P19332 (TAU_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 123.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Microtubule-associated protein tau Alternative name(s): Neurofibrillary tangle protein Paired helical filament-tau Short name=PHF-tau | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 752 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. Ref.9 |
| 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. 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 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. 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
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 752 | 751 | Microtubule-associated protein tau | PRO_0000072746 | |||||||
Regions | |||||||||||
| Repeat | 555 – 585 | 31 | Tau/MAP 1 | ||||||||
| Repeat | 586 – 616 | 31 | Tau/MAP 2 | ||||||||
| Repeat | 617 – 647 | 31 | Tau/MAP 3 | ||||||||
| Repeat | 648 – 679 | 32 | Tau/MAP 4 | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||||
| Modified residue | 18 | 1 | Phosphotyrosine; by FYN By similarity | ||||||||
| Modified residue | 35 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 100 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 204 | 1 | Phosphoserine; by SGK1 By similarity | ||||||||
| Modified residue | 464 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 476 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 486 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 489 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 492 | 1 | Phosphothreonine Ref.7 | ||||||||
| Modified residue | 508 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 509 | 1 | Phosphoserine Ref.7 | ||||||||
| Modified residue | 510 | 1 | Phosphoserine Ref.7 | ||||||||
| Modified residue | 513 | 1 | Phosphoserine; by CK1, PDPK1 and TTBK1 Ref.7 | ||||||||
| Modified residue | 516 | 1 | Phosphothreonine; by CK1 and PDPK1 | ||||||||
| Modified residue | 523 | 1 | Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity | ||||||||
| Modified residue | 525 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 528 | 1 | Phosphothreonine Probable | ||||||||
| Modified residue | 542 | 1 | Phosphothreonine; by GSK3-beta and PDPK1 By similarity | ||||||||
| Modified residue | 546 | 1 | Phosphoserine Ref.7 | ||||||||
| Modified residue | 548 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 573 | 1 | Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK By similarity | ||||||||
| Modified residue | 596 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 600 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 604 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 616 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 635 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 663 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 667 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 707 | 1 | Phosphoserine; by CK1 and PDPK1 Ref.7 | ||||||||
| Modified residue | 711 | 1 | Phosphoserine Ref.7 | ||||||||
| Modified residue | 714 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 715 | 1 | Phosphoserine; by CK1 and PDPK1 Ref.7 | ||||||||
| Modified residue | 720 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 723 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 725 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 727 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 733 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 738 | 1 | Phosphothreonine By similarity | ||||||||
| Disulfide bond | 602 ↔ 633 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 34 – 91 | 58 | Missing in isoform Tau-F. | VSP_003191 | |||||||
| Alternative sequence | 63 – 91 | 29 | Missing in isoform Tau-C and isoform Tau-G. | VSP_003192 | |||||||
| Alternative sequence | 114 – 367 | 254 | Missing in isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Tau-G. | VSP_003193 | |||||||
| Alternative sequence | 387 – 452 | 66 | Missing in isoform Tau-B, isoform Tau-C, isoform Tau-E, isoform Tau-F and isoform Tau-G. | VSP_003194 | |||||||
| Alternative sequence | 586 – 616 | 31 | Missing in isoform Tau-G. | VSP_003195 | |||||||
| Alternative sequence | 752 | 1 | L → KPVLLSSEVWNYSHDFGHHT DLGL in isoform Tau-H. | VSP_003196 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 255 | 1 | F → L Ref.2 | ||||||||
| Sequence conflict | 284 | 1 | G → A Ref.2 | ||||||||
| Sequence conflict | 292 | 1 | H → D Ref.2 | ||||||||
| Sequence conflict | 618 | 1 | H → Q Ref.2 | ||||||||
| Sequence conflict | 618 | 1 | H → Q in CAA55889. Ref.3 | ||||||||
| Sequence conflict | 618 | 1 | H → Q Ref.4 | ||||||||
| Sequence conflict | 705 | 1 | Y → H in CAA55889. Ref.3 | ||||||||
| Sequence conflict | 734 | 1 | P → A Ref.2 | ||||||||
Sequences
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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. |
| IPI | IPI00230972. IPI00679178. IPI00679181. IPI00679236. IPI00679248. IPI00758434. IPI00817094. IPI00957830. |
| PIR | A38235. JS0306. S46264. |
| UniGene | Rn.2455. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-41779N. |
| MINT | MINT-1037362. |
PTM databases | |
| PhosphoSite | P19332. |
Proteomic databases | |
| PaxDb | P19332. |
| PRIDE | P19332. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | RGD:69329. rat. |
Organism-specific databases | |
| RGD | 69329. Mapt. |
Phylogenomic databases | |
| eggNOG | NOG148882. |
| HOGENOM | HOG000231029. |
| HOVERGEN | HBG000991. |
| OrthoDB | EOG4B8JDC. |
Gene expression databases | |
| ArrayExpress | P19332. |
| Genevestigator | P19332. |
| GermOnline | ENSRNOG00000005133. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR027324. MAP2/MAP4/Tau. IPR001084. Tau/MAP_tubulin-bd_rpt. IPR002955. Tau_protein. [Graphical view] |
| PANTHER | PTHR11501. PTHR11501. 1 hit. |
| Pfam | PF00418. Tubulin-binding. 4 hits. [Graphical view] |
| PRINTS | PR01261. TAUPROTEIN. |
| PROSITE | PS00229. TAU_MAP_1. 4 hits. PS51491. TAU_MAP_2. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P19332. |
| ChEMBL | CHEMBL1075117. |
Entry information
| Entry name | TAU_RAT | ||||||||
| Accession | Primary (citable) accession number: P19332 Secondary accession number(s): Q63567, Q63677, Q9QW06 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
