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P10637 (TAU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein tau
Alternative name(s):
Neurofibrillary tangle protein
Paired helical filament-tau
Short name=PHF-tau
Gene names
Name:Mapt
Synonyms:Mtapt, Tau
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.12

Subcellular location

Cytoplasm › cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell projection › axon. Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.

Tissue specificity

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 stage

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.

Domain

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

Post-translational modification

Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome 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 By similarity. 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. Ref.9 Ref.13 Ref.15

Involvement in disease

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.

Sequence similarities

Contains 4 Tau/MAP repeats.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMAcetylation
Disulfide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from genetic interaction PubMed 19074461. Source: MGI

axon cargo transport

Inferred from genetic interaction PubMed 20829454. Source: MGI

axon extension

Inferred from mutant phenotype PubMed 11891784PubMed 16536727. Source: MGI

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion transport along microtubule

Inferred from mutant phenotype PubMed 16536727. Source: MGI

negative regulation of intracellular transport

Inferred from mutant phenotype PubMed 16536727. Source: MGI

neuron migration

Inferred from mutant phenotype PubMed 19695252. Source: MGI

positive regulation of axon extension

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of microtubule polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of autophagy

Inferred from electronic annotation. Source: Compara

regulation of microtubule-based movement

Inferred from direct assay PubMed 18202255. Source: MGI

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

cilium axoneme

Inferred from direct assay PubMed 19004860. Source: MGI

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule

Inferred from direct assay PubMed 12074840. Source: MGI

nuclear periphery

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from direct assay PubMed 20338169. Source: MGI

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

tubulin complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionlipoprotein particle binding

Inferred from electronic annotation. Source: Compara

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform Tau-A (identifier: P10637-2)

The sequence of this isoform differs from the canonical sequence as follows:
     114-350: Missing.
     368-433: Missing.
Isoform Tau-B (identifier: P10637-3)

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
Isoform Tau-C (identifier: P10637-4)

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-350: Missing.
     368-433: Missing.
     567-597: Missing.
Isoform Tau-D (identifier: P10637-5)

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-350: Missing.
     368-433: Missing.
Isoform Tau-E (identifier: P10637-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 733732Microtubule-associated protein tau
PRO_0000072742

Regions

Repeat536 – 56631Tau/MAP 1
Repeat567 – 59731Tau/MAP 2
Repeat598 – 62831Tau/MAP 3
Repeat629 – 66032Tau/MAP 4

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue181Phosphotyrosine; by FYN By similarity
Modified residue351Phosphoserine By similarity
Modified residue1001Phosphothreonine Ref.17
Modified residue1881Phosphoserine; by SGK1 By similarity
Modified residue4451Phosphothreonine By similarity
Modified residue4571Phosphothreonine Ref.16
Modified residue4671Phosphothreonine By similarity
Modified residue4701Phosphoserine Ref.17
Modified residue4731Phosphothreonine Ref.17
Modified residue4891Phosphotyrosine Ref.17
Modified residue4901Phosphoserine Ref.11 Ref.16
Modified residue4911Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue4941Phosphoserine; by CK1, PDPK1 and TTBK1 Ref.11 Ref.16 Ref.17
Modified residue4971Phosphothreonine; by CK1 and PDPK1 Ref.16 Ref.17
Modified residue5041Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity
Modified residue5061Phosphoserine By similarity
Modified residue5091Phosphothreonine By similarity
Modified residue5231Phosphothreonine; by GSK3-beta and PDPK1 By similarity
Modified residue5271Phosphoserine Ref.14
Modified residue5291Phosphoserine; by PHK By similarity
Modified residue5541Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK Ref.13 Ref.15
Modified residue5771Phosphoserine; by PHK By similarity
Modified residue5811Phosphoserine; by PHK By similarity
Modified residue5851Phosphoserine By similarity
Modified residue5971Phosphoserine By similarity
Modified residue6161Phosphoserine By similarity
Modified residue6441Phosphoserine; by PHK By similarity
Modified residue6481Phosphoserine By similarity
Modified residue6881Phosphoserine; by CK1 and PDPK1 Ref.11 Ref.16 Ref.17 Ref.18 Ref.19
Modified residue6921Phosphoserine Ref.11 Ref.16 Ref.17 Ref.18 Ref.19
Modified residue6951Phosphothreonine Ref.11 Ref.16 Ref.17
Modified residue6961Phosphoserine; by CK1 and PDPK1 Ref.10 Ref.11 Ref.16 Ref.18
Modified residue7011Phosphoserine Ref.10 Ref.19
Modified residue7041Phosphoserine Ref.11
Modified residue7061Phosphothreonine Ref.10 Ref.11
Modified residue7081Phosphoserine Ref.10
Modified residue7141Phosphoserine By similarity
Modified residue7191Phosphothreonine By similarity
Disulfide bond583 ↔ 614 By similarity

Natural variations

Alternative sequence34 – 9158Missing in isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.
VSP_003185
Alternative sequence92 – 11322Missing in isoform Tau-E.
VSP_003186
Alternative sequence114 – 350237Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.
VSP_003187
Alternative sequence368 – 43366Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.
VSP_003188
Alternative sequence567 – 59731Missing in isoform Tau-B and isoform Tau-C.
VSP_003189
Alternative sequence7331L → KAALLSSQVWNYSHDLATIT DLGL in isoform Tau-B.
VSP_003190

Experimental info

Sequence conflict31D → N Ref.1
Sequence conflict91D → N Ref.1
Sequence conflict4051S → C in CAM14797. Ref.5
Sequence conflict5281P → T in CAA78121. Ref.2
Sequence conflict5491R → G in AAH14748. Ref.6
Sequence conflict6721E → Q Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform PNS-Tau [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 80C0D50AC5F64E6F

FASTA73376,243
        10         20         30         40         50         60 
MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT 

        70         80         90        100        110        120 
AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT PNQEDQAAGH VTQGRREGQA 

       130        140        150        160        170        180 
PDLGTSDWTR QQVSSMSGAP LLPQGLREAT CQPSGTRPED IEKSHPASEL LRRGPPQKEG 

       190        200        210        220        230        240 
WGQDRLGSEE EVDEDLTVDE SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG 

       250        260        270        280        290        300 
SVPLPADFFS KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV 

       310        320        330        340        350        360 
VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK ARVASKDRTG 

       370        380        390        400        410        420 
NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS SPAVSPEPAT SPKHVSSVTP 

       430        440        450        460        470        480 
RNGSPGTKQM KLKGADGKTG AKIATPRGAA SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP 

       490        500        510        520        530        540 
PKSGERSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV 

       550        560        570        580        590        600 
PMPDLKNVRS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI 

       610        620        630        640        650        660 
VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN 

       670        680        690        700        710        720 
KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL 

       730 
ADEVSASLAK QGL

« Hide

Isoform Tau-A [UniParc].

Checksum: E3C55BF8F2F901EC
Show »

FASTA43044,893
Isoform Tau-B [UniParc].

Checksum: D1CAB2EF89CDD7C0
Show »

FASTA36438,200
Isoform Tau-C [UniParc].

Checksum: 478641931A5A4143
Show »

FASTA34135,714
Isoform Tau-D [UniParc].

Checksum: B9427D315AD962B7
Show »

FASTA37238,961
Isoform Tau-E [UniParc].

Checksum: 3FB530E1CF1E4CA5
Show »

FASTA35036,740

References

« Hide 'large scale' references
[1]"Primary structure of high molecular weight tau present in the peripheral nervous system."
Couchie D., Mavilia C., Georgieff I.S., Liem R.K.H., Shelanski M.L., Nunez J.
Proc. Natl. Acad. Sci. U.S.A. 89:4378-4381(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNS-TAU).
Tissue: Neuroblastoma.
[2]"Expression of three- and four-repeat tau isoforms in mouse liver."
Kenner L., el-Shabrawi Y., Hutter H., Forstner M., Zatloukal K., Hoefler G., Preisegger K.-H., Kurzbauer R., Denk H.
Hepatology 20:1086-1089(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A; TAU-D AND TAU-E).
Strain: Him OF1.
Tissue: Brain, Kidney and Liver.
[3]"The primary structure and heterogeneity of tau protein from mouse brain."
Lee G., Cowan N.J., Kirschner M.
Science 239:285-288(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B AND TAU-C).
Tissue: Brain.
[4]"Molecular diversity at the carboxyl terminus of human and rat tau."
Sawa A., Oyama F., Matsushita M., Ihara Y.
Brain Res. Mol. Brain Res. 27:111-117(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM TAU-B).
Strain: ICR.
Tissue: Brain.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAU-D).
Tissue: Eye.
[7]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 504-513; 535-546; 591-609 AND 646-661, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[8]"High molecular weight tau proteins and acquisition of neuronal polarity in peripheral nervous system."
Couchie D., Gache Y., Mavilia C., Guilleminot J., Bridoux A.-M., Nivez M.-P., Nunez J.
C. R. Acad. Sci. III, Sci. Vie 316:404-409(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Phosphorylation of tau by fyn: implications for Alzheimer's disease."
Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M., Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.
J. Neurosci. 24:2304-2312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FYN.
[10]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-701; THR-706 AND SER-708, MASS SPECTROMETRY.
Tissue: Embryonic brain.
[11]"Proteomic analysis of in vivo phosphorylated synaptic proteins."
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.
J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-491; SER-494; SER-688; SER-692; THR-695; SER-696; SER-704 AND THR-706, MASS SPECTROMETRY.
Tissue: Forebrain.
[12]"Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation."
Babu J.R., Geetha T., Wooten M.W.
J. Neurochem. 94:192-203(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMC2.
[13]"Mammalian SAD kinases are required for neuronal polarization."
Kishi M., Pan Y.A., Crump J.G., Sanes J.R.
Science 307:929-932(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-554.
[14]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523 AND SER-527, MASS SPECTROMETRY.
Tissue: Brain.
[15]"LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons."
Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W., Raines A.N., Sanes J.R., Polleux F.
Cell 129:549-563(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-554.
[16]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-457; SER-490; SER-491; SER-494; THR-497; SER-688; SER-692; THR-695 AND SER-696, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[17]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-470; THR-473; TYR-489; SER-494; THR-497; SER-688; SER-692 AND THR-695, MASS SPECTROMETRY.
Tissue: Brain cortex.
[18]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-688; SER-692 AND SER-696, MASS SPECTROMETRY.
Tissue: Liver.
[19]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523; SER-688; SER-692 AND SER-701, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00230408.
IPI00331265.
IPI00407807.
IPI00465469.
IPI00468678.
IPI00649104.
PIRA28820.
A45301.
B28820.
RefSeqNP_001033698.1. NM_001038609.1.
NP_034968.3. NM_010838.3.
UniGeneMm.1287.

3D structure databases

ProteinModelPortalP10637.
ModBaseSearch...

Protein-protein interaction databases

IntActP10637. 2 interactions.
MINTMINT-3974107.

PTM databases

PhosphoSiteP10637.

Proteomic databases

PaxDbP10637.
PRIDEP10637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100347; ENSMUSP00000097919; ENSMUSG00000018411.
ENSMUST00000106988; ENSMUSP00000102601; ENSMUSG00000018411.
ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411.
GeneID17762.
KEGGmmu:17762.
UCSCuc011yga.1. mouse.

Organism-specific databases

CTD4137.
MGIMGI:97180. Mapt.

Phylogenomic databases

eggNOGNOG148882.
GeneTreeENSGT00530000063491.
HOVERGENHBG000991.
KOK04380.
OrthoDBEOG4B8JDC.

Gene expression databases

ArrayExpressP10637.
BgeeP10637.
CleanExMM_MAPT.
GenevestigatorP10637.
GermOnlineENSMUSG00000018411. Mus musculus.

Family and domain databases

InterProIPR027324. MAP2/MAP4/Tau.
IPR001084. Tau/MAP_tubulin-bd_rpt.
IPR002955. Tau_protein.
[Graphical view]
PANTHERPTHR11501. PTHR11501. 1 hit.
PfamPF00418. Tubulin-binding. 4 hits.
[Graphical view]
PRINTSPR01261. TAUPROTEIN.
PROSITEPS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPT. mouse.
NextBio292453.
SOURCESearch...

Entry information

Entry nameTAU_MOUSE
AccessionPrimary (citable) accession number: P10637
Secondary accession number(s): A2A5Y9 expand/collapse secondary AC list , P10638, Q60684, Q60685, Q60686, Q62286, Q91WK4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents