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P10637

- TAU_MOUSE

UniProt

P10637 - TAU_MOUSE

Protein

Microtubule-associated protein tau

Gene

Mapt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.

    GO - Molecular functioni

    1. lipoprotein particle binding Source: Ensembl
    2. microtubule binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein kinase binding Source: BHF-UCL

    GO - Biological processi

    1. adult walking behavior Source: MGI
    2. axon cargo transport Source: MGI
    3. axon extension Source: MGI
    4. axonogenesis Source: MGI
    5. microtubule cytoskeleton organization Source: UniProtKB
    6. mitochondrion transport along microtubule Source: MGI
    7. negative regulation of intracellular transport Source: MGI
    8. neuron migration Source: MGI
    9. positive regulation of axon extension Source: UniProtKB
    10. positive regulation of microtubule polymerization Source: UniProtKB
    11. regulation of autophagy Source: Ensembl
    12. regulation of microtubule-based movement Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein tau
    Alternative name(s):
    Neurofibrillary tangle protein
    Paired helical filament-tau
    Short name:
    PHF-tau
    Gene namesi
    Name:Mapt
    Synonyms:Mtapt, Tau
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97180. Mapt.

    Subcellular locationi

    Cytoplasmcytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectionaxon
    Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. axoneme Source: MGI
    3. cytoplasm Source: MGI
    4. cytosol Source: UniProtKB-SubCell
    5. growth cone Source: UniProtKB
    6. microtubule Source: UniProtKB-KW
    7. microtubule cytoskeleton Source: MGI
    8. nuclear periphery Source: Ensembl
    9. nucleus Source: MGI
    10. plasma membrane Source: UniProtKB
    11. tubulin complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    May be involved in the pathogenesis of cytoplasmic inclusions (as Mallory bodies) in livers of mice chronically intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-dihydrocollidine), a model for human alcoholic hepatitis. Alteration of Tau (abnormal phosphorylation and cross-linking) could contribute to Mallory bodies formation and disturbance of microtubule function in alcoholic liver disease.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 733732Microtubule-associated protein tauPRO_0000072742Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei18 – 181Phosphotyrosine; by FYNBy similarity
    Modified residuei35 – 351PhosphoserineBy similarity
    Modified residuei188 – 1881Phosphoserine; by SGK1By similarity
    Modified residuei369 – 3691PhosphoserineBy similarity
    Modified residuei445 – 4451PhosphothreonineBy similarity
    Modified residuei467 – 4671PhosphothreonineBy similarity
    Modified residuei473 – 4731PhosphothreonineBy similarity
    Modified residuei489 – 4891PhosphotyrosineBy similarity
    Modified residuei490 – 4901PhosphoserineBy similarity
    Modified residuei491 – 4911PhosphoserineBy similarity
    Modified residuei494 – 4941Phosphoserine; by CK1, PDPK1 and TTBK12 Publications
    Modified residuei497 – 4971Phosphothreonine; by CK1 and PDPK11 Publication
    Modified residuei504 – 5041Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity
    Modified residuei506 – 5061PhosphoserineBy similarity
    Modified residuei509 – 5091PhosphothreonineBy similarity
    Modified residuei523 – 5231Phosphothreonine; by GSK3-beta and PDPK1By similarity
    Modified residuei527 – 5271PhosphoserineBy similarity
    Modified residuei529 – 5291Phosphoserine; by PHKBy similarity
    Modified residuei554 – 5541Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK3 Publications
    Modified residuei577 – 5771Phosphoserine; by PHKBy similarity
    Modified residuei581 – 5811Phosphoserine; by PHKBy similarity
    Disulfide bondi583 ↔ 614By similarity
    Modified residuei585 – 5851PhosphoserineBy similarity
    Modified residuei597 – 5971PhosphoserineBy similarity
    Modified residuei616 – 6161PhosphoserineBy similarity
    Modified residuei644 – 6441Phosphoserine; by PHKBy similarity
    Modified residuei648 – 6481PhosphoserineBy similarity
    Modified residuei688 – 6881Phosphoserine; by CK1 and PDPK12 Publications
    Modified residuei692 – 6921Phosphoserine2 Publications
    Modified residuei695 – 6951PhosphothreonineBy similarity
    Modified residuei696 – 6961Phosphoserine; by CK1 and PDPK12 Publications
    Modified residuei701 – 7011Phosphoserine2 Publications
    Modified residuei708 – 7081PhosphoserineBy similarity
    Modified residuei714 – 7141PhosphoserineBy similarity
    Modified residuei719 – 7191PhosphothreonineBy similarity

    Post-translational modificationi

    Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome By similarity.By similarity
    Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1: CDK1, CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in mitosis), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C. Phosphorylation at Ser-554 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylation at Ser-188 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP10637.
    PaxDbiP10637.
    PRIDEiP10637.

    PTM databases

    PhosphoSiteiP10637.

    Expressioni

    Tissue specificityi

    Expressed in neurons and at a lower level in the liver and kidney. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

    Developmental stagei

    Shorter forms or low molecular weight tau (lMW-tau) are generally expressed at early development stages and longer forms or high molecular weight tau (hMW-tau) in the adult brain.

    Gene expression databases

    ArrayExpressiP10637.
    BgeeiP10637.
    CleanExiMM_MAPT.
    GenevestigatoriP10637.

    Interactioni

    Subunit structurei

    Interacts with SQSTM1 when polyubiquitinated By similarity. Interacts with PSMC2 through SQSTM1. Interacts with FKBP4. Binds to CSNK1D By similarity. Interacts with SGK1 By similarity. Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-369 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bin1O085392EBI-774043,EBI-775152
    Pacsin1Q616445EBI-774043,EBI-2255561

    Protein-protein interaction databases

    BioGridi201589. 9 interactions.
    IntActiP10637. 8 interactions.
    MINTiMINT-3974107.

    Structurei

    3D structure databases

    ProteinModelPortaliP10637.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati536 – 56631Tau/MAP 1Add
    BLAST
    Repeati567 – 59731Tau/MAP 2Add
    BLAST
    Repeati598 – 62831Tau/MAP 3Add
    BLAST
    Repeati629 – 66032Tau/MAP 4Add
    BLAST

    Domaini

    The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.

    Sequence similaritiesi

    Contains 4 Tau/MAP repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG148882.
    GeneTreeiENSGT00530000063491.
    HOVERGENiHBG000991.
    KOiK04380.
    OrthoDBiEOG738045.
    TreeFamiTF316358.

    Family and domain databases

    InterProiIPR027324. MAP2/MAP4/Tau.
    IPR001084. MAP_tubulin-bd_rpt.
    IPR002955. Tau.
    [Graphical view]
    PANTHERiPTHR11501. PTHR11501. 1 hit.
    PfamiPF00418. Tubulin-binding. 4 hits.
    [Graphical view]
    PRINTSiPR01261. TAUPROTEIN.
    PROSITEiPS00229. TAU_MAP_1. 4 hits.
    PS51491. TAU_MAP_2. 4 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist. Isoforms differ from each other by the presence or absence of up to 5 of the 14 exons. One of these optional exons contains the additional tau/MAP repeat. Two different C-termini are obtained either by the retention or the splicing of intron 13/14.

    Isoform PNS-Tau (identifier: P10637-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS    50
    ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT 100
    PNQEDQAAGH VTQGRREGQA PDLGTSDWTR QQVSSMSGAP LLPQGLREAT 150
    CQPSGTRPED IEKSHPASEL LRRGPPQKEG WGQDRLGSEE EVDEDLTVDE 200
    SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG SVPLPADFFS 250
    KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV 300
    VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK 350
    ARVASKDRTG NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS 400
    SPAVSPEPAT SPKHVSSVTP RNGSPGTKQM KLKGADGKTG AKIATPRGAA 450
    SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP PKSGERSGYS SPGSPGTPGS 500
    RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV PMPDLKNVRS 550
    KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI 600
    VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD 650
    NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL 700
    SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL 733
    Length:733
    Mass (Da):76,243
    Last modified:January 23, 2007 - v3
    Checksum:i80C0D50AC5F64E6F
    GO
    Isoform Tau-A (identifier: P10637-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         114-350: Missing.
         368-433: Missing.

    Show »
    Length:430
    Mass (Da):44,893
    Checksum:iE3C55BF8F2F901EC
    GO
    Isoform Tau-B (identifier: P10637-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         34-91: Missing.
         114-350: Missing.
         368-433: Missing.
         567-597: Missing.
         733-733: L → KAALLSSQVWNYSHDLATITDLGL

    Show »
    Length:364
    Mass (Da):38,200
    Checksum:iD1CAB2EF89CDD7C0
    GO
    Isoform Tau-C (identifier: P10637-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         34-91: Missing.
         114-350: Missing.
         368-433: Missing.
         567-597: Missing.

    Show »
    Length:341
    Mass (Da):35,714
    Checksum:i478641931A5A4143
    GO
    Isoform Tau-D (identifier: P10637-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         34-91: Missing.
         114-350: Missing.
         368-433: Missing.

    Show »
    Length:372
    Mass (Da):38,961
    Checksum:iB9427D315AD962B7
    GO
    Isoform Tau-E (identifier: P10637-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         34-91: Missing.
         92-113: Missing.
         114-350: Missing.
         368-433: Missing.

    Show »
    Length:350
    Mass (Da):36,740
    Checksum:i3FB530E1CF1E4CA5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31D → N(PubMed:1374898)Curated
    Sequence conflicti9 – 91D → N(PubMed:1374898)Curated
    Sequence conflicti405 – 4051S → C in CAM14797. (PubMed:19468303)Curated
    Sequence conflicti528 – 5281P → T in CAA78121. (PubMed:7927211)Curated
    Sequence conflicti549 – 5491R → G in AAH14748. (PubMed:15489334)Curated
    Sequence conflicti672 – 6721E → Q(PubMed:1374898)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei34 – 9158Missing in isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E. 3 PublicationsVSP_003185Add
    BLAST
    Alternative sequencei92 – 11322Missing in isoform Tau-E. 1 PublicationVSP_003186Add
    BLAST
    Alternative sequencei114 – 350237Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E. 3 PublicationsVSP_003187Add
    BLAST
    Alternative sequencei368 – 43366Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E. 3 PublicationsVSP_003188Add
    BLAST
    Alternative sequencei567 – 59731Missing in isoform Tau-B and isoform Tau-C. 1 PublicationVSP_003189Add
    BLAST
    Alternative sequencei733 – 7331L → KAALLSSQVWNYSHDLATIT DLGL in isoform Tau-B. 1 PublicationVSP_003190

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12914 mRNA. Translation: AAA58343.1.
    U12915 mRNA. Translation: AAA58344.1.
    U12916 mRNA. Translation: AAA58345.1.
    Z12133 mRNA. Translation: CAA78121.1.
    M93266 mRNA. No translation available.
    M18775 mRNA. Translation: AAA40165.1.
    M18776 mRNA. Translation: AAA40166.1.
    D30627 Genomic DNA. Translation: BAA18878.1.
    AL593843 Genomic DNA. Translation: CAM14797.1.
    BC014748 mRNA. Translation: AAH14748.1.
    CCDSiCCDS25527.1. [P10637-2]
    CCDS25528.1. [P10637-5]
    PIRiA28820.
    A45301.
    B28820.
    RefSeqiNP_001033698.1. NM_001038609.2. [P10637-2]
    NP_001272383.1. NM_001285454.1. [P10637-3]
    NP_001272384.1. NM_001285455.1. [P10637-6]
    NP_001272385.1. NM_001285456.1. [P10637-4]
    NP_034968.3. NM_010838.4. [P10637-5]
    UniGeneiMm.1287.

    Genome annotation databases

    EnsembliENSMUST00000100347; ENSMUSP00000097919; ENSMUSG00000018411. [P10637-2]
    ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411. [P10637-5]
    GeneIDi17762.
    KEGGimmu:17762.
    UCSCiuc007lwf.1. mouse. [P10637-3]
    uc007lwi.1. mouse. [P10637-4]
    uc011yga.1. mouse. [P10637-6]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12914 mRNA. Translation: AAA58343.1 .
    U12915 mRNA. Translation: AAA58344.1 .
    U12916 mRNA. Translation: AAA58345.1 .
    Z12133 mRNA. Translation: CAA78121.1 .
    M93266 mRNA. No translation available.
    M18775 mRNA. Translation: AAA40165.1 .
    M18776 mRNA. Translation: AAA40166.1 .
    D30627 Genomic DNA. Translation: BAA18878.1 .
    AL593843 Genomic DNA. Translation: CAM14797.1 .
    BC014748 mRNA. Translation: AAH14748.1 .
    CCDSi CCDS25527.1. [P10637-2 ]
    CCDS25528.1. [P10637-5 ]
    PIRi A28820.
    A45301.
    B28820.
    RefSeqi NP_001033698.1. NM_001038609.2. [P10637-2 ]
    NP_001272383.1. NM_001285454.1. [P10637-3 ]
    NP_001272384.1. NM_001285455.1. [P10637-6 ]
    NP_001272385.1. NM_001285456.1. [P10637-4 ]
    NP_034968.3. NM_010838.4. [P10637-5 ]
    UniGenei Mm.1287.

    3D structure databases

    ProteinModelPortali P10637.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201589. 9 interactions.
    IntActi P10637. 8 interactions.
    MINTi MINT-3974107.

    PTM databases

    PhosphoSitei P10637.

    Proteomic databases

    MaxQBi P10637.
    PaxDbi P10637.
    PRIDEi P10637.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100347 ; ENSMUSP00000097919 ; ENSMUSG00000018411 . [P10637-2 ]
    ENSMUST00000106992 ; ENSMUSP00000102605 ; ENSMUSG00000018411 . [P10637-5 ]
    GeneIDi 17762.
    KEGGi mmu:17762.
    UCSCi uc007lwf.1. mouse. [P10637-3 ]
    uc007lwi.1. mouse. [P10637-4 ]
    uc011yga.1. mouse. [P10637-6 ]

    Organism-specific databases

    CTDi 4137.
    MGIi MGI:97180. Mapt.

    Phylogenomic databases

    eggNOGi NOG148882.
    GeneTreei ENSGT00530000063491.
    HOVERGENi HBG000991.
    KOi K04380.
    OrthoDBi EOG738045.
    TreeFami TF316358.

    Enzyme and pathway databases

    Reactomei REACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

    Miscellaneous databases

    ChiTaRSi MAPT. mouse.
    NextBioi 292453.
    PROi P10637.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10637.
    Bgeei P10637.
    CleanExi MM_MAPT.
    Genevestigatori P10637.

    Family and domain databases

    InterProi IPR027324. MAP2/MAP4/Tau.
    IPR001084. MAP_tubulin-bd_rpt.
    IPR002955. Tau.
    [Graphical view ]
    PANTHERi PTHR11501. PTHR11501. 1 hit.
    Pfami PF00418. Tubulin-binding. 4 hits.
    [Graphical view ]
    PRINTSi PR01261. TAUPROTEIN.
    PROSITEi PS00229. TAU_MAP_1. 4 hits.
    PS51491. TAU_MAP_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of high molecular weight tau present in the peripheral nervous system."
      Couchie D., Mavilia C., Georgieff I.S., Liem R.K.H., Shelanski M.L., Nunez J.
      Proc. Natl. Acad. Sci. U.S.A. 89:4378-4381(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNS-TAU).
      Tissue: Neuroblastoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A; TAU-D AND TAU-E).
      Strain: Him OF1.
      Tissue: Brain, Kidney and Liver.
    3. "The primary structure and heterogeneity of tau protein from mouse brain."
      Lee G., Cowan N.J., Kirschner M.
      Science 239:285-288(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B AND TAU-C).
      Tissue: Brain.
    4. "Molecular diversity at the carboxyl terminus of human and rat tau."
      Sawa A., Oyama F., Matsushita M., Ihara Y.
      Brain Res. Mol. Brain Res. 27:111-117(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM TAU-B).
      Strain: ICR.
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAU-D).
      Tissue: Eye.
    7. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 504-513; 535-546; 591-609 AND 646-661, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    8. "High molecular weight tau proteins and acquisition of neuronal polarity in peripheral nervous system."
      Couchie D., Gache Y., Mavilia C., Guilleminot J., Bridoux A.-M., Nivez M.-P., Nunez J.
      C. R. Acad. Sci. III, Sci. Vie 316:404-409(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. Cited for: PHOSPHORYLATION BY FYN.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    11. "Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation."
      Babu J.R., Geetha T., Wooten M.W.
      J. Neurochem. 94:192-203(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMC2.
    12. "Mammalian SAD kinases are required for neuronal polarization."
      Kishi M., Pan Y.A., Crump J.G., Sanes J.R.
      Science 307:929-932(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-554.
    13. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    14. "LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons."
      Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W., Raines A.N., Sanes J.R., Polleux F.
      Cell 129:549-563(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-554.
    15. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-688; SER-692 AND SER-696, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiTAU_MOUSE
    AccessioniPrimary (citable) accession number: P10637
    Secondary accession number(s): A2A5Y9
    , P10638, Q60684, Q60685, Q60686, Q62286, Q91WK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3