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Q6TS35

- TAU_SPECI

UniProt

Q6TS35 - TAU_SPECI

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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

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 430429Microtubule-associated protein tauPRO_0000232454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei18 – 181Phosphotyrosine; by FYN By similarity
Modified residuei33 – 331Phosphoserine By similarity
Modified residuei37 – 371Phosphothreonine By similarity
Modified residuei142 – 1421Phosphothreonine By similarity
Modified residuei164 – 1641Phosphothreonine By similarity
Modified residuei170 – 1701Phosphothreonine
Modified residuei186 – 1861Phosphotyrosine By similarity
Modified residuei187 – 1871Phosphoserine
Modified residuei188 – 1881Phosphoserine
Modified residuei191 – 1911Phosphoserine; by CK1, PDPK1 and TTBK1
Modified residuei194 – 1941Phosphothreonine; by CK1 and PDPK1
Modified residuei199 – 1991Phosphoserine Inferred
Modified residuei201 – 2011Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity
Modified residuei203 – 2031Phosphoserine By similarity
Modified residuei206 – 2061Phosphothreonine By similarity
Modified residuei220 – 2201Phosphothreonine; by GSK3-beta and PDPK1 By similarity
Modified residuei224 – 2241Phosphoserine By similarity
Modified residuei226 – 2261Phosphoserine; by PHK By similarity
Modified residuei251 – 2511Phosphoserine; also in form PHF-tau-like found during hibernation; by MARK1, BRSK1, BRSK2 and PHK Inferred
Modified residuei274 – 2741Phosphoserine; by PHK By similarity
Modified residuei278 – 2781Phosphoserine; by PHK By similarity
Disulfide bondi280 ↔ 311 By similarity
Modified residuei282 – 2821Phosphoserine By similarity
Modified residuei294 – 2941Phosphoserine By similarity
Modified residuei313 – 3131Phosphoserine By similarity
Modified residuei341 – 3411Phosphoserine; by PHK By similarity
Modified residuei345 – 3451Phosphoserine; in form PHF-tau-like found during hibernation Inferred
Modified residuei385 – 3851Phosphoserine; by CK1 and PDPK1
Modified residuei389 – 3891Phosphoserine By similarity
Modified residuei392 – 3921Phosphothreonine By similarity
Modified residuei393 – 3931Phosphoserine; by CK1 and PDPK1
Modified residuei398 – 3981Phosphoserine By similarity
Modified residuei405 – 4051Phosphoserine By similarity
Modified residuei411 – 4111Phosphoserine By similarity
Modified residuei416 – 4161Phosphothreonine By similarity

Post-translational modificationi

Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome 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.1 Publication
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.

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.

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.

« Hide

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: March 19, 2014
This is version 61 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

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