Skip Header

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

Microtubule-associated protein tau

Gene

MAPT

Organism
Capra hircus (Goat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein tau
Alternative name(s):
Neurofibrillary tangle protein
Paired helical filament-tau
Short name:
PHF-tau
Gene namesi
Name:MAPT
Synonyms:TAU
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

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_00000727372 – 403Microtubule-associated protein tauAdd BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei19Phosphotyrosine; by FYNBy similarity1
Cross-linki33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei35PhosphoserineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei60PhosphothreonineBy similarity1
Modified residuei71PhosphothreonineBy similarity1
Modified residuei115PhosphothreonineBy similarity1
Modified residuei117Omega-N-methylarginineBy similarity1
Modified residuei125N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei125N6-acetyllysine; alternateBy similarity1
Modified residuei131PhosphothreonineBy similarity1
Modified residuei137PhosphothreonineBy similarity1
Modified residuei138PhosphothreonineBy similarity1
Modified residuei143PhosphothreonineBy similarity1
Modified residuei153PhosphoserineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei159PhosphotyrosineBy similarity1
Modified residuei160PhosphoserineBy similarity1
Modified residuei161PhosphoserineBy similarity1
Modified residuei164Phosphoserine; by CK1, PDPK1 and TTBK1By similarity1
Modified residuei167Phosphothreonine; by CK1 and PDPK1By similarity1
Modified residuei174Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity1
Modified residuei176PhosphoserineBy similarity1
Modified residuei179PhosphothreonineBy similarity1
Modified residuei187N6-acetyllysineBy similarity1
Modified residuei193Phosphothreonine; by GSK3-beta and PDPK1By similarity1
Modified residuei197PhosphoserineBy similarity1
Modified residuei199Phosphoserine; by PHKBy similarity1
Cross-linki216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei221N6-acetyllysine; alternateBy similarity1
Modified residuei221N6-methyllysine; alternateBy similarity1
Cross-linki221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei224Phosphoserine; by MARK1, BRSK1, BRSK2 and PHKBy similarity1
Cross-linki229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei243N6-acetyllysine; alternateBy similarity1
Cross-linki243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei247Phosphoserine; by PHKBy similarity1
Modified residuei251Phosphoserine; by PHKBy similarity1
Modified residuei252N6-acetyllysineBy similarity1
Disulfide bondi253 ↔ 284By similarity
Modified residuei255PhosphoserineBy similarity1
Modified residuei260N6-acetyllysine; alternateBy similarity1
Cross-linki260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei267PhosphoserineBy similarity1
Modified residuei273N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei273N6-acetyllysine; alternateBy similarity1
Cross-linki273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei279N6-acetyllysine; alternateBy similarity1
Cross-linki279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei283N6-acetyllysine; alternateBy similarity1
Cross-linki283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei286PhosphoserineBy similarity1
Modified residuei293N6-acetyllysine; alternateBy similarity1
Cross-linki293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei305N6-acetyllysine; alternateBy similarity1
Cross-linki305Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei309N6-acetyllysine; alternateBy similarity1
Cross-linki309Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei311Omega-N-methylarginineBy similarity1
Modified residuei314Phosphoserine; by PHKBy similarity1
Cross-linki315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei318PhosphoserineBy similarity1
Modified residuei331N6-acetyllysine; alternateBy similarity1
Cross-linki331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei347N6-acetyllysine; alternateBy similarity1
Cross-linki347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei356PhosphotyrosineBy similarity1
Modified residuei358Phosphoserine; by CK1 and PDPK1By similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei365PhosphothreonineBy similarity1
Modified residuei366Phosphoserine; by CK1 and PDPK1By similarity1
Modified residuei371PhosphoserineBy similarity1
Modified residuei378PhosphoserineBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei389PhosphothreonineBy 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-224 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

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiO02828.

Expressioni

Tissue specificityi

Expressed in neurons.

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
Repeati206 – 236Tau/MAP 1Add BLAST31
Repeati237 – 267Tau/MAP 2Add BLAST31
Repeati268 – 298Tau/MAP 3Add BLAST31
Repeati299 – 330Tau/MAP 4Add BLAST32

Domaini

The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. Isoforms differ from each other by the presence or absence of two exons. One of these optional exons contains the additional tau/MAP repeat.
Isoform Tau-A (identifier: O02828-1) [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
MAEPRQEFDV MEDHAQGDYT LQDHEGDMEP GLKESPLQTP ADDGSEEPGS
60 70 80 90 100
ETSDAKSTPT AEAEEAGIGD TSNLEDQAAG HVTQARMVSK GKDGTGPDDK
110 120 130 140 150
KAKGADGKPG TKIATPRGAA PPGQKGQANA TRIPAKTTPT PKTSPGTGES
160 170 180 190 200
GKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSA
210 220 230 240 250
AKSRLQAAPG PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ
260 270 280 290 300
SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE
310 320 330 340 350
VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH
360 370 380 390 400
GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK

QGL
Length:403
Mass (Da):41,848
Last modified:January 23, 2007 - v3
Checksum:i259D0302E1A339C7
GO
Isoform Tau-B (identifier: O02828-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-62: Missing.
     237-267: Missing.

Show »
Length:343
Mass (Da):35,685
Checksum:iC39513E2F60FD9C8
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00317334 – 62Missing in isoform Tau-B. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_003174237 – 267Missing in isoform Tau-B. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83347 mRNA. Translation: AAB50785.1.
UniGeneiChi.1323.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83347 mRNA. Translation: AAB50785.1.
UniGeneiChi.1323.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO02828.

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_CAPHI
AccessioniPrimary (citable) accession number: O02828
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.