Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6TS35

- TAU_SPECI

UniProt

Q6TS35 - TAU_SPECI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. microtubule Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
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 – 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.

« Hide

        10         20         30         40         50
MAEPRQEFDT AEDHAEGYAL LQDQEGEHGL KASPLQTPAD DGPEEPVSET
60 70 80 90 100
SDAKSTPTAE DVTAPLVDER TPGEQAATQP PTDIPEGTTA EEAGIGDTPN
110 120 130 140 150
MEDQAAGHVT QARMVSKGKE GTGSEDRKAK GADSKTGTKI ATPRGTAPPG
160 170 180 190 200
QKGTANATRI PAKTTPSPKT PPGTGEPAKS GDRSGYSSPG SPGTPGSRSR
210 220 230 240 250
TPSLPTPPTR EPKKVAVVRT PPKSPSSTKS RLQTAPVPMP DLKNVRSKIG
260 270 280 290 300
STENLKHQPG GGKVQIINKK LDLSNVQSKC GSKDNIKHVP GGGSVQIVYK
310 320 330 340 350
PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ SKIGSLDNIT
360 370 380 390 400
HVPGGGNKKI ETHKLTFREN AKAKTDHGAE IVYKSPVVSG DTSPRHLSNV
410 420 430
SSTGSINMVD SPQLATLADE VSASLAKQGL
Length:430
Mass (Da):44,803
Last modified:January 23, 2007 - v3
Checksum:i5ED2B0EB0DFADAF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 63 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