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P19332 (TAU_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length752 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. 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. Ref.9

Subcellular location

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.

Tissue specificity

Expressed in neurons. The larger forms (isoform tau-Aand 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 stage

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

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.

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. Ref.7

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_processapoptotic process

Inferred from direct assay PubMed 15750210. Source: RGD

brain development

Inferred from expression pattern PubMed 19540327. Source: RGD

female pregnancy

Inferred from expression pattern PubMed 22884690. Source: RGD

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from direct assay PubMed 12420308. Source: RGD

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule-based process

Non-traceable author statement PubMed 12805366. Source: RGD

neuron differentiation

Non-traceable author statement PubMed 15043998. Source: RGD

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

response to nutrient

Inferred from direct assay PubMed 16495207. Source: RGD

response to organic substance

Inferred from direct assay PubMed 16389547. Source: RGD

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

axonal growth cone

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from direct assay PubMed 15623521. Source: RGD

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

tubulin complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.9. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23986251PubMed 23035120. Source: IntAct

protein domain specific binding

Inferred from mutant phenotype PubMed 10580117. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 16982696. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

A6NAR82EBI-7080713,EBI-8755852From a different organism.
Pacsin1Q616446EBI-8758676,EBI-2255561From a different organism.

Alternative products

This entry describes 8 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 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)

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.
Isoform Tau-B (identifier: P19332-2)

Also known as: Big-tau; HMW-tau;

The sequence of this isoform differs from the canonical sequence as follows:
     387-452: Missing.
Isoform Tau-C (identifier: P19332-3)

The sequence of this isoform differs from the canonical sequence as follows:
     63-91: Missing.
     114-367: Missing.
     387-452: Missing.
Isoform Tau-D (identifier: P19332-4)

Also known as: SC2;

The sequence of this isoform differs from the canonical sequence as follows:
     114-367: Missing.
Isoform Tau-E (identifier: P19332-5)

The sequence of this isoform differs from the canonical sequence as follows:
     114-367: Missing.
     387-452: Missing.
Isoform Tau-F (identifier: P19332-6)

The sequence of this isoform differs from the canonical sequence as follows:
     34-91: Missing.
     114-367: Missing.
     387-452: Missing.
Isoform Tau-G (identifier: P19332-7)

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.
Isoform Tau-H (identifier: P19332-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 752751Microtubule-associated protein tau
PRO_0000072746

Regions

Repeat555 – 58531Tau/MAP 1
Repeat586 – 61631Tau/MAP 2
Repeat617 – 64731Tau/MAP 3
Repeat648 – 67932Tau/MAP 4

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue181Phosphotyrosine; by FYN By similarity
Modified residue351Phosphoserine By similarity
Modified residue2041Phosphoserine; by SGK1 By similarity
Modified residue3881Phosphoserine By similarity
Modified residue4641Phosphothreonine By similarity
Modified residue4861Phosphothreonine By similarity
Modified residue4921Phosphothreonine Ref.7
Modified residue5081Phosphotyrosine By similarity
Modified residue5091Phosphoserine Ref.7
Modified residue5101Phosphoserine Ref.7
Modified residue5131Phosphoserine; by CK1, PDPK1 and TTBK1 Ref.7
Modified residue5161Phosphothreonine; by CK1 and PDPK1
Modified residue5231Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity
Modified residue5251Phosphoserine By similarity
Modified residue5281Phosphothreonine Probable
Modified residue5421Phosphothreonine; by GSK3-beta and PDPK1 By similarity
Modified residue5461Phosphoserine Ref.7
Modified residue5481Phosphoserine; by PHK By similarity
Modified residue5731Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK By similarity
Modified residue5961Phosphoserine; by PHK By similarity
Modified residue6001Phosphoserine; by PHK By similarity
Modified residue6041Phosphoserine By similarity
Modified residue6161Phosphoserine By similarity
Modified residue6351Phosphoserine By similarity
Modified residue6631Phosphoserine; by PHK By similarity
Modified residue6671Phosphoserine By similarity
Modified residue7071Phosphoserine; by CK1 and PDPK1 Ref.7
Modified residue7111Phosphoserine Ref.7
Modified residue7141Phosphothreonine By similarity
Modified residue7151Phosphoserine; by CK1 and PDPK1 Ref.7
Modified residue7201Phosphoserine By similarity
Modified residue7271Phosphoserine By similarity
Modified residue7331Phosphoserine By similarity
Modified residue7381Phosphothreonine By similarity
Disulfide bond602 ↔ 633 By similarity

Natural variations

Alternative sequence34 – 9158Missing in isoform Tau-F.
VSP_003191
Alternative sequence63 – 9129Missing in isoform Tau-C and isoform Tau-G.
VSP_003192
Alternative sequence114 – 367254Missing in isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Tau-G.
VSP_003193
Alternative sequence387 – 45266Missing in isoform Tau-B, isoform Tau-C, isoform Tau-E, isoform Tau-F and isoform Tau-G.
VSP_003194
Alternative sequence586 – 61631Missing in isoform Tau-G.
VSP_003195
Alternative sequence7521L → KPVLLSSEVWNYSHDFGHHT DLGL in isoform Tau-H.
VSP_003196

Experimental info

Sequence conflict2551F → L Ref.2
Sequence conflict2841G → A Ref.2
Sequence conflict2921H → D Ref.2
Sequence conflict6181H → Q Ref.2
Sequence conflict6181H → Q in CAA55889. Ref.3
Sequence conflict6181H → Q Ref.4
Sequence conflict7051Y → H in CAA55889. Ref.3
Sequence conflict7341P → A Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Tau-A (SC1) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 915DCA04EF0B2902

FASTA75278,564
        10         20         30         40         50         60 
MAEPRQEFDT MEDQAGDYTM LQDQEGDMDH GLKESPPQPP ADDGSEEPGS ETSDAKSTPT 

        70         80         90        100        110        120 
AEDVTAPLVE ERAPDKQATA QSHTEIPEGT TAEEAGIGDT PNMEDQAAGH VTQEPQKVEI 

       130        140        150        160        170        180 
FSQSLLVEPG RREGQAPDSG ISDWTHQQVP SMSGAPLPPQ GLREATHQPL GTRPEDVERS 

       190        200        210        220        230        240 
HPASELLWQE SPQKEAWGKD RLGSEEEVDE DITMDESSQE SPPSQASLAP GTATPQARSV 

       250        260        270        280        290        300 
SASGVSGETT SIPGFPAEGS IPLPADFFSK VSAETQASPP EGPGTGPSEE GHEAAPEFTF 

       310        320        330        340        350        360 
HVEIKASAPK EQDLEGATVV GAPAEEQKAR GPSVGKGTKE ASLLEPTDKQ PAAGLPGRPV 

       370        380        390        400        410        420 
SRVPQLKARV AGVSKDRTGN DEKKAKTSTP SCAKTPSNRP CLSPTRPTPG SSDPLIKPSS 

       430        440        450        460        470        480 
PAVCPEPATS PKYVSSVTPR NGSPGTKQMK LKGADGKTGA KIATPRGAAT PGQKGTSNAT 

       490        500        510        520        530        540 
RIPAKTTPSP KTPPGSGEPP KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV 

       550        560        570        580        590        600 
RTPPKSPSAS KSRLQTAPVP MPDLKNVRSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS 

       610        620        630        640        650        660 
KCGSKDNIKH VPGGGSVHIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR 

       670        680        690        700        710        720 
VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS 

       730        740        750 
NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL 

« Hide

Isoform Tau-B (Big-tau) (HMW-tau) [UniParc].

Checksum: F3709D1844C3763D
Show »

FASTA68671,774
Isoform Tau-C [UniParc].

Checksum: 4ED13493B947A5E7
Show »

FASTA40342,048
Isoform Tau-D (SC2) [UniParc].

Checksum: 6DC5958544984730
Show »

FASTA49851,912
Isoform Tau-E [UniParc].

Checksum: BBBC0DF6D0394D72
Show »

FASTA43245,122
Isoform Tau-F [UniParc].

Checksum: 2323D277377BDBB7
Show »

FASTA37439,152
Isoform Tau-G (Fetal-tau) [UniParc].

Checksum: D4A2BD9C6DEAD376
Show »

FASTA37238,801
Isoform Tau-H [UniParc].

Checksum: AF16994BB897B2DE
Show »

FASTA77581,185

References

[1]"Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system."
Goedert M., Spillantini M.G., Crowther R.A.
Proc. Natl. Acad. Sci. U.S.A. 89:1983-1987(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
Tissue: Pheochromocytoma.
[2]"Expression of high molecular weight tau in the central and peripheral nervous systems."
Georgieff I.S., Liem R.K.H., Couchie D., Mavilia C., Nunez J., Shelanski M.L.
J. Cell Sci. 105:729-737(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-B).
Tissue: Spinal ganglion.
[3]"Complete sequence of 3'-untranslated region of tau from rat central nervous system. Implications for mRNA heterogeneity."
Sadot E., Marx R., Barg J., Behar L., Ginzburg I.
J. Mol. Biol. 241:325-331(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-F).
Strain: Wistar.
Tissue: Brain.
[4]"Developmentally regulated expression of specific tau sequences."
Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L.
Neuron 2:1389-1397(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-G).
Tissue: Brain.
[5]"Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA."
Kanai Y., Takemura R., Oshima T., Mori H., Ihara Y., Yanagisawa M., Masaki T., Hirokawa N.
J. Cell Biol. 109:1173-1184(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-E AND TAU-C).
[6]"Diversity of high-molecular-weight tau proteins in different regions of the nervous system."
Mavilia C., Couchie D., Nunez J.
J. Neurochem. 63:2300-2306(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 360-461 (ISOFORM TAU-A), NUCLEOTIDE SEQUENCE OF 106-113 AND 368-461 (ISOFORM TAU-D).
Tissue: Spinal cord.
[7]"In vivo phosphorylation sites in fetal and adult rat tau."
Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M., Titani K., Arai T., Kosik K.S., Ihara Y.
J. Biol. Chem. 268:25712-25717(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 492-501; 506-515; 523-532; 537-551 AND 698-726, PHOSPHORYLATION AT THR-492; SER-509; SER-510; SER-513; THR-528; THR-542; SER-546; SER-707; SER-711 AND SER-715.
[8]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 697-752 (ISOFORMS TAU-A; TAU-B; TAU-C; TAU-D; TAU-E; TAU-F AND TAU-G), NUCLEOTIDE SEQUENCE [MRNA] OF 752-775 (ISOFORM TAU-H).
Strain: Sprague-Dawley.
Tissue: Brain.
[9]"A role for FKBP52 in Tau protein function."
Chambraud B., Sardin E., Giustiniani J., Dounane O., Schumacher M., Goedert M., Baulieu E.E.
Proc. Natl. Acad. Sci. U.S.A. 107:2658-2663(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FKBP4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84156 mRNA. Translation: AAA42204.1.
X79321 mRNA. Translation: CAA55889.1.
D30628 Genomic DNA. No translation available.
D30629 mRNA. No translation available.
PIRA38235.
JS0306.
S46264.
UniGeneRn.2455.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-41779N.
IntActP19332. 3 interactions.
MINTMINT-1037362.

Chemistry

BindingDBP19332.
ChEMBLCHEMBL1075117.

PTM databases

PhosphoSiteP19332.

Proteomic databases

PaxDbP19332.
PRIDEP19332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:69329. rat. [P19332-1]

Organism-specific databases

RGD69329. Mapt.

Phylogenomic databases

eggNOGNOG148882.
HOGENOMHOG000231029.
HOVERGENHBG000991.
PhylomeDBP19332.

Gene expression databases

GenevestigatorP19332.

Family and domain databases

InterProIPR027324. MAP2/MAP4/Tau.
IPR001084. MAP_tubulin-bd_rpt.
IPR002955. Tau.
[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

PROP19332.

Entry information

Entry nameTAU_RAT
AccessionPrimary (citable) accession number: P19332
Secondary accession number(s): Q63567, Q63677, Q9QW06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families