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P10637

- TAU_MOUSE

UniProt

P10637 - TAU_MOUSE

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Protein
Microtubule-associated protein tau
Gene
Mapt, Mtapt, Tau
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. lipoprotein particle binding Source: Ensembl
  2. microtubule binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. protein kinase binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. axon cargo transport Source: MGI
  3. axon extension Source: MGI
  4. axonogenesis Source: MGI
  5. microtubule cytoskeleton organization Source: UniProtKB
  6. mitochondrion transport along microtubule Source: MGI
  7. negative regulation of intracellular transport Source: MGI
  8. neuron migration Source: MGI
  9. positive regulation of axon extension Source: UniProtKB
  10. positive regulation of microtubule polymerization Source: UniProtKB
  11. regulation of autophagy Source: Ensembl
  12. regulation of microtubule-based movement Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_210562. 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
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97180. Mapt.

Subcellular locationi

Cytoplasmcytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectionaxon
Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. axoneme Source: MGI
  3. cytoplasm Source: MGI
  4. cytosol Source: UniProtKB-SubCell
  5. growth cone Source: UniProtKB
  6. microtubule Source: UniProtKB-KW
  7. microtubule cytoskeleton Source: MGI
  8. nuclear periphery Source: Ensembl
  9. nucleus Source: MGI
  10. plasma membrane Source: UniProtKB
  11. 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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 733732Microtubule-associated protein tau
PRO_0000072742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei18 – 181Phosphotyrosine; by FYN By similarity
Modified residuei35 – 351Phosphoserine By similarity
Modified residuei188 – 1881Phosphoserine; by SGK1 By similarity
Modified residuei369 – 3691Phosphoserine By similarity
Modified residuei445 – 4451Phosphothreonine By similarity
Modified residuei467 – 4671Phosphothreonine By similarity
Modified residuei473 – 4731Phosphothreonine By similarity
Modified residuei489 – 4891Phosphotyrosine By similarity
Modified residuei490 – 4901Phosphoserine By similarity
Modified residuei491 – 4911Phosphoserine By similarity
Modified residuei494 – 4941Phosphoserine; by CK1, PDPK1 and TTBK11 Publication
Modified residuei497 – 4971Phosphothreonine; by CK1 and PDPK1
Modified residuei504 – 5041Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity
Modified residuei506 – 5061Phosphoserine By similarity
Modified residuei509 – 5091Phosphothreonine By similarity
Modified residuei523 – 5231Phosphothreonine; by GSK3-beta and PDPK1 By similarity
Modified residuei527 – 5271Phosphoserine By similarity
Modified residuei529 – 5291Phosphoserine; by PHK By similarity
Modified residuei554 – 5541Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK2 Publications
Modified residuei577 – 5771Phosphoserine; by PHK By similarity
Modified residuei581 – 5811Phosphoserine; by PHK By similarity
Disulfide bondi583 ↔ 614 By similarity
Modified residuei585 – 5851Phosphoserine By similarity
Modified residuei597 – 5971Phosphoserine By similarity
Modified residuei616 – 6161Phosphoserine By similarity
Modified residuei644 – 6441Phosphoserine; by PHK By similarity
Modified residuei648 – 6481Phosphoserine By similarity
Modified residuei688 – 6881Phosphoserine; by CK1 and PDPK11 Publication
Modified residuei692 – 6921Phosphoserine1 Publication
Modified residuei695 – 6951Phosphothreonine By similarity
Modified residuei696 – 6961Phosphoserine; by CK1 and PDPK11 Publication
Modified residuei701 – 7011Phosphoserine1 Publication
Modified residuei708 – 7081Phosphoserine By similarity
Modified residuei714 – 7141Phosphoserine By similarity
Modified residuei719 – 7191Phosphothreonine By similarity

Post-translational modificationi

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. 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.3 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10637.
PaxDbiP10637.
PRIDEiP10637.

PTM databases

PhosphoSiteiP10637.

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

ArrayExpressiP10637.
BgeeiP10637.
CleanExiMM_MAPT.
GenevestigatoriP10637.

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.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi201589. 9 interactions.
IntActiP10637. 8 interactions.
MINTiMINT-3974107.

Structurei

3D structure databases

ProteinModelPortaliP10637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati536 – 56631Tau/MAP 1
Add
BLAST
Repeati567 – 59731Tau/MAP 2
Add
BLAST
Repeati598 – 62831Tau/MAP 3
Add
BLAST
Repeati629 – 66032Tau/MAP 4
Add
BLAST

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG148882.
GeneTreeiENSGT00530000063491.
HOVERGENiHBG000991.
KOiK04380.
OrthoDBiEOG738045.
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. Align

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

MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS    50
ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT 100
PNQEDQAAGH VTQGRREGQA PDLGTSDWTR QQVSSMSGAP LLPQGLREAT 150
CQPSGTRPED IEKSHPASEL LRRGPPQKEG WGQDRLGSEE EVDEDLTVDE 200
SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG SVPLPADFFS 250
KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV 300
VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK 350
ARVASKDRTG NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS 400
SPAVSPEPAT SPKHVSSVTP RNGSPGTKQM KLKGADGKTG AKIATPRGAA 450
SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP PKSGERSGYS SPGSPGTPGS 500
RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV PMPDLKNVRS 550
KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI 600
VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD 650
NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL 700
SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL 733
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei34 – 9158Missing in isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.
VSP_003185Add
BLAST
Alternative sequencei92 – 11322Missing in isoform Tau-E.
VSP_003186Add
BLAST
Alternative sequencei114 – 350237Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.
VSP_003187Add
BLAST
Alternative sequencei368 – 43366Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.
VSP_003188Add
BLAST
Alternative sequencei567 – 59731Missing in isoform Tau-B and isoform Tau-C.
VSP_003189Add
BLAST
Alternative sequencei733 – 7331L → KAALLSSQVWNYSHDLATIT DLGL in isoform Tau-B.
VSP_003190

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31D → N1 Publication
Sequence conflicti9 – 91D → N1 Publication
Sequence conflicti405 – 4051S → C in CAM14797. 1 Publication
Sequence conflicti528 – 5281P → T in CAA78121. 1 Publication
Sequence conflicti549 – 5491R → G in AAH14748. 1 Publication
Sequence conflicti672 – 6721E → Q1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. mouse. [P10637-3]
uc007lwi.1. mouse. [P10637-4]
uc011yga.1. mouse. [P10637-6]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25527.1. [P10637-2 ]
CCDS25528.1. [P10637-5 ]
PIRi A28820.
A45301.
B28820.
RefSeqi NP_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 ]
UniGenei Mm.1287.

3D structure databases

ProteinModelPortali P10637.
ModBasei Search...

Protein-protein interaction databases

BioGridi 201589. 9 interactions.
IntActi P10637. 8 interactions.
MINTi MINT-3974107.

PTM databases

PhosphoSitei P10637.

Proteomic databases

MaxQBi P10637.
PaxDbi P10637.
PRIDEi P10637.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000100347 ; ENSMUSP00000097919 ; ENSMUSG00000018411 . [P10637-2 ]
ENSMUST00000106992 ; ENSMUSP00000102605 ; ENSMUSG00000018411 . [P10637-5 ]
GeneIDi 17762.
KEGGi mmu:17762.
UCSCi uc007lwf.1. mouse. [P10637-3 ]
uc007lwi.1. mouse. [P10637-4 ]
uc011yga.1. mouse. [P10637-6 ]

Organism-specific databases

CTDi 4137.
MGIi MGI:97180. Mapt.

Phylogenomic databases

eggNOGi NOG148882.
GeneTreei ENSGT00530000063491.
HOVERGENi HBG000991.
KOi K04380.
OrthoDBi EOG738045.
TreeFami TF316358.

Enzyme and pathway databases

Reactomei REACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

Miscellaneous databases

ChiTaRSi MAPT. mouse.
NextBioi 292453.
PROi P10637.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10637.
Bgeei P10637.
CleanExi MM_MAPT.
Genevestigatori P10637.

Family and domain databases

InterProi IPR027324. MAP2/MAP4/Tau.
IPR001084. MAP_tubulin-bd_rpt.
IPR002955. Tau.
[Graphical view ]
PANTHERi PTHR11501. PTHR11501. 1 hit.
Pfami PF00418. Tubulin-binding. 4 hits.
[Graphical view ]
PRINTSi PR01261. TAUPROTEIN.
PROSITEi PS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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, IDENTIFICATION BY 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. Cited for: PHOSPHORYLATION BY FYN.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  11. "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.
  12. "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.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  14. "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.
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-688; SER-692 AND SER-696, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: September 3, 2014
This is version 162 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

External Data

Dasty 3

Similar proteinsi