ID TAU_BOVIN Reviewed; 448 AA. AC P29172; P29173; Q28185; Q28186; Q28187; Q28188; Q28189; Q28190; Q32KT2; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 184. DE RecName: Full=Microtubule-associated protein tau; DE AltName: Full=Neurofibrillary tangle protein; DE AltName: Full=Paired helical filament-tau; DE Short=PHF-tau; GN Name=MAPT; Synonyms=TAU; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A; TAU-B; TAU-G AND TAU-H). RC TISSUE=Brain; RX PubMed=2498649; DOI=10.1128/mcb.9.4.1381-1388.1989; RA Himmler A., Drechsel D., Kirschner M.W., Martin D.W. Jr.; RT "Tau consists of a set of proteins with repeated C-terminal microtubule- RT binding domains and variable N-terminal domains."; RL Mol. Cell. Biol. 9:1381-1388(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TAU-A; TAU-B; TAU-C; TAU-D; RP TAU-E; TAU-F; TAU-I; TAU-J; TAU-K; TAU-L; TAU-M; TAU-N; TAU-O; TAU-P; RP TAU-Q; TAU-R; TAU-S AND TAU-T). RC TISSUE=Brain; RX PubMed=2498650; DOI=10.1128/mcb.9.4.1389-1396.1989; RA Himmler A.; RT "Structure of the bovine tau gene: alternatively spliced transcripts RT generate a protein family."; RL Mol. Cell. Biol. 9:1389-1396(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAU-F). RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP GLYCOSYLATION. RX PubMed=8910513; DOI=10.1074/jbc.271.46.28741; RA Arnold C.S., Johnson G.V.W., Cole R.N., Dong D.L.-Y., Lee M., Hart G.W.; RT "The microtubule-associated protein tau is extensively modified with O- RT linked N-acetylglucosamine."; RL J. Biol. Chem. 271:28741-28744(1996). 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 (By CC similarity). Binds to CSNK1D (By similarity). Interacts with SGK1 (By CC similarity). Interacts with PIN1 (By similarity). Interacts with LRRK2 CC (By similarity). Interacts with LRP1, leading to endocytosis; this CC interaction is reduced in the presence of LRPAP1/RAP (By similarity). CC {ECO:0000250|UniProtKB:P10636, ECO:0000250|UniProtKB:P10637, CC ECO:0000250|UniProtKB:P19332}. CC -!- INTERACTION: CC P29172; P63104: YWHAZ; Xeno; NbExp=2; IntAct=EBI-7291149, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral CC membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell CC projection, axon. Cytoplasm {ECO:0000250|UniProtKB:P10636}. Cell CC projection, dendrite {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. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=20; CC Comment=Additional isoforms seem to exist. Isoforms differ from each CC other by the presence or absence of up to 6 of the 14 exons. One of CC these optional exons contains the additional tau/MAP repeat. Tau-A CC cDNA has been constructed from two overlapping cDNAs by CC PubMed:2498649: Tau-G and Tau-H sequences begin with exon 6 or a part CC of it (exon 6 is missing in isoforms that begin with exon 1). 3 CC different C-termini are obtained either by the retention or the CC splicing of intron 13/14 (2 different 5' splice donors).; CC Name=Tau-A; Synonyms=PBT43I12; CC IsoId=P29172-1; Sequence=Displayed; CC Name=Tau-B; Synonyms=PBT43-12; CC IsoId=P29172-2; Sequence=VSP_003169; CC Name=Tau-C; CC IsoId=P29172-3; Sequence=VSP_003169, VSP_003170; CC Name=Tau-D; CC IsoId=P29172-4; Sequence=VSP_003167; CC Name=Tau-E; CC IsoId=P29172-5; Sequence=VSP_003167, VSP_003169; CC Name=Tau-F; CC IsoId=P29172-6; Sequence=VSP_003167, VSP_003169, VSP_003170; CC Name=Tau-G; Synonyms=PBT4; CC IsoId=P29172-7; Sequence=VSP_003165, VSP_003169; CC Name=Tau-H; Synonyms=PBT7; CC IsoId=P29172-8; Sequence=VSP_003166, VSP_003169; CC Name=Tau-I; CC IsoId=P29172-9; Sequence=VSP_003171; CC Name=Tau-J; CC IsoId=P29172-10; Sequence=VSP_003167, VSP_003169, VSP_003171; CC Name=Tau-K; CC IsoId=P29172-11; Sequence=VSP_003167, VSP_003169, VSP_003170, CC VSP_003171; CC Name=Tau-L; CC IsoId=P29172-12; Sequence=VSP_003167, VSP_003168, VSP_003171; CC Name=Tau-M; CC IsoId=P29172-13; Sequence=VSP_003167, VSP_003168, VSP_003169, CC VSP_003171; CC Name=Tau-N; CC IsoId=P29172-14; Sequence=VSP_003167, VSP_003168, VSP_003169, CC VSP_003170, VSP_003171; CC Name=Tau-O; CC IsoId=P29172-15; Sequence=VSP_003172; CC Name=Tau-P; CC IsoId=P29172-16; Sequence=VSP_003167, VSP_003169, VSP_003172; CC Name=Tau-Q; CC IsoId=P29172-17; Sequence=VSP_003167, VSP_003169, VSP_003170, CC VSP_003172; CC Name=Tau-R; CC IsoId=P29172-18; Sequence=VSP_003167, VSP_003168, VSP_003172; CC Name=Tau-S; CC IsoId=P29172-19; Sequence=VSP_003167, VSP_003168, VSP_003169, CC VSP_003172; CC Name=Tau-T; CC IsoId=P29172-20; Sequence=VSP_003167, VSP_003168, VSP_003169, CC VSP_003170, VSP_003172; CC -!- TISSUE SPECIFICITY: Expressed in neurons. CC -!- INDUCTION: During neurite outgrowth. 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: Phosphorylation 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). Phosphorylation at CC Ser-269 by BRSK1 and BRSK2 in neurons affects ability to bind CC microtubules and plays a role in neuron polarization. Phosphorylated by CC PHK. Dephosphorylation at several serine and threonine residues by the CC serine/threonine phosphatase PPP5C (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P10636}. CC -!- PTM: O-glycosylated; contains at least 4 GlcNAc. Site-specific or CC stoichiometric changes in glycosylation may modulate tau function and CC also play a role in PHF's formation. {ECO:0000269|PubMed:8910513}. 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; L34953; AAA51609.1; -; mRNA. DR EMBL; L34940; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34942; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34943; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34947; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34949; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; L34952; AAA51609.1; JOINED; Genomic_DNA. DR EMBL; M26157; AAA30770.1; -; mRNA. DR EMBL; M26158; AAA30771.1; -; mRNA. DR EMBL; M26178; AAA51601.1; ALT_SEQ; Genomic_DNA. DR EMBL; L34940; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34942; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34943; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34947; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34949; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51601.1; JOINED; Genomic_DNA. DR EMBL; M26178; AAA51602.1; ALT_SEQ; Genomic_DNA. DR EMBL; L34940; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34943; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34949; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51602.1; JOINED; Genomic_DNA. DR EMBL; M26178; AAA51603.1; ALT_SEQ; Genomic_DNA. DR EMBL; L34940; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34943; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51603.1; JOINED; Genomic_DNA. DR EMBL; M26178; AAA51604.1; ALT_SEQ; Genomic_DNA. DR EMBL; L34940; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34947; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34949; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51604.1; JOINED; Genomic_DNA. DR EMBL; M26178; AAA51605.1; ALT_SEQ; Genomic_DNA. DR EMBL; L34940; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34949; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51605.1; JOINED; Genomic_DNA. DR EMBL; M26178; AAA51606.1; ALT_SEQ; Genomic_DNA. DR EMBL; L34940; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; L34941; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; L34944; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; L34946; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; L34948; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; L34950; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; L34951; AAA51606.1; JOINED; Genomic_DNA. DR EMBL; BC109941; AAI09942.1; -; mRNA. DR PIR; A31939; QRBOT1. DR PIR; B31939; QRBOT2. DR RefSeq; NP_776531.1; NM_174106.2. [P29172-1] DR AlphaFoldDB; P29172; -. DR BMRB; P29172; -. DR SMR; P29172; -. DR BioGRID; 158649; 7. DR IntAct; P29172; 4. DR MINT; P29172; -. DR BindingDB; P29172; -. DR ChEMBL; CHEMBL3638363; -. DR iPTMnet; P29172; -. DR PaxDb; 9913-ENSBTAP00000054412; -. DR Ensembl; ENSBTAT00000042687.4; ENSBTAP00000040320.4; ENSBTAG00000017512.6. [P29172-6] DR Ensembl; ENSBTAT00000064492.2; ENSBTAP00000054412.1; ENSBTAG00000017512.6. [P29172-15] DR Ensembl; ENSBTAT00000065509.2; ENSBTAP00000056351.2; ENSBTAG00000017512.6. [P29172-16] DR Ensembl; ENSBTAT00000065660.2; ENSBTAP00000056547.1; ENSBTAG00000017512.6. [P29172-18] DR GeneID; 281296; -. DR KEGG; bta:281296; -. DR CTD; 4137; -. DR VEuPathDB; HostDB:ENSBTAG00000017512; -. DR eggNOG; KOG2418; Eukaryota. DR GeneTree; ENSGT00940000155494; -. DR HOGENOM; CLU_021741_3_1_1; -. DR InParanoid; P29172; -. DR TreeFam; TF316358; -. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000017512; Expressed in prefrontal cortex and 99 other cell types or tissues. DR ExpressionAtlas; P29172; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008017; F:microtubule binding; IEA:InterPro. DR GO; GO:1905689; P:positive regulation of diacylglycerol kinase activity; IDA:ParkinsonsUK-UCL. 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; Disulfide bond; Glycoprotein; Isopeptide bond; KW Membrane; Methylation; Microtubule; Phosphoprotein; Reference proteome; KW Repeat; Secreted; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P10636" FT CHAIN 2..448 FT /note="Microtubule-associated protein tau" FT /id="PRO_0000072736" FT REPEAT 251..281 FT /note="Tau/MAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824" FT REPEAT 282..312 FT /note="Tau/MAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824" FT REPEAT 313..343 FT /note="Tau/MAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824" FT REPEAT 344..375 FT /note="Tau/MAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824" FT REGION 1..264 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 405..424 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 121..136 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..179 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..424 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 19 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19332" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19332" FT MOD_RES 58 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 60 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P19332" FT MOD_RES 100 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 144 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 146 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 154 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 154 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 160 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 166 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 167 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 172 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 204 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 212 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 219 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 221 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 224 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 232 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 238 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 242 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 266 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 266 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 288 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 296 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 297 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 305 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 318 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 318 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 324 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 328 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 338 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 350 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 354 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 356 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 376 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 392 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 401 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 403 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 410 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10637" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 416 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 429 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT MOD_RES 434 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10636" FT DISULFID 298..329 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 261 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P10636" FT CROSSLNK 266 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 274 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 288 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 305 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 318 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10636" FT CROSSLNK 324 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 328 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 338 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 350 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 354 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 360 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P10636" FT CROSSLNK 376 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 382 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P10637" FT CROSSLNK 392 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..131 FT /note="MAEPRQEFDVMEDHAQGDYTLQDQEGDMDPGLKESPLQTPADDGSEEPGSET FT SDAKSTPTAEDATAPLVDEGAPGEQAAAQAPAEIPEGTAAEEAGIGDTSNLEDQAAGHV FT TQARMVSKGKDGTGPDDKKT -> MPLNHYLPYLFLVSVLFQFVPFSHVLTFILILFMF FT MFKPSTPSSAKTLKNRPCLSPKRPTPGSSDPLIKPSSPAVCPEPSSSPKHVSSVTPRTG FT NSGAKEMKVK (in isoform Tau-G)" FT /evidence="ECO:0000303|PubMed:2498649" FT /id="VSP_003165" FT VAR_SEQ 1..131 FT /note="MAEPRQEFDVMEDHAQGDYTLQDQEGDMDPGLKESPLQTPADDGSEEPGSET FT SDAKSTPTAEDATAPLVDEGAPGEQAAAQAPAEIPEGTAAEEAGIGDTSNLEDQAAGHV FT TQARMVSKGKDGTGPDDKKT -> MKVK (in isoform Tau-H)" FT /evidence="ECO:0000303|PubMed:2498649" FT /id="VSP_003166" FT VAR_SEQ 63..91 FT /note="Missing (in isoform Tau-D, isoform Tau-E, isoform FT Tau-F, isoform Tau-J, isoform Tau-K, isoform Tau-L, isoform FT Tau-M, isoform Tau-N, isoform Tau-P, isoform Tau-Q, isoform FT Tau-R, isoform Tau-S and isoform Tau-T)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_003167" FT VAR_SEQ 92..113 FT /note="Missing (in isoform Tau-L, isoform Tau-M, isoform FT Tau-N, isoform Tau-R, isoform Tau-S and isoform Tau-T)" FT /evidence="ECO:0000305" FT /id="VSP_003168" FT VAR_SEQ 175..192 FT /note="Missing (in isoform Tau-B, isoform Tau-C, isoform FT Tau-E, isoform Tau-F, isoform Tau-G, isoform Tau-H, isoform FT Tau-J, isoform Tau-K, isoform Tau-M, isoform Tau-N, isoform FT Tau-P, isoform Tau-Q, isoform Tau-S and isoform Tau-T)" FT /evidence="ECO:0000303|PubMed:2498649, ECO:0000303|Ref.3" FT /id="VSP_003169" FT VAR_SEQ 282..312 FT /note="Missing (in isoform Tau-C, isoform Tau-F, isoform FT Tau-K, isoform Tau-N, isoform Tau-Q and isoform Tau-T)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_003170" FT VAR_SEQ 439..448 FT /note="VSASLAKQGL -> PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPS FT R (in isoform Tau-I, isoform Tau-J, isoform Tau-K, isoform FT Tau-L, isoform Tau-M and isoform Tau-N)" FT /evidence="ECO:0000305" FT /id="VSP_003171" FT VAR_SEQ 447..448 FT /note="GL -> ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPM FT GRHLLYTKGEVKEGEVQTPGPPSL (in isoform Tau-O, isoform Tau-P, FT isoform Tau-Q, isoform Tau-R, isoform Tau-S and isoform FT Tau-T)" FT /evidence="ECO:0000305" FT /id="VSP_003172" SQ SEQUENCE 448 AA; 46333 MW; 821638A9C4809602 CRC64; MAEPRQEFDV MEDHAQGDYT LQDQEGDMDP GLKESPLQTP ADDGSEEPGS ETSDAKSTPT AEDATAPLVD EGAPGEQAAA QAPAEIPEGT AAEEAGIGDT SNLEDQAAGH VTQARMVSKG KDGTGPDDKK TKGADGKPGT KIATPRGAAP PGQKGQANAT RIPAKTTPTP KTSPATMQVQ KKPPPAGAKS ERGESGKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP KKVAVVRTPP KSPSAAKSRL QAAPGPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG GGQVEVKSEK LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK AKTDHGAEIV YKSPVVSGDT SPRHLSNVSS TGSIDMVDSP QLATLADEVS ASLAKQGL //