
RX PubMed=9614189; DOI=10.1091/mbc.9.6.1495;
RA Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K.,
RA Trinczek B., Biernat J., Godemann R., Mandelkow E.-M., Mandelkow E.;
RT "The endogenous and cell cycle-dependent phosphorylation of tau protein in
RT living cells: implications for Alzheimer's disease.";
RL Mol. Biol. Cell 9:1495-1512(1998).
RN [24]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=10747907; DOI=10.1074/jbc.m000389200;
RA Maas T., Eidenmueller J., Brandt R.;
RT "Interaction of tau with the neural membrane cortex is regulated by
RT phosphorylation at sites that are modified in paired helical filaments.";
RL J. Biol. Chem. 275:15733-15740(2000).
RN [25]
RP PHOSPHORYLATION AT SER-519; THR-522; SER-713 AND SER-721 BY CSNK1D/CK1, AND
RP INTERACTION WITH CSNK1D.
RX PubMed=14761950; DOI=10.1074/jbc.m314116200;
RA Li G., Yin H., Kuret J.;
RT "Casein kinase 1 delta phosphorylates tau and disrupts its binding to
RT microtubules.";
RL J. Biol. Chem. 279:15938-15945(2004).
RN [26]
RP PHOSPHORYLATION AT THR-548 BY GSK3B.
RX PubMed=14690523; DOI=10.1111/j.1471-4159.2004.02155.x;
RA Cho J.H., Johnson G.V.;
RT "Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta
RT (GSK3beta) plays a critical role in regulating tau's ability to bind and
RT stabilize microtubules.";
RL J. Neurochem. 88:349-358(2004).
RN [27]
RP PHOSPHORYLATION AT TYR-18 BY FYN.
RX PubMed=14999081; DOI=10.1523/jneurosci.4162-03.2004;
RA Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M.,
RA Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.;
RT "Phosphorylation of tau by fyn: implications for Alzheimer's disease.";
RL J. Neurosci. 24:2304-2312(2004).
RN [28]
RP INTERACTION WITH SQSTM1, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=15953362; DOI=10.1111/j.1471-4159.2005.03181.x;
RA Babu J.R., Geetha T., Wooten M.W.;
RT "Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal
RT degradation.";
RL J. Neurochem. 94:192-203(2005).
RN [29]
RP PHOSPHORYLATION AT THR-498; SER-516; SER-519; THR-522; THR-529; SER-531;
RP THR-548; SER-552; SER-579; SER-713; SER-721 AND SER-726, AND
RP DEPHOSPHORYLATION AT THR-498; SER-516; SER-519; THR-522; THR-529; SER-531;
RP THR-548; SER-552; SER-579; SER-713; SER-721 AND SER-726 BY PPP5C.
RX PubMed=15546861; DOI=10.1074/jbc.m410775200;
RA Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.;
RT "Dephosphorylation of tau by protein phosphatase 5: impairment in
RT Alzheimer's disease.";
RL J. Biol. Chem. 280:1790-1796(2005).
RN [30]
RP PHOSPHORYLATION AT TYR-514; SER-515; SER-516; SER-519; SER-733; SER-739 AND
RP THR-744.
RX PubMed=16923168; DOI=10.1111/j.1471-4159.2006.04059.x;
RA Sato S., Cerny R.L., Buescher J.L., Ikezu T.;
RT "Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is
RT involved in tau phosphorylation and aggregation.";
RL J. Neurochem. 98:1573-1584(2006).
RN [31]
RP PHOSPHORYLATION AT SER-214 BY SGK1, AND INTERACTION WITH SGK1.
RX PubMed=16982696; DOI=10.1128/mcb.01017-06;
RA Yang Y.C., Lin C.H., Lee E.H.;
RT "Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite
RT formation through microtubule depolymerization by SGK1 and by SGK1
RT phosphorylation of tau.";
RL Mol. Cell. Biol. 26:8357-8370(2006).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [33]
RP PHOSPHORYLATION BY CSNK1D/CK1.
RX PubMed=17562708; DOI=10.1074/jbc.m703269200;
RA Hanger D.P., Byers H.L., Wray S., Leung K.-Y., Saxton M.J., Seereeram A.,
RA Reynolds C.H., Ward M.A., Anderton B.H.;
RT "Novel phosphorylation sites in tau from Alzheimer brain support a role for
RT casein kinase 1 in disease pathogenesis.";
RL J. Biol. Chem. 282:23645-23654(2007).
RN [34]
RP PHOSPHORYLATION AT THR-529 BY DYRK2.
RX PubMed=18599021; DOI=10.1016/j.bcp.2008.05.021;
RA Yoshida K.;
RT "Role for DYRK family kinases on regulation of apoptosis.";
RL Biochem. Pharmacol. 76:1389-1394(2008).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [37]
RP GLYCOSYLATION, PHOSPHORYLATION AT SER-516; SER-519; THR-522; THR-529;
RP SER-531; THR-534; SER-579; SER-713; SER-721 AND SER-739, AND ASSOCIATION
RP WITH ALZHEIMER DISEASE.
RX PubMed=19451179; DOI=10.1093/brain/awp099;
RA Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K.,
RA Gong C.X.;
RT "Reduced O-GlcNAcylation links lower brain glucose metabolism and tau
RT pathology in Alzheimer's disease.";
RL Brain 132:1820-1832(2009).
RN [38]
RP INTERACTION WITH EPM2A.
RX PubMed=19542233; DOI=10.1074/jbc.m109.009688;
RA Puri R., Suzuki T., Yamakawa K., Ganesh S.;
RT "Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an
RT animal model for Lafora disease.";
RL J. Biol. Chem. 284:22657-22663(2009).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-717; SER-721 AND
RP SER-726, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [41]
RP GLYCOSYLATION AT SER-525; SER-555 AND SER-717, PHOSPHORYLATION AT SER-519;
RP SER-713 SER-717 AND SER-721, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21327254; DOI=10.1039/c0mb00337a;
RA Smet-Nocca C., Broncel M., Wieruszeski J.M., Tokarski C., Hanoulle X.,
RA Leroy A., Landrieu I., Rolando C., Lippens G., Hackenberger C.P.;
RT "Identification of O-GlcNAc sites within peptides of the Tau protein and
RT their impact on phosphorylation.";
RL Mol. Biosyst. 7:1420-1429(2011).
RN [42]
RP FUNCTION, AND PHOSPHORYLATION AT THR-529 AND SER-579.
RX PubMed=21985311; DOI=10.1111/j.1471-4159.2011.07523.x;
RA Yoshida H., Goedert M.;
RT "Phosphorylation of microtubule-associated protein tau by AMPK-related
RT kinases.";
RL J. Neurochem. 120:165-176(2012).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-548; SER-552;
RP SER-713 AND SER-721, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [44]
RP INTERACTION WITH MARK1; MARK2; MARK3 AND MARK4, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-579.
RX PubMed=23666762; DOI=10.1007/s12017-013-8232-3;
RA Gu G.J., Lund H., Wu D., Blokzijl A., Classon C., von Euler G.,
RA Landegren U., Sunnemark D., Kamali-Moghaddam M.;
RT "Role of individual MARK isoforms in phosphorylation of tau at Ser262 in
RT Alzheimer's disease.";
RL NeuroMolecular Med. 15:458-469(2013).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [46]
RP INTERACTION WITH LRRK2, AND SUBCELLULAR LOCATION.
RX PubMed=26014385; DOI=10.1007/s12035-015-9209-z;
RA Guerreiro P.S., Gerhardt E., Lopes da Fonseca T., Baehr M., Outeiro T.F.,
RA Eckermann K.;
RT "LRRK2 Promotes Tau Accumulation, Aggregation and Release.";
RL Mol. Neurobiol. 53:3124-3135(2016).
RN [47]
RP INTERACTION WITH LRP1.
RX PubMed=32296178; DOI=10.1038/s41586-020-2156-5;
RA Rauch J.N., Luna G., Guzman E., Challis C., Sibih Y.E., Leshuk C.,
RA Hernandez I., Wegmann S., Hyman B.T., Gradinaru V., Kampmann M.,
RA Kosik K.S.;
RT "LRP1 is a master regulator of tau uptake and spread.";
RL Nature 580:381-385(2020).
RN [48]
RP STRUCTURE BY NMR OF 542-554 IN COMPLEX WITH PIN1.
RX PubMed=11313338; DOI=10.1074/jbc.m010327200;
RA Wintjens R., Wieruszeski J.-M., Drobecq H., Rousselot-Pailley P., Buee L.,
RA Lippens G., Landrieu I.;
RT "1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine
RT peptides.";
RL J. Biol. Chem. 276:25150-25156(2001).
RN [49]
RP SUBCELLULAR LOCATION.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [50]
RP REVIEW ON VARIANTS.
RX PubMed=10899436; DOI=10.1016/s0925-4439(00)00037-5;
RA Goedert M., Spillantini M.G.;
RT "Tau mutations in frontotemporal dementia FTDP-17 and their relevance for
RT Alzheimer's disease.";
RL Biochim. Biophys. Acta 1502:110-121(2000).
RN [51]
RP VARIANT FTD MET-654, VARIANTS ASN-285; ALA-289; HIS-441 AND PRO-447, AND
RP INVOLVEMENT IN FTD.
RX PubMed=9629852; DOI=10.1002/ana.410430617;
RA Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L.,
RA Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D.;
RT "Tau is a candidate gene for chromosome 17 frontotemporal dementia.";
RL Ann. Neurol. 43:815-825(1998).
RN [52]
RP ERRATUM OF PUBMED:9629852.
RA Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L.,
RA Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D.;
RL Ann. Neurol. 44:428-428(1998).
RN [53]
RP VARIANT FTD LEU-618.
RX PubMed=9736786; DOI=10.1093/hmg/7.11.1825;
RA Dumanchin C., Camuzat A., Campion D., Verpillat P., Hannequin D.,
RA Dubois B., Saugier-Veber P., Martin C., Penet C., Charbonnier F., Agid Y.,
RA Frebourg T., Brice A.;
RT "Segregation of a missense mutation in the microtubule-associated protein
RT tau gene with familial frontotemporal dementia and parkinsonism.";
RL Hum. Mol. Genet. 7:1825-1829(1998).
RN [54]
RP VARIANTS FTD VAL-589; LEU-618 AND TRP-723.
RX PubMed=9641683; DOI=10.1038/31508;
RA Hutton M., Lendon C.L., Rizzu P., Baker M., Froelich S., Houlden H.,
RA Pickering-Brown S., Chakraverty S., Isaacs A., Grover A., Hackett J.,
RA Adamson J., Lincoln S., Dickson D., Davies P., Petersen R.C., Stevens M.,
RA de Graaff E., Wauters E., van Baren J., Hillebrand M., Joosse M.,
RA Kwon J.M., Nowotny P., Che L.K., Norton J., Morris J.C., Reed L.A.,
RA Trojanowski J., Basun H., Lannfelt L., Neystat M., Fahn S., Dark F.,
RA Tannenberg T., Dodd P.R., Hayward N., Kwok J.B.J., Schofield P.R.,
RA Andreadis A., Snowden J., Craufurd D., Neary D., Owen F., Oostra B.A.,
RA Hardy J., Goate A., van Swieten J., Mann D., Lynch T., Heutink P.;
RT "Association of missense and 5'-splice-site mutations in tau with the
RT inherited dementia FTDP-17.";
RL Nature 393:702-705(1998).
RN [55]
RP VARIANTS FTD LYS-596 AND LEU-618.
RX PubMed=9789048; DOI=10.1073/pnas.95.22.13103;
RA Clark L.N., Poorkaj P., Wszolek Z., Geschwind D.H., Nasreddine Z.S.,
RA Miller B., Li D., Payami H., Awert F., Markopoulou K., Andreadis A.,
RA D'Souza I., Lee V.M.-Y., Reed L., Trojanowski J.Q., Zhukareva V., Bird T.,
RA Schellenberg G., Wilhelmsen K.C.;
RT "Pathogenic implications of mutations in the tau gene in pallido-ponto-
RT nigral degeneration and related neurodegenerative disorders linked to
RT chromosome 17.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13103-13107(1998).
RN [56]
RP VARIANT PPND LYS-596.
RX PubMed=10412802; DOI=10.1007/s004010051052;
RA Delisle M.-B., Murrell J.R., Richardson R., Trofatter J.A., Rascol O.,
RA Soulages X., Mohr M., Calvas P., Ghetti B.;
RT "A mutation at codon 279 (N279K) in exon 10 of the Tau gene causes a
RT tauopathy with dementia and supranuclear palsy.";
RL Acta Neuropathol. 98:62-77(1999).
RN [57]
RP VARIANTS FTD VAL-589; LYS-597 DEL; LEU-618 AND TRP-723.
RX PubMed=9973279; DOI=10.1086/302256;
RA Rizzu P., Van Swieten J.C., Joosse M., Hasegawa M., Stevens M., Tibben A.,
RA Niermeijer M.F., Hillebrand M., Ravid R., Oostra B.A., Goedert M.,
RA van Duijn C.M., Heutink P.;
RT "High prevalence of mutations in the microtubule-associated protein tau in
RT a population study of frontotemporal dementia in the Netherlands.";
RL Am. J. Hum. Genet. 64:414-421(1999).
RN [58]
RP VARIANT FTD SER-618.
RX PubMed=10553987;
RX DOI=10.1002/1531-8249(199911)46:5<708::aid-ana5>3.0.co;2-k;
RA Sperfeld A.D., Collatz M.B., Baier H., Palmbach M., Storch A., Schwarz J.,
RA Tatsch K., Reske S., Joosse M., Heutink P., Ludolph A.C.;
RT "FTDP-17: an early-onset phenotype with parkinsonism and epileptic seizures
RT caused by a novel mutation.";
RL Ann. Neurol. 46:708-715(1999).
RN [59]
RP VARIANTS FTD LEU-618; MET-654 AND TRP-723.
RX PubMed=10214944; DOI=10.1016/s0014-5793(99)00294-x;
RA Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M., Yen S.H.;
RT "Accelerated filament formation from tau protein with specific FTDP-17
RT missense mutations.";
RL FEBS Lett. 447:195-199(1999).
RN [60]
RP VARIANT FTD/CBD SER-618.
RX PubMed=10374757; DOI=10.1097/00005072-199906000-00011;
RA Bugiani O., Murrell J.R., Giaccone G., Hasegawa M., Ghigo G., Tabaton M.,
RA Morbin M., Primavera A., Carella F., Solaro C., Grisoli M., Savoiardo M.,
RA Spillantini M.G., Tagliavini F., Goedert M., Ghetti B.;
RT "Frontotemporal dementia and corticobasal degeneration in a family with a
RT P301S mutation in tau.";
RL J. Neuropathol. Exp. Neurol. 58:667-677(1999).
RN [61]
RP VARIANT PIDB ARG-706.
RX PubMed=10604746; DOI=10.1097/00005072-199912000-00002;
RA Murrell J.R., Spillantini M.G., Zolo P., Guazzelli M., Smith M.J.,
RA Hasegawa M., Redi F., Crowther R.A., Pietrini P., Ghetti B., Goedert M.;
RT "Tau gene mutation G389R causes a tauopathy with abundant pick body-like
RT inclusions and axonal deposits.";
RL J. Neuropathol. Exp. Neurol. 58:1207-1226(1999).
RN [62]
RP VARIANT FTD LYS-596.
RX PubMed=10489057; DOI=10.1212/wnl.53.4.864;
RA Yasuda M., Kawamata T., Komure O., Kuno S., D'Souza I., Poorkaj P.,
RA Kawai J., Tanimukai S., Yamamoto Y., Hasegawa H., Sasahara M., Hazama F.,
RA Schellenberg G.D., Tanaka C.;
RT "A mutation in the microtubule-associated protein tau in pallido-nigro-
RT luysian degeneration.";
RL Neurology 53:864-868(1999).
RN [63]
RP VARIANTS PSNP1 ASN-285 AND ALA-289.
RX PubMed=10534245; DOI=10.1212/wnl.53.7.1421;
RA Higgins J.J., Adler R.L., Loveless J.M.;
RT "Mutational analysis of the tau gene in progressive supranuclear palsy.";
RL Neurology 53:1421-1424(1999).
RN [64]
RP VARIANT FTD ASN-622.
RX PubMed=10208578; DOI=10.1097/00001756-199902250-00010;
RA Iijima M., Tabira T., Poorkaj P., Schellenberg G.D., Trojanowski J.Q.,
RA Lee V.M.-Y., Schmidt M.L., Takahashi K., Nabika T., Matsumoto T.,
RA Yamashita Y., Yoshioka S., Ishino H.;
RT "A distinct familial presenile dementia with a novel missense mutation in
RT the tau gene.";
RL NeuroReport 10:497-501(1999).
RN [65]
RP VARIANT FTD VAL-659.
RX PubMed=11117541;
RX DOI=10.1002/1531-8249(200012)48:6<850::aid-ana5>3.0.co;2-v;
RA Lippa C.F., Zhukareva V., Kawarai T., Uryu K., Shafiq M., Nee L.E.,
RA Grafman J., Liang Y., St George-Hyslop P.H., Trojanowski J.Q., Lee V.M.-Y.;
RT "Frontotemporal dementia with novel tau pathology and a Glu342Val tau
RT mutation.";
RL Ann. Neurol. 48:850-858(2000).
RN [66]
RP VARIANTS PIDB THR-574 AND ARG-706, AND CHARACTERIZATION OF VARIANTS PIDB
RP THR-574 AND ARG-706.
RX PubMed=11117542;
RX DOI=10.1002/1531-8249(200012)48:6<859::aid-ana6>3.0.co;2-1;
RA Pickering-Brown S., Baker M., Yen S.-H., Liu W.-K., Hasegawa M., Cairns N.,
RA Lantos P.L., Rossor M., Iwatsubo T., Davies Y., Allsop D., Furlong R.,
RA Owen F., Hardy J., Mann D., Hutton M.;
RT "Pick's disease is associated with mutations in the tau gene.";
RL Ann. Neurol. 48:859-867(2000).
RN [67]
RP VARIANT PIDB THR-574.
RX PubMed=11089577; DOI=10.1093/jnen/59.11.990;
RA Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R.,
RA Xuereb J.H., Crowther R.A., Spillantini M.G.;
RT "Tau gene mutation K257T causes a tauopathy similar to Pick's disease.";
RL J. Neuropathol. Exp. Neurol. 59:990-1001(2000).
RN [68]
RP VARIANT FTD LYS-596.
RX PubMed=10802785; DOI=10.1212/wnl.54.9.1787;
RA Arima K., Kowalska A., Hasegawa M., Mukoyama M., Watanabe R., Kawai M.,
RA Takahashi K., Iwatsubo T., Tabira T., Sunohara N.;
RT "Two brothers with frontotemporal dementia and parkinsonism with an N279K
RT mutation of the tau gene.";
RL Neurology 54:1787-1795(2000).
RN [69]
RP VARIANT FTD SER-618.
RX PubMed=11071507; DOI=10.1212/wnl.55.8.1224;
RA Yasuda M., Yokoyama K., Nakayasu T., Nishimura Y., Matsui M., Yokoyama T.,
RA Miyoshi K., Tanaka C.;
RT "A Japanese patient with frontotemporal dementia and parkinsonism by a tau
RT P301S mutation.";
RL Neurology 55:1224-1227(2000).
RN [70]
RP VARIANT FTD HIS-613.
RX PubMed=11585254; DOI=10.1007/s004010000333;
RA Iseki E., Matsumura T., Marui W., Hino H., Odawara T., Sugiyama N.,
RA Suzuki K., Sawada H., Arai T., Kosaka K.;
RT "Familial frontotemporal dementia and parkinsonism with a novel N296H
RT mutation in exon 10 of the tau gene and a widespread tau accumulation in
RT the glial cells.";
RL Acta Neuropathol. 102:285-292(2001).
RN [71]
RP VARIANT PSNP1 ASN-613 DEL.
RX PubMed=11220749;
RX DOI=10.1002/1531-8249(20010201)49:2<263::aid-ana50>3.0.co;2-k;
RA Pastor P., Pastor E., Carnero C., Vela R., Garcia T., Amer G., Tolosa E.,
RA Oliva R.;
RT "Familial atypical progressive supranuclear palsy associated with
RT homozygosity for the delN296 mutation in the tau gene.";
RL Ann. Neurol. 49:263-267(2001).
RN [72]
RP VARIANT PIDB ILE-686, AND CHARACTERIZATION OF VARIANT PIDB ILE-686.
RX PubMed=11601501; DOI=10.1002/ana.1223;
RA Neumann M., Schulz-Schaeffer W., Crowther R.A., Smith M.J.,
RA Spillantini M.G., Goedert M., Kretzschmar H.A.;
RT "Pick's disease associated with the novel Tau gene mutation K369I.";
RL Ann. Neurol. 50:503-513(2001).
RN [73]
RP CHARACTERIZATION OF VARIANT FTD TRP-723.
RX PubMed=11278002; DOI=10.1016/s0014-5793(01)02267-0;
RA Connell J.W., Gibb G.M., Betts J.C., Blackstock W.P., Gallo J.-M.,
RA Lovestone S., Hutton M., Anderton B.H.;
RT "Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by
RT glycogen synthase kinase 3beta identified by mass spectrometry demonstrate
RT certain mutations exert long-range conformational changes.";
RL FEBS Lett. 493:40-44(2001).
RN [74]
RP VARIANT FTD LYS-596.
RX PubMed=12473774; DOI=10.1212/01.wnl.0000038909.49164.4b;
RA Tsuboi Y., Baker M., Hutton M.L., Uitti R.J., Rascol O., Delisle M.-B.,
RA Soulages X., Murrell J.R., Ghetti B., Yasuda M., Komure O., Kuno S.,
RA Arima K., Sunohara N., Kobayashi T., Mizuno Y., Wszolek Z.K.;
RT "Clinical and genetic studies of families with the tau N279K mutation
RT (FTDP-17).";
RL Neurology 59:1791-1793(2002).
RN [75]
RP VARIANT PIDB PHE-637, AND CHARACTERIZATION OF VARIANT PIDB PHE-637.
RX PubMed=11891833; DOI=10.1002/ana.10140;
RA Rosso S.M., Van Herpen E., Deelen W., Kamphorst W., Severijnen L.-A.,
RA Willemsen R., Ravid R., Niermeijer M.F., Dooijes D., Smith M.J.,
RA Goedert M., Heutink P., Van Swieten J.C.;
RT "A novel tau mutation, S320F, causes a tauopathy with inclusions similar to
RT those in Pick's disease.";
RL Ann. Neurol. 51:373-376(2002).
RN [76]
RP VARIANT FTD HIS-5, AND CHARACTERIZATION OF VARIANT FTD HIS-5.
RX PubMed=11921059; DOI=10.1002/ana.10163;
RA Hayashi S., Toyoshima Y., Hasegawa M., Umeda Y., Wakabayashi K.,
RA Tokiguchi S., Iwatsubo T., Takahashi H.;
RT "Late-onset frontotemporal dementia with a novel exon 1 (Arg5His) tau gene
RT mutation.";
RL Ann. Neurol. 51:525-530(2002).
RN [77]
RP VARIANT PSNP1 LEU-5, AND CHARACTERIZATION OF VARIANT PSNP1 LEU-5.
RX PubMed=12325083; DOI=10.1002/ana.10340;
RA Poorkaj P., Muma N.A., Zhukareva V., Cochran E.J., Shannon K.M., Hurtig H.,
RA Koller W.C., Bird T.D., Trojanowski J.Q., Lee V.M.-Y., Schellenberg G.D.;
RT "An R5L tau mutation in a subject with a progressive supranuclear palsy
RT phenotype.";
RL Ann. Neurol. 52:511-516(2002).
RN [78]
RP CHARACTERIZATION OF VARIANTS FTD ASN-613 DEL AND HIS-613.
RX PubMed=11906000; DOI=10.1046/j.0022-3042.2001.00729.x;
RA Yoshida H., Crowther R.A., Goedert M.;
RT "Functional effects of tau gene mutations deltaN296 and N296H.";
RL J. Neurochem. 80:548-551(2002).
RN [79]
RP VARIANT FTD TRP-723.
RX PubMed=11889249; DOI=10.1212/wnl.58.5.811;
RA Saito Y., Geyer A., Sasaki R., Kuzuhara S., Nanba E., Miyasaka T.,
RA Suzuki K., Murayama S.;
RT "Early-onset, rapidly progressive familial tauopathy with R406W mutation.";
RL Neurology 58:811-813(2002).
RN [80]
RP VARIANT FTD VAL-583, AND CHARACTERIZATION OF VARIANT FTD VAL-583.
RX PubMed=12509859; DOI=10.1002/ana.10447;
RA Kobayashi T., Ota S., Tanaka K., Ito Y., Hasegawa M., Umeda Y., Motoi Y.,
RA Takanashi M., Yasuhara M., Anno M., Mizuno Y., Mori H.;
RT "A novel L266V mutation of the tau gene causes frontotemporal dementia with
RT a unique tau pathology.";
RL Ann. Neurol. 53:133-137(2003).
RN [81]
RP VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669, AND CHARACTERIZATION OF
RP VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669.
RX PubMed=14595660; DOI=10.1002/ana.10747;
RA Nicholl D.J., Greenstone M.A., Clarke C.E., Rizzu P., Crooks D., Crowe A.,
RA Trojanowski J.Q., Lee V.M.-Y., Heutink P.;
RT "An English kindred with a novel recessive tauopathy and respiratory
RT failure.";
RL Ann. Neurol. 54:682-686(2003).
RN [82]
RP VARIANT FTD/ALZHEIMER DISEASE TRP-723, AND INVOLVEMENT IN ALZHEIMER
RP DISEASE.
RX PubMed=14517953; DOI=10.1002/humu.10269;
RA Rademakers R., Dermaut B., Peeters K., Cruts M., Heutink P., Goate A.,
RA Van Broeckhoven C.;
RT "Tau (MAPT) mutation arg406trp presenting clinically with Alzheimer disease
RT does not share a common founder in western Europe.";
RL Hum. Mutat. 22:409-411(2003).
RN [83]
RP VARIANT ATYPICAL PSNP1 ASN-613 DEL.
RX PubMed=14991829; DOI=10.1002/ana.20006;
RA Rossi G., Gasparoli E., Pasquali C., Di Fede G., Testa D., Albanese A.,
RA Bracco F., Tagliavini F.;
RT "Progressive supranuclear palsy and Parkinson's disease in a family with a
RT new mutation in the tau gene.";
RL Ann. Neurol. 55:448-448(2004).
RN [84]
RP VARIANT PSNP1/ATYPICAL PSNP1 ASN-613 DEL.
RX PubMed=14991828; DOI=10.1002/ana.20025;
RA Oliva R., Pastor P.;
RT "Tau gene delN296 mutation, Parkinson's disease, and atypical supranuclear
RT palsy.";
RL Ann. Neurol. 55:448-449(2004).
RN [85]
RP VARIANT FTD SER-618.
RX PubMed=16240366; DOI=10.1002/ana.20668;
RA Yasuda M., Nakamura Y., Kawamata T., Kaneyuki H., Maeda K., Komure O.;
RT "Phenotypic heterogeneity within a new family with the MAPT P301S
RT mutation.";
RL Ann. Neurol. 58:920-928(2005).
RN [86]
RP VARIANT PSNP1 VAL-620.
RX PubMed=16157753; DOI=10.1001/archneur.62.9.1444;
RA Ros R., Thobois S., Streichenberger N., Kopp N., Sanchez M.P., Perez M.,
RA Hoenicka J., Avila J., Honnorat J., de Yebenes J.G.;
RT "A new mutation of the tau gene, G303V, in early-onset familial progressive
RT supranuclear palsy.";
RL Arch. Neurol. 62:1444-1450(2005).
RN [87]
RP VARIANT FTD MET-634.
RX PubMed=15883319; DOI=10.1212/01.wnl.0000160116.65034.12;
RA Zarranz J.J., Ferrer I., Lezcano E., Forcadas M.I., Eizaguirre B.,
RA Atares B., Puig B., Gomez-Esteban J.C., Fernandez-Maiztegui C., Rouco I.,
RA Perez-Concha T., Fernandez M., Rodriguez O., Rodriguez-Martinez A.B.,
RA de Pancorbo M.M., Pastor P., Perez-Tur J.;
RT "A novel mutation (K317M) in the MAPT gene causes FTDP and motor neuron
RT disease.";
RL Neurology 64:1578-1585(2005).
RN [88]
RP VARIANTS MET-17; ALA-30 AND ILE-617.
RX PubMed=20020531; DOI=10.1002/humu.21152;
RA Guerreiro R.J., Washecka N., Hardy J., Singleton A.;
RT "A thorough assessment of benign genetic variability in GRN and MAPT.";
RL Hum. Mutat. 31:E1126-E1140(2010).
RN [89]
RP VARIANT FTD/ALZHEIMER DISEASE TRP-723.
RX PubMed=26086902; DOI=10.1016/j.gene.2015.06.033;
RA Behnam M., Ghorbani F., Shin J.H., Kim D.S., Jang H., Nouri N., Sedghi M.,
RA Salehi M., Ansari B., Basiri K.;
RT "Homozygous MAPT R406W mutation causing FTDP phenotype: A unique instance
RT of a unique mutation.";
RL Gene 570:150-152(2015).
RN [90]
RP VARIANT FTD ARG-590, CHARACTERIZATION OF VARIANT FTD ARG-590, AND FUNCTION.
RX PubMed=32961270; DOI=10.1016/j.nbd.2020.105079;
RA Sandberg A., Ling H., Gearing M., Dombroski B., Cantwell L., R'Bibo L.,
RA Levey A., Schellenberg G.D., Hardy J., Wood N., Fernius J., Nystroem S.,
RA Svensson S., Thor S., Hammarstroem P., Revesz T., Mok K.Y.;
RT "Fibrillation and molecular characteristics are coherent with clinical and
RT pathological features of 4-repeat tauopathy caused by MAPT variant G273R.";
RL Neurobiol. Dis. 146:105079-105079(2020).
CC -!- FUNCTION: Promotes microtubule assembly and stability, and might be
CC involved in the establishment and maintenance of neuronal polarity
CC (PubMed:21985311). The C-terminus binds axonal microtubules while the
CC N-terminus binds neural plasma membrane components, suggesting that tau
CC functions as a linker protein between both (PubMed:21985311,
CC PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT
CC localization (in the neuronal cell) in the domain of the cell body
CC defined by the centrosome. The short isoforms allow plasticity of the
CC cytoskeleton whereas the longer isoforms may preferentially play a role
CC in its stabilization. {ECO:0000269|PubMed:21985311,
CC ECO:0000269|PubMed:32961270}.
CC -!- SUBUNIT: Interacts with MARK1, MARK2, MARK3 AND MARK4
CC (PubMed:23666762). Interacts with PSMC2 through SQSTM1 (By similarity).
CC Interacts with SQSTM1 when polyubiquitinated (PubMed:15953362).
CC Interacts with FKBP4 (By similarity). Binds to CSNK1D
CC (PubMed:14761950). Interacts with SGK1 (PubMed:16982696). Interacts
CC with EPM2A; the interaction dephosphorylates MAPT at Ser-396
CC (PubMed:19542233). Interacts with PIN1 (PubMed:11313338). Interacts
CC with LRRK2 (PubMed:26014385). Interacts with LRP1, leading to
CC endocytosis; this interaction is reduced in the presence of LRPAP1/RAP
CC (PubMed:32296178). {ECO:0000250|UniProtKB:P10637,
CC ECO:0000250|UniProtKB:P19332, ECO:0000269|PubMed:11313338,
CC ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15953362,
CC ECO:0000269|PubMed:16982696, ECO:0000269|PubMed:19542233,
CC ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:26014385,
CC ECO:0000269|PubMed:32296178}.
CC -!- INTERACTION:
CC P10636; P31749: AKT1; NbExp=2; IntAct=EBI-366182, EBI-296087;
CC P10636; PRO_0000001987 [P02649]: APOE; NbExp=3; IntAct=EBI-366182, EBI-9209835;
CC P10636; P05067: APP; NbExp=8; IntAct=EBI-366182, EBI-77613;
CC P10636; PRO_0000000092 [P05067]: APP; NbExp=5; IntAct=EBI-366182, EBI-821758;
CC P10636; Q9HC96: CAPN10; NbExp=3; IntAct=EBI-366182, EBI-3915761;
CC P10636; Q9NR30: DDX21; NbExp=3; IntAct=EBI-366182, EBI-357942;
CC P10636; Q92608-2: DOCK2; NbExp=3; IntAct=EBI-366182, EBI-25875570;
CC P10636; P06241: FYN; NbExp=3; IntAct=EBI-366182, EBI-515315;
CC P10636; P49841: GSK3B; NbExp=4; IntAct=EBI-366182, EBI-373586;
CC P10636; P11142: HSPA8; NbExp=5; IntAct=EBI-366182, EBI-351896;
CC P10636; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-366182, EBI-10274069;
CC P10636; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-366182, EBI-726739;
CC P10636; P10636: MAPT; NbExp=3; IntAct=EBI-366182, EBI-366182;
CC P10636; P04156: PRNP; NbExp=2; IntAct=EBI-366182, EBI-977302;
CC P10636; P46779: RPL28; NbExp=4; IntAct=EBI-366182, EBI-366357;
CC P10636; P43004: SLC1A2; NbExp=4; IntAct=EBI-366182, EBI-3440986;
CC P10636; Q9UNE7: STUB1; NbExp=2; IntAct=EBI-366182, EBI-357085;
CC P10636; Q9UNE7-1: STUB1; NbExp=5; IntAct=EBI-366182, EBI-15687717;
CC P10636; O15195-2: VILL; NbExp=3; IntAct=EBI-366182, EBI-21845957;
CC P10636; P63104: YWHAZ; NbExp=8; IntAct=EBI-366182, EBI-347088;
CC P10636; Q9C0A1: ZFHX2; NbExp=3; IntAct=EBI-366182, EBI-25850811;
CC P10636-2; P06241: FYN; NbExp=2; IntAct=EBI-7796412, EBI-515315;
CC P10636-2; Q5S007: LRRK2; NbExp=3; IntAct=EBI-7796412, EBI-5323863;
CC P10636-2; P31947: SFN; NbExp=2; IntAct=EBI-7796412, EBI-476295;
CC P10636-2; P63104: YWHAZ; NbExp=2; IntAct=EBI-7796412, EBI-347088;
CC P10636-3; P63104: YWHAZ; NbExp=9; IntAct=EBI-7145070, EBI-347088;
CC P10636-5; P06241: FYN; NbExp=2; IntAct=EBI-21313635, EBI-515315;
CC P10636-6; P02649: APOE; NbExp=3; IntAct=EBI-7796455, EBI-1222467;
CC P10636-6; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-7796455, EBI-25840379;
CC P10636-6; Q92608-2: DOCK2; NbExp=3; IntAct=EBI-7796455, EBI-25875570;
CC P10636-6; P06241: FYN; NbExp=3; IntAct=EBI-7796455, EBI-515315;
CC P10636-6; P11142: HSPA8; NbExp=3; IntAct=EBI-7796455, EBI-351896;
CC P10636-6; O60260-5: PRKN; NbExp=3; IntAct=EBI-7796455, EBI-21251460;
CC P10636-6; P37840: SNCA; NbExp=3; IntAct=EBI-7796455, EBI-985879;
CC P10636-6; Q9C0A1: ZFHX2; NbExp=3; IntAct=EBI-7796455, EBI-25850811;
CC P10636-7; O00499-1: BIN1; NbExp=5; IntAct=EBI-6926270, EBI-6926280;
CC P10636-8; P07355: ANXA2; NbExp=7; IntAct=EBI-366233, EBI-352622;
CC P10636-8; P08133: ANXA6; NbExp=2; IntAct=EBI-366233, EBI-352541;
CC P10636-8; O00499-1: BIN1; NbExp=6; IntAct=EBI-366233, EBI-6926280;
CC P10636-8; Q14203: DCTN1; NbExp=9; IntAct=EBI-366233, EBI-724352;
CC P10636-8; P26196: DDX6; NbExp=7; IntAct=EBI-366233, EBI-351257;
CC P10636-8; Q13451: FKBP5; NbExp=8; IntAct=EBI-366233, EBI-306914;
CC P10636-8; P06241: FYN; NbExp=9; IntAct=EBI-366233, EBI-515315;
CC P10636-8; P49841: GSK3B; NbExp=9; IntAct=EBI-366233, EBI-373586;
CC P10636-8; P08238: HSP90AB1; NbExp=11; IntAct=EBI-366233, EBI-352572;
CC P10636-8; Q92743: HTRA1; NbExp=6; IntAct=EBI-366233, EBI-352256;
CC P10636-8; Q5S007: LRRK2; NbExp=9; IntAct=EBI-366233, EBI-5323863;
CC P10636-8; P10636-8: MAPT; NbExp=6; IntAct=EBI-366233, EBI-366233;
CC P10636-8; O43347: MSI1; NbExp=2; IntAct=EBI-366233, EBI-726515;
CC P10636-8; Q96DH6: MSI2; NbExp=2; IntAct=EBI-366233, EBI-2462339;
CC P10636-8; P37840: SNCA; NbExp=3; IntAct=EBI-366233, EBI-985879;
CC P10636-8; Q71U36: TUBA1A; NbExp=4; IntAct=EBI-366233, EBI-302552;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10747907,
CC ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:26014385}. Cell
CC membrane {ECO:0000269|PubMed:10747907}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10747907}; Cytoplasmic side
CC {ECO:0000269|PubMed:10747907}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10747907}. Cell projection, axon
CC {ECO:0000269|PubMed:10747907}. Cell projection, dendrite
CC {ECO:0000269|PubMed:23666762}. Secreted {ECO:0000269|PubMed:32272059}.
CC Note=Mostly found in the axons of neurons, in the cytosol and in
CC association with plasma membrane components (PubMed:10747907). Can be
CC secreted; the secretion is dependent on protein unfolding and
CC facilitated by the cargo receptor TMED10; it results in protein
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) followed by vesicle entry and secretion
CC (PubMed:32272059). {ECO:0000269|PubMed:10747907,
CC ECO:0000269|PubMed:32272059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=Additional isoforms seem to exist. Isoforms differ from each
CC other by the presence or absence of up to 5 of the 15 exons. One of
CC these optional exons contains the additional tau/MAP repeat.;
CC Name=PNS-tau;
CC IsoId=P10636-1; Sequence=Displayed;
CC Name=Fetal-tau; Synonyms=0N3R {ECO:0000303|PubMed:9789048};
CC IsoId=P10636-2; Sequence=VSP_003176, VSP_003177, VSP_003179,
CC VSP_003180, VSP_003181;
CC Name=Tau-A;
CC IsoId=P10636-3; Sequence=VSP_003175, VSP_003176, VSP_003177,
CC VSP_003178, VSP_003179, VSP_003180,
CC VSP_003181;
CC Name=Tau-B; Synonyms=1N3R {ECO:0000303|PubMed:9789048};
CC IsoId=P10636-4; Sequence=VSP_003177, VSP_003179, VSP_003180,
CC VSP_003181;
CC Name=Tau-C; Synonyms=Tau-3, 2N3R {ECO:0000303|PubMed:9789048};
CC IsoId=P10636-5; Sequence=VSP_003179, VSP_003180, VSP_003181;
CC Name=Tau-D; Synonyms=0N4R {ECO:0000303|PubMed:9789048};
CC IsoId=P10636-6; Sequence=VSP_003176, VSP_003177, VSP_003179,
CC VSP_003180;
CC Name=Tau-E; Synonyms=1N4R {ECO:0000303|PubMed:9789048};
CC IsoId=P10636-7; Sequence=VSP_003177, VSP_003179, VSP_003180;
CC Name=Tau-F; Synonyms=Tau-4, 2N4R {ECO:0000303|PubMed:9789048};
CC IsoId=P10636-8; Sequence=VSP_003179, VSP_003180;
CC Name=Tau-G;
CC IsoId=P10636-9; Sequence=VSP_026780;
CC -!- TISSUE SPECIFICITY: Expressed in neurons. Isoform PNS-tau is expressed
CC in the peripheral nervous system while the others are expressed in the
CC central nervous system.
CC -!- DEVELOPMENTAL STAGE: Four-repeat (type II) TAU/MAPT is expressed in an
CC adult-specific manner and is not found in fetal brain, whereas three-
CC repeat (type I) TAU/MAPT is found in both adult and fetal brain.
CC -!- DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms contain 3
CC repeats while type II isoforms contain 4 repeats.
CC -!- PTM: Phosphorylation at serine and threonine residues in S-P or T-P
CC motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3,
CC MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in
CC mitosis, and in the form associated with paired helical filaments (PHF-
CC tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule
CC affinity-regulating kinase (MARK1, MARK2, MARK3 or MARK4), causing
CC detachment from microtubules, and their disassembly (PubMed:7706316,
CC PubMed:23666762). Phosphorylation decreases with age. Phosphorylation
CC within tau/MAP's repeat domain or in flanking regions seems to reduce
CC tau/MAP's interaction with, respectively, microtubules or plasma
CC membrane components (PubMed:7706316). Phosphorylation on Ser-610, Ser-
CC 622, Ser-641 and Ser-673 in several isoforms during mitosis.
CC Phosphorylation at Ser-548 by GSK3B reduces ability to bind and
CC stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2
CC in neurons affects ability to bind microtubules and plays a role in
CC neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-
CC 606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates
CC microtubule depolymerization and neurite formation in hippocampal
CC neurons. There is a reciprocal down-regulation of phosphorylation and
CC O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-
CC GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-
CC 721 reduces glycosylation by a factor of 2 and 4 respectively.
CC Phosphorylation on Ser-721 is reduced by about 41.5% by GlcNAcylation
CC on Ser-717. Dephosphorylated at several serine and threonine residues
CC by the serine/threonine phosphatase PPP5C.
CC {ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:14761950,
CC ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603,
CC ECO:0000269|PubMed:16982696, ECO:0000269|PubMed:19451179,
CC ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:21985311,
CC ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:7706316,
CC ECO:0000269|PubMed:8999860, ECO:0000269|PubMed:9614189}.
CC -!- PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke
CC SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau
CC can be modified by three different forms of polyubiquitination. 'Lys-
CC 48'-linked polyubiquitination is the major form, 'Lys-6'-linked and
CC 'Lys-11'-linked polyubiquitination also occur. {ECO:0000250,
CC ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16443603}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation content is around 8.2%. There is
CC reciprocal down-regulation of phosphorylation and O-GlcNAcylation.
CC Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on
CC this site, while phosphorylation on Ser-713 and Ser-721 reduces O-
CC GlcNAcylation by a factor of 2 and 4 respectively. O-GlcNAcylation on
CC Ser-717 decreases the phosphorylation on Ser-721 by about 41.5%.
CC {ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861,
CC ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179,
CC ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189}.
CC -!- PTM: Glycation of PHF-tau, but not normal brain TAU/MAPT. Glycation is
CC a non-enzymatic post-translational modification that involves a
CC covalent linkage between a sugar and an amino group of a protein
CC molecule forming ketoamine. Subsequent oxidation, fragmentation and/or
CC cross-linking of ketoamine leads to the production of advanced
CC glycation endproducts (AGES). Glycation may play a role in stabilizing
CC PHF aggregation leading to tangle formation in AD.
CC -!- DISEASE: Note=In Alzheimer disease, the neuronal cytoskeleton in the
CC brain is progressively disrupted and replaced by tangles of paired
CC helical filaments (PHF) and straight filaments, mainly composed of
CC hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). O-GlcNAcylation
CC is greatly reduced in Alzheimer disease brain cerebral cortex leading
CC to an increase in TAU/MAPT phosphorylations.
CC {ECO:0000269|PubMed:14517953, ECO:0000269|PubMed:26086902}.
CC -!- DISEASE: Frontotemporal dementia (FTD) [MIM:600274]: A form of dementia
CC characterized by pathologic finding of frontotemporal lobar
CC degeneration, presenile dementia with behavioral changes, deterioration
CC of cognitive capacities and loss of memory. In some cases, parkinsonian
CC symptoms are prominent. Neuropathological changes include
CC frontotemporal atrophy often associated with atrophy of the basal
CC ganglia, substantia nigra, amygdala. In most cases, protein tau
CC deposits are found in glial cells and/or neurons.
CC {ECO:0000269|PubMed:10208578, ECO:0000269|PubMed:10214944,
CC ECO:0000269|PubMed:10374757, ECO:0000269|PubMed:10489057,
CC ECO:0000269|PubMed:10553987, ECO:0000269|PubMed:10802785,
CC ECO:0000269|PubMed:11071507, ECO:0000269|PubMed:11117541,
CC ECO:0000269|PubMed:11278002, ECO:0000269|PubMed:11585254,
CC ECO:0000269|PubMed:11889249, ECO:0000269|PubMed:11906000,
CC ECO:0000269|PubMed:11921059, ECO:0000269|PubMed:12473774,
CC ECO:0000269|PubMed:12509859, ECO:0000269|PubMed:14517953,
CC ECO:0000269|PubMed:15883319, ECO:0000269|PubMed:16240366,
CC ECO:0000269|PubMed:26086902, ECO:0000269|PubMed:32961270,
CC ECO:0000269|PubMed:9629852, ECO:0000269|PubMed:9641683,
CC ECO:0000269|PubMed:9736786, ECO:0000269|PubMed:9789048,
CC ECO:0000269|PubMed:9973279}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pick disease of the brain (PIDB) [MIM:172700]: A rare form of
CC dementia pathologically defined by severe atrophy, neuronal loss and
CC gliosis. It is characterized by the occurrence of tau-positive
CC inclusions, swollen neurons (Pick cells) and argentophilic neuronal
CC inclusions known as Pick bodies that disproportionally affect the
CC frontal and temporal cortical regions. Clinical features include
CC aphasia, apraxia, confusion, anomia, memory loss and personality
CC deterioration. {ECO:0000269|PubMed:10604746,
CC ECO:0000269|PubMed:11089577, ECO:0000269|PubMed:11117542,
CC ECO:0000269|PubMed:11601501, ECO:0000269|PubMed:11891833}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Defects in MAPT are a cause of corticobasal degeneration
CC (CBD). It is marked by extrapyramidal signs and apraxia and can be
CC associated with memory loss. Neuropathologic features may overlap
CC Alzheimer disease, progressive supranuclear palsy, and Parkinson
CC disease.
CC -!- DISEASE: Progressive supranuclear palsy 1 (PSNP1) [MIM:601104]:
CC Characterized by akinetic-rigid syndrome, supranuclear gaze palsy,
CC pyramidal tract dysfunction, pseudobulbar signs and cognitive
CC capacities deterioration. Neurofibrillary tangles and gliosis but no
CC amyloid plaques are found in diseased brains. Most cases appear to be
CC sporadic, with a significant association with a common haplotype
CC including the MAPT gene and the flanking regions. Familial cases show
CC an autosomal dominant pattern of transmission with incomplete
CC penetrance; genetic analysis of a few cases showed the occurrence of
CC tau mutations, including a deletion of Asn-613.
CC {ECO:0000269|PubMed:10534245, ECO:0000269|PubMed:11220749,
CC ECO:0000269|PubMed:12325083, ECO:0000269|PubMed:14991828,
CC ECO:0000269|PubMed:14991829, ECO:0000269|PubMed:16157753}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Parkinson-dementia syndrome (PARDE) [MIM:260540]: A syndrome
CC characterized by parkinsonism, tremor, rigidity, dementia,
CC ophthalmoparesis and pyramidal signs. Neurofibrillary degeneration
CC occurs in the hippocampus, basal ganglia and brainstem nuclei. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Alzforum; Note=MAPT mutations;
CC URL="https://www.alzforum.org/mutations/search?genes%255B%255D=348";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Vita minima - Issue 68 of
CC March 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/068";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Tau protein entry;
CC URL="https://en.wikipedia.org/wiki/Tau_protein";
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DR EMBL; J03778; AAA60615.1; -; mRNA.
DR EMBL; X14474; CAA32636.1; -; mRNA.
DR EMBL; AF047863; AAC04277.1; -; Genomic_DNA.
DR EMBL; AF027491; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF047856; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF047857; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF027492; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF047858; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF027493; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF047859; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF047860; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF047862; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF027494; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF027495; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF027496; AAC04277.1; JOINED; Genomic_DNA.
DR EMBL; AF027491; AAC04278.1; -; Genomic_DNA.
DR EMBL; AF027492; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF027493; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF047860; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF047862; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF027495; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF027496; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF047863; AAC04278.1; JOINED; Genomic_DNA.
DR EMBL; AF027491; AAC04279.1; -; Genomic_DNA.
DR EMBL; AF047856; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF047857; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF027492; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF027493; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF047860; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF047862; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF027494; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF027495; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF027496; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF047863; AAC04279.1; JOINED; Genomic_DNA.
DR EMBL; AF047861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY730549; AAU45390.1; -; mRNA.
DR EMBL; BT006772; AAP35418.1; -; mRNA.
DR EMBL; AC004139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000558; AAH00558.1; -; mRNA.
DR EMBL; BC098281; AAH98281.1; -; mRNA.
DR EMBL; BC099721; AAH99721.1; -; mRNA.
DR EMBL; BC101936; AAI01937.1; -; mRNA.
DR EMBL; BC114504; AAI14505.1; -; mRNA.
DR EMBL; BC114948; AAI14949.1; -; mRNA.
DR EMBL; AY526356; AAS17881.1; -; mRNA.
DR EMBL; M25298; AAA57264.1; -; mRNA.
DR EMBL; BN000503; CAG26750.1; -; mRNA.
DR CCDS; CCDS11499.1; -. [P10636-8]
DR CCDS; CCDS11500.1; -. [P10636-6]
DR CCDS; CCDS11501.1; -. [P10636-1]
DR CCDS; CCDS11502.1; -. [P10636-2]
DR CCDS; CCDS45715.1; -. [P10636-9]
DR CCDS; CCDS45716.1; -. [P10636-7]
DR CCDS; CCDS56033.1; -. [P10636-5]
DR PIR; I52232; I52232.
DR PIR; JS0370; QRHUT1.
DR PIR; PN0001; QRHUT2.
DR PIR; S26663; S26663.
DR RefSeq; NP_001116538.2; NM_001123066.3. [P10636-9]
DR RefSeq; NP_001116539.1; NM_001123067.3. [P10636-7]
DR RefSeq; NP_001190181.1; NM_001203252.1. [P10636-5]
DR RefSeq; NP_005901.2; NM_005910.5. [P10636-8]
DR RefSeq; NP_058518.1; NM_016834.4. [P10636-6]
DR RefSeq; NP_058519.3; NM_016835.4. [P10636-1]
DR RefSeq; NP_058525.1; NM_016841.4. [P10636-2]
DR PDB; 1I8H; NMR; -; A=542-554.
DR PDB; 2MZ7; NMR; -; A=584-629.
DR PDB; 2ON9; X-ray; 1.51 A; A/B=623-628.
DR PDB; 3OVL; X-ray; 1.81 A; A=623-628.
DR PDB; 4E0M; X-ray; 1.75 A; A/B/C/D=622-634.
DR PDB; 4E0N; X-ray; 1.65 A; A/B/C/D=622-634.
DR PDB; 4E0O; X-ray; 1.82 A; A/B/C/D=622-634.
DR PDB; 4FL5; X-ray; 1.90 A; P/Q=527-536.
DR PDB; 4GLR; X-ray; 1.90 A; A/B=541-557.
DR PDB; 4NP8; X-ray; 1.51 A; A=623-628.
DR PDB; 4TQE; X-ray; 1.60 A; A=532-547.
DR PDB; 4Y32; X-ray; 1.70 A; C/D=528-534.
DR PDB; 4Y3B; X-ray; 1.80 A; C/D=528-534.
DR PDB; 4Y5I; X-ray; 1.40 A; F/G=528-534.
DR PDB; 5DMG; X-ray; 2.50 A; P/X/Z=733-747.
DR PDB; 5E2V; X-ray; 1.64 A; P=511-528.
DR PDB; 5E2W; X-ray; 1.50 A; P=511-528.
DR PDB; 5HF3; X-ray; 1.80 A; B=528-534.
DR PDB; 5K7N; EM; 1.10 A; Z=623-628.
DR PDB; 5MO3; X-ray; 1.69 A; A=615-628.
DR PDB; 5MP1; X-ray; 3.10 A; A/B/E/I=615-628.
DR PDB; 5MP3; X-ray; 2.75 A; C/D=609-638.
DR PDB; 5MP5; X-ray; 2.31 A; I/J/K=615-628.
DR PDB; 5N5A; NMR; -; A=571-607.
DR PDB; 5N5B; NMR; -; A=609-636.
DR PDB; 5NVB; NMR; -; A=571-585.
DR PDB; 5O3L; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J=623-695.
DR PDB; 5O3O; EM; 3.50 A; A/B/C/D/E/F/G/H/I/J=623-695.
DR PDB; 5O3T; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J=623-695.
DR PDB; 5V5B; EM; 1.50 A; A=591-600.
DR PDB; 5V5C; EM; 1.25 A; A=592-597.
DR PDB; 5ZIA; X-ray; 2.60 A; C/F/J/N/Q/R=552-560.
DR PDB; 5ZV3; X-ray; 2.09 A; A=52-71.
DR PDB; 6BB4; X-ray; 2.10 A; P/Q/R=703-725.
DR PDB; 6CVJ; EM; 3.20 A; D=514-717.
DR PDB; 6CVN; EM; 3.90 A; D=514-717.
DR PDB; 6DC8; X-ray; 1.80 A; P=696-725.
DR PDB; 6DC9; X-ray; 3.00 A; P/Q=696-725.
DR PDB; 6DCA; X-ray; 2.60 A; P/Q/R/S=696-725.
DR PDB; 6FBW; X-ray; 1.45 A; B/D=528-533.
DR PDB; 6FI5; X-ray; 1.70 A; B=529-533.
DR PDB; 6GK7; X-ray; 2.95 A; A=625-635.
DR PDB; 6GK8; X-ray; 2.85 A; I=52-71.
DR PDB; 6GX5; EM; 3.20 A; A/B/C=602-695.
DR PDB; 6H06; X-ray; 2.63 A; G/I/J/K=721-746.
DR PDB; 6HRE; EM; 3.20 A; A/B/C/D/E/F=1-758.
DR PDB; 6HRF; EM; 3.30 A; A/B/C/D/E/F=1-758.
DR PDB; 6LRA; X-ray; 1.90 A; C=592-597.
DR PDB; 6N4P; X-ray; 1.85 A; A/C=5-10.
DR PDB; 6NK4; EM; 1.99 A; A=591-599.
DR PDB; 6NWP; EM; 2.30 A; A/B/C/D/E/F=1-758.
DR PDB; 6NWQ; EM; 3.40 A; A/B/C/D/E/F=1-758.
DR PDB; 6ODG; X-ray; 1.00 A; A/B=622-627.
DR PDB; 6PXR; X-ray; 1.56 A; A=15-22.
DR PDB; 6QJH; EM; 3.30 A; A/B/C=589-647.
DR PDB; 6QJM; EM; 3.30 A; A/B/C=591-638.
DR PDB; 6QJP; EM; 3.50 A; A/B/C=591-638.
DR PDB; 6QJQ; EM; 3.70 A; A/B/C/D/E/F=620-647.
DR PDB; 6TJO; EM; 3.20 A; A/B/C=1-758.
DR PDB; 6TJX; EM; 3.00 A; A/B/C/D/E/F=1-758.
DR PDB; 6VH7; EM; 3.80 A; A/B/C/E/F/G=591-697.
DR PDB; 6VHA; EM; 4.30 A; E/F/G=591-697.
DR PDB; 6VHL; EM; 3.30 A; E/F=621-697.
DR PDB; 6VI3; EM; 3.30 A; E/F=621-697.
DR PDB; 6XLI; X-ray; 2.00 A; E/F/P=527-539.
DR PDB; 7MKF; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7MKG; EM; 3.07 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7MKH; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7NRQ; EM; 2.76 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7NRS; EM; 2.68 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7NRT; EM; 2.68 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7NRV; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7NRX; EM; 3.55 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7P65; EM; 2.70 A; A/B/C/D/E=1-758.
DR PDB; 7P66; EM; 3.00 A; A/B/C/D/E=1-758.
DR PDB; 7P67; EM; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7P68; EM; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7P6A; EM; 1.90 A; A/B/C/D/E=1-758.
DR PDB; 7P6B; EM; 2.20 A; A/B/C/D/E=1-758.
DR PDB; 7P6C; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J=1-758.
DR PDB; 7P6D; EM; 3.30 A; A/B/C/D/E=1-758.
DR PDB; 7P6E; EM; 3.40 A; A/B/C/D/E/F/I/J/Q/R=1-758.
DR PDB; 7PQC; EM; 4.10 A; O=519-712.
DR PDB; 7PQP; EM; 4.10 A; O=519-712.
DR PDB; 7QJV; EM; 3.29 A; A/B/C/D/E/F/G/H/I/J/K/L=1-758.
DR PDB; 7QJW; EM; 2.81 A; A/B/C/D/E/F=1-758.
DR PDB; 7QJX; EM; 2.99 A; A/B/C/D/E/F/G/H/I/J/K/L=1-758.
DR PDB; 7QJY; EM; 3.14 A; A/B/C/D/E/F=1-758.
DR PDB; 7QJZ; EM; 3.40 A; A/B/C/D/E/F=1-758.
DR PDB; 7QK1; EM; 3.03 A; A/B/C/D/E/F=1-758.
DR PDB; 7QK2; EM; 2.61 A; A/B/C/D/E/F=1-758.
DR PDB; 7QK3; EM; 2.44 A; A/B/C=1-758.
DR PDB; 7QK5; EM; 1.92 A; A/B/C/D/E/F/G/H/K=1-758.
DR PDB; 7QK6; EM; 2.27 A; A/B/C=1-758.
DR PDB; 7QKF; EM; 2.83 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKG; EM; 3.36 A; A/B/C=1-758.
DR PDB; 7QKH; EM; 3.17 A; A/B/C/D/E/G=1-758.
DR PDB; 7QKI; EM; 3.13 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKJ; EM; 3.26 A; A/B/C/D/E/F/G/H/I/J/K/L=1-758.
DR PDB; 7QKK; EM; 2.80 A; A/B/C=1-758.
DR PDB; 7QKL; EM; 2.07 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKM; EM; 2.66 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKU; EM; 2.57 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKV; EM; 3.23 A; A/B/C/D/E/F/G/H/I=1-758.
DR PDB; 7QKW; EM; 2.32 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKX; EM; 3.16 A; A/B/C/D/E/G=1-758.
DR PDB; 7QKY; EM; 1.86 A; A/B/C/D/E/F=1-758.
DR PDB; 7QKZ; EM; 2.65 A; A/B/C/D/E/F/G/H/I=1-758.
DR PDB; 7QL0; EM; 3.13 A; A/B/C/D/E/c=1-758.
DR PDB; 7QL1; EM; 3.34 A; A/C/D=1-758.
DR PDB; 7QL2; EM; 2.95 A; A/B/C=1-758.
DR PDB; 7QL3; EM; 3.32 A; A/B/C/D/E/F=1-758.
DR PDB; 7QL4; EM; 3.20 A; A/B/C/D/E/F=1-758.
DR PDB; 7R4T; EM; 2.75 A; A/B/C/D/E/F=1-758.
DR PDB; 7R5H; EM; 2.59 A; A/B/C/D/E/F=1-758.
DR PDB; 7SP1; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-758.
DR PDB; 7U0Z; EM; 4.20 A; A/B/C=589-698.
DR PDBsum; 1I8H; -.
DR PDBsum; 2MZ7; -.
DR PDBsum; 2ON9; -.
DR PDBsum; 3OVL; -.
DR PDBsum; 4E0M; -.
DR PDBsum; 4E0N; -.
DR PDBsum; 4E0O; -.
DR PDBsum; 4FL5; -.
DR PDBsum; 4GLR; -.
DR PDBsum; 4NP8; -.
DR PDBsum; 4TQE; -.
DR PDBsum; 4Y32; -.
DR PDBsum; 4Y3B; -.
DR PDBsum; 4Y5I; -.
DR PDBsum; 5DMG; -.
DR PDBsum; 5E2V; -.
DR PDBsum; 5E2W; -.
DR PDBsum; 5HF3; -.
DR PDBsum; 5K7N; -.
DR PDBsum; 5MO3; -.
DR PDBsum; 5MP1; -.
DR PDBsum; 5MP3; -.
DR PDBsum; 5MP5; -.
DR PDBsum; 5N5A; -.
DR PDBsum; 5N5B; -.
DR PDBsum; 5NVB; -.
DR PDBsum; 5O3L; -.
DR PDBsum; 5O3O; -.
DR PDBsum; 5O3T; -.
DR PDBsum; 5V5B; -.
DR PDBsum; 5V5C; -.
DR PDBsum; 5ZIA; -.
DR PDBsum; 5ZV3; -.
DR PDBsum; 6BB4; -.
DR PDBsum; 6CVJ; -.
DR PDBsum; 6CVN; -.
DR PDBsum; 6DC8; -.
DR PDBsum; 6DC9; -.
DR PDBsum; 6DCA; -.
DR PDBsum; 6FBW; -.
DR PDBsum; 6FI5; -.
DR PDBsum; 6GK7; -.
DR PDBsum; 6GK8; -.
DR PDBsum; 6GX5; -.
DR PDBsum; 6H06; -.
DR PDBsum; 6HRE; -.
DR PDBsum; 6HRF; -.
DR PDBsum; 6LRA; -.
DR PDBsum; 6N4P; -.
DR PDBsum; 6NK4; -.
DR PDBsum; 6NWP; -.
DR PDBsum; 6NWQ; -.
DR PDBsum; 6ODG; -.
DR PDBsum; 6PXR; -.
DR PDBsum; 6QJH; -.
DR PDBsum; 6QJM; -.
DR PDBsum; 6QJP; -.
DR PDBsum; 6QJQ; -.
DR PDBsum; 6TJO; -.
DR PDBsum; 6TJX; -.
DR PDBsum; 6VH7; -.
DR PDBsum; 6VHA; -.
DR PDBsum; 6VHL; -.
DR PDBsum; 6VI3; -.
DR PDBsum; 6XLI; -.
DR PDBsum; 7MKF; -.
DR PDBsum; 7MKG; -.
DR PDBsum; 7MKH; -.
DR PDBsum; 7NRQ; -.
DR PDBsum; 7NRS; -.
DR PDBsum; 7NRT; -.
DR PDBsum; 7NRV; -.
DR PDBsum; 7NRX; -.
DR PDBsum; 7P65; -.
DR PDBsum; 7P66; -.
DR PDBsum; 7P67; -.
DR PDBsum; 7P68; -.
DR PDBsum; 7P6A; -.
DR PDBsum; 7P6B; -.
DR PDBsum; 7P6C; -.
DR PDBsum; 7P6D; -.
DR PDBsum; 7P6E; -.
DR PDBsum; 7PQC; -.
DR PDBsum; 7PQP; -.
DR PDBsum; 7QJV; -.
DR PDBsum; 7QJW; -.
DR PDBsum; 7QJX; -.
DR PDBsum; 7QJY; -.
DR PDBsum; 7QJZ; -.
DR PDBsum; 7QK1; -.
DR PDBsum; 7QK2; -.
DR PDBsum; 7QK3; -.
DR PDBsum; 7QK5; -.
DR PDBsum; 7QK6; -.
DR PDBsum; 7QKF; -.
DR PDBsum; 7QKG; -.
DR PDBsum; 7QKH; -.
DR PDBsum; 7QKI; -.
DR PDBsum; 7QKJ; -.
DR PDBsum; 7QKK; -.
DR PDBsum; 7QKL; -.
DR PDBsum; 7QKM; -.
DR PDBsum; 7QKU; -.
DR PDBsum; 7QKV; -.
DR PDBsum; 7QKW; -.
DR PDBsum; 7QKX; -.
DR PDBsum; 7QKY; -.
DR PDBsum; 7QKZ; -.
DR PDBsum; 7QL0; -.
DR PDBsum; 7QL1; -.
DR PDBsum; 7QL2; -.
DR PDBsum; 7QL3; -.
DR PDBsum; 7QL4; -.
DR PDBsum; 7R4T; -.
DR PDBsum; 7R5H; -.
DR PDBsum; 7SP1; -.
DR PDBsum; 7U0Z; -.
DR AlphaFoldDB; P10636; -.
DR BMRB; P10636; -.
DR SASBDB; P10636; -.
DR SMR; P10636; -.
DR BioGRID; 110308; 399.
DR CORUM; P10636; -.
DR DIP; DIP-29753N; -.
DR ELM; P10636; -.
DR IntAct; P10636; 593.
DR MINT; P10636; -.
DR STRING; 9606.ENSP00000340820; -.
DR BindingDB; P10636; -.
DR ChEMBL; CHEMBL1293224; -.
DR DrugBank; DB00637; Astemizole.
DR DrugBank; DB01248; Docetaxel.
DR DrugBank; DB14914; Flortaucipir F-18.
DR DrugBank; DB00448; Lansoprazole.
DR DrugBank; DB01229; Paclitaxel.
DR DrugCentral; P10636; -.
DR GlyConnect; 2885; 1 O-Linked glycan (6 sites).
DR GlyGen; P10636; 21 sites, 1 O-linked glycan (21 sites).
DR iPTMnet; P10636; -.
DR MetOSite; P10636; -.
DR PhosphoSitePlus; P10636; -.
DR BioMuta; MAPT; -.
DR DMDM; 334302961; -.
DR EPD; P10636; -.
DR jPOST; P10636; -.
DR MassIVE; P10636; -.
DR MaxQB; P10636; -.
DR PaxDb; P10636; -.
DR PeptideAtlas; P10636; -.
DR PRIDE; P10636; -.
DR ProteomicsDB; 52624; -. [P10636-1]
DR ProteomicsDB; 52625; -. [P10636-2]
DR ProteomicsDB; 52626; -. [P10636-3]
DR ProteomicsDB; 52627; -. [P10636-4]
DR ProteomicsDB; 52628; -. [P10636-5]
DR ProteomicsDB; 52629; -. [P10636-6]
DR ProteomicsDB; 52630; -. [P10636-7]
DR ProteomicsDB; 52631; -. [P10636-8]
DR ProteomicsDB; 52632; -. [P10636-9]
DR TopDownProteomics; P10636-3; -. [P10636-3]
DR ABCD; P10636; 85 sequenced antibodies.
DR Antibodypedia; 3124; 5572 antibodies from 53 providers.
DR DNASU; 4137; -.
DR Ensembl; ENST00000334239.12; ENSP00000334886.8; ENSG00000186868.17. [P10636-2]
DR Ensembl; ENST00000351559.10; ENSP00000303214.7; ENSG00000186868.17. [P10636-8]
DR Ensembl; ENST00000415613.6; ENSP00000410838.2; ENSG00000186868.17. [P10636-9]
DR Ensembl; ENST00000420682.6; ENSP00000413056.2; ENSG00000186868.17. [P10636-7]
DR Ensembl; ENST00000431008.7; ENSP00000389250.3; ENSG00000186868.17. [P10636-5]
DR Ensembl; ENST00000446361.7; ENSP00000408975.3; ENSG00000186868.17. [P10636-6]
DR Ensembl; ENST00000535772.6; ENSP00000443028.2; ENSG00000186868.17. [P10636-4]
DR Ensembl; ENST00000571987.5; ENSP00000458742.1; ENSG00000186868.17. [P10636-1]
DR Ensembl; ENST00000574436.5; ENSP00000460965.1; ENSG00000186868.17. [P10636-8]
DR Ensembl; ENST00000612872.4; ENSP00000478602.1; ENSG00000277956.4. [P10636-7]
DR Ensembl; ENST00000613360.4; ENSP00000483784.1; ENSG00000276155.4. [P10636-7]
DR Ensembl; ENST00000620070.4; ENSP00000484491.1; ENSG00000277956.4. [P10636-8]
DR Ensembl; ENST00000620818.4; ENSP00000484321.1; ENSG00000277956.4. [P10636-5]
DR Ensembl; ENST00000620981.4; ENSP00000481769.1; ENSG00000276155.4. [P10636-5]
DR Ensembl; ENST00000621329.4; ENSP00000477703.1; ENSG00000276155.4. [P10636-8]
DR Ensembl; ENST00000622106.2; ENSP00000482244.1; ENSG00000277956.4. [P10636-6]
DR Ensembl; ENST00000622728.1; ENSP00000479142.1; ENSG00000276155.4. [P10636-6]
DR Ensembl; ENST00000626571.2; ENSP00000486039.1; ENSG00000276155.4. [P10636-6]
DR Ensembl; ENST00000628393.2; ENSP00000487570.1; ENSG00000276155.4. [P10636-2]
DR Ensembl; ENST00000631447.1; ENSP00000488373.1; ENSG00000277956.4. [P10636-5]
DR Ensembl; ENST00000632500.1; ENSP00000487837.1; ENSG00000277956.4. [P10636-7]
DR Ensembl; ENST00000633047.1; ENSP00000488245.1; ENSG00000277956.4. [P10636-2]
DR Ensembl; ENST00000634049.1; ENSP00000487819.1; ENSG00000277956.4. [P10636-8]
DR Ensembl; ENST00000680542.1; ENSP00000505258.1; ENSG00000186868.17. [P10636-7]
DR GeneID; 4137; -.
DR KEGG; hsa:4137; -.
DR UCSC; uc002ijr.5; human. [P10636-1]
DR CTD; 4137; -.
DR DisGeNET; 4137; -.
DR GeneCards; MAPT; -.
DR HGNC; HGNC:6893; MAPT.
DR HPA; ENSG00000186868; Tissue enhanced (brain, skeletal muscle).
DR MalaCards; MAPT; -.
DR MIM; 157140; gene+phenotype.
DR MIM; 172700; phenotype.
DR MIM; 260540; phenotype.
DR MIM; 600274; phenotype.
DR MIM; 601104; phenotype.
DR neXtProt; NX_P10636; -.
DR NIAGADS; ENSG00000186868; -.
DR OpenTargets; ENSG00000186868; -.
DR Orphanet; 275864; Behavioral variant of frontotemporal dementia.
DR Orphanet; 240071; Classic progressive supranuclear palsy syndrome.
DR Orphanet; 100070; Progressive non-fluent aphasia.
DR Orphanet; 240103; Progressive supranuclear palsy-corticobasal syndrome.
DR Orphanet; 240085; Progressive supranuclear palsy-parkinsonism syndrome.
DR Orphanet; 240112; Progressive supranuclear palsy-progressive non-fluent aphasia syndrome.
DR Orphanet; 240094; Progressive supranuclear palsy-pure akinesia with gait freezing syndrome.
DR Orphanet; 100069; Semantic dementia.
DR PharmGKB; PA238; -.
DR VEuPathDB; HostDB:ENSG00000186868; -.
DR eggNOG; KOG2418; Eukaryota.
DR GeneTree; ENSGT00940000155494; -.
DR HOGENOM; CLU_021741_2_0_1; -.
DR InParanoid; P10636; -.
DR OrthoDB; 716848at2759; -.
DR TreeFam; TF316358; -.
DR PathwayCommons; P10636; -.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs. [P10636-8]
DR SABIO-RK; P10636; -.
DR SignaLink; P10636; -.
DR SIGNOR; P10636; -.
DR BioGRID-ORCS; 4137; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; MAPT; human.
DR EvolutionaryTrace; P10636; -.
DR GeneWiki; Tau_protein; -.
DR GenomeRNAi; 4137; -.
DR Pharos; P10636; Tclin.
DR PRO; PR:P10636; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P10636; protein.
DR Bgee; ENSG00000186868; Expressed in cortical plate and 102 other tissues.
DR ExpressionAtlas; P10636; baseline and differential.
DR Genevisible; P10636; HS.
DR GO; GO:0030673; C:axolemma; IDA:CAFA.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; TAS:ARUK-UCL.
DR GO; GO:0005576; C:extracellular region; NAS:ARUK-UCL.
DR GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0044304; C:main axon; ISS:ARUK-UCL.
DR GO; GO:0045121; C:membrane raft; ISS:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:CAFA.
DR GO; GO:0005739; C:mitochondrion; TAS:ARUK-UCL.
DR GO; GO:0097418; C:neurofibrillary tangle; IDA:CAFA.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045298; C:tubulin complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ARUK-UCL.
DR GO; GO:0034452; F:dynactin binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0099077; F:histone-dependent DNA binding; TAS:ARUK-UCL.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0071813; F:lipoprotein particle binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0099609; F:microtubule lateral binding; IMP:CAFA.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; TAS:ARUK-UCL.
DR GO; GO:0035091; F:phosphatidylinositol binding; TAS:ARUK-UCL.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; TAS:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:ARUK-UCL.
DR GO; GO:0003723; F:RNA binding; TAS:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; TAS:ARUK-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; TAS:ARUK-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:ParkinsonsUK-UCL.
DR GO; GO:1990000; P:amyloid fibril formation; IMP:CAFA.
DR GO; GO:0048143; P:astrocyte activation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0061564; P:axon development; TAS:ARUK-UCL.
DR GO; GO:0098930; P:axonal transport; TAS:ParkinsonsUK-UCL.
DR GO; GO:0019896; P:axonal transport of mitochondrion; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007267; P:cell-cell signaling; NAS:ARUK-UCL.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; TAS:ARUK-UCL.
DR GO; GO:0034605; P:cellular response to heat; TAS:ParkinsonsUK-UCL.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; TAS:ARUK-UCL.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; TAS:ARUK-UCL.
DR GO; GO:0021954; P:central nervous system neuron development; TAS:ARUK-UCL.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; TAS:ParkinsonsUK-UCL.
DR GO; GO:0048699; P:generation of neurons; NAS:UniProtKB.
DR GO; GO:0006475; P:internal protein amino acid acetylation; TAS:ARUK-UCL.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL.
DR GO; GO:0007613; P:memory; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001774; P:microglial cell activation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IDA:ARUK-UCL.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0033673; P:negative regulation of kinase activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; IGI:ARUK-UCL.
DR GO; GO:1902988; P:neurofibrillary tangle assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0072386; P:plus-end-directed organelle transport along microtubule; TAS:ParkinsonsUK-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR GO; GO:1905689; P:positive regulation of diacylglycerol kinase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903829; P:positive regulation of protein localization; IMP:CAFA.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051260; P:protein homooligomerization; IMP:ARUK-UCL.
DR GO; GO:0051258; P:protein polymerization; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IGI:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IDA:ARUK-UCL.
DR GO; GO:1900034; P:regulation of cellular response to heat; IMP:ParkinsonsUK-UCL.
DR GO; GO:0033044; P:regulation of chromosome organization; TAS:ARUK-UCL.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; TAS:ARUK-UCL.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:CAFA.
DR GO; GO:0031113; P:regulation of microtubule polymerization; TAS:ARUK-UCL.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:CAFA.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IC:ParkinsonsUK-UCL.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; TAS:ARUK-UCL.
DR GO; GO:0010288; P:response to lead ion; ISS:ARUK-UCL.
DR GO; GO:0016072; P:rRNA metabolic process; TAS:ARUK-UCL.
DR GO; GO:0034063; P:stress granule assembly; TAS:ARUK-UCL.
DR GO; GO:0097435; P:supramolecular fiber organization; IDA:CAFA.
DR GO; GO:0007416; P:synapse assembly; IMP:ARUK-UCL.
DR GO; GO:0050808; P:synapse organization; IMP:ParkinsonsUK-UCL.
DR DisProt; DP01100; -. [P10636-8]
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR InterPro; IPR002955; Tau.
DR Pfam; PF00418; Tubulin-binding; 4.
DR PRINTS; PR01261; TAUPROTEIN.
DR PROSITE; PS00229; TAU_MAP_1; 4.
DR PROSITE; PS51491; TAU_MAP_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Alzheimer disease;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycation;
KW Glycoprotein; Isopeptide bond; Membrane; Methylation; Microtubule;
KW Neurodegeneration; Parkinsonism; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1512244"
FT CHAIN 2..758
FT /note="Microtubule-associated protein tau"
FT /id="PRO_0000072739"
FT REPEAT 561..591
FT /note="Tau/MAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824,
FT ECO:0000305|PubMed:7706316"
FT REPEAT 592..622
FT /note="Tau/MAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824,
FT ECO:0000305|PubMed:7706316"
FT REPEAT 623..653
FT /note="Tau/MAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824,
FT ECO:0000305|PubMed:7706316"
FT REPEAT 654..685
FT /note="Tau/MAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824,
FT ECO:0000305|PubMed:7706316"
FT REGION 1..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..685
FT /note="Microtubule-binding domain"
FT /evidence="ECO:0000269|PubMed:7706316"
FT REGION 715..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 24
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 44
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 67
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 381
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 391
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 392
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 394
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 465
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 497
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 507
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 541
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 557
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 571
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 574
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 584
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 591
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 607
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 611
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 615
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 628
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 634
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 638
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 648
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 657
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 660
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 687
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 692
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 700
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 702
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 712
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT SITE 755
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9326300"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1512244"
FT MOD_RES 18
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:14999081"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 214
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000269|PubMed:16982696"
FT MOD_RES 396
FT /note="Phosphoserine; in PHF-tau"
FT /evidence="ECO:0000269|PubMed:1899488"
FT MOD_RES 470
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000269|PubMed:9614189"
FT MOD_RES 472
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 480
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 484
FT /note="Deamidated asparagine; in tau and PHF-tau; partial"
FT /evidence="ECO:0000269|PubMed:1512244"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 498
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000269|PubMed:15546861"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 514
FT /note="Phosphotyrosine; by TTBK1"
FT /evidence="ECO:0000269|PubMed:16923168"
FT MOD_RES 515
FT /note="Phosphoserine; by PDPK1 and TTBK1"
FT /evidence="ECO:0000269|PubMed:16923168"
FT MOD_RES 516
FT /note="Phosphoserine; by PDPK1 and TTBK1"
FT /evidence="ECO:0000269|PubMed:15546861,
FT ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179,
FT ECO:0000269|PubMed:9614189"
FT MOD_RES 519
FT /note="Phosphoserine; by CK1, PDPK1 and TTBK1"
FT /evidence="ECO:0000269|PubMed:14761950,
FT ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168,
FT ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254,
FT ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 522
FT /note="Phosphothreonine; by CK1 and PDPK1"
FT /evidence="ECO:0000269|PubMed:14761950,
FT ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:19451179"
FT MOD_RES 529
FT /note="Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1"
FT /evidence="ECO:0000269|PubMed:15546861,
FT ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19451179,
FT ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:9614189"
FT MOD_RES 531
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:15546861,
FT ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179,
FT ECO:0000269|PubMed:9614189"
FT MOD_RES 534
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:19451179"
FT MOD_RES 542
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 548
FT /note="Phosphothreonine; by GSK3-beta and PDPK1"
FT /evidence="ECO:0000269|PubMed:14690523,
FT ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 552
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000269|PubMed:15546861,
FT ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 554
FT /note="Phosphoserine; by PHK"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:8999860"
FT MOD_RES 576
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 576
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 579
FT /note="Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1,
FT BRSK2 and PHK"
FT /evidence="ECO:0000269|PubMed:15546861,
FT ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179,
FT ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:23666762,
FT ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860,
FT ECO:0000269|PubMed:9614189"
FT MOD_RES 596
FT /note="Deamidated asparagine; in tau and PHF-tau; partial"
FT /evidence="ECO:0000269|PubMed:1512244"
FT MOD_RES 598
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 602
FT /note="Phosphoserine; by PHK"
FT /evidence="ECO:0000269|PubMed:8999860"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7706316"
FT MOD_RES 615
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 622
FT /note="Phosphoserine; by PHK"
FT /evidence="ECO:0000269|PubMed:7706316,
FT ECO:0000269|PubMed:8999860"
FT MOD_RES 628
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 628
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 634
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 638
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7706316"
FT MOD_RES 648
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 660
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 664
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 666
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 669
FT /note="Phosphoserine; by PHK"
FT /evidence="ECO:0000269|PubMed:8999860"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7706316"
FT MOD_RES 686
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 702
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 711
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 713
FT /note="Phosphoserine; by CK1 and PDPK1"
FT /evidence="ECO:0000269|PubMed:14761950,
FT ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254,
FT ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 717
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 720
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 721
FT /note="Phosphoserine; by CK1 and PDPK1"
FT /evidence="ECO:0000269|PubMed:14761950,
FT ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:19451179,
FT ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15546861,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 733
FT /note="Phosphoserine; by CaMK2 and TTBK1"
FT /evidence="ECO:0000269|PubMed:16923168"
FT MOD_RES 739
FT /note="Phosphoserine; by PDPK1 and TTBK1"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179,
FT ECO:0000269|PubMed:9614189"
FT MOD_RES 744
FT /note="Phosphothreonine; by TTBK1"
FT /evidence="ECO:0000269|PubMed:16923168"
FT CARBOHYD 87
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 383
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 467
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 480
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 491
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 525
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:21327254"
FT CARBOHYD 542
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 551
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 555
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:21327254"
FT CARBOHYD 576
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 597
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 598
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 664
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 670
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 686
FT /note="N-linked (Glc) (glycation) lysine; in PHF-tau; in
FT vitro"
FT /evidence="ECO:0000269|PubMed:9326300"
FT CARBOHYD 717
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:21327254"
FT DISULFID 608..639
FT /evidence="ECO:0000250"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 571
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); in PHF-tau"
FT /evidence="ECO:0000269|PubMed:16443603"
FT CROSSLNK 576
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 615
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); in PHF-tau"
FT /evidence="ECO:0000269|PubMed:16443603"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); in PHF-tau"
FT /evidence="ECO:0000269|PubMed:16443603"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 692
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 702
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT VAR_SEQ 1..44
FT /note="MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLK -> MLRA
FT LQQRKR (in isoform Tau-A)"
FT /evidence="ECO:0000303|PubMed:2516729"
FT /id="VSP_003175"
FT VAR_SEQ 45..73
FT /note="Missing (in isoform Tau-A, isoform Tau-D and isoform
FT Fetal-tau)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2498079, ECO:0000303|PubMed:2516729,
FT ECO:0000303|PubMed:3131773, ECO:0000303|Ref.7"
FT /id="VSP_003176"
FT VAR_SEQ 74..102
FT /note="Missing (in isoform Tau-A, isoform Tau-B, isoform
FT Tau-D, isoform Tau-E and isoform Fetal-tau)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2484340, ECO:0000303|PubMed:2498079,
FT ECO:0000303|PubMed:2516729, ECO:0000303|PubMed:3131773,
FT ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_003177"
FT VAR_SEQ 103..104
FT /note="Missing (in isoform Tau-A)"
FT /evidence="ECO:0000303|PubMed:2516729"
FT /id="VSP_003178"
FT VAR_SEQ 125..375
FT /note="Missing (in isoform Tau-A, isoform Tau-B, isoform
FT Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and
FT isoform Fetal-tau)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2484340, ECO:0000303|PubMed:2498079,
FT ECO:0000303|PubMed:2516729, ECO:0000303|PubMed:3131773,
FT ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_003179"
FT VAR_SEQ 395..460
FT /note="Missing (in isoform Tau-A, isoform Tau-B, isoform
FT Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and
FT isoform Fetal-tau)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2484340, ECO:0000303|PubMed:2498079,
FT ECO:0000303|PubMed:2516729, ECO:0000303|PubMed:3131773,
FT ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_003180"
FT VAR_SEQ 502
FT /note="S -> SATKQVQRRPPPAGPRSER (in isoform Tau-G)"
FT /evidence="ECO:0000305"
FT /id="VSP_026780"
FT VAR_SEQ 592..622
FT /note="Missing (in isoform Tau-A, isoform Tau-B, isoform
FT Tau-C and isoform Fetal-tau)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2484340, ECO:0000303|PubMed:2516729,
FT ECO:0000303|PubMed:3131773, ECO:0000303|Ref.7"
FT /id="VSP_003181"
FT VARIANT 5
FT /note="R -> H (in FTD; reduces the ability of tau to
FT promote microtubule assembly and promotes fibril formation
FT in vitro; dbSNP:rs63750959)"
FT /evidence="ECO:0000269|PubMed:11921059"
FT /id="VAR_019660"
FT VARIANT 5
FT /note="R -> L (in PSNP1; delays assembly initiation and
FT lowers the mass of microtubules formed; but the assembly
FT rate is increased compared to normal tau;
FT dbSNP:rs63750959)"
FT /evidence="ECO:0000269|PubMed:12325083"
FT /id="VAR_019661"
FT VARIANT 17
FT /note="T -> M (in dbSNP:rs144611688)"
FT /evidence="ECO:0000269|PubMed:20020531"
FT /id="VAR_064622"
FT VARIANT 30
FT /note="T -> A (in dbSNP:rs748728879)"
FT /evidence="ECO:0000269|PubMed:20020531"
FT /id="VAR_064623"
FT VARIANT 285
FT /note="D -> N (risk factor for PSNP1; dbSNP:rs62063786)"
FT /evidence="ECO:0000269|PubMed:10534245,
FT ECO:0000269|PubMed:9629852"
FT /id="VAR_010340"
FT VARIANT 289
FT /note="V -> A (risk factor for PSNP1; dbSNP:rs62063787)"
FT /evidence="ECO:0000269|PubMed:10534245,
FT ECO:0000269|PubMed:9629852"
FT /id="VAR_010341"
FT VARIANT 370
FT /note="R -> W (in dbSNP:rs17651549)"
FT /id="VAR_056121"
FT VARIANT 441
FT /note="Y -> H (in dbSNP:rs2258689)"
FT /evidence="ECO:0000269|PubMed:1420178,
FT ECO:0000269|PubMed:15365985, ECO:0000269|PubMed:9629852"
FT /id="VAR_010342"
FT VARIANT 447
FT /note="S -> P (in dbSNP:rs10445337)"
FT /evidence="ECO:0000269|PubMed:9629852"
FT /id="VAR_010343"
FT VARIANT 574
FT /note="K -> T (in PIDB; reduces the ability to promote
FT microtubule assembly by 70%; dbSNP:rs63750129)"
FT /evidence="ECO:0000269|PubMed:11089577,
FT ECO:0000269|PubMed:11117542"
FT /id="VAR_010344"
FT VARIANT 583
FT /note="L -> V (in FTD; less able to promote microtubule
FT assembly than wild-type tau; dbSNP:rs63750349)"
FT /evidence="ECO:0000269|PubMed:12509859"
FT /id="VAR_019662"
FT VARIANT 589
FT /note="G -> V (in FTD; dbSNP:rs63750376)"
FT /evidence="ECO:0000269|PubMed:9641683,
FT ECO:0000269|PubMed:9973279"
FT /id="VAR_010345"
FT VARIANT 590
FT /note="G -> R (in FTD; increased aggregation propensity and
FT altered binding affinity towards microtubules and F-actin;
FT dbSNP:rs1247408229)"
FT /evidence="ECO:0000269|PubMed:32961270"
FT /id="VAR_084361"
FT VARIANT 596
FT /note="N -> K (in FTD; with parkinsonism;
FT dbSNP:rs63750756)"
FT /evidence="ECO:0000269|PubMed:10412802,
FT ECO:0000269|PubMed:10489057, ECO:0000269|PubMed:10802785,
FT ECO:0000269|PubMed:12473774, ECO:0000269|PubMed:9789048"
FT /id="VAR_010346"
FT VARIANT 597
FT /note="Missing (in FTD; dbSNP:rs63750688)"
FT /evidence="ECO:0000269|PubMed:9973279"
FT /id="VAR_010347"
FT VARIANT 613
FT /note="N -> H (in FTD; reduced the ability of tau to
FT promote microtubule assembly without having a significant
FT effect on tau filament formation; effects at both the RNA
FT and the protein level; dbSNP:rs63750416)"
FT /evidence="ECO:0000269|PubMed:11585254,
FT ECO:0000269|PubMed:11906000"
FT /id="VAR_019663"
FT VARIANT 613
FT /note="Missing (in PSNP1/atypical PSNP1; heterozygosity may
FT be a risk factor for both a PSNP1-like syndrome and
FT Parkinson disease; reduced the ability of tau to promote
FT microtubule assembly without having a significant effect on
FT tau filament formation; effects at both the RNA and the
FT protein level)"
FT /evidence="ECO:0000269|PubMed:11220749,
FT ECO:0000269|PubMed:11906000, ECO:0000269|PubMed:14991828,
FT ECO:0000269|PubMed:14991829"
FT /id="VAR_019664"
FT VARIANT 617
FT /note="V -> I (in dbSNP:rs116733906)"
FT /evidence="ECO:0000269|PubMed:20020531"
FT /id="VAR_064624"
FT VARIANT 618
FT /note="P -> L (in FTD; most common mutation; reduction in
FT the ability to promote microtubule assembly; accelerates
FT aggregation of tau into filaments; dbSNP:rs63751273)"
FT /evidence="ECO:0000269|PubMed:10214944,
FT ECO:0000269|PubMed:9641683, ECO:0000269|PubMed:9736786,
FT ECO:0000269|PubMed:9789048, ECO:0000269|PubMed:9973279"
FT /id="VAR_010348"
FT VARIANT 618
FT /note="P -> S (in FTD and CBD; reduction in the ability to
FT promote microtubule assembly; dbSNP:rs63751438)"
FT /evidence="ECO:0000269|PubMed:10374757,
FT ECO:0000269|PubMed:10553987, ECO:0000269|PubMed:11071507,
FT ECO:0000269|PubMed:16240366"
FT /id="VAR_010349"
FT VARIANT 620
FT /note="G -> V (in PSNP1; dbSNP:rs63751391)"
FT /evidence="ECO:0000269|PubMed:16157753"
FT /id="VAR_037439"
FT VARIANT 622
FT /note="S -> N (in FTD; minimal parkinsonism; very early age
FT of onset; dbSNP:rs63751165)"
FT /evidence="ECO:0000269|PubMed:10208578"
FT /id="VAR_010350"
FT VARIANT 634
FT /note="K -> M (in FTD; dbSNP:rs63750092)"
FT /evidence="ECO:0000269|PubMed:15883319"
FT /id="VAR_037440"
FT VARIANT 637
FT /note="S -> F (in PIDB; markedly reduced ability of tau to
FT promote microtubule assembly; dbSNP:rs63750635)"
FT /evidence="ECO:0000269|PubMed:11891833"
FT /id="VAR_019665"
FT VARIANT 654
FT /note="V -> M (in FTD; ultrastructural and biochemical
FT characteristics indistinguishable from Alzheimer disease;
FT accelerates aggregation of tau into filaments;
FT dbSNP:rs63750570)"
FT /evidence="ECO:0000269|PubMed:10214944,
FT ECO:0000269|PubMed:9629852"
FT /id="VAR_010351"
FT VARIANT 659
FT /note="E -> V (in FTD; dbSNP:rs63750711)"
FT /evidence="ECO:0000269|PubMed:11117541"
FT /id="VAR_019666"
FT VARIANT 669
FT /note="S -> L (in fatal respiratory hypoventilation;
FT unusual apparent autosomal recessive inheritance; reduced
FT binding to microtubules as well as increased fibrillization
FT and aggregation; dbSNP:rs63750425)"
FT /evidence="ECO:0000269|PubMed:14595660"
FT /id="VAR_019667"
FT VARIANT 686
FT /note="K -> I (in PIDB; 90% reduction in the rate of
FT microtubule assembly; dbSNP:rs63751264)"
FT /evidence="ECO:0000269|PubMed:11601501"
FT /id="VAR_019668"
FT VARIANT 706
FT /note="G -> R (in PIDB; in vitro the mutation reduces the
FT ability of tau to promote microtubule assembly by 25 to
FT 30%; dbSNP:rs63750512)"
FT /evidence="ECO:0000269|PubMed:10604746,
FT ECO:0000269|PubMed:11117542"
FT /id="VAR_010352"
FT VARIANT 723
FT /note="R -> W (in FTD/Alzheimer disease; accelerates
FT aggregation of tau into filaments; reduces tau
FT phosphorylation in cells compared to both the wild-type and
FT other mutant forms; dbSNP:rs63750424)"
FT /evidence="ECO:0000269|PubMed:10214944,
FT ECO:0000269|PubMed:11278002, ECO:0000269|PubMed:11889249,
FT ECO:0000269|PubMed:14517953, ECO:0000269|PubMed:26086902,
FT ECO:0000269|PubMed:9641683, ECO:0000269|PubMed:9973279"
FT /id="VAR_010353"
FT MUTAGEN 515
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 516
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 519
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 531
FT /note="S->A: No decrease in microtubule-binding and
FT nucleation activity after in vitro phosphorylation of
FT mutant protein."
FT MUTAGEN 548
FT /note="T->A: 50% Decrease in microtubule-binding after in
FT vitro phosphorylation of mutant protein."
FT MUTAGEN 548
FT /note="T->E: No association with plasma membrane."
FT MUTAGEN 552
FT /note="S->A: 70% decrease in microtubule-binding after in
FT vitro phosphorylation of mutant protein."
FT MUTAGEN 552
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 579
FT /note="S->A: 8% decrease in microtubule-binding after in
FT vitro phosphorylation of mutant protein."
FT MUTAGEN 713
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 721
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 726
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 730
FT /note="S->E: No association with plasma membrane."
FT MUTAGEN 739
FT /note="S->E: No association with plasma membrane."
FT CONFLICT 48
FT /note="L -> P (in Ref. 6; AAU45390)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="H -> L (in Ref. 5; AAC04277)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="K -> M (in Ref. 12; AAS17881)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="K -> S (in Ref. 12; AAS17881)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="V -> Q (in Ref. 17; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="S -> K (in Ref. 17; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6N4P"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5ZV3"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5ZV3"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:6CVJ"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:5N5A"
FT STRAND 592..610
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:7P65"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:5MP5"
FT TURN 622..624
FT /evidence="ECO:0007829|PDB:5N5B"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:4E0N"
FT STRAND 634..640
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 654..657
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:7P6A"
FT STRAND 686..695
FT /evidence="ECO:0007829|PDB:7P6A"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:6H06"
SQ 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
