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Protein

Microtubule-associated protein tau

Gene

MAPT

Organism
Spermophilus citellus (European suslik) (Citellus citellus)
Status
Reviewed-Annotation score: 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

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002324542 – 430Microtubule-associated protein tauAdd BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei18Phosphotyrosine; by FYNBy similarity1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei33PhosphoserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei56PhosphothreonineBy similarity1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei98PhosphothreonineBy similarity1
Modified residuei142PhosphothreonineBy similarity1
Modified residuei144Omega-N-methylarginineBy similarity1
Modified residuei152N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei152N6-acetyllysine; alternateBy similarity1
Modified residuei158PhosphothreonineBy similarity1
Modified residuei164PhosphothreonineBy similarity1
Modified residuei165PhosphothreonineBy similarity1
Modified residuei170Phosphothreonine1 Publication1
Modified residuei180PhosphoserineBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei186PhosphotyrosineBy similarity1
Modified residuei187Phosphoserine1 Publication1
Modified residuei188Phosphoserine1 Publication1
Modified residuei191Phosphoserine; by CK1, PDPK1 and TTBK11 Publication1
Modified residuei194Phosphothreonine; by CK1 and PDPK11 Publication1
Modified residuei199Phosphoserine1 Publication1
Modified residuei201Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity1
Modified residuei203PhosphoserineBy similarity1
Modified residuei206PhosphothreonineBy similarity1
Modified residuei214N6-acetyllysineBy similarity1
Modified residuei220Phosphothreonine; by GSK3-beta and PDPK1By similarity1
Modified residuei224PhosphoserineBy similarity1
Modified residuei226Phosphoserine; by PHKBy similarity1
Cross-linki243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei248N6-acetyllysine; alternateBy similarity1
Modified residuei248N6-methyllysine; alternateBy similarity1
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei251Phosphoserine; also in form PHF-tau-like found during hibernation; by MARK1, BRSK1, BRSK2 and PHK1 Publication1
Cross-linki256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei270N6-acetyllysine; alternateBy similarity1
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei274Phosphoserine; by PHKBy similarity1
Modified residuei278Phosphoserine; by PHKBy similarity1
Modified residuei279N6-acetyllysineBy similarity1
Disulfide bondi280 ↔ 311By similarity
Modified residuei282PhosphoserineBy similarity1
Modified residuei287N6-acetyllysine; alternateBy similarity1
Cross-linki287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei294PhosphoserineBy similarity1
Modified residuei300N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei300N6-acetyllysine; alternateBy similarity1
Cross-linki300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei306N6-acetyllysine; alternateBy similarity1
Cross-linki306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei310N6-acetyllysine; alternateBy similarity1
Cross-linki310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei313PhosphoserineBy similarity1
Modified residuei320N6-acetyllysine; alternateBy similarity1
Cross-linki320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei332N6-acetyllysine; alternateBy similarity1
Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei336N6-acetyllysine; alternateBy similarity1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei338Omega-N-methylarginineBy similarity1
Modified residuei341Phosphoserine; by PHKBy similarity1
Cross-linki342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei345Phosphoserine; in form PHF-tau-like found during hibernation1 Publication1
Modified residuei358N6-acetyllysine; alternateBy similarity1
Cross-linki358Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki364Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei374N6-acetyllysine; alternateBy similarity1
Cross-linki374Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei383PhosphotyrosineBy similarity1
Modified residuei385Phosphoserine; by CK1 and PDPK11 Publication1
Modified residuei389PhosphoserineBy similarity1
Modified residuei392PhosphothreonineBy similarity1
Modified residuei393Phosphoserine; by CK1 and PDPK11 Publication1
Modified residuei398PhosphoserineBy similarity1
Modified residuei405PhosphoserineBy similarity1
Modified residuei411PhosphoserineBy similarity1
Modified residuei416PhosphothreonineBy similarity1

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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ6TS35.

PTM databases

iPTMnetiQ6TS35.

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)DescriptionActionsGraphical viewLength
Repeati233 – 263Tau/MAP 1Add BLAST31
Repeati264 – 294Tau/MAP 2Add BLAST31
Repeati295 – 325Tau/MAP 3Add BLAST31
Repeati326 – 357Tau/MAP 4Add BLAST32

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. AlignAdd to basket

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

ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ6TS35.

Proteomic databases

PRIDEiQ6TS35.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

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: July 6, 2016
This is version 69 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.