TAU_BOVIN - dbPTM
TAU_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAU_BOVIN
UniProt AC P29172
Protein Name Microtubule-associated protein tau
Gene Name MAPT
Organism Bos taurus (Bovine).
Sequence Length 448
Subcellular Localization Cytoplasm, cytosol. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, axon. Cytoplasm . Cell projection, dendrite . Mostly found in the axons of neurons, in the cytosol and in association with pla
Protein Description 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 MAEPRQEFDVMEDHAQGDYTLQDQEGDMDPGLKESPLQTPADDGSEEPGSETSDAKSTPTAEDATAPLVDEGAPGEQAAAQAPAEIPEGTAAEEAGIGDTSNLEDQAAGHVTQARMVSKGKDGTGPDDKKTKGADGKPGTKIATPRGAAPPGQKGQANATRIPAKTTPTPKTSPATMQVQKKPPPAGAKSERGESGKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSAAKSRLQAAPGPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEPRQEFD
------CCCCCCCCC
35.19-
19PhosphorylationEDHAQGDYTLQDQEG
CHHCCCCCCCCCCCC
19.04-
35PhosphorylationMDPGLKESPLQTPAD
CCCCCCCCCCCCCCC
29.35-
50PhosphorylationDGSEEPGSETSDAKS
CCCCCCCCCCCCCCC
48.71-
58PhosphorylationETSDAKSTPTAEDAT
CCCCCCCCCCHHHCC
24.77-
60PhosphorylationSDAKSTPTAEDATAP
CCCCCCCCHHHCCCC
42.65-
100PhosphorylationEEAGIGDTSNLEDQA
HHCCCCCCCCHHHHH
17.82-
144PhosphorylationKPGTKIATPRGAAPP
CCCCEECCCCCCCCC
19.59-
146MethylationGTKIATPRGAAPPGQ
CCEECCCCCCCCCCC
42.92-
154"N6,N6-dimethyllysine"GAAPPGQKGQANATR
CCCCCCCCCCCCCCC
59.93-
154AcetylationGAAPPGQKGQANATR
CCCCCCCCCCCCCCC
59.93-
154MethylationGAAPPGQKGQANATR
CCCCCCCCCCCCCCC
59.93-
160PhosphorylationQKGQANATRIPAKTT
CCCCCCCCCCCCCCC
29.01-
166PhosphorylationATRIPAKTTPTPKTS
CCCCCCCCCCCCCCC
39.86-
167PhosphorylationTRIPAKTTPTPKTSP
CCCCCCCCCCCCCCC
25.18-
172PhosphorylationKTTPTPKTSPATMQV
CCCCCCCCCCCEEEE
40.94-
198PhosphorylationERGESGKSGDRSGYS
CCCCCCCCCCCCCCC
49.83-
202PhosphorylationSGKSGDRSGYSSPGS
CCCCCCCCCCCCCCC
46.99-
204PhosphorylationKSGDRSGYSSPGSPG
CCCCCCCCCCCCCCC
13.76-
205PhosphorylationSGDRSGYSSPGSPGT
CCCCCCCCCCCCCCC
33.31-
206PhosphorylationGDRSGYSSPGSPGTP
CCCCCCCCCCCCCCC
25.4629541418
209PhosphorylationSGYSSPGSPGTPGSR
CCCCCCCCCCCCCCC
24.4429541418
212PhosphorylationSSPGSPGTPGSRSRT
CCCCCCCCCCCCCCC
28.06-
219PhosphorylationTPGSRSRTPSLPTPP
CCCCCCCCCCCCCCC
20.62-
221PhosphorylationGSRSRTPSLPTPPTR
CCCCCCCCCCCCCCC
46.50-
224PhosphorylationSRTPSLPTPPTREPK
CCCCCCCCCCCCCCC
47.39-
232AcetylationPPTREPKKVAVVRTP
CCCCCCCEEEEEECC
46.25-
238PhosphorylationKKVAVVRTPPKSPSA
CEEEEEECCCCCHHH
32.12-
242PhosphorylationVVRTPPKSPSAAKSR
EEECCCCCHHHHHHH
29.84-
244PhosphorylationRTPPKSPSAAKSRLQ
ECCCCCHHHHHHHHH
48.20-
266MethylationDLKNVKSKIGSTENL
CHHHHHHHCCCCCCC
45.42-
266AcetylationDLKNVKSKIGSTENL
CHHHHHHHCCCCCCC
45.42-
269PhosphorylationNVKSKIGSTENLKHQ
HHHHHCCCCCCCCCC
35.70-
288AcetylationKVQIINKKLDLSNVQ
CEEEECCEECHHHHH
42.62-
292PhosphorylationINKKLDLSNVQSKCG
ECCEECHHHHHHHCC
34.32-
296PhosphorylationLDLSNVQSKCGSKDN
ECHHHHHHHCCCCCC
26.15-
297AcetylationDLSNVQSKCGSKDNI
CHHHHHHHCCCCCCC
26.06-
300PhosphorylationNVQSKCGSKDNIKHV
HHHHHCCCCCCCEEC
46.43-
305AcetylationCGSKDNIKHVPGGGS
CCCCCCCEECCCCCC
44.82-
312PhosphorylationKHVPGGGSVQIVYKP
EECCCCCCEEEEEEC
17.70-
318"N6,N6-dimethyllysine"GSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.89-
318AcetylationGSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.89-
318MethylationGSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.89-
324AcetylationYKPVDLSKVTSKCGS
EECCCHHHHHHCCCC
57.75-
328AcetylationDLSKVTSKCGSLGNI
CHHHHHHCCCCCCCC
33.00-
331PhosphorylationKVTSKCGSLGNIHHK
HHHHCCCCCCCCCCC
42.44-
338AcetylationSLGNIHHKPGGGQVE
CCCCCCCCCCCCCEE
31.06-
350AcetylationQVEVKSEKLDFKDRV
CEEEEEEECCHHHHH
61.52-
354AcetylationKSEKLDFKDRVQSKI
EEEECCHHHHHHHHH
44.27-
356MethylationEKLDFKDRVQSKIGS
EECCHHHHHHHHHCC
29.03-
359PhosphorylationDFKDRVQSKIGSLDN
CHHHHHHHHHCCCCC
24.31-
363PhosphorylationRVQSKIGSLDNITHV
HHHHHHCCCCCCEEC
35.70-
376AcetylationHVPGGGNKKIETHKL
ECCCCCCCCCEEEEC
59.40-
392AcetylationFRENAKAKTDHGAEI
EHHHCCCCCCCCCEE
54.50-
401PhosphorylationDHGAEIVYKSPVVSG
CCCCEEEEECCCCCC
16.0629541418
403PhosphorylationGAEIVYKSPVVSGDT
CCEEEEECCCCCCCC
12.7729541418
407PhosphorylationVYKSPVVSGDTSPRH
EEECCCCCCCCCCCH
31.0529541418
410PhosphorylationSPVVSGDTSPRHLSN
CCCCCCCCCCCHHCC
44.1229541418
411PhosphorylationPVVSGDTSPRHLSNV
CCCCCCCCCCHHCCC
25.3629541418
416PhosphorylationDTSPRHLSNVSSTGS
CCCCCHHCCCCCCCC
29.1228710545
419PhosphorylationPRHLSNVSSTGSIDM
CCHHCCCCCCCCCCC
26.8329541418
420PhosphorylationRHLSNVSSTGSIDMV
CHHCCCCCCCCCCCC
32.2929541418
421PhosphorylationHLSNVSSTGSIDMVD
HHCCCCCCCCCCCCC
27.6929541418
423PhosphorylationSNVSSTGSIDMVDSP
CCCCCCCCCCCCCCH
18.5929541418
429PhosphorylationGSIDMVDSPQLATLA
CCCCCCCCHHHHHHH
11.79-
434PhosphorylationVDSPQLATLADEVSA
CCCHHHHHHHHHHHH
30.94-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
202SPhosphorylationKinaseTTBK1Q5TCY1
PSP
209SPhosphorylationKinaseTTBK1Q5TCY1
PSP
212TPhosphorylationKinaseTTBK1Q5TCY1
PSP
242SPhosphorylationKinaseTTBK1Q5TCY1
PSP
403SPhosphorylationKinaseTTBK1Q5TCY1
PSP
411SPhosphorylationKinaseTTBK1Q5TCY1
PSP
423SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
423SPhosphorylationKinaseCAMK-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAU_BOVIN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TAU_BOVIN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBA4A_HUMANTUBA4Aphysical
19681044

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAU_BOVIN

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Related Literatures of Post-Translational Modification

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