P29172 (TAU_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 107.
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 | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 448 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 By similarity. Interacts with FKBP4. Binds to CSNK1D By similarity. |
| 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. |
| Induction | During neurite outgrowth. |
| 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. Phosphorylation at Ser-269 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated by PHK By similarity. O-glycosylated; contains at least 4 GlcNAc. Site-specific or stoichiometric changes in glycosylation may modulate tau function and also play a role in PHF's formation. Ref.4 |
| Sequence similarities | Contains 4 Tau/MAP repeats. |
Ontologies
Alternative products
| This entry describes 20 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 6 of the 14 exons. One of these optional exons contains the additional tau/MAP repeat. Tau-A cDNA has been constructed from two overlapping cDNAs by PubMed:2498649: Tau-G and Tau-H sequences begin with exon 6 or a part of it (exon 6 is missing in isoforms that begin with exon 1). 3 different C-termini are obtained either by the retention or the splicing of intron 13/14 (2 different 5' splice donors). | ||||||
| Isoform Tau-A (identifier: P29172-1) Also known as: PBT43I12; 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: P29172-2) Also known as: PBT43-12; The sequence of this isoform differs from the canonical sequence as follows: 175-192: Missing. | ||||||
| Isoform Tau-C (identifier: P29172-3) The sequence of this isoform differs from the canonical sequence as follows: 175-192: Missing. 282-312: Missing. | ||||||
| Isoform Tau-D (identifier: P29172-4) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. | ||||||
| Isoform Tau-E (identifier: P29172-5) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 175-192: Missing. | ||||||
| Isoform Tau-F (identifier: P29172-6) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 175-192: Missing. 282-312: Missing. | ||||||
| Isoform Tau-G (identifier: P29172-7) Also known as: PBT4; The sequence of this isoform differs from the canonical sequence as follows: 1-131: MAEPRQEFDV...DGTGPDDKKT → MPLNHYLPYL...NSGAKEMKVK 175-192: Missing. | ||||||
| Isoform Tau-H (identifier: P29172-8) Also known as: PBT7; The sequence of this isoform differs from the canonical sequence as follows: 1-131: MAEPRQEFDV...DGTGPDDKKT → MKVK 175-192: Missing. | ||||||
| Isoform Tau-I (identifier: P29172-9) The sequence of this isoform differs from the canonical sequence as follows: 439-448: VSASLAKQGL → PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPSR | ||||||
| Isoform Tau-J (identifier: P29172-10) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 175-192: Missing. 439-448: VSASLAKQGL → PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPSR | ||||||
| Isoform Tau-K (identifier: P29172-11) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 175-192: Missing. 282-312: Missing. 439-448: VSASLAKQGL → PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPSR | ||||||
| Isoform Tau-L (identifier: P29172-12) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 92-113: Missing. 439-448: VSASLAKQGL → PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPSR | ||||||
| Isoform Tau-M (identifier: P29172-13) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 92-113: Missing. 175-192: Missing. 439-448: VSASLAKQGL → PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPSR | ||||||
| Isoform Tau-N (identifier: P29172-14) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 92-113: Missing. 175-192: Missing. 282-312: Missing. 439-448: VSASLAKQGL → PCVCPHHACVSAVRSLVTACPLTTSCCPEFPASPPTPSR | ||||||
| Isoform Tau-O (identifier: P29172-15) The sequence of this isoform differs from the canonical sequence as follows: 447-448: GL → ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPMGRHLLYTKGEVKEGEVQTPGPPSL | ||||||
| Isoform Tau-P (identifier: P29172-16) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 175-192: Missing. 447-448: GL → ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPMGRHLLYTKGEVKEGEVQTPGPPSL | ||||||
| Isoform Tau-Q (identifier: P29172-17) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 175-192: Missing. 282-312: Missing. 447-448: GL → ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPMGRHLLYTKGEVKEGEVQTPGPPSL | ||||||
| Isoform Tau-R (identifier: P29172-18) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 92-113: Missing. 447-448: GL → ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPMGRHLLYTKGEVKEGEVQTPGPPSL | ||||||
| Isoform Tau-S (identifier: P29172-19) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 92-113: Missing. 175-192: Missing. 447-448: GL → ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPMGRHLLYTKGEVKEGEVQTPGPPSL | ||||||
| Isoform Tau-T (identifier: P29172-20) The sequence of this isoform differs from the canonical sequence as follows: 63-91: Missing. 92-113: Missing. 175-192: Missing. 282-312: Missing. 447-448: GL → ALRLPPPRLCVCRAEPGHCLSPHYVMLSRVPRLATHPFSVMDIVPMGRHLLYTKGEVKEGEVQTPGPPSL |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 448 | 447 | Microtubule-associated protein tau | PRO_0000072736 | |||||||
Regions | |||||||||||
| Repeat | 251 – 281 | 31 | Tau/MAP 1 | ||||||||
| Repeat | 282 – 312 | 31 | Tau/MAP 2 | ||||||||
| Repeat | 313 – 343 | 31 | Tau/MAP 3 | ||||||||
| Repeat | 344 – 375 | 32 | Tau/MAP 4 | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||||
| Modified residue | 19 | 1 | Phosphotyrosine; by FYN By similarity | ||||||||
| Modified residue | 35 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 39 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 100 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 144 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 166 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 172 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 204 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 205 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 206 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 209 | 1 | Phosphoserine; by CK1, PDPK1 and TTBK1 By similarity | ||||||||
| Modified residue | 212 | 1 | Phosphothreonine; by CK1 and PDPK1 By similarity | ||||||||
| Modified residue | 219 | 1 | Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity | ||||||||
| Modified residue | 221 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 224 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 238 | 1 | Phosphothreonine; by GSK3-beta and PDPK1 By similarity | ||||||||
| Modified residue | 242 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 244 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 269 | 1 | Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK By similarity | ||||||||
| Modified residue | 292 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 296 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 300 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 312 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 331 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 359 | 1 | Phosphoserine; by PHK By similarity | ||||||||
| Modified residue | 363 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 403 | 1 | Phosphoserine; by CK1 and PDPK1 By similarity | ||||||||
| Modified residue | 407 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 410 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 411 | 1 | Phosphoserine; by CK1 and PDPK1 By similarity | ||||||||
| Modified residue | 416 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 419 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 421 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 423 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 429 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 434 | 1 | Phosphothreonine By similarity | ||||||||
| Disulfide bond | 298 ↔ 329 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1 – 131 | 131 | MAEPR…DDKKT → MPLNHYLPYLFLVSVLFQFV PFSHVLTFILILFMFMFKPS TPSSAKTLKNRPCLSPKRPT PGSSDPLIKPSSPAVCPEPS SSPKHVSSVTPRTGNSGAKE MKVK in isoform Tau-G. | VSP_003165 | |||||||
| Alternative sequence | 1 – 131 | 131 | MAEPR…DDKKT → MKVK in isoform Tau-H. | VSP_003166 | |||||||
| Alternative sequence | 63 – 91 | 29 | Missing in isoform Tau-D, isoform Tau-E, isoform Tau-F, isoform Tau-J, isoform Tau-K, isoform Tau-L, isoform Tau-M, isoform Tau-N, isoform Tau-P, isoform Tau-Q, isoform Tau-R, isoform Tau-S and isoform Tau-T. | VSP_003167 | |||||||
| Alternative sequence | 92 – 113 | 22 | Missing in isoform Tau-L, isoform Tau-M, isoform Tau-N, isoform Tau-R, isoform Tau-S and isoform Tau-T. | VSP_003168 | |||||||
| Alternative sequence | 175 – 192 | 18 | Missing in isoform Tau-B, isoform Tau-C, isoform Tau-E, isoform Tau-F, isoform Tau-G, isoform Tau-H, isoform Tau-J, isoform Tau-K, isoform Tau-M, isoform Tau-N, isoform Tau-P, isoform Tau-Q, isoform Tau-S and isoform Tau-T. | VSP_003169 | |||||||
| Alternative sequence | 282 – 312 | 31 | Missing in isoform Tau-C, isoform Tau-F, isoform Tau-K, isoform Tau-N, isoform Tau-Q and isoform Tau-T. | VSP_003170 | |||||||
| Alternative sequence | 439 – 448 | 10 | VSASLAKQGL → PCVCPHHACVSAVRSLVTAC PLTTSCCPEFPASPPTPSR in isoform Tau-I, isoform Tau-J, isoform Tau-K, isoform Tau-L, isoform Tau-M and isoform Tau-N. | VSP_003171 | |||||||
| Alternative sequence | 447 – 448 | 2 | GL → ALRLPPPRLCVCRAEPGHCL SPHYVMLSRVPRLATHPFSV MDIVPMGRHLLYTKGEVKEG EVQTPGPPSL in isoform Tau-O, isoform Tau-P, isoform Tau-Q, isoform Tau-R, isoform Tau-S and isoform Tau-T. | VSP_003172 | |||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains." Himmler A., Drechsel D., Kirschner M.W., Martin D.W. Jr. Mol. Cell. Biol. 9:1381-1388(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A; TAU-B; TAU-G AND TAU-H). Tissue: Brain. |
| [2] | "Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family." Himmler A. Mol. Cell. Biol. 9:1389-1396(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TAU-A; TAU-B; TAU-C; TAU-D; TAU-E; TAU-F; TAU-I; TAU-J; TAU-K; TAU-L; TAU-M; TAU-N; TAU-O; TAU-P; TAU-Q; TAU-R; TAU-S AND TAU-T). Tissue: Brain. |
| [3] | NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAU-F). Strain: Crossbred X Angus. Tissue: Liver. |
| [4] | "The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine." Arnold C.S., Johnson G.V.W., Cole R.N., Dong D.L.-Y., Lee M., Hart G.W. J. Biol. Chem. 271:28741-28744(1996) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L34953 L34952 Genomic DNA. Translation: AAA51609.1.M26157 mRNA. Translation: AAA30770.1. M26158 mRNA. Translation: AAA30771.1. M26178 L34951 Genomic DNA. Translation: AAA51601.1. Sequence problems.M26178 L34951 Genomic DNA. Translation: AAA51602.1. Sequence problems.M26178 L34951 Genomic DNA. Translation: AAA51603.1. Sequence problems.M26178 L34951 Genomic DNA. Translation: AAA51604.1. Sequence problems.M26178 L34951 Genomic DNA. Translation: AAA51605.1. Sequence problems.M26178 L34951 Genomic DNA. Translation: AAA51606.1. Sequence problems.BC109941 mRNA. Translation: AAI09942.1. |
| IPI | IPI00688243. IPI00689184. IPI00689650. IPI00691424. IPI00691678. IPI00693156. IPI00695008. IPI00695963. IPI00702850. IPI00703952. IPI00705840. IPI00706820. IPI00707389. IPI00710658. IPI00710788. IPI00713146. IPI00713909. IPI00716398. IPI00717925. IPI00718776. |
| PIR | QRBOT1. A31939. QRBOT2. B31939. |
| RefSeq | NP_776531.1. NM_174106.2. |
| UniGene | Bt.34217. |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P29172. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000023284; ENSBTAP00000023284; ENSBTAG00000017512. ENSBTAT00000042687; ENSBTAP00000040320; ENSBTAG00000017512. ENSBTAT00000064492; ENSBTAP00000054412; ENSBTAG00000017512. ENSBTAT00000064966; ENSBTAP00000054994; ENSBTAG00000017512. ENSBTAT00000065509; ENSBTAP00000056351; ENSBTAG00000017512. ENSBTAT00000065660; ENSBTAP00000056547; ENSBTAG00000017512. |
| GeneID | 281296. |
| KEGG | bta:281296. |
Organism-specific databases | |
| CTD | 4137. |
Phylogenomic databases | |
| eggNOG | NOG148882. |
| GeneTree | ENSGT00530000063491. |
| HOVERGEN | HBG000991. |
| InParanoid | P29172. |
| KO | K04380. |
| OMA | AGHVTQX. |
| OrthoDB | EOG4B8JDC. |
Gene expression databases | |
| ArrayExpress | P29172. |
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 | |
| NextBio | 20805325. |
Entry information
| Entry name | TAU_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P29172 Secondary accession number(s): P29173 Q32KT2 | ||||||||
| 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
