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Q6TS35

- TAU_SPECI

UniProt

Q6TS35 - TAU_SPECI

Protein

Microtubule-associated protein tau

Gene

MAPT

Organism
Spermophilus citellus (European suslik) (Citellus citellus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (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.1 Publication

    GO - Biological processi

    1. hibernation Source: UniProtKB-KW

    Keywords - Biological processi

    Hibernation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein tau
    Gene namesi
    Name:MAPT
    OrganismiSpermophilus citellus (European suslik) (Citellus citellus)
    Taxonomic identifieri9997 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniSpermophilus

    Subcellular locationi

    Cytoplasmcytosol By similarity. 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.By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB-SubCell
    3. microtubule Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    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 – 430429Microtubule-associated protein tauPRO_0000232454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei18 – 181Phosphotyrosine; by FYNBy similarity
    Modified residuei33 – 331PhosphoserineBy similarity
    Modified residuei37 – 371PhosphothreonineBy similarity
    Modified residuei142 – 1421PhosphothreonineBy similarity
    Modified residuei164 – 1641PhosphothreonineBy similarity
    Modified residuei170 – 1701Phosphothreonine1 Publication
    Modified residuei186 – 1861PhosphotyrosineBy similarity
    Modified residuei187 – 1871Phosphoserine1 Publication
    Modified residuei188 – 1881Phosphoserine1 Publication
    Modified residuei191 – 1911Phosphoserine; by CK1, PDPK1 and TTBK11 Publication
    Modified residuei194 – 1941Phosphothreonine; by CK1 and PDPK11 Publication
    Modified residuei199 – 1991Phosphoserine1 Publication
    Modified residuei201 – 2011Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity
    Modified residuei203 – 2031PhosphoserineBy similarity
    Modified residuei206 – 2061PhosphothreonineBy similarity
    Modified residuei220 – 2201Phosphothreonine; by GSK3-beta and PDPK1By similarity
    Modified residuei224 – 2241PhosphoserineBy similarity
    Modified residuei226 – 2261Phosphoserine; by PHKBy similarity
    Modified residuei251 – 2511Phosphoserine; also in form PHF-tau-like found during hibernation; by MARK1, BRSK1, BRSK2 and PHK1 Publication
    Modified residuei274 – 2741Phosphoserine; by PHKBy similarity
    Modified residuei278 – 2781Phosphoserine; by PHKBy similarity
    Disulfide bondi280 ↔ 311By similarity
    Modified residuei282 – 2821PhosphoserineBy similarity
    Modified residuei294 – 2941PhosphoserineBy similarity
    Modified residuei313 – 3131PhosphoserineBy similarity
    Modified residuei341 – 3411Phosphoserine; by PHKBy similarity
    Modified residuei345 – 3451Phosphoserine; in form PHF-tau-like found during hibernation1 Publication
    Modified residuei385 – 3851Phosphoserine; by CK1 and PDPK11 Publication
    Modified residuei389 – 3891PhosphoserineBy similarity
    Modified residuei392 – 3921PhosphothreonineBy similarity
    Modified residuei393 – 3931Phosphoserine; by CK1 and PDPK11 Publication
    Modified residuei398 – 3981PhosphoserineBy similarity
    Modified residuei405 – 4051PhosphoserineBy similarity
    Modified residuei411 – 4111PhosphoserineBy similarity
    Modified residuei416 – 4161PhosphothreonineBy 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. Phosphorylation at Ser-345 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 By similarity.By similarity
    Hyperphosphorylated (in particular at Thr-170, Ser-191, Thr-194, Ser-251, and Ser-345) during hibernation. Phosphorylation is fully reversible after arousal. Highly phosphorylated tau contains a number of paired helical filaments (PHFs)-like epitopes. PHF-like phosphorylation is not associated with fibril formation. Distribution of PHF-like tau is more intense in the entorhinal cortex, hippocampus and isocortical areas. PHF-like phosphorylation-dephosphorylation during hibernation cycle is synchronized with regression-re-establishment of afferentation. It may reflect a protective mechanism in an unfavorable environment.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ6TS35.

    Interactioni

    Subunit structurei

    Interacts with SQSTM1 when polyubiquitinated. Interacts with PSMC2 through SQSTM1 By similarity. Interacts with FKBP4. Binds to CSNK1D By similarity.By similarity

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati233 – 26331Tau/MAP 1Add
    BLAST
    Repeati264 – 29431Tau/MAP 2Add
    BLAST
    Repeati295 – 32531Tau/MAP 3Add
    BLAST
    Repeati326 – 35732Tau/MAP 4Add
    BLAST

    Domaini

    The tau/MAP repeat binds to tubulin.By similarity

    Sequence similaritiesi

    Contains 4 Tau/MAP repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOVERGENiHBG000991.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. 6 isoforms have been detected in the adult brain. The pattern of isoforms and their relative expression levels are unaffected during hibernation cycle.

    Isoform 1 (identifier: Q6TS35-1) [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.

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    MAEPRQEFDT AEDHAEGYAL LQDQEGEHGL KASPLQTPAD DGPEEPVSET    50
    SDAKSTPTAE DVTAPLVDER TPGEQAATQP PTDIPEGTTA EEAGIGDTPN 100
    MEDQAAGHVT QARMVSKGKE GTGSEDRKAK GADSKTGTKI ATPRGTAPPG 150
    QKGTANATRI PAKTTPSPKT PPGTGEPAKS GDRSGYSSPG SPGTPGSRSR 200
    TPSLPTPPTR EPKKVAVVRT PPKSPSSTKS RLQTAPVPMP DLKNVRSKIG 250
    STENLKHQPG GGKVQIINKK LDLSNVQSKC GSKDNIKHVP GGGSVQIVYK 300
    PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ SKIGSLDNIT 350
    HVPGGGNKKI ETHKLTFREN AKAKTDHGAE IVYKSPVVSG DTSPRHLSNV 400
    SSTGSINMVD SPQLATLADE VSASLAKQGL 430
    Length:430
    Mass (Da):44,803
    Last modified:January 23, 2007 - v3
    Checksum:i5ED2B0EB0DFADAF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY388477 mRNA. Translation: AAQ92319.1.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Vita minima - Issue 68 of March 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY388477 mRNA. Translation: AAQ92319.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q6TS35.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG000991.

    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. "Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals."
      Arendt T., Stieler J., Strijkstra A.M., Hut R.A., Ruediger J., Van der Zee E.A., Harkany T., Holzer M., Haertig W.
      J. Neurosci. 23:6972-6981(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, PHOSPHORYLATION, FUNCTION DURING HIBERNATION.

    Entry informationi

    Entry nameiTAU_SPECI
    AccessioniPrimary (citable) accession number: Q6TS35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 62 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3