P19332
uniprot
P19332
canonical
amino_acid_sequence
MAEPRQEFDTMEDQAGDYTMLQDQEGDMDHGLKESPPQPPADDGSEEPGSETSDAKSTPTAEDVTAPLVEERAPDKQATAQSHTEIPEGTTAEEAGIGDTPNMEDQAAGHVTQEPQKVEIFSQSLLVEPGRREGQAPDSGISDWTHQQVPSMSGAPLPPQGLREATHQPLGTRPEDVERSHPASELLWQESPQKEAWGKDRLGSEEEVDEDITMDESSQESPPSQASLAPGTATPQARSVSASGVSGETTSIPGFPAEGSIPLPADFFSKVSAETQASPPEGPGTGPSEEGHEAAPEFTFHVEIKASAPKEQDLEGATVVGAPAEEQKARGPSVGKGTKEASLLEPTDKQPAAGLPGRPVSRVPQLKARVAGVSKDRTGNDEKKAKTSTPSCAKTPSNRPCLSPTRPTPGSSDPLIKPSSPAVCPEPATSPKYVSSVTPRNGSPGTKQMKLKGADGKTGAKIATPRGAATPGQKGTSNATRIPAKTTPSPKTPPGSGEPPKSGERSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSASKSRLQTAPVPMPDLKNVRSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVHIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
uniprot
proteins
function
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.
uniprot
proteins
mass_dalton
78564
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: 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, MARK2, MARK3, MARK4), causing detachment from microtubules, and their disassembly (By similarity). 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). {ECO:0000250, ECO:0000250|UniProtKB:P10636}.
uniprot
proteins
pubmed
1542696
uniprot
proteins
pubmed
20133804
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2504728
uniprot
proteins
pubmed
2560640
uniprot
proteins
pubmed
7877441
uniprot
proteins
pubmed
7964751
uniprot
proteins
pubmed
8057376
uniprot
proteins
pubmed
8245007
uniprot
proteins
pubmed
8408300
uniprot
proteins
sequence_length
752
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10636}. Cell membrane {ECO:0000250|UniProtKB:P10636}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10636}; Cytoplasmic side {ECO:0000250|UniProtKB:P10636}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10636}. Cell projection, axon {ECO:0000250|UniProtKB:P10636}. Cell projection, dendrite {ECO:0000250|UniProtKB:P10636}. Secreted {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P10636}.
uniprot
proteins