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TAU_CAPHI
ID   TAU_CAPHI               Reviewed;         403 AA.
AC   O02828;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 117.
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   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A AND TAU-B).
RC   TISSUE=Brain cortex;
RX   PubMed=8858947; DOI=10.1046/j.1471-4159.1996.67041622.x;
RA   Nelson P.T., Stefansson K., Gulcher J., Saper C.B.;
RT   "Molecular evolution of tau protein: implications for Alzheimer's
RT   disease.";
RL   J. Neurochem. 67:1622-1632(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   -!- 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}. Note=Mostly found in the axons of
CC       neurons, in the cytosol and in association with plasma membrane
CC       components. {ECO:0000250|UniProtKB:P10636}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist. Isoforms differ from each
CC         other by the presence or absence of two exons. One of these optional
CC         exons contains the additional tau/MAP repeat.;
CC       Name=Tau-A;
CC         IsoId=O02828-1; Sequence=Displayed;
CC       Name=Tau-B;
CC         IsoId=O02828-2; Sequence=VSP_003173, VSP_003174;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons.
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-224 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}.
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DR   EMBL; S83347; AAB50785.1; -; mRNA.
DR   RefSeq; XP_017920784.1; XM_018065295.1. [O02828-1]
DR   RefSeq; XP_017920788.1; XM_018065299.1. [O02828-2]
DR   AlphaFoldDB; O02828; -.
DR   BMRB; O02828; -.
DR   SMR; O02828; -.
DR   Ensembl; ENSCHIT00000040079; ENSCHIP00000032204; ENSCHIG00000026221. [O02828-1]
DR   GeneID; 100860820; -.
DR   CTD; 4137; -.
DR   GeneTree; ENSGT00940000155494; -.
DR   OrthoDB; 716848at2759; -.
DR   Proteomes; UP000291000; Chromosome 19.
DR   Bgee; ENSCHIG00000026221; Expressed in frontal cortex and 16 other tissues.
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: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   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   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Cytoskeleton; Disulfide bond; Isopeptide bond; Membrane;
KW   Methylation; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CHAIN           2..403
FT                   /note="Microtubule-associated protein tau"
FT                   /id="PRO_0000072737"
FT   REPEAT          206..236
FT                   /note="Tau/MAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REPEAT          237..267
FT                   /note="Tau/MAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REPEAT          268..298
FT                   /note="Tau/MAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REPEAT          299..330
FT                   /note="Tau/MAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REGION          1..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..379
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         71
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         115
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         117
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         125
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         125
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         131
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         138
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         143
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         159
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         167
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         174
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         179
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         187
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         193
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         221
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         221
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         243
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         260
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         273
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         273
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         283
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         293
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         305
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         309
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         311
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         331
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         347
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         356
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         365
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         389
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   DISULFID        253..284
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        216
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CROSSLNK        221
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        229
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        243
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        260
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        273
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CROSSLNK        279
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        283
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        293
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        309
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        315
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CROSSLNK        331
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        337
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        347
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..62
FT                   /note="Missing (in isoform Tau-B)"
FT                   /evidence="ECO:0000303|PubMed:8858947"
FT                   /id="VSP_003173"
FT   VAR_SEQ         237..267
FT                   /note="Missing (in isoform Tau-B)"
FT                   /evidence="ECO:0000303|PubMed:8858947"
FT                   /id="VSP_003174"
SQ   SEQUENCE   403 AA;  41848 MW;  259D0302E1A339C7 CRC64;
     MAEPRQEFDV MEDHAQGDYT LQDHEGDMEP GLKESPLQTP ADDGSEEPGS ETSDAKSTPT
     AEAEEAGIGD TSNLEDQAAG HVTQARMVSK GKDGTGPDDK KAKGADGKPG TKIATPRGAA
     PPGQKGQANA TRIPAKTTPT PKTSPGTGES GKSGDRSGYS SPGSPGTPGS RSRTPSLPTP
     PTREPKKVAV VRTPPKSPSA AKSRLQAAPG PMPDLKNVKS KIGSTENLKH QPGGGKVQII
     NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE
     VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV
     VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL
 
 
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