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P19332

- TAU_RAT

UniProt

P19332 - TAU_RAT

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Protein

Microtubule-associated protein tau

Gene

Mapt

Organism
Rattus norvegicus (Rat)
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. enzyme binding Source: UniProtKB
  2. microtubule binding Source: UniProtKB
  3. protein complex binding Source: RGD
  4. protein domain specific binding Source: RGD
  5. protein kinase binding Source: RGD
  6. protein phosphatase 2A binding Source: RGD

GO - Biological processi

  1. apoptotic process Source: RGD
  2. brain development Source: RGD
  3. female pregnancy Source: RGD
  4. intrinsic apoptotic signaling pathway in response to oxidative stress Source: RGD
  5. microtubule-based process Source: RGD
  6. microtubule cytoskeleton organization Source: UniProtKB
  7. neuron differentiation Source: RGD
  8. positive regulation of axon extension Source: UniProtKB
  9. positive regulation of microtubule polymerization Source: UniProtKB
  10. response to nutrient Source: RGD
  11. 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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi69329. 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. axonal growth cone Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. growth cone Source: UniProtKB
  5. microtubule Source: UniProtKB-KW
  6. neuron projection Source: RGD
  7. plasma membrane Source: UniProtKB
  8. tubulin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 752751Microtubule-associated protein tauPRO_0000072746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei18 – 181Phosphotyrosine; by FYNBy similarity
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei204 – 2041Phosphoserine; by SGK1By similarity
Modified residuei388 – 3881PhosphoserineBy similarity
Modified residuei464 – 4641PhosphothreonineBy similarity
Modified residuei486 – 4861PhosphothreonineBy similarity
Modified residuei492 – 4921Phosphothreonine1 Publication
Modified residuei508 – 5081PhosphotyrosineBy similarity
Modified residuei509 – 5091Phosphoserine1 Publication
Modified residuei510 – 5101Phosphoserine1 Publication
Modified residuei513 – 5131Phosphoserine; by CK1, PDPK1 and TTBK11 Publication
Modified residuei516 – 5161Phosphothreonine; by CK1 and PDPK1
Modified residuei523 – 5231Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1By similarity
Modified residuei525 – 5251PhosphoserineBy similarity
Modified residuei528 – 5281Phosphothreonine1 Publication
Modified residuei542 – 5421Phosphothreonine; by GSK3-beta and PDPK1By similarity
Modified residuei546 – 5461Phosphoserine1 Publication
Modified residuei548 – 5481Phosphoserine; by PHKBy similarity
Modified residuei573 – 5731Phosphoserine; by MARK1, BRSK1, BRSK2 and PHKBy similarity
Modified residuei596 – 5961Phosphoserine; by PHKBy similarity
Modified residuei600 – 6001Phosphoserine; by PHKBy similarity
Disulfide bondi602 ↔ 633By similarity
Modified residuei604 – 6041PhosphoserineBy similarity
Modified residuei616 – 6161PhosphoserineBy similarity
Modified residuei635 – 6351PhosphoserineBy similarity
Modified residuei663 – 6631Phosphoserine; by PHKBy similarity
Modified residuei667 – 6671PhosphoserineBy similarity
Modified residuei707 – 7071Phosphoserine; by CK1 and PDPK11 Publication
Modified residuei711 – 7111Phosphoserine1 Publication
Modified residuei714 – 7141PhosphothreonineBy similarity
Modified residuei715 – 7151Phosphoserine; by CK1 and PDPK11 Publication
Modified residuei720 – 7201PhosphoserineBy similarity
Modified residuei727 – 7271PhosphoserineBy similarity
Modified residuei733 – 7331PhosphoserineBy similarity
Modified residuei738 – 7381PhosphothreonineBy similarity

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, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19332.
PRIDEiP19332.

PTM databases

PhosphoSiteiP19332.

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.

Gene expression databases

GenevestigatoriP19332.

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.

Protein-protein interaction databases

DIPiDIP-41779N.
IntActiP19332. 3 interactions.
MINTiMINT-1037362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati555 – 58531Tau/MAP 1Add
BLAST
Repeati586 – 61631Tau/MAP 2Add
BLAST
Repeati617 – 64731Tau/MAP 3Add
BLAST
Repeati648 – 67932Tau/MAP 4Add
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.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG148882.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551F → L(PubMed:8408300)Curated
Sequence conflicti284 – 2841G → A(PubMed:8408300)Curated
Sequence conflicti292 – 2921H → D(PubMed:8408300)Curated
Sequence conflicti618 – 6181H → Q(PubMed:8408300)Curated
Sequence conflicti618 – 6181H → Q in CAA55889. (PubMed:8057376)Curated
Sequence conflicti618 – 6181H → Q(PubMed:2560640)Curated
Sequence conflicti705 – 7051Y → H in CAA55889. (PubMed:8057376)Curated
Sequence conflicti734 – 7341P → A(PubMed:8408300)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei34 – 9158Missing in isoform Tau-F. 1 PublicationVSP_003191Add
BLAST
Alternative sequencei63 – 9129Missing in isoform Tau-C and isoform Tau-G. 2 PublicationsVSP_003192Add
BLAST
Alternative sequencei114 – 367254Missing in isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Tau-G. 3 PublicationsVSP_003193Add
BLAST
Alternative sequencei387 – 45266Missing in isoform Tau-B, isoform Tau-C, isoform Tau-E, isoform Tau-F and isoform Tau-G. 5 PublicationsVSP_003194Add
BLAST
Alternative sequencei586 – 61631Missing in isoform Tau-G. 1 PublicationVSP_003195Add
BLAST
Alternative sequencei752 – 7521L → KPVLLSSEVWNYSHDFGHHT DLGL in isoform Tau-H. 1 PublicationVSP_003196

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.
PIRi A38235.
JS0306.
S46264.
UniGenei Rn.2455.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41779N.
IntActi P19332. 3 interactions.
MINTi MINT-1037362.

Chemistry

BindingDBi P19332.
ChEMBLi CHEMBL1075117.

PTM databases

PhosphoSitei P19332.

Proteomic databases

PaxDbi P19332.
PRIDEi P19332.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:69329. rat. [P19332-1 ]

Organism-specific databases

RGDi 69329. Mapt.

Phylogenomic databases

eggNOGi NOG148882.
HOGENOMi HOG000231029.
HOVERGENi HBG000991.
InParanoidi P19332.
PhylomeDBi P19332.

Miscellaneous databases

PROi P19332.

Gene expression databases

Genevestigatori P19332.

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

  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. Cited for: INTERACTION WITH FKBP4.

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: October 29, 2014
This is version 135 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

External Data

Dasty 3