Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Microtubule-associated protein tau  

UniProtKB / Swiss-Prot ID :  TAU_SPECI

Gene Name (Synonyms) : 
MAPT  

Species :  Spermophilus citellus (European suslik) (Citellus citellus). 

Subcellular Localization :  Cytoplasm, cytosol (By similarity). 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 

Protein 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. 

Protein Sequence MAEPRQEFDTAEDHAEGYALLQDQEGEHGLKASPLQTPADDGPEEPVSETSDAKSTPTAEDVTAPLVDER...
Predicted Secondary Structure CCCHHHHHHHHHHHCCCCEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
170Phosphothreonine.PSPKTPPGT
CCCCCCCCC
37.79UniProtKB
Link-
187Phosphoserine.RSGYSSPGS
CCCCCCCCC
33.31UniProtKB
Link-
188Phosphoserine.SGYSSPGSP
CCCCCCCCC
25.46UniProtKB
Link-
191Phosphoserine; by CK1, PDPK1 and TTBK1.SSPGSPGTP
CCCCCCCCC
24.44UniProtKB
Link-
194Phosphothreonine; by CK1 and PDPK1.GSPGTPGSR
CCCCCCCCC
28.06UniProtKB
Link-
201Phosphothreonine.SRSRTPSLP
CCCCCCCCC
20.62UniProtKB
Link-
251Phosphoserine; in form PHF-tau-like foundduring hibernation; by MARK1, BRSK1 andSKIGSTENL
CCCCCCCCC
35.70UniProtKB
Link-
385Phosphoserine; by CK1 and PDPK1.IVYKSPVVS
EEEECCCCC
12.77UniProtKB
Link-
393Phosphoserine; by CK1 and PDPK1.SGDTSPRHL
CCCCCCCCC
25.36UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures