TAU_RAT
ID TAU_RAT Reviewed; 752 AA.
AC P19332; Q63567; Q63677; Q9QW06;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 184.
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|RGD:69329}; Synonyms=Mtapt, Tau;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
RC TISSUE=Pheochromocytoma;
RX PubMed=1542696; DOI=10.1073/pnas.89.5.1983;
RA Goedert M., Spillantini M.G., Crowther R.A.;
RT "Cloning of a big tau microtubule-associated protein characteristic of the
RT peripheral nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1983-1987(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
RC TISSUE=Spinal ganglion;
RX PubMed=8408300; DOI=10.1242/jcs.105.3.729;
RA Georgieff I.S., Liem R.K.H., Couchie D., Mavilia C., Nunez J.,
RA Shelanski M.L.;
RT "Expression of high molecular weight tau in the central and peripheral
RT nervous systems.";
RL J. Cell Sci. 105:729-737(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-F).
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8057376; DOI=10.1006/jmbi.1994.1508;
RA Sadot E., Marx R., Barg J., Behar L., Ginzburg I.;
RT "Complete sequence of 3'-untranslated region of tau from rat central
RT nervous system. Implications for mRNA heterogeneity.";
RL J. Mol. Biol. 241:325-331(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-G).
RC TISSUE=Brain;
RX PubMed=2560640; DOI=10.1016/0896-6273(89)90077-9;
RA Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L.;
RT "Developmentally regulated expression of specific tau sequences.";
RL Neuron 2:1389-1397(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-C).
RX PubMed=2504728; DOI=10.1083/jcb.109.3.1173;
RA Kanai Y., Takemura R., Oshima T., Mori H., Ihara Y., Yanagisawa M.,
RA Masaki T., Hirokawa N.;
RT "Expression of multiple tau isoforms and microtubule bundle formation in
RT fibroblasts transfected with a single tau cDNA.";
RL J. Cell Biol. 109:1173-1184(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 360-461 (ISOFORM TAU-A), AND NUCLEOTIDE SEQUENCE OF
RP 106-113 AND 368-461 (ISOFORM TAU-D).
RC TISSUE=Spinal cord;
RX PubMed=7964751; DOI=10.1046/j.1471-4159.1994.63062300.x;
RA Mavilia C., Couchie D., Nunez J.;
RT "Diversity of high-molecular-weight tau proteins in different regions of
RT the nervous system.";
RL J. Neurochem. 63:2300-2306(1994).
RN [7]
RP PROTEIN SEQUENCE OF 492-501; 506-515; 523-532; 537-551 AND 698-726, AND
RP PHOSPHORYLATION AT THR-492; SER-509; SER-510; SER-513; THR-528; THR-542;
RP SER-546; SER-707; SER-711 AND SER-715.
RX PubMed=8245007; DOI=10.1016/s0021-9258(19)74447-0;
RA Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M.,
RA Titani K., Arai T., Kosik K.S., Ihara Y.;
RT "In vivo phosphorylation sites in fetal and adult rat tau.";
RL J. Biol. Chem. 268:25712-25717(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 697-752 (ISOFORMS TAU-A; TAU-B; TAU-C;
RP TAU-D; TAU-E; TAU-F AND TAU-G), AND NUCLEOTIDE SEQUENCE [MRNA] OF 752-775
RP (ISOFORM TAU-H).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7877441; DOI=10.1016/0169-328x(94)90191-0;
RA Sawa A., Oyama F., Matsushita M., Ihara Y.;
RT "Molecular diversity at the carboxyl terminus of human and rat tau.";
RL Brain Res. Mol. Brain Res. 27:111-117(1994).
RN [9]
RP INTERACTION WITH FKBP4.
RX PubMed=20133804; DOI=10.1073/pnas.0914957107;
RA Chambraud B., Sardin E., Giustiniani J., Dounane O., Schumacher M.,
RA Goedert M., Baulieu E.E.;
RT "A role for FKBP52 in Tau protein function.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2658-2663(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-50; THR-60; SER-191;
RP SER-204; SER-489; THR-492; SER-509; SER-510; SER-513; SER-525; THR-528;
RP THR-542; SER-546; SER-667; SER-707; SER-711; THR-714; SER-715; SER-727 AND
RP SER-733, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Promotes microtubule assembly and stability, and might be
CC involved in the establishment and maintenance of neuronal polarity. The
CC C-terminus binds axonal microtubules while the N-terminus binds neural
CC plasma membrane components, suggesting that tau functions as a linker
CC protein between both. Axonal polarity is predetermined by tau
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.
CC -!- SUBUNIT: Interacts with MARK1, MARK2, MARK3 AND MARK4 (By similarity).
CC Interacts with SQSTM1 when polyubiquitinated (By similarity). Interacts
CC with PSMC2 through SQSTM1 (By similarity). Interacts with FKBP4
CC (PubMed:20133804). Binds to CSNK1D (By similarity). Interacts with SGK1
CC (By similarity). Interacts with EPM2A; the interaction dephosphorylates
CC MAPT at Ser-388 (By similarity). Interacts with PIN1 (By similarity).
CC Interacts with LRRK2 (By similarity). Interacts with LRP1, leading to
CC endocytosis; this interaction is reduced in the presence of LRPAP1/RAP
CC (By similarity). {ECO:0000250|UniProtKB:P10636,
CC ECO:0000250|UniProtKB:P10637, ECO:0000269|PubMed:20133804}.
CC -!- INTERACTION:
CC P19332-5; Q61644: Pacsin1; Xeno; NbExp=6; IntAct=EBI-8758676, EBI-2255561;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P10636}. Cell membrane
CC {ECO:0000250|UniProtKB:P10636}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10636}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10636}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P10636}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P10636}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P10636}. Secreted
CC {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of
CC neurons, in the cytosol and in association with plasma membrane
CC components. Can be secreted; the secretion is dependent on protein
CC unfolding and facilitated by the cargo receptor TMED10; it results in
CC protein translocation from the cytoplasm into the ERGIC (endoplasmic
CC reticulum-Golgi intermediate compartment) followed by vesicle entry and
CC secretion. {ECO:0000250|UniProtKB:P10636}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist. Isoforms differ from each
CC other by the presence or absence of up to 4 of the 14 exons. Two
CC different C-termini are obtained either by the retention or the
CC splicing of intron 13/14.;
CC Name=Tau-A; Synonyms=SC1;
CC IsoId=P19332-1; Sequence=Displayed;
CC Name=Tau-B; Synonyms=Big-tau, HMW-tau;
CC IsoId=P19332-2; Sequence=VSP_003194;
CC Name=Tau-C;
CC IsoId=P19332-3; Sequence=VSP_003192, VSP_003193, VSP_003194;
CC Name=Tau-D; Synonyms=SC2;
CC IsoId=P19332-4; Sequence=VSP_003193;
CC Name=Tau-E;
CC IsoId=P19332-5; Sequence=VSP_003193, VSP_003194;
CC Name=Tau-F;
CC IsoId=P19332-6; Sequence=VSP_003191, VSP_003193, VSP_003194;
CC Name=Tau-G; Synonyms=Fetal-tau;
CC IsoId=P19332-7; Sequence=VSP_003192, VSP_003193, VSP_003194,
CC VSP_003195;
CC Name=Tau-H;
CC IsoId=P19332-8; Sequence=VSP_003196;
CC -!- TISSUE SPECIFICITY: Expressed in neurons. The larger forms (isoform
CC tau-A and isoform tau-B) are preferentially expressed in the peripheral
CC nervous system while the other are expressed in the central nervous
CC system. Low amounts of the larger forms are also found in limited areas
CC of the CNS.
CC -!- DEVELOPMENTAL STAGE: During the immediate postnatal period, the dorsal
CC root ganglia express all isoforms whereas only the larger forms persist
CC in the adults.
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: Polyubiquitinated. Requires functional TRAF6 and may provoke
CC SQSTM1-dependent degradation by the proteasome (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated at various serine and threonine residues in S-P or
CC T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5,
CC GSK3, MAPK) (a few sites per protein in interphase, more in mitosis),
CC and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-
CC regulating kinase (MARK1, MARK2, MARK3, MARK4), causing detachment from
CC microtubules, and their disassembly (By similarity). Fetal Tau is much
CC more phosphorylated than adult Tau. Phosphorylation at Ser-573 by BRSK1
CC and BRSK2 in neurons affects ability to bind microtubules and plays a
CC role in neuron polarization. Phosphorylated by PHK. Dephosphorylation
CC at several serine and threonine residues by the serine/threonine
CC phosphatase PPP5C. Phosphorylation at Ser-204 by SGK1 mediates
CC microtubule depolymerization and neurite formation in hippocampal
CC neurons (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10636}.
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DR EMBL; M84156; AAA42204.1; -; mRNA.
DR EMBL; X79321; CAA55889.1; -; mRNA.
DR EMBL; D30628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D30629; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A38235; A38235.
DR PIR; JS0306; JS0306.
DR PIR; S46264; S46264.
DR AlphaFoldDB; P19332; -.
DR BMRB; P19332; -.
DR SMR; P19332; -.
DR DIP; DIP-41779N; -.
DR IntAct; P19332; 181.
DR MINT; P19332; -.
DR STRING; 10116.ENSRNOP00000006856; -.
DR BindingDB; P19332; -.
DR ChEMBL; CHEMBL1075117; -.
DR iPTMnet; P19332; -.
DR PhosphoSitePlus; P19332; -.
DR jPOST; P19332; -.
DR PaxDb; P19332; -.
DR PRIDE; P19332; -.
DR UCSC; RGD:69329; rat. [P19332-1]
DR RGD; 69329; Mapt.
DR eggNOG; KOG2418; Eukaryota.
DR InParanoid; P19332; -.
DR PhylomeDB; P19332; -.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR PRO; PR:P19332; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030673; C:axolemma; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0044304; C:main axon; IDA:ARUK-UCL.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IDA:CACAO.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:CAFA.
DR GO; GO:0097418; C:neurofibrillary tangle; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0034399; C:nuclear periphery; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
DR GO; GO:0045298; C:tubulin complex; ISS:UniProtKB.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:ARUK-UCL.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:CAFA.
DR GO; GO:0099609; F:microtubule lateral binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IDA:RGD.
DR GO; GO:0008088; P:axo-dendritic transport; ISO:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:RGD.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; NAS:RGD.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; IMP:RGD.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISO:RGD.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:RGD.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:RGD.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; NAS:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IMP:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:1903829; P:positive regulation of protein localization; ISO:RGD.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:RGD.
DR GO; GO:0051258; P:protein polymerization; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:1900034; P:regulation of cellular response to heat; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:RGD.
DR GO; GO:0060632; P:regulation of microtubule-based movement; ISO:RGD.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0010288; P:response to lead ion; IDA:ARUK-UCL.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
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 Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond;
KW Isopeptide bond; Membrane; Methylation; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CHAIN 2..752
FT /note="Microtubule-associated protein tau"
FT /id="PRO_0000072746"
FT REPEAT 555..585
FT /note="Tau/MAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 586..616
FT /note="Tau/MAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 617..647
FT /note="Tau/MAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 648..679
FT /note="Tau/MAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REGION 1..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 18
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 100
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 466
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 474
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 474
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 513
FT /note="Phosphoserine; by CK1, PDPK1 and TTBK1"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 536
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 542
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 570
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 570
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 592
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 601
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 609
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 622
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 622
FT /note="N6-acetyllysine; 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 632
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 642
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 654
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 658
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 660
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 680
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 696
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 705
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 707
FT /note="Phosphoserine; by CK1 and PDPK1"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 714
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 715
FT /note="Phosphoserine; by CK1 and PDPK1"
FT /evidence="ECO:0000269|PubMed:8245007,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 738
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT DISULFID 602..633
FT /evidence="ECO:0000250"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 642
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 658
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)"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 680
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT VAR_SEQ 34..91
FT /note="Missing (in isoform Tau-F)"
FT /evidence="ECO:0000303|PubMed:8057376"
FT /id="VSP_003191"
FT VAR_SEQ 63..91
FT /note="Missing (in isoform Tau-C and isoform Tau-G)"
FT /evidence="ECO:0000303|PubMed:2504728,
FT ECO:0000303|PubMed:2560640"
FT /id="VSP_003192"
FT VAR_SEQ 114..367
FT /note="Missing (in isoform Tau-C, isoform Tau-D, isoform
FT Tau-E, isoform Tau-F and isoform Tau-G)"
FT /evidence="ECO:0000303|PubMed:2504728,
FT ECO:0000303|PubMed:2560640, ECO:0000303|PubMed:8057376"
FT /id="VSP_003193"
FT VAR_SEQ 387..452
FT /note="Missing (in isoform Tau-B, isoform Tau-C, isoform
FT Tau-E, isoform Tau-F and isoform Tau-G)"
FT /evidence="ECO:0000303|PubMed:1542696,
FT ECO:0000303|PubMed:2504728, ECO:0000303|PubMed:2560640,
FT ECO:0000303|PubMed:8057376, ECO:0000303|PubMed:8408300"
FT /id="VSP_003194"
FT VAR_SEQ 586..616
FT /note="Missing (in isoform Tau-G)"
FT /evidence="ECO:0000303|PubMed:2560640"
FT /id="VSP_003195"
FT VAR_SEQ 752
FT /note="L -> KPVLLSSEVWNYSHDFGHHTDLGL (in isoform Tau-H)"
FT /evidence="ECO:0000303|PubMed:7877441"
FT /id="VSP_003196"
FT CONFLICT 255
FT /note="F -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="H -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="H -> Q (in Ref. 2, 3; CAA55889 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="Y -> H (in Ref. 3; CAA55889)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="P -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ 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
