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 24-JAN-2024, entry version 192. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 182. DR MINT; P19332; -. DR STRING; 10116.ENSRNOP00000040951; -. DR BindingDB; P19332; -. DR ChEMBL; CHEMBL1075117; -. DR GlyGen; P19332; 7 sites, 1 O-linked glycan (7 sites). DR iPTMnet; P19332; -. DR PhosphoSitePlus; P19332; -. DR jPOST; P19332; -. DR PaxDb; 10116-ENSRNOP00000006856; -. DR UCSC; RGD:69329; rat. [P19332-1] DR AGR; RGD:69329; -. 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 Reactome; R-RNO-9833482; PKR-mediated signaling. 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; IBA:GO_Central. 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: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:0051087; F:protein-folding chaperone binding; IPI:ARUK-UCL. 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: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:0006974; P:DNA damage response; ISO:RGD. DR GO; GO:0007565; P:female pregnancy; IEP:RGD. DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:RGD. DR GO; GO:0046907; P:intracellular transport; 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: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: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: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; IPR027324; MAP2/MAP4/Tau. DR InterPro; IPR001084; MAP_tubulin-bd_rpt. DR InterPro; IPR002955; Tau. DR PANTHER; PTHR11501; MICROTUBULE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR11501:SF14; MICROTUBULE-ASSOCIATED PROTEIN TAU; 1. 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 //