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_RAT

Gene Name (Synonyms) : 
Mapt, Mtapt, Tau  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :  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. 

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 MAEPRQEFDTMEDQAGDYTMLQDQEGDMDHGLKESPPQPPADDGSEEPGSETSDAKSTPTAEDVTAPLVE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
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
172PhosphothreonineQPLGTRPED
CCCCCCCCC
51.22PhosphoELM
Link-
191PhosphoserineLWQESPQKE
CCCCCCCCC
19.96PhosphoELM
Link-
224PhosphoserineESPPSQASL
CCCCCCCCC
41.59PhosphoELM
Link-
227PhosphoserinePSQASLAPG
CCCCCCCCC
19.89PhosphoELM
Link-
388PhosphoserineKAKTSTPSC
CCCCCCCCC
37.30PhosphoELM
Link-
492PhosphothreoninePSPKTPPGS
CCCCCCCCC
37.79Phosphositeplus
Link-
492Phosphothreonine.PSPKTPPGS
CCCCCCCCC
37.79UniProtKB
Link-
509PhosphoserineRSGYSSPGS
CCCCCCCCC
33.31PhosphoELM
Link-
509PhosphoserineRSGYSSPGS
CCCCCCCCC
33.31Phosphositeplus
Link-
509Phosphoserine.RSGYSSPGS
CCCCCCCCC
33.31UniProtKB
Link-
510PhosphoserineSGYSSPGSP
CCCCCCCCC
25.46Phosphositeplus
Link-
510Phosphoserine.SGYSSPGSP
CCCCCCCCC
25.46UniProtKB
Link-
513PhosphoserineSSPGSPGTP
CCCCCCCCC
24.44PhosphoELM
Link-
513PhosphoserineSSPGSPGTP
CCCCCCCCC
24.44Phosphositeplus
Link-
513Phosphoserine; by CK1, PDPK1 and TTBK1.SSPGSPGTP
CCCCCCCCC
24.44UniProtKB
Link-
516PhosphothreonineGSPGTPGSR
CCCCCCCCC
28.06Phosphositeplus
Link-
516Phosphothreonine; by CK1 and PDPK1.GSPGTPGSR
CCCCCCCCC
28.06UniProtKB
Link-
523PhosphothreonineSRSRTPSLP
CCCCCCCCC
20.62Phosphositeplus
Link-
525PhosphoserineSRTPSLPTP
CCCCCCCCC
46.50Phosphositeplus
Link-
528PhosphothreoninePSLPTPPTR
CCCCCCCCC
47.39Phosphositeplus
Link-
542PhosphothreonineAVVRTPPKS
CCCCCCCCC
32.12Phosphositeplus
Link-
546PhosphoserineTPPKSPSAS
CCCCCCCCC
29.84Phosphositeplus
Link-
546Phosphoserine.TPPKSPSAS
CCCCCCCCC
29.84UniProtKB
Link-
552PhosphoserineSASKSRLQT
CCCCCCCCC
35.41Phosphositeplus
Link-
573PhosphoserineSKIGSTENL
CCCCCCCCC
35.70Phosphositeplus
Link-
635PhosphoserineSKCGSLGNI
CCCCCCCCC
42.44Phosphositeplus
Link-
667PhosphoserineSKIGSLDNI
HHCCCHHHC
35.70Phosphositeplus
Link-
707PhosphoserineIVYKSPVVS
EEEECCCCC
12.77Phosphositeplus
Link-
707Phosphoserine; by CK1 and PDPK1.IVYKSPVVS
EEEECCCCC
12.77UniProtKB
Link-
711PhosphoserineSPVVSGDTS
CCCCCCCCC
31.05PhosphoELM
Link-
711PhosphoserineSPVVSGDTS
CCCCCCCCC
31.05Phosphositeplus
Link-
711Phosphoserine.SPVVSGDTS
CCCCCCCCC
31.05UniProtKB
Link-
714PhosphothreonineVSGDTSPRH
CCCCCCCCC
44.12Phosphositeplus
Link-
715PhosphoserineSGDTSPRHL
CCCCCCCCC
25.36PhosphoELM
Link-
715PhosphoserineSGDTSPRHL
CCCCCCCCC
25.36Phosphositeplus
Link-
715Phosphoserine; by CK1 and PDPK1.SGDTSPRHL
CCCCCCCCC
25.36UniProtKB
Link-
727PhosphoserineSSTGSIDMV
CCCCCEECC
18.59Phosphositeplus
Link-
733PhosphoserineDMVDSPQLA
ECCCCCCHH
11.79Phosphositeplus
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
Phosphorylation
ReferencePubMed
"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).
Cited for: PROTEIN SEQUENCE OF 492-501; 506-515; 523-532; 537-551 AND 698-726,AND PHOSPHORYLATION AT THR-492; SER-509; SER-510; SER-513; THR-528;THR-542; SER-546; SER-707; SER-711 AND SER-715.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures