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Q6TS35 (TAU_SPECI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein tau
Gene names
Name:MAPT
OrganismSpermophilus citellus (European suslik) (Citellus citellus)
Taxonomic identifier9997 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniSpermophilus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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

Subcellular location

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.

Domain

The tau/MAP repeat binds to tubulin By similarity.

Post-translational modification

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. Ref.1

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. Ref.1

Sequence similarities

Contains 4 Tau/MAP repeats.

Ontologies

Keywords
   Biological processHibernation
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMAcetylation
Disulfide bond
Phosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological_processhibernation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaxon

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 430429Microtubule-associated protein tau
PRO_0000232454

Regions

Repeat233 – 26331Tau/MAP 1
Repeat264 – 29431Tau/MAP 2
Repeat295 – 32531Tau/MAP 3
Repeat326 – 35732Tau/MAP 4

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue181Phosphotyrosine; by FYN By similarity
Modified residue331Phosphoserine By similarity
Modified residue371Phosphothreonine By similarity
Modified residue1421Phosphothreonine By similarity
Modified residue1641Phosphothreonine By similarity
Modified residue1701Phosphothreonine
Modified residue1861Phosphotyrosine By similarity
Modified residue1871Phosphoserine
Modified residue1881Phosphoserine
Modified residue1911Phosphoserine; by CK1, PDPK1 and TTBK1
Modified residue1941Phosphothreonine; by CK1 and PDPK1
Modified residue1991Phosphoserine Probable
Modified residue2011Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2061Phosphothreonine By similarity
Modified residue2201Phosphothreonine; by GSK3-beta and PDPK1 By similarity
Modified residue2241Phosphoserine By similarity
Modified residue2261Phosphoserine; by PHK By similarity
Modified residue2511Phosphoserine; also in form PHF-tau-like found during hibernation; by MARK1, BRSK1, BRSK2 and PHK Probable
Modified residue2741Phosphoserine; by PHK By similarity
Modified residue2781Phosphoserine; by PHK By similarity
Modified residue2821Phosphoserine By similarity
Modified residue2941Phosphoserine By similarity
Modified residue3131Phosphoserine By similarity
Modified residue3411Phosphoserine; by PHK By similarity
Modified residue3451Phosphoserine; in form PHF-tau-like found during hibernation Probable
Modified residue3851Phosphoserine; by CK1 and PDPK1
Modified residue3891Phosphoserine By similarity
Modified residue3921Phosphothreonine By similarity
Modified residue3931Phosphoserine; by CK1 and PDPK1
Modified residue3981Phosphoserine By similarity
Modified residue4051Phosphoserine By similarity
Modified residue4111Phosphoserine By similarity
Modified residue4161Phosphothreonine By similarity
Disulfide bond280 ↔ 311 By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5ED2B0EB0DFADAF0

FASTA43044,803
        10         20         30         40         50         60 
MAEPRQEFDT AEDHAEGYAL LQDQEGEHGL KASPLQTPAD DGPEEPVSET SDAKSTPTAE 

        70         80         90        100        110        120 
DVTAPLVDER TPGEQAATQP PTDIPEGTTA EEAGIGDTPN MEDQAAGHVT QARMVSKGKE 

       130        140        150        160        170        180 
GTGSEDRKAK GADSKTGTKI ATPRGTAPPG QKGTANATRI PAKTTPSPKT PPGTGEPAKS 

       190        200        210        220        230        240 
GDRSGYSSPG SPGTPGSRSR TPSLPTPPTR EPKKVAVVRT PPKSPSSTKS RLQTAPVPMP 

       250        260        270        280        290        300 
DLKNVRSKIG STENLKHQPG GGKVQIINKK LDLSNVQSKC GSKDNIKHVP GGGSVQIVYK 

       310        320        330        340        350        360 
PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ SKIGSLDNIT HVPGGGNKKI 

       370        380        390        400        410        420 
ETHKLTFREN AKAKTDHGAE IVYKSPVVSG DTSPRHLSNV SSTGSINMVD SPQLATLADE 

       430 
VSASLAKQGL 

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References

[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.

Web resources

Protein Spotlight

Vita minima - Issue 68 of March 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY388477 mRNA. Translation: AAQ92319.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ6TS35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000991.

Family and domain databases

InterProIPR027324. MAP2/MAP4/Tau.
IPR001084. MAP_tubulin-bd_rpt.
IPR002955. Tau.
[Graphical view]
PANTHERPTHR11501. PTHR11501. 1 hit.
PfamPF00418. Tubulin-binding. 4 hits.
[Graphical view]
PRINTSPR01261. TAUPROTEIN.
PROSITEPS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAU_SPECI
AccessionPrimary (citable) accession number: Q6TS35
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries