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

 TAU_RAT                 Reviewed;         752 AA.
P19332; Q63567; Q63677; Q9QW06;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 155.
RecName: Full=Microtubule-associated protein tau;
AltName: Full=Neurofibrillary tangle protein;
AltName: Full=Paired helical filament-tau;
Short=PHF-tau;
Name=Mapt; Synonyms=Mtapt, Tau;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
TISSUE=Pheochromocytoma;
PubMed=1542696; DOI=10.1073/pnas.89.5.1983;
Goedert M., Spillantini M.G., Crowther R.A.;
"Cloning of a big tau microtubule-associated protein characteristic of
the peripheral nervous system.";
Proc. Natl. Acad. Sci. U.S.A. 89:1983-1987(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
TISSUE=Spinal ganglion;
PubMed=8408300;
Georgieff I.S., Liem R.K.H., Couchie D., Mavilia C., Nunez J.,
Shelanski M.L.;
"Expression of high molecular weight tau in the central and peripheral
nervous systems.";
J. Cell Sci. 105:729-737(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-F).
STRAIN=Wistar; TISSUE=Brain;
PubMed=8057376; DOI=10.1006/jmbi.1994.1508;
Sadot E., Marx R., Barg J., Behar L., Ginzburg I.;
"Complete sequence of 3'-untranslated region of tau from rat central
nervous system. Implications for mRNA heterogeneity.";
J. Mol. Biol. 241:325-331(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-G).
TISSUE=Brain;
PubMed=2560640; DOI=10.1016/0896-6273(89)90077-9;
Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L.;
"Developmentally regulated expression of specific tau sequences.";
Neuron 2:1389-1397(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-C).
PubMed=2504728; DOI=10.1083/jcb.109.3.1173;
Kanai Y., Takemura R., Oshima T., Mori H., Ihara Y., Yanagisawa M.,
Masaki T., Hirokawa N.;
"Expression of multiple tau isoforms and microtubule bundle formation
in fibroblasts transfected with a single tau cDNA.";
J. Cell Biol. 109:1173-1184(1989).
[6]
NUCLEOTIDE SEQUENCE OF 360-461 (ISOFORM TAU-A), AND NUCLEOTIDE
SEQUENCE OF 106-113 AND 368-461 (ISOFORM TAU-D).
TISSUE=Spinal cord;
PubMed=7964751;
Mavilia C., Couchie D., Nunez J.;
"Diversity of high-molecular-weight tau proteins in different regions
of the nervous system.";
J. Neurochem. 63:2300-2306(1994).
[7]
PROTEIN SEQUENCE OF 492-501; 506-515; 523-532; 537-551 AND 698-726,
AND PHOSPHORYLATION AT THR-492; SER-509; SER-510; SER-513; THR-528;
THR-542; SER-546; SER-707; SER-711 AND SER-715.
PubMed=8245007;
Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M.,
Titani K., Arai T., Kosik K.S., Ihara Y.;
"In vivo phosphorylation sites in fetal and adult rat tau.";
J. Biol. Chem. 268:25712-25717(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 697-752 (ISOFORMS TAU-A; TAU-B;
TAU-C; TAU-D; TAU-E; TAU-F AND TAU-G), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 752-775 (ISOFORM TAU-H).
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7877441; DOI=10.1016/0169-328X(94)90191-0;
Sawa A., Oyama F., Matsushita M., Ihara Y.;
"Molecular diversity at the carboxyl terminus of human and rat tau.";
Brain Res. Mol. Brain Res. 27:111-117(1994).
[9]
INTERACTION WITH FKBP4.
PubMed=20133804; DOI=10.1073/pnas.0914957107;
Chambraud B., Sardin E., Giustiniani J., Dounane O., Schumacher M.,
Goedert M., Baulieu E.E.;
"A role for FKBP52 in Tau protein function.";
Proc. Natl. Acad. Sci. U.S.A. 107:2658-2663(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-50; THR-60;
SER-191; SER-204; SER-489; THR-492; SER-509; SER-510; SER-513;
SER-525; THR-528; THR-542; SER-546; SER-667; SER-707; SER-711;
THR-714; SER-715; SER-727 AND SER-733, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Promotes microtubule assembly and stability, and might
be involved in the establishment and maintenance of neuronal
polarity. The C-terminus binds axonal microtubules while the N-
terminus binds neural plasma membrane components, suggesting that
tau functions as a linker protein between both. Axonal polarity is
predetermined by tau localization (in the neuronal cell) in the
domain of the cell body defined by the centrosome. The short
isoforms allow plasticity of the cytoskeleton whereas the longer
isoforms may preferentially play a role in its stabilization.
-!- SUBUNIT: Interacts with SQSTM1 when polyubiquitinated. Interacts
with PSMC2 through SQSTM1. Binds to CSNK1D (By similarity).
Interacts with FKBP4. Interacts with SGK1 (By similarity).
Interacts with EPM2A; the interaction dephosphorylates MAPT at
Ser-388 (By similarity). {ECO:0000250}.
-!- INTERACTION:
A6NAR8:- (xeno); NbExp=2; IntAct=EBI-7080713, EBI-8755852;
Q61644:Pacsin1 (xeno); NbExp=6; IntAct=EBI-8758676, EBI-2255561;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Cytoplasm,
cytoskeleton. Cell projection, axon. Note=Mostly found in the
axons of neurons, in the cytosol and in association with plasma
membrane components.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist. Isoforms differ from
each other by the presence or absence of up to 4 of the 14
exons. Two different C-termini are obtained either by the
retention or the splicing of intron 13/14.;
Name=Tau-A; Synonyms=SC1;
IsoId=P19332-1; Sequence=Displayed;
Name=Tau-B; Synonyms=Big-tau, HMW-tau;
IsoId=P19332-2; Sequence=VSP_003194;
Name=Tau-C;
IsoId=P19332-3; Sequence=VSP_003192, VSP_003193, VSP_003194;
Name=Tau-D; Synonyms=SC2;
IsoId=P19332-4; Sequence=VSP_003193;
Name=Tau-E;
IsoId=P19332-5; Sequence=VSP_003193, VSP_003194;
Name=Tau-F;
IsoId=P19332-6; Sequence=VSP_003191, VSP_003193, VSP_003194;
Name=Tau-G; Synonyms=Fetal-tau;
IsoId=P19332-7; Sequence=VSP_003192, VSP_003193, VSP_003194,
VSP_003195;
Name=Tau-H;
IsoId=P19332-8; Sequence=VSP_003196;
-!- TISSUE SPECIFICITY: Expressed in neurons. The larger forms
(isoform tau-A and isoform tau-B) are preferentially expressed in
the peripheral nervous system while the other are expressed in the
central nervous system. Low amounts of the larger forms are also
found in limited areas of the CNS.
-!- DEVELOPMENTAL STAGE: During the immediate postnatal period, the
dorsal root ganglia express all isoforms whereas only the larger
forms persist in the adults.
-!- DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms
contain 3 repeats while type II isoforms contain 4 repeats.
-!- PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke
SQSTM1-dependent degradation by the proteasome (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated at various serine and threonine residues in S-
P or T-P motifs by proline-directed protein kinases (PDPK1: CDK1,
CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in
mitosis), and at serine residues in K-X-G-S motifs by
MAP/microtubule affinity-regulating kinase (MARK1 or MARK2),
causing detachment from microtubules, and their disassembly. Fetal
Tau is much more phosphorylated than adult Tau. Phosphorylation at
Ser-573 by BRSK1 and BRSK2 in neurons affects ability to bind
microtubules and plays a role in neuron polarization.
Phosphorylated by PHK. Dephosphorylation at several serine and
threonine residues by the serine/threonine phosphatase PPP5C.
Phosphorylation at Ser-204 by SGK1 mediates microtubule
depolymerization and neurite formation in hippocampal neurons (By
similarity). {ECO:0000250}.
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EMBL; M84156; AAA42204.1; -; mRNA.
EMBL; X79321; CAA55889.1; -; mRNA.
EMBL; D30628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D30629; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A38235; A38235.
PIR; JS0306; JS0306.
PIR; S46264; S46264.
UniGene; Rn.2455; -.
SMR; P19332; -.
DIP; DIP-41779N; -.
IntAct; P19332; 5.
MINT; MINT-1037362; -.
STRING; 10116.ENSRNOP00000006856; -.
BindingDB; P19332; -.
ChEMBL; CHEMBL1075117; -.
iPTMnet; P19332; -.
PhosphoSitePlus; P19332; -.
PaxDb; P19332; -.
PRIDE; P19332; -.
UCSC; RGD:69329; rat. [P19332-1]
RGD; 69329; Mapt.
eggNOG; KOG2418; Eukaryota.
eggNOG; ENOG4111J07; LUCA.
HOGENOM; HOG000231029; -.
HOVERGEN; HBG000991; -.
InParanoid; P19332; -.
PhylomeDB; P19332; -.
PRO; PR:P19332; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030673; C:axolemma; ISO:RGD.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
GO; GO:0005930; C:axoneme; ISO:RGD.
GO; GO:0044297; C:cell body; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0044304; C:main axon; IDA:RGD.
GO; GO:0005874; C:microtubule; IDA:CACAO.
GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:CAFA.
GO; GO:0097418; C:neurofibrillary tangle; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; ISO:RGD.
GO; GO:0034399; C:nuclear periphery; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0014069; C:postsynaptic density; ISO:RGD.
GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
GO; GO:0045298; C:tubulin complex; ISS:UniProtKB.
GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0071813; F:lipoprotein particle binding; ISO:RGD.
GO; GO:0008017; F:microtubule binding; IDA:CAFA.
GO; GO:0099609; F:microtubule lateral binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
GO; GO:0048018; F:receptor ligand activity; ISO:RGD.
GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
GO; GO:0007628; P:adult walking behavior; ISO:RGD.
GO; GO:1990000; P:amyloid fibril formation; ISO:RGD.
GO; GO:0006915; P:apoptotic process; IDA:RGD.
GO; GO:0008088; P:axo-dendritic transport; ISO:RGD.
GO; GO:0048675; P:axon extension; ISO:RGD.
GO; GO:0007409; P:axonogenesis; ISO:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:RGD.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:RGD.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0007017; P:microtubule-based process; NAS:RGD.
GO; GO:0047497; P:mitochondrion transport along microtubule; ISO:RGD.
GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0032387; P:negative regulation of intracellular transport; ISO:RGD.
GO; GO:0033673; P:negative regulation of kinase activity; ISO:RGD.
GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:RGD.
GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:RGD.
GO; GO:0030182; P:neuron differentiation; NAS:RGD.
GO; GO:0001764; P:neuron migration; ISO:RGD.
GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
GO; GO:1903829; P:positive regulation of cellular protein localization; ISO:RGD.
GO; GO:1900454; P:positive regulation of long term synaptic depression; IMP:RGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:RGD.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:RGD.
GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:RGD.
GO; GO:1900034; P:regulation of cellular response to heat; ISO:RGD.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:RGD.
GO; GO:0060632; P:regulation of microtubule-based movement; ISO:RGD.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:RGD.
GO; GO:0007584; P:response to nutrient; IDA:RGD.
GO; GO:0010033; P:response to organic substance; IDA:RGD.
GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
GO; GO:0050808; P:synapse organization; ISO:RGD.
InterPro; IPR001084; MAP_tubulin-bd_rpt.
InterPro; IPR002955; Tau.
Pfam; PF00418; Tubulin-binding; 4.
PRINTS; PR01261; TAUPROTEIN.
PROSITE; PS00229; TAU_MAP_1; 4.
PROSITE; PS51491; TAU_MAP_2; 4.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Disulfide bond; Isopeptide bond; Membrane; Methylation; Microtubule;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P10636}.
CHAIN 2 752 Microtubule-associated protein tau.
/FTId=PRO_0000072746.
REPEAT 555 585 Tau/MAP 1.
REPEAT 586 616 Tau/MAP 2.
REPEAT 617 647 Tau/MAP 3.
REPEAT 648 679 Tau/MAP 4.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 18 18 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 58 58 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 60 60 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 100 100 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 464 464 Phosphothreonine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 466 466 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 474 474 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 474 474 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 480 480 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 486 486 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 487 487 Phosphothreonine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 492 492 Phosphothreonine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 506 506 Phosphoserine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 508 508 Phosphotyrosine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 513 513 Phosphoserine; by CK1, PDPK1 and TTBK1.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 516 516 Phosphothreonine; by CK1 and PDPK1.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 523 523 Phosphothreonine; by BRSK1, BRSK2, DYRK2
and PDPK1.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 528 528 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 536 536 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 542 542 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 542 542 Phosphothreonine; by GSK3-beta and PDPK1.
{ECO:0000250}.
MOD_RES 546 546 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 548 548 Phosphoserine; by PHK.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 570 570 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 570 570 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 573 573 Phosphoserine; by MARK1, BRSK1, BRSK2 and
PHK. {ECO:0000250|UniProtKB:P10636}.
MOD_RES 592 592 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 596 596 Phosphoserine; by PHK.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 600 600 Phosphoserine; by PHK.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 601 601 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 609 609 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 622 622 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 622 622 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 628 628 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 632 632 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 642 642 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 654 654 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 658 658 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 660 660 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 663 663 Phosphoserine; by PHK.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 680 680 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 696 696 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 705 705 Phosphotyrosine.
{ECO:0000250|UniProtKB:P10637}.
MOD_RES 707 707 Phosphoserine; by CK1 and PDPK1.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 711 711 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 714 714 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 715 715 Phosphoserine; by CK1 and PDPK1.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8245007}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000250|UniProtKB:P10636}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 733 733 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 738 738 Phosphothreonine.
{ECO:0000250|UniProtKB:P10636}.
DISULFID 602 633 {ECO:0000250}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 565 565 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10636}.
CROSSLNK 570 570 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 578 578 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 592 592 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 609 609 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 622 622 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10636}.
CROSSLNK 628 628 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 632 632 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 642 642 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 654 654 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 658 658 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 664 664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10636}.
CROSSLNK 680 680 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 686 686 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10637}.
CROSSLNK 696 696 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10637}.
VAR_SEQ 34 91 Missing (in isoform Tau-F).
{ECO:0000303|PubMed:8057376}.
/FTId=VSP_003191.
VAR_SEQ 63 91 Missing (in isoform Tau-C and isoform
Tau-G). {ECO:0000303|PubMed:2504728,
ECO:0000303|PubMed:2560640}.
/FTId=VSP_003192.
VAR_SEQ 114 367 Missing (in isoform Tau-C, isoform Tau-D,
isoform Tau-E, isoform Tau-F and isoform
Tau-G). {ECO:0000303|PubMed:2504728,
ECO:0000303|PubMed:2560640,
ECO:0000303|PubMed:8057376}.
/FTId=VSP_003193.
VAR_SEQ 387 452 Missing (in isoform Tau-B, isoform Tau-C,
isoform Tau-E, isoform Tau-F and isoform
Tau-G). {ECO:0000303|PubMed:1542696,
ECO:0000303|PubMed:2504728,
ECO:0000303|PubMed:2560640,
ECO:0000303|PubMed:8057376,
ECO:0000303|PubMed:8408300}.
/FTId=VSP_003194.
VAR_SEQ 586 616 Missing (in isoform Tau-G).
{ECO:0000303|PubMed:2560640}.
/FTId=VSP_003195.
VAR_SEQ 752 752 L -> KPVLLSSEVWNYSHDFGHHTDLGL (in isoform
Tau-H). {ECO:0000303|PubMed:7877441}.
/FTId=VSP_003196.
CONFLICT 255 255 F -> L (in Ref. 2). {ECO:0000305}.
CONFLICT 284 284 G -> A (in Ref. 2). {ECO:0000305}.
CONFLICT 292 292 H -> D (in Ref. 2). {ECO:0000305}.
CONFLICT 618 618 H -> Q (in Ref. 2, 3; CAA55889 and 4).
{ECO:0000305}.
CONFLICT 705 705 Y -> H (in Ref. 3; CAA55889).
{ECO:0000305}.
CONFLICT 734 734 P -> A (in Ref. 2). {ECO:0000305}.
SEQUENCE 752 AA; 78564 MW; 915DCA04EF0B2902 CRC64;
MAEPRQEFDT MEDQAGDYTM LQDQEGDMDH GLKESPPQPP ADDGSEEPGS ETSDAKSTPT
AEDVTAPLVE ERAPDKQATA QSHTEIPEGT TAEEAGIGDT PNMEDQAAGH VTQEPQKVEI
FSQSLLVEPG RREGQAPDSG ISDWTHQQVP SMSGAPLPPQ GLREATHQPL GTRPEDVERS
HPASELLWQE SPQKEAWGKD RLGSEEEVDE DITMDESSQE SPPSQASLAP GTATPQARSV
SASGVSGETT SIPGFPAEGS IPLPADFFSK VSAETQASPP EGPGTGPSEE GHEAAPEFTF
HVEIKASAPK EQDLEGATVV GAPAEEQKAR GPSVGKGTKE ASLLEPTDKQ PAAGLPGRPV
SRVPQLKARV AGVSKDRTGN DEKKAKTSTP SCAKTPSNRP CLSPTRPTPG SSDPLIKPSS
PAVCPEPATS PKYVSSVTPR NGSPGTKQMK LKGADGKTGA KIATPRGAAT PGQKGTSNAT
RIPAKTTPSP KTPPGSGEPP KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV
RTPPKSPSAS KSRLQTAPVP MPDLKNVRSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS
KCGSKDNIKH VPGGGSVHIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR
VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS
NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL


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