TAU_BOVIN
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 03-AUG-2022, entry version 178.
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}.
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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 STRING; 9913.ENSBTAP00000054412; -.
DR BindingDB; P29172; -.
DR ChEMBL; CHEMBL3638363; -.
DR iPTMnet; P29172; -.
DR PaxDb; P29172; -.
DR Ensembl; ENSBTAT00000042687; ENSBTAP00000040320; ENSBTAG00000017512. [P29172-6]
DR Ensembl; ENSBTAT00000064492; ENSBTAP00000054412; ENSBTAG00000017512. [P29172-15]
DR Ensembl; ENSBTAT00000065509; ENSBTAP00000056351; ENSBTAG00000017512. [P29172-16]
DR Ensembl; ENSBTAT00000065660; ENSBTAP00000056547; ENSBTAG00000017512. [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 OrthoDB; 480212at2759; -.
DR TreeFam; TF316358; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000017512; Expressed in prefrontal cortex and 99 other tissues.
DR ExpressionAtlas; P29172; baseline.
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:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1905689; P:positive regulation of diacylglycerol kinase activity; IDA:ParkinsonsUK-UCL.
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; 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
