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Protein

Microtubule-associated protein tau

Gene

Mapt

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • adult walking behavior Source: MGI
  • axo-dendritic transport Source: MGI
  • axon extension Source: MGI
  • axonogenesis Source: MGI
  • microtubule cytoskeleton organization Source: UniProtKB
  • mitochondrion transport along microtubule Source: MGI
  • negative regulation of intracellular transport Source: MGI
  • neuron migration Source: MGI
  • positive regulation of axon extension Source: UniProtKB
  • positive regulation of microtubule polymerization Source: UniProtKB
  • regulation of autophagy Source: MGI
  • regulation of microtubule-based movement Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:97180. Mapt.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • axoneme Source: MGI
  • cell body Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic ribonucleoprotein granule Source: MGI
  • cytosol Source: UniProtKB-SubCell
  • dendrite Source: MGI
  • growth cone Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: GO_Central
  • microtubule cytoskeleton Source: MGI
  • nuclear periphery Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: MGI
  • tubulin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

May be involved in the pathogenesis of cytoplasmic inclusions (as Mallory bodies) in livers of mice chronically intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-dihydrocollidine), a model for human alcoholic hepatitis. Alteration of Tau (abnormal phosphorylation and cross-linking) could contribute to Mallory bodies formation and disturbance of microtubule function in alcoholic liver disease.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000727422 – 733Microtubule-associated protein tauAdd BLAST732

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei18Phosphotyrosine; by FYN1 Publication1
Cross-linki33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei35PhosphoserineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei58Phosphothreonine1 Publication1
Modified residuei60PhosphothreonineBy similarity1
Modified residuei100Phosphothreonine1 Publication1
Modified residuei115Omega-N-methylarginine1 Publication1
Modified residuei188PhosphoserineCombined sources1
Modified residuei369PhosphoserineBy similarity1
Modified residuei445PhosphothreonineBy similarity1
Modified residuei447Omega-N-methylarginine1 Publication1
Modified residuei451Phosphoserine1 Publication1
Modified residuei455N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei455N6-acetyllysine; alternate1 Publication1
Modified residuei461Phosphothreonine1 Publication1
Modified residuei467Phosphothreonine1 Publication1
Modified residuei468PhosphothreonineCombined sources1
Modified residuei470PhosphoserineCombined sources1 Publication1
Modified residuei473Phosphothreonine1 Publication1
Modified residuei477Phosphoserine1 Publication1
Modified residuei483Phosphoserine1 Publication1
Modified residuei487Phosphoserine1 Publication1
Modified residuei489PhosphotyrosineCombined sources1
Modified residuei490PhosphoserineCombined sources1 Publication1
Modified residuei491PhosphoserineCombined sources1 Publication1
Modified residuei494PhosphoserineCombined sources1 Publication1
Modified residuei497PhosphothreonineCombined sources1 Publication1
Modified residuei504Phosphothreonine1 Publication1
Modified residuei506Phosphoserine1 Publication1
Modified residuei509Phosphothreonine1 Publication1
Modified residuei517N6-acetyllysine1 Publication1
Modified residuei523PhosphothreonineCombined sources1 Publication1
Modified residuei527Phosphoserine1 Publication1
Modified residuei529Phosphoserine1 Publication1
Modified residuei531Phosphoserine1 Publication1
Cross-linki546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei551N6-acetyllysine; alternate1 Publication1
Modified residuei551N6-methyllysine; alternate1 Publication1
Cross-linki551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei554Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK3 Publications1
Cross-linki559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei573N6-acetyllysine; alternate1 Publication1
Cross-linki573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei577PhosphoserineBy similarity1
Modified residuei581PhosphoserineBy similarity1
Modified residuei582N6-acetyllysine1 Publication1
Disulfide bondi583 ↔ 614By similarity
Modified residuei585PhosphoserineBy similarity1
Modified residuei590N6-acetyllysine; alternate1 Publication1
Cross-linki590Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei597PhosphoserineBy similarity1
Modified residuei603N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei603N6-acetyllysine; alternate1 Publication1
Cross-linki603Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei609N6-acetyllysine; alternate1 Publication1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei613N6-acetyllysine; alternate1 Publication1
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei616PhosphoserineBy similarity1
Modified residuei623N6-acetyllysine; alternate1 Publication1
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei635N6-acetyllysine; alternate1 Publication1
Cross-linki635Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei639N6-acetyllysine; alternate1 Publication1
Cross-linki639Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei641Omega-N-methylarginine1 Publication1
Modified residuei644PhosphoserineBy similarity1
Cross-linki645Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei648Phosphoserine1 Publication1
Modified residuei661N6-acetyllysine; alternate1 Publication1
Cross-linki661Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki667Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei677N6-acetyllysine; alternate1 Publication1
Cross-linki677Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei686PhosphotyrosineCombined sources1 Publication1
Modified residuei688PhosphoserineCombined sources1 Publication1
Modified residuei692Phosphoserine; alternateCombined sources1 Publication1
Glycosylationi692O-linked (GlcNAc...); alternate1 Publication1
Modified residuei695PhosphothreonineCombined sources1
Modified residuei696PhosphoserineCombined sources1
Modified residuei701PhosphoserineCombined sources1
Modified residuei708PhosphoserineCombined sources1 Publication1
Modified residuei714PhosphoserineCombined sources1
Modified residuei719PhosphothreonineBy 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. Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C. Phosphorylation at Ser-554 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylation at Ser-188 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiP10637.
PaxDbiP10637.
PeptideAtlasiP10637.
PRIDEiP10637.

PTM databases

iPTMnetiP10637.
PhosphoSitePlusiP10637.

Expressioni

Tissue specificityi

Expressed in neurons and at a lower level in the liver and kidney. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

Developmental stagei

Shorter forms or low molecular weight tau (lMW-tau) are generally expressed at early development stages and longer forms or high molecular weight tau (hMW-tau) in the adult brain.

Gene expression databases

BgeeiENSMUSG00000018411.
CleanExiMM_MAPT.
ExpressionAtlasiP10637. baseline and differential.
GenevisibleiP10637. MM.

Interactioni

Subunit structurei

Interacts with SQSTM1 when polyubiquitinated (By similarity). Interacts with PSMC2 through SQSTM1. Interacts with FKBP4. Binds to CSNK1D (By similarity). Interacts with SGK1 (By similarity). Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-369 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Bin1O085392EBI-774043,EBI-775152
Pacsin1Q616445EBI-774043,EBI-2255561

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201589. 16 interactors.
IntActiP10637. 9 interactors.
MINTiMINT-3974107.
STRINGi10090.ENSMUSP00000097919.

Structurei

3D structure databases

ProteinModelPortaliP10637.
SMRiP10637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati536 – 566Tau/MAP 1Add BLAST31
Repeati567 – 597Tau/MAP 2Add BLAST31
Repeati598 – 628Tau/MAP 3Add BLAST31
Repeati629 – 660Tau/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.
GeneTreeiENSGT00530000063491.
HOVERGENiHBG000991.
InParanoidiP10637.
KOiK04380.
TreeFamiTF316358.

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 (6)i

Sequence statusi: Complete.

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

This entry describes 6 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 5 of the 14 exons. One of these optional exons contains the additional tau/MAP repeat. Two different C-termini are obtained either by the retention or the splicing of intron 13/14.
Isoform PNS-Tau (identifier: P10637-1) [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
MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS
60 70 80 90 100
ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT
110 120 130 140 150
PNQEDQAAGH VTQGRREGQA PDLGTSDWTR QQVSSMSGAP LLPQGLREAT
160 170 180 190 200
CQPSGTRPED IEKSHPASEL LRRGPPQKEG WGQDRLGSEE EVDEDLTVDE
210 220 230 240 250
SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG SVPLPADFFS
260 270 280 290 300
KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV
310 320 330 340 350
VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK
360 370 380 390 400
ARVASKDRTG NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS
410 420 430 440 450
SPAVSPEPAT SPKHVSSVTP RNGSPGTKQM KLKGADGKTG AKIATPRGAA
460 470 480 490 500
SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP PKSGERSGYS SPGSPGTPGS
510 520 530 540 550
RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV PMPDLKNVRS
560 570 580 590 600
KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI
610 620 630 640 650
VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD
660 670 680 690 700
NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL
710 720 730
SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL
Length:733
Mass (Da):76,243
Last modified:January 23, 2007 - v3
Checksum:i80C0D50AC5F64E6F
GO
Isoform Tau-A (identifier: P10637-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-350: Missing.
     368-433: Missing.

Show »
Length:430
Mass (Da):44,893
Checksum:iE3C55BF8F2F901EC
GO
Isoform Tau-B (identifier: P10637-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-350: Missing.
     368-433: Missing.
     567-597: Missing.
     733-733: L → KAALLSSQVWNYSHDLATITDLGL

Show »
Length:364
Mass (Da):38,200
Checksum:iD1CAB2EF89CDD7C0
GO
Isoform Tau-C (identifier: P10637-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-350: Missing.
     368-433: Missing.
     567-597: Missing.

Show »
Length:341
Mass (Da):35,714
Checksum:i478641931A5A4143
GO
Isoform Tau-D (identifier: P10637-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-350: Missing.
     368-433: Missing.

Show »
Length:372
Mass (Da):38,961
Checksum:iB9427D315AD962B7
GO
Isoform Tau-E (identifier: P10637-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     92-113: Missing.
     114-350: Missing.
     368-433: Missing.

Show »
Length:350
Mass (Da):36,740
Checksum:i3FB530E1CF1E4CA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3D → N (PubMed:1374898).Curated1
Sequence conflicti9D → N (PubMed:1374898).Curated1
Sequence conflicti405S → C in CAM14797 (PubMed:19468303).Curated1
Sequence conflicti528P → T in CAA78121 (PubMed:7927211).Curated1
Sequence conflicti549R → G in AAH14748 (PubMed:15489334).Curated1
Sequence conflicti672E → Q (PubMed:1374898).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00318534 – 91Missing in isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E. 3 PublicationsAdd BLAST58
Alternative sequenceiVSP_00318692 – 113Missing in isoform Tau-E. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_003187114 – 350Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E. 3 PublicationsAdd BLAST237
Alternative sequenceiVSP_003188368 – 433Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E. 3 PublicationsAdd BLAST66
Alternative sequenceiVSP_003189567 – 597Missing in isoform Tau-B and isoform Tau-C. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_003190733L → KAALLSSQVWNYSHDLATIT DLGL in isoform Tau-B. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12914 mRNA. Translation: AAA58343.1.
U12915 mRNA. Translation: AAA58344.1.
U12916 mRNA. Translation: AAA58345.1.
Z12133 mRNA. Translation: CAA78121.1.
M93266 mRNA. No translation available.
M18775 mRNA. Translation: AAA40165.1.
M18776 mRNA. Translation: AAA40166.1.
D30627 Genomic DNA. Translation: BAA18878.1.
AL593843 Genomic DNA. Translation: CAM14797.1.
BC014748 mRNA. Translation: AAH14748.1.
CCDSiCCDS25527.1. [P10637-2]
CCDS25528.1. [P10637-5]
PIRiA28820.
A45301.
B28820.
RefSeqiNP_001033698.1. NM_001038609.2. [P10637-2]
NP_001272383.1. NM_001285454.1. [P10637-3]
NP_001272384.1. NM_001285455.1. [P10637-6]
NP_001272385.1. NM_001285456.1. [P10637-4]
NP_034968.3. NM_010838.4. [P10637-5]
UniGeneiMm.1287.

Genome annotation databases

EnsembliENSMUST00000100347; ENSMUSP00000097919; ENSMUSG00000018411. [P10637-2]
ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411. [P10637-5]
GeneIDi17762.
KEGGimmu:17762.
UCSCiuc007lwf.2. mouse. [P10637-3]
uc007lwg.2. mouse. [P10637-2]
uc007lwi.2. mouse. [P10637-4]
uc011yga.2. mouse. [P10637-6]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12914 mRNA. Translation: AAA58343.1.
U12915 mRNA. Translation: AAA58344.1.
U12916 mRNA. Translation: AAA58345.1.
Z12133 mRNA. Translation: CAA78121.1.
M93266 mRNA. No translation available.
M18775 mRNA. Translation: AAA40165.1.
M18776 mRNA. Translation: AAA40166.1.
D30627 Genomic DNA. Translation: BAA18878.1.
AL593843 Genomic DNA. Translation: CAM14797.1.
BC014748 mRNA. Translation: AAH14748.1.
CCDSiCCDS25527.1. [P10637-2]
CCDS25528.1. [P10637-5]
PIRiA28820.
A45301.
B28820.
RefSeqiNP_001033698.1. NM_001038609.2. [P10637-2]
NP_001272383.1. NM_001285454.1. [P10637-3]
NP_001272384.1. NM_001285455.1. [P10637-6]
NP_001272385.1. NM_001285456.1. [P10637-4]
NP_034968.3. NM_010838.4. [P10637-5]
UniGeneiMm.1287.

3D structure databases

ProteinModelPortaliP10637.
SMRiP10637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201589. 16 interactors.
IntActiP10637. 9 interactors.
MINTiMINT-3974107.
STRINGi10090.ENSMUSP00000097919.

PTM databases

iPTMnetiP10637.
PhosphoSitePlusiP10637.

Proteomic databases

MaxQBiP10637.
PaxDbiP10637.
PeptideAtlasiP10637.
PRIDEiP10637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100347; ENSMUSP00000097919; ENSMUSG00000018411. [P10637-2]
ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411. [P10637-5]
GeneIDi17762.
KEGGimmu:17762.
UCSCiuc007lwf.2. mouse. [P10637-3]
uc007lwg.2. mouse. [P10637-2]
uc007lwi.2. mouse. [P10637-4]
uc011yga.2. mouse. [P10637-6]

Organism-specific databases

CTDi4137.
MGIiMGI:97180. Mapt.

Phylogenomic databases

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOVERGENiHBG000991.
InParanoidiP10637.
KOiK04380.
TreeFamiTF316358.

Enzyme and pathway databases

ReactomeiR-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.

Miscellaneous databases

ChiTaRSiMapt. mouse.
PROiP10637.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018411.
CleanExiMM_MAPT.
ExpressionAtlasiP10637. baseline and differential.
GenevisibleiP10637. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P10637
Secondary accession number(s): A2A5Y9
, P10638, Q60684, Q60685, Q60686, Q62286, Q91WK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 184 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.