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P19332

- TAU_RAT

UniProt

P19332 - TAU_RAT

Protein

Microtubule-associated protein tau

Gene

Mapt

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (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. enzyme binding Source: UniProtKB
    2. microtubule binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein domain specific binding Source: RGD
    5. protein kinase binding Source: RGD

    GO - Biological processi

    1. apoptotic process Source: RGD
    2. brain development Source: RGD
    3. female pregnancy Source: RGD
    4. intrinsic apoptotic signaling pathway in response to oxidative stress Source: RGD
    5. microtubule-based process Source: RGD
    6. microtubule cytoskeleton organization Source: UniProtKB
    7. neuron differentiation Source: RGD
    8. positive regulation of axon extension Source: UniProtKB
    9. positive regulation of microtubule polymerization Source: UniProtKB
    10. response to nutrient Source: RGD
    11. response to organic substance Source: RGD

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69329. 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. axonal growth cone Source: UniProtKB
    3. cytosol Source: UniProtKB-SubCell
    4. growth cone Source: UniProtKB
    5. microtubule Source: UniProtKB-KW
    6. neuron projection Source: RGD
    7. plasma membrane Source: UniProtKB
    8. tubulin complex Source: UniProtKB

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 752751Microtubule-associated protein tauPRO_0000072746Add
    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 residuei204 – 2041Phosphoserine; by SGK1By similarity
    Modified residuei388 – 3881PhosphoserineBy similarity
    Modified residuei464 – 4641PhosphothreonineBy similarity
    Modified residuei486 – 4861PhosphothreonineBy similarity
    Modified residuei492 – 4921Phosphothreonine1 Publication
    Modified residuei508 – 5081PhosphotyrosineBy similarity
    Modified residuei509 – 5091Phosphoserine1 Publication
    Modified residuei510 – 5101Phosphoserine1 Publication
    Modified residuei513 – 5131Phosphoserine; by CK1, PDPK1 and TTBK11 Publication
    Modified residuei516 – 5161Phosphothreonine; by CK1 and PDPK1
    Modified residuei523 – 5231Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity
    Modified residuei525 – 5251PhosphoserineBy similarity
    Modified residuei528 – 5281Phosphothreonine1 Publication
    Modified residuei542 – 5421Phosphothreonine; by GSK3-beta and PDPK1By similarity
    Modified residuei546 – 5461Phosphoserine1 Publication
    Modified residuei548 – 5481Phosphoserine; by PHKBy similarity
    Modified residuei573 – 5731Phosphoserine; by MARK1, BRSK1, BRSK2 and PHKBy similarity
    Modified residuei596 – 5961Phosphoserine; by PHKBy similarity
    Modified residuei600 – 6001Phosphoserine; by PHKBy similarity
    Disulfide bondi602 ↔ 633By similarity
    Modified residuei604 – 6041PhosphoserineBy similarity
    Modified residuei616 – 6161PhosphoserineBy similarity
    Modified residuei635 – 6351PhosphoserineBy similarity
    Modified residuei663 – 6631Phosphoserine; by PHKBy similarity
    Modified residuei667 – 6671PhosphoserineBy similarity
    Modified residuei707 – 7071Phosphoserine; by CK1 and PDPK11 Publication
    Modified residuei711 – 7111Phosphoserine1 Publication
    Modified residuei714 – 7141PhosphothreonineBy similarity
    Modified residuei715 – 7151Phosphoserine; by CK1 and PDPK11 Publication
    Modified residuei720 – 7201PhosphoserineBy similarity
    Modified residuei727 – 7271PhosphoserineBy similarity
    Modified residuei733 – 7331PhosphoserineBy similarity
    Modified residuei738 – 7381PhosphothreonineBy similarity

    Post-translational modificationi

    Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome By similarity.By similarity
    Phosphorylated 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. Fetal Tau is much more phosphorylated than adult Tau. Phosphorylation at Ser-573 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C. Phosphorylation at Ser-204 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

    PaxDbiP19332.
    PRIDEiP19332.

    PTM databases

    PhosphoSiteiP19332.

    Expressioni

    Tissue specificityi

    Expressed in neurons. The larger forms (isoform tau-A and isoform tau-B) are preferentially expressed in the peripheral nervous system while the other are expressed in the central nervous system. Low amounts of the larger forms are also found in limited areas of the CNS.

    Developmental stagei

    During the immediate postnatal period, the dorsal root ganglia express all isoforms whereas only the larger forms persist in the adults.

    Gene expression databases

    GenevestigatoriP19332.

    Interactioni

    Subunit structurei

    Interacts with SQSTM1 when polyubiquitinated. Interacts with PSMC2 through SQSTM1. Binds to CSNK1D By similarity. Interacts with FKBP4. Interacts with SGK1 By similarity. Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-388 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A6NAR82EBI-7080713,EBI-8755852From a different organism.
    Pacsin1Q616446EBI-8758676,EBI-2255561From a different organism.

    Protein-protein interaction databases

    DIPiDIP-41779N.
    IntActiP19332. 3 interactions.
    MINTiMINT-1037362.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati555 – 58531Tau/MAP 1Add
    BLAST
    Repeati586 – 61631Tau/MAP 2Add
    BLAST
    Repeati617 – 64731Tau/MAP 3Add
    BLAST
    Repeati648 – 67932Tau/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.
    HOGENOMiHOG000231029.
    HOVERGENiHBG000991.
    PhylomeDBiP19332.

    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 (8)i

    Sequence statusi: Complete.

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

    This entry describes 8 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 4 of the 14 exons. Two different C-termini are obtained either by the retention or the splicing of intron 13/14.

    Isoform Tau-A (identifier: P19332-1) [UniParc]FASTAAdd to Basket

    Also known as: SC1

    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

    MAEPRQEFDT MEDQAGDYTM LQDQEGDMDH GLKESPPQPP ADDGSEEPGS    50
    ETSDAKSTPT AEDVTAPLVE ERAPDKQATA QSHTEIPEGT TAEEAGIGDT 100
    PNMEDQAAGH VTQEPQKVEI FSQSLLVEPG RREGQAPDSG ISDWTHQQVP 150
    SMSGAPLPPQ GLREATHQPL GTRPEDVERS HPASELLWQE SPQKEAWGKD 200
    RLGSEEEVDE DITMDESSQE SPPSQASLAP GTATPQARSV SASGVSGETT 250
    SIPGFPAEGS IPLPADFFSK VSAETQASPP EGPGTGPSEE GHEAAPEFTF 300
    HVEIKASAPK EQDLEGATVV GAPAEEQKAR GPSVGKGTKE ASLLEPTDKQ 350
    PAAGLPGRPV SRVPQLKARV AGVSKDRTGN DEKKAKTSTP SCAKTPSNRP 400
    CLSPTRPTPG SSDPLIKPSS PAVCPEPATS PKYVSSVTPR NGSPGTKQMK 450
    LKGADGKTGA KIATPRGAAT PGQKGTSNAT RIPAKTTPSP KTPPGSGEPP 500
    KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSAS 550
    KSRLQTAPVP MPDLKNVRSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS 600
    KCGSKDNIKH VPGGGSVHIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV 650
    KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG 700
    AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ 750
    GL 752
    Length:752
    Mass (Da):78,564
    Last modified:January 23, 2007 - v3
    Checksum:i915DCA04EF0B2902
    GO
    Isoform Tau-B (identifier: P19332-2) [UniParc]FASTAAdd to Basket

    Also known as: Big-tau, HMW-tau

    The sequence of this isoform differs from the canonical sequence as follows:
         387-452: Missing.

    Show »
    Length:686
    Mass (Da):71,774
    Checksum:iF3709D1844C3763D
    GO
    Isoform Tau-C (identifier: P19332-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         63-91: Missing.
         114-367: Missing.
         387-452: Missing.

    Show »
    Length:403
    Mass (Da):42,048
    Checksum:i4ED13493B947A5E7
    GO
    Isoform Tau-D (identifier: P19332-4) [UniParc]FASTAAdd to Basket

    Also known as: SC2

    The sequence of this isoform differs from the canonical sequence as follows:
         114-367: Missing.

    Show »
    Length:498
    Mass (Da):51,912
    Checksum:i6DC5958544984730
    GO
    Isoform Tau-E (identifier: P19332-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         114-367: Missing.
         387-452: Missing.

    Show »
    Length:432
    Mass (Da):45,122
    Checksum:iBBBC0DF6D0394D72
    GO
    Isoform Tau-F (identifier: P19332-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         34-91: Missing.
         114-367: Missing.
         387-452: Missing.

    Show »
    Length:374
    Mass (Da):39,152
    Checksum:i2323D277377BDBB7
    GO
    Isoform Tau-G (identifier: P19332-7) [UniParc]FASTAAdd to Basket

    Also known as: Fetal-tau

    The sequence of this isoform differs from the canonical sequence as follows:
         63-91: Missing.
         114-367: Missing.
         387-452: Missing.
         586-616: Missing.

    Show »
    Length:372
    Mass (Da):38,801
    Checksum:iD4A2BD9C6DEAD376
    GO
    Isoform Tau-H (identifier: P19332-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         752-752: L → KPVLLSSEVWNYSHDFGHHTDLGL

    Show »
    Length:775
    Mass (Da):81,185
    Checksum:iAF16994BB897B2DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551F → L(PubMed:8408300)Curated
    Sequence conflicti284 – 2841G → A(PubMed:8408300)Curated
    Sequence conflicti292 – 2921H → D(PubMed:8408300)Curated
    Sequence conflicti618 – 6181H → Q(PubMed:8408300)Curated
    Sequence conflicti618 – 6181H → Q in CAA55889. (PubMed:8057376)Curated
    Sequence conflicti618 – 6181H → Q(PubMed:2560640)Curated
    Sequence conflicti705 – 7051Y → H in CAA55889. (PubMed:8057376)Curated
    Sequence conflicti734 – 7341P → A(PubMed:8408300)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei34 – 9158Missing in isoform Tau-F. 1 PublicationVSP_003191Add
    BLAST
    Alternative sequencei63 – 9129Missing in isoform Tau-C and isoform Tau-G. 2 PublicationsVSP_003192Add
    BLAST
    Alternative sequencei114 – 367254Missing in isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Tau-G. 3 PublicationsVSP_003193Add
    BLAST
    Alternative sequencei387 – 45266Missing in isoform Tau-B, isoform Tau-C, isoform Tau-E, isoform Tau-F and isoform Tau-G. 5 PublicationsVSP_003194Add
    BLAST
    Alternative sequencei586 – 61631Missing in isoform Tau-G. 1 PublicationVSP_003195Add
    BLAST
    Alternative sequencei752 – 7521L → KPVLLSSEVWNYSHDFGHHT DLGL in isoform Tau-H. 1 PublicationVSP_003196

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84156 mRNA. Translation: AAA42204.1.
    X79321 mRNA. Translation: CAA55889.1.
    D30628 Genomic DNA. No translation available.
    D30629 mRNA. No translation available.
    PIRiA38235.
    JS0306.
    S46264.
    UniGeneiRn.2455.

    Genome annotation databases

    UCSCiRGD:69329. rat. [P19332-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84156 mRNA. Translation: AAA42204.1 .
    X79321 mRNA. Translation: CAA55889.1 .
    D30628 Genomic DNA. No translation available.
    D30629 mRNA. No translation available.
    PIRi A38235.
    JS0306.
    S46264.
    UniGenei Rn.2455.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-41779N.
    IntActi P19332. 3 interactions.
    MINTi MINT-1037362.

    Chemistry

    BindingDBi P19332.
    ChEMBLi CHEMBL1075117.

    PTM databases

    PhosphoSitei P19332.

    Proteomic databases

    PaxDbi P19332.
    PRIDEi P19332.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:69329. rat. [P19332-1 ]

    Organism-specific databases

    RGDi 69329. Mapt.

    Phylogenomic databases

    eggNOGi NOG148882.
    HOGENOMi HOG000231029.
    HOVERGENi HBG000991.
    PhylomeDBi P19332.

    Miscellaneous databases

    PROi P19332.

    Gene expression databases

    Genevestigatori P19332.

    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. "Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system."
      Goedert M., Spillantini M.G., Crowther R.A.
      Proc. Natl. Acad. Sci. U.S.A. 89:1983-1987(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
      Tissue: Pheochromocytoma.
    2. "Expression of high molecular weight tau in the central and peripheral nervous systems."
      Georgieff I.S., Liem R.K.H., Couchie D., Mavilia C., Nunez J., Shelanski M.L.
      J. Cell Sci. 105:729-737(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
      Tissue: Spinal ganglion.
    3. "Complete sequence of 3'-untranslated region of tau from rat central nervous system. Implications for mRNA heterogeneity."
      Sadot E., Marx R., Barg J., Behar L., Ginzburg I.
      J. Mol. Biol. 241:325-331(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-F).
      Strain: Wistar.
      Tissue: Brain.
    4. "Developmentally regulated expression of specific tau sequences."
      Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L.
      Neuron 2:1389-1397(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-G).
      Tissue: Brain.
    5. "Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA."
      Kanai Y., Takemura R., Oshima T., Mori H., Ihara Y., Yanagisawa M., Masaki T., Hirokawa N.
      J. Cell Biol. 109:1173-1184(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-C).
    6. "Diversity of high-molecular-weight tau proteins in different regions of the nervous system."
      Mavilia C., Couchie D., Nunez J.
      J. Neurochem. 63:2300-2306(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 360-461 (ISOFORM TAU-A), NUCLEOTIDE SEQUENCE OF 106-113 AND 368-461 (ISOFORM TAU-D).
      Tissue: Spinal cord.
    7. "In vivo phosphorylation sites in fetal and adult rat tau."
      Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M., Titani K., Arai T., Kosik K.S., Ihara Y.
      J. Biol. Chem. 268:25712-25717(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 492-501; 506-515; 523-532; 537-551 AND 698-726, PHOSPHORYLATION AT THR-492; SER-509; SER-510; SER-513; THR-528; THR-542; SER-546; SER-707; SER-711 AND SER-715.
    8. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 697-752 (ISOFORMS TAU-A; TAU-B; TAU-C; TAU-D; TAU-E; TAU-F AND TAU-G), NUCLEOTIDE SEQUENCE [MRNA] OF 752-775 (ISOFORM TAU-H).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    9. Cited for: INTERACTION WITH FKBP4.

    Entry informationi

    Entry nameiTAU_RAT
    AccessioniPrimary (citable) accession number: P19332
    Secondary accession number(s): Q63567, Q63677, Q9QW06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3