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Protein

Microtubule-associated protein tau

Gene

Mapt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • Hsp90 protein binding Source: RGD
  • microtubule binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase 2A binding Source: RGD

GO - Biological processi

  • apoptotic process Source: RGD
  • brain development Source: RGD
  • female pregnancy Source: RGD
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: RGD
  • memory Source: RGD
  • microtubule-based process Source: RGD
  • microtubule cytoskeleton organization Source: UniProtKB
  • neuron differentiation Source: RGD
  • neuron projection development Source: GO_Central
  • positive regulation of axon extension Source: UniProtKB
  • positive regulation of long term synaptic depression Source: RGD
  • positive regulation of microtubule polymerization Source: UniProtKB
  • response to nutrient Source: RGD
  • response to organic substance Source: RGD
Complete GO annotation...

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:Mtapt, Tau
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69329. Mapt.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • axonal growth cone Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • growth cone Source: UniProtKB
  • main axon Source: RGD
  • microtubule Source: CACAO
  • microtubule associated complex Source: GO_Central
  • neuron projection Source: RGD
  • plasma membrane Source: UniProtKB
  • tubulin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000727462 – 752Microtubule-associated protein tauAdd BLAST751

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei18Phosphotyrosine; by FYNBy similarity1
Cross-linki33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei35PhosphoserineCombined sources1
Modified residuei50PhosphoserineCombined sources1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei60PhosphothreonineCombined sources1
Modified residuei100PhosphothreonineBy similarity1
Modified residuei191PhosphoserineCombined sources1
Modified residuei204PhosphoserineCombined sources1
Modified residuei388PhosphoserineBy similarity1
Modified residuei464PhosphothreonineBy similarity1
Modified residuei466Omega-N-methylarginineBy similarity1
Modified residuei474N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei474N6-acetyllysine; alternateBy similarity1
Modified residuei480PhosphothreonineBy similarity1
Modified residuei486PhosphothreonineBy similarity1
Modified residuei487PhosphothreonineBy similarity1
Modified residuei489PhosphoserineCombined sources1
Modified residuei492PhosphothreonineCombined sources1 Publication1
Modified residuei496PhosphoserineBy similarity1
Modified residuei502PhosphoserineBy similarity1
Modified residuei506PhosphoserineBy similarity1
Modified residuei508PhosphotyrosineBy similarity1
Modified residuei509PhosphoserineCombined sources1 Publication1
Modified residuei510PhosphoserineCombined sources1 Publication1
Modified residuei513Phosphoserine; by CK1, PDPK1 and TTBK1Combined sources1 Publication1
Modified residuei516Phosphothreonine; by CK1 and PDPK1By similarity1
Modified residuei523Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity1
Modified residuei525PhosphoserineCombined sources1
Modified residuei528PhosphothreonineCombined sources1
Modified residuei536N6-acetyllysineBy similarity1
Modified residuei542PhosphothreonineCombined sources1
Modified residuei542Phosphothreonine; by GSK3-beta and PDPK1By similarity1
Modified residuei546PhosphoserineCombined sources1 Publication1
Modified residuei548Phosphoserine; by PHKBy similarity1
Cross-linki565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei570N6-acetyllysine; alternateBy similarity1
Modified residuei570N6-methyllysine; alternateBy similarity1
Cross-linki570Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei573Phosphoserine; by MARK1, BRSK1, BRSK2 and PHKBy similarity1
Cross-linki578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei592N6-acetyllysine; alternateBy similarity1
Cross-linki592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei596Phosphoserine; by PHKBy similarity1
Modified residuei600Phosphoserine; by PHKBy similarity1
Modified residuei601N6-acetyllysineBy similarity1
Disulfide bondi602 ↔ 633By similarity
Modified residuei604PhosphoserineBy similarity1
Modified residuei609N6-acetyllysine; alternateBy similarity1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei616PhosphoserineBy similarity1
Modified residuei622N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei622N6-acetyllysine; alternateBy similarity1
Cross-linki622Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei628N6-acetyllysine; alternateBy similarity1
Cross-linki628Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei632N6-acetyllysine; alternateBy similarity1
Cross-linki632Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei635PhosphoserineBy similarity1
Modified residuei642N6-acetyllysine; alternateBy similarity1
Cross-linki642Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei654N6-acetyllysine; alternateBy similarity1
Cross-linki654Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei658N6-acetyllysine; alternateBy similarity1
Cross-linki658Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei660Omega-N-methylarginineBy similarity1
Modified residuei663Phosphoserine; by PHKBy similarity1
Cross-linki664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei667PhosphoserineCombined sources1
Modified residuei680N6-acetyllysine; alternateBy similarity1
Cross-linki680Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki686Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei696N6-acetyllysine; alternateBy similarity1
Cross-linki696Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei705PhosphotyrosineBy similarity1
Modified residuei707Phosphoserine; by CK1 and PDPK1Combined sources1 Publication1
Modified residuei711PhosphoserineCombined sources1 Publication1
Modified residuei714PhosphothreonineCombined sources1
Modified residuei715Phosphoserine; by CK1 and PDPK1Combined sources1 Publication1
Modified residuei720PhosphoserineBy similarity1
Modified residuei727PhosphoserineCombined sources1
Modified residuei733PhosphoserineCombined sources1
Modified residuei738PhosphothreonineBy similarity1

Post-translational modificationi

Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity).By similarity
Phosphorylated 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. Fetal Tau is much more phosphorylated than adult Tau. Phosphorylation at Ser-573 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. Phosphorylation at Ser-204 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP19332.
PRIDEiP19332.

PTM databases

iPTMnetiP19332.
PhosphoSitePlusiP19332.

Expressioni

Tissue specificityi

Expressed in neurons. The larger forms (isoform tau-A and isoform tau-B) are preferentially expressed in the peripheral nervous system while the other are expressed in the central nervous system. Low amounts of the larger forms are also found in limited areas of the CNS.

Developmental stagei

During the immediate postnatal period, the dorsal root ganglia express all isoforms whereas only the larger forms persist in the adults.

Interactioni

Subunit structurei

Interacts with SQSTM1 when polyubiquitinated. Interacts with PSMC2 through SQSTM1. Binds to CSNK1D (By similarity). Interacts with FKBP4. Interacts with SGK1 (By similarity). Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-388 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
A6NAR82EBI-7080713,EBI-8755852From a different organism.
Pacsin1Q616446EBI-8758676,EBI-2255561From a different organism.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • Hsp90 protein binding Source: RGD
  • microtubule binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase 2A binding Source: RGD

Protein-protein interaction databases

DIPiDIP-41779N.
IntActiP19332. 3 interactors.
MINTiMINT-1037362.
STRINGi10116.ENSRNOP00000006856.

Chemistry databases

BindingDBiP19332.

Structurei

3D structure databases

ProteinModelPortaliP19332.
SMRiP19332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati555 – 585Tau/MAP 1Add BLAST31
Repeati586 – 616Tau/MAP 2Add BLAST31
Repeati617 – 647Tau/MAP 3Add BLAST31
Repeati648 – 679Tau/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

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
HOGENOMiHOG000231029.
HOVERGENiHBG000991.
InParanoidiP19332.
PhylomeDBiP19332.

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 (8)i

Sequence statusi: Complete.

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

This entry describes 8 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 up to 4 of the 14 exons. Two different C-termini are obtained either by the retention or the splicing of intron 13/14.
Isoform Tau-A (identifier: P19332-1) [UniParc]FASTAAdd to basket
Also known as: SC1

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 MEDQAGDYTM LQDQEGDMDH GLKESPPQPP ADDGSEEPGS
60 70 80 90 100
ETSDAKSTPT AEDVTAPLVE ERAPDKQATA QSHTEIPEGT TAEEAGIGDT
110 120 130 140 150
PNMEDQAAGH VTQEPQKVEI FSQSLLVEPG RREGQAPDSG ISDWTHQQVP
160 170 180 190 200
SMSGAPLPPQ GLREATHQPL GTRPEDVERS HPASELLWQE SPQKEAWGKD
210 220 230 240 250
RLGSEEEVDE DITMDESSQE SPPSQASLAP GTATPQARSV SASGVSGETT
260 270 280 290 300
SIPGFPAEGS IPLPADFFSK VSAETQASPP EGPGTGPSEE GHEAAPEFTF
310 320 330 340 350
HVEIKASAPK EQDLEGATVV GAPAEEQKAR GPSVGKGTKE ASLLEPTDKQ
360 370 380 390 400
PAAGLPGRPV SRVPQLKARV AGVSKDRTGN DEKKAKTSTP SCAKTPSNRP
410 420 430 440 450
CLSPTRPTPG SSDPLIKPSS PAVCPEPATS PKYVSSVTPR NGSPGTKQMK
460 470 480 490 500
LKGADGKTGA KIATPRGAAT PGQKGTSNAT RIPAKTTPSP KTPPGSGEPP
510 520 530 540 550
KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSAS
560 570 580 590 600
KSRLQTAPVP MPDLKNVRSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS
610 620 630 640 650
KCGSKDNIKH VPGGGSVHIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV
660 670 680 690 700
KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG
710 720 730 740 750
AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ

GL
Length:752
Mass (Da):78,564
Last modified:January 23, 2007 - v3
Checksum:i915DCA04EF0B2902
GO
Isoform Tau-B (identifier: P19332-2) [UniParc]FASTAAdd to basket
Also known as: Big-tau, HMW-tau

The sequence of this isoform differs from the canonical sequence as follows:
     387-452: Missing.

Show »
Length:686
Mass (Da):71,774
Checksum:iF3709D1844C3763D
GO
Isoform Tau-C (identifier: P19332-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-91: Missing.
     114-367: Missing.
     387-452: Missing.

Show »
Length:403
Mass (Da):42,048
Checksum:i4ED13493B947A5E7
GO
Isoform Tau-D (identifier: P19332-4) [UniParc]FASTAAdd to basket
Also known as: SC2

The sequence of this isoform differs from the canonical sequence as follows:
     114-367: Missing.

Show »
Length:498
Mass (Da):51,912
Checksum:i6DC5958544984730
GO
Isoform Tau-E (identifier: P19332-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-367: Missing.
     387-452: Missing.

Show »
Length:432
Mass (Da):45,122
Checksum:iBBBC0DF6D0394D72
GO
Isoform Tau-F (identifier: P19332-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-367: Missing.
     387-452: Missing.

Show »
Length:374
Mass (Da):39,152
Checksum:i2323D277377BDBB7
GO
Isoform Tau-G (identifier: P19332-7) [UniParc]FASTAAdd to basket
Also known as: Fetal-tau

The sequence of this isoform differs from the canonical sequence as follows:
     63-91: Missing.
     114-367: Missing.
     387-452: Missing.
     586-616: Missing.

Show »
Length:372
Mass (Da):38,801
Checksum:iD4A2BD9C6DEAD376
GO
Isoform Tau-H (identifier: P19332-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     752-752: L → KPVLLSSEVWNYSHDFGHHTDLGL

Show »
Length:775
Mass (Da):81,185
Checksum:iAF16994BB897B2DE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti255F → L (PubMed:8408300).Curated1
Sequence conflicti284G → A (PubMed:8408300).Curated1
Sequence conflicti292H → D (PubMed:8408300).Curated1
Sequence conflicti618H → Q (PubMed:8408300).Curated1
Sequence conflicti618H → Q in CAA55889 (PubMed:8057376).Curated1
Sequence conflicti618H → Q (PubMed:2560640).Curated1
Sequence conflicti705Y → H in CAA55889 (PubMed:8057376).Curated1
Sequence conflicti734P → A (PubMed:8408300).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00319134 – 91Missing in isoform Tau-F. 1 PublicationAdd BLAST58
Alternative sequenceiVSP_00319263 – 91Missing in isoform Tau-C and isoform Tau-G. 2 PublicationsAdd BLAST29
Alternative sequenceiVSP_003193114 – 367Missing in isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Tau-G. 3 PublicationsAdd BLAST254
Alternative sequenceiVSP_003194387 – 452Missing in isoform Tau-B, isoform Tau-C, isoform Tau-E, isoform Tau-F and isoform Tau-G. 5 PublicationsAdd BLAST66
Alternative sequenceiVSP_003195586 – 616Missing in isoform Tau-G. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_003196752L → KPVLLSSEVWNYSHDFGHHT DLGL in isoform Tau-H. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84156 mRNA. Translation: AAA42204.1.
X79321 mRNA. Translation: CAA55889.1.
D30628 Genomic DNA. No translation available.
D30629 mRNA. No translation available.
PIRiA38235.
JS0306.
S46264.
UniGeneiRn.2455.

Genome annotation databases

UCSCiRGD:69329. rat. [P19332-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84156 mRNA. Translation: AAA42204.1.
X79321 mRNA. Translation: CAA55889.1.
D30628 Genomic DNA. No translation available.
D30629 mRNA. No translation available.
PIRiA38235.
JS0306.
S46264.
UniGeneiRn.2455.

3D structure databases

ProteinModelPortaliP19332.
SMRiP19332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41779N.
IntActiP19332. 3 interactors.
MINTiMINT-1037362.
STRINGi10116.ENSRNOP00000006856.

Chemistry databases

BindingDBiP19332.
ChEMBLiCHEMBL1075117.

PTM databases

iPTMnetiP19332.
PhosphoSitePlusiP19332.

Proteomic databases

PaxDbiP19332.
PRIDEiP19332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:69329. rat. [P19332-1]

Organism-specific databases

RGDi69329. Mapt.

Phylogenomic databases

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
HOGENOMiHOG000231029.
HOVERGENiHBG000991.
InParanoidiP19332.
PhylomeDBiP19332.

Miscellaneous databases

PROiP19332.

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_RAT
AccessioniPrimary (citable) accession number: P19332
Secondary accession number(s): Q63567, Q63677, Q9QW06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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.