TAU_MOUSE - dbPTM
TAU_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAU_MOUSE
UniProt AC P10637
Protein Name Microtubule-associated protein tau
Gene Name Mapt
Organism Mus musculus (Mouse).
Sequence Length 733
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 MADPRQEFDTMEDHAGDYTLLQDQEGDMDHGLKESPPQPPADDGAEEPGSETSDAKSTPTAEDVTAPLVDERAPDKQAAAQPHTEIPEGITAEEAGIGDTPNQEDQAAGHVTQGRREGQAPDLGTSDWTRQQVSSMSGAPLLPQGLREATCQPSGTRPEDIEKSHPASELLRRGPPQKEGWGQDRLGSEEEVDEDLTVDESSQDSPPSQASLTPGRAAPQAGSGSVCGETASVPGLPTEGSVPLPADFFSKVSAETQASQPEGPGTGPMEEGHEAAPEFTFHVEIKASTPKEQDLEGATVVGVPGEEQKAQTQGPSVGKGTKEASLQEPPGKQPAAGLPGRPVSRVPQLKARVASKDRTGNDEKKAKTSTPSCAKAPSHRPCLSPTRPTLGSSDPLIKPSSPAVSPEPATSPKHVSSVTPRNGSPGTKQMKLKGADGKTGAKIATPRGAASPAQKGTSNATRIPAKTTPSPKTPPGSGEPPKSGERSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSASKSRLQTAPVPMPDLKNVRSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
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------MADPRQEFD
------CCCHHHHCC
35.20-
18PhosphorylationMEDHAGDYTLLQDQE
CHHCCCCCEEEECCC
9.8114999081
33UbiquitinationGDMDHGLKESPPQPP
CCCCCCCCCCCCCCC
61.8226192747
35PhosphorylationMDHGLKESPPQPPAD
CCCCCCCCCCCCCCC
40.0525195567
42 (in isoform 3)Phosphorylation-61.7325521595
42 (in isoform 4)Phosphorylation-61.7325521595
42 (in isoform 5)Phosphorylation-61.7325521595
50PhosphorylationDGAEEPGSETSDAKS
CCCCCCCCCCCCCCC
48.7125521595
52PhosphorylationAEEPGSETSDAKSTP
CCCCCCCCCCCCCCC
33.3425521595
53PhosphorylationEEPGSETSDAKSTPT
CCCCCCCCCCCCCCC
31.3625521595
54 (in isoform 3)Phosphorylation-66.4926643407
54 (in isoform 4)Phosphorylation-66.4926643407
54 (in isoform 5)Phosphorylation-66.4926643407
57PhosphorylationSETSDAKSTPTAEDV
CCCCCCCCCCCHHHC
41.1425521595
58PhosphorylationETSDAKSTPTAEDVT
CCCCCCCCCCHHHCC
24.7725521595
60PhosphorylationSDAKSTPTAEDVTAP
CCCCCCCCHHHCCCC
42.6525521595
60 (in isoform 3)Phosphorylation-42.6526643407
60 (in isoform 4)Phosphorylation-42.6526643407
60 (in isoform 5)Phosphorylation-42.6526643407
65PhosphorylationTPTAEDVTAPLVDER
CCCHHHCCCCCCCCC
34.5729899451
100PhosphorylationEEAGIGDTPNQEDQA
HHCCCCCCCCHHHHH
20.9426192747
100 (in isoform 2)Phosphorylation-20.9430372032
112 (in isoform 2)Phosphorylation-21.4526643407
115MethylationAGHVTQGRREGQAPD
CCCCCCCCCCCCCCC
24.5326192747
118 (in isoform 2)Phosphorylation-27.4326643407
135PhosphorylationWTRQQVSSMSGAPLL
HHHHHHHHCCCCCCC
20.3628464351
188PhosphorylationWGQDRLGSEEEVDED
CCCCCCCCHHHCCCC
46.5626239621
197PhosphorylationEEVDEDLTVDESSQD
HHCCCCCCCCCCCCC
37.9326239621
201PhosphorylationEDLTVDESSQDSPPS
CCCCCCCCCCCCCCC
28.9226239621
202PhosphorylationDLTVDESSQDSPPSQ
CCCCCCCCCCCCCCC
35.6426239621
205PhosphorylationVDESSQDSPPSQASL
CCCCCCCCCCCCCCC
30.9523737553
208PhosphorylationSSQDSPPSQASLTPG
CCCCCCCCCCCCCCC
41.5923737553
211PhosphorylationDSPPSQASLTPGRAA
CCCCCCCCCCCCCCC
25.7421183079
213PhosphorylationPPSQASLTPGRAAPQ
CCCCCCCCCCCCCCC
22.6223384938
223PhosphorylationRAAPQAGSGSVCGET
CCCCCCCCCCCCCCC
30.8029899451
225PhosphorylationAPQAGSGSVCGETAS
CCCCCCCCCCCCCCC
18.8729899451
288PhosphorylationFHVEIKASTPKEQDL
EEEEEECCCCCCCCC
39.9926239621
289PhosphorylationHVEIKASTPKEQDLE
EEEEECCCCCCCCCC
43.1526239621
299PhosphorylationEQDLEGATVVGVPGE
CCCCCCCEEECCCCH
26.9523984901
355PhosphorylationQLKARVASKDRTGND
HHHHHHHCCCCCCCH
32.0328382018
369PhosphorylationDEKKAKTSTPSCAKA
HHHHCCCCCCCHHCC
37.30-
378PhosphorylationPSCAKAPSHRPCLSP
CCHHCCCCCCCCCCC
36.6726643407
384PhosphorylationPSHRPCLSPTRPTLG
CCCCCCCCCCCCCCC
30.8326643407
386PhosphorylationHRPCLSPTRPTLGSS
CCCCCCCCCCCCCCC
46.0025195567
389PhosphorylationCLSPTRPTLGSSDPL
CCCCCCCCCCCCCCC
40.2226643407
392PhosphorylationPTRPTLGSSDPLIKP
CCCCCCCCCCCCCCC
34.3826643407
393PhosphorylationTRPTLGSSDPLIKPS
CCCCCCCCCCCCCCC
41.2626643407
400O-linked_GlycosylationSDPLIKPSSPAVSPE
CCCCCCCCCCCCCCC
43.9130059200
416PhosphorylationATSPKHVSSVTPRNG
CCCCCCCCCCCCCCC
20.8626643407
417PhosphorylationTSPKHVSSVTPRNGS
CCCCCCCCCCCCCCC
28.9926643407
419PhosphorylationPKHVSSVTPRNGSPG
CCCCCCCCCCCCCCC
20.6226643407
424PhosphorylationSVTPRNGSPGTKQMK
CCCCCCCCCCCCEEE
24.5726643407
445PhosphorylationKTGAKIATPRGAASP
CCCCCEECCCCCCCH
19.5922324799
447MethylationGAKIATPRGAASPAQ
CCCEECCCCCCCHHH
42.9226192747
451PhosphorylationATPRGAASPAQKGTS
ECCCCCCCHHHCCCC
21.8928382018
455"N6,N6-dimethyllysine"GAASPAQKGTSNATR
CCCCHHHCCCCCCCC
67.28-
455AcetylationGAASPAQKGTSNATR
CCCCHHHCCCCCCCC
67.2826192747
455MethylationGAASPAQKGTSNATR
CCCCHHHCCCCCCCC
67.2826192747
457PhosphorylationASPAQKGTSNATRIP
CCHHHCCCCCCCCCC
26.3329899451
461PhosphorylationQKGTSNATRIPAKTT
HCCCCCCCCCCCCCC
33.1226192747
467PhosphorylationATRIPAKTTPSPKTP
CCCCCCCCCCCCCCC
46.1518388127
468PhosphorylationTRIPAKTTPSPKTPP
CCCCCCCCCCCCCCC
22.5125521595
470PhosphorylationIPAKTTPSPKTPPGS
CCCCCCCCCCCCCCC
36.6225521595
473PhosphorylationKTTPSPKTPPGSGEP
CCCCCCCCCCCCCCC
37.7925521595
477PhosphorylationSPKTPPGSGEPPKSG
CCCCCCCCCCCCCCC
45.8425521595
483PhosphorylationGSGEPPKSGERSGYS
CCCCCCCCCCCCCCC
52.2225521595
487PhosphorylationPPKSGERSGYSSPGS
CCCCCCCCCCCCCCC
37.4725521595
489PhosphorylationKSGERSGYSSPGSPG
CCCCCCCCCCCCCCC
13.7625521595
490PhosphorylationSGERSGYSSPGSPGT
CCCCCCCCCCCCCCC
33.3125521595
491PhosphorylationGERSGYSSPGSPGTP
CCCCCCCCCCCCCCC
25.4625521595
494PhosphorylationSGYSSPGSPGTPGSR
CCCCCCCCCCCCCCC
24.4425521595
497PhosphorylationSSPGSPGTPGSRSRT
CCCCCCCCCCCCCCC
28.0625521595
500PhosphorylationGSPGTPGSRSRTPSL
CCCCCCCCCCCCCCC
28.4325521595
502PhosphorylationPGTPGSRSRTPSLPT
CCCCCCCCCCCCCCC
42.0524925903
504PhosphorylationTPGSRSRTPSLPTPP
CCCCCCCCCCCCCCC
20.6215249677
506PhosphorylationGSRSRTPSLPTPPTR
CCCCCCCCCCCCCCC
46.5025521595
509PhosphorylationSRTPSLPTPPTREPK
CCCCCCCCCCCCCCC
47.3925521595
512PhosphorylationPSLPTPPTREPKKVA
CCCCCCCCCCCCEEE
49.2024925903
517AcetylationPPTREPKKVAVVRTP
CCCCCCCEEEEEECC
46.2526192747
523PhosphorylationKKVAVVRTPPKSPSA
CEEEEEECCCCCCCC
32.1225521595
527PhosphorylationVVRTPPKSPSASKSR
EEECCCCCCCCCCCC
29.8425521595
529O-linked_GlycosylationRTPPKSPSASKSRLQ
ECCCCCCCCCCCCCC
52.8730059200
529PhosphorylationRTPPKSPSASKSRLQ
ECCCCCCCCCCCCCC
52.8725521595
531PhosphorylationPPKSPSASKSRLQTA
CCCCCCCCCCCCCCC
35.1924925903
533PhosphorylationKSPSASKSRLQTAPV
CCCCCCCCCCCCCCC
35.4129899451
537PhosphorylationASKSRLQTAPVPMPD
CCCCCCCCCCCCCCC
37.2029899451
546UbiquitinationPVPMPDLKNVRSKIG
CCCCCCHHHHHHHCC
61.86-
551AcetylationDLKNVRSKIGSTENL
CHHHHHHHCCCCCCC
40.2926192747
551MethylationDLKNVRSKIGSTENL
CHHHHHHHCCCCCCC
40.2926192747
551UbiquitinationDLKNVRSKIGSTENL
CHHHHHHHCCCCCCC
40.2926192747
554PhosphorylationNVRSKIGSTENLKHQ
HHHHHCCCCCCCCCC
35.7025521595
555PhosphorylationVRSKIGSTENLKHQP
HHHHCCCCCCCCCCC
24.5522324799
559UbiquitinationIGSTENLKHQPGGGK
CCCCCCCCCCCCCCC
52.3426192747
573AcetylationKVQIINKKLDLSNVQ
CEEEECCEECHHHHH
42.6226192747
573UbiquitinationKVQIINKKLDLSNVQ
CEEEECCEECHHHHH
42.6226192747
577PhosphorylationINKKLDLSNVQSKCG
ECCEECHHHHHHHCC
34.3225777480
581PhosphorylationLDLSNVQSKCGSKDN
ECHHHHHHHCCCCCC
26.1520415495
582AcetylationDLSNVQSKCGSKDNI
CHHHHHHHCCCCCCC
26.0626192747
582UbiquitinationDLSNVQSKCGSKDNI
CHHHHHHHCCCCCCC
26.06-
585PhosphorylationNVQSKCGSKDNIKHV
HHHHHCCCCCCCEEC
46.43-
590AcetylationCGSKDNIKHVPGGGS
CCCCCCCEECCCCCC
44.8226192747
590UbiquitinationCGSKDNIKHVPGGGS
CCCCCCCEECCCCCC
44.8226192747
597PhosphorylationKHVPGGGSVQIVYKP
EECCCCCCEEEEEEC
17.7020047950
602PhosphorylationGGSVQIVYKPVDLSK
CCCEEEEEECCCHHH
15.94-
603"N6,N6-dimethyllysine"GSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.89-
603AcetylationGSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.8926192747
603MethylationGSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.8926192747
603UbiquitinationGSVQIVYKPVDLSKV
CCEEEEEECCCHHHH
27.8926192747
609AcetylationYKPVDLSKVTSKCGS
EECCCHHHHHHCCCC
57.7526192747
609UbiquitinationYKPVDLSKVTSKCGS
EECCCHHHHHHCCCC
57.7526192747
613AcetylationDLSKVTSKCGSLGNI
CHHHHHHCCCCCCCC
33.0026192747
613UbiquitinationDLSKVTSKCGSLGNI
CHHHHHHCCCCCCCC
33.0026192747
614S-nitrosocysteineLSKVTSKCGSLGNIH
HHHHHHCCCCCCCCC
4.48-
614S-nitrosylationLSKVTSKCGSLGNIH
HHHHHHCCCCCCCCC
4.4822178444
616PhosphorylationKVTSKCGSLGNIHHK
HHHHCCCCCCCCCCC
42.4429899451
623AcetylationSLGNIHHKPGGGQVE
CCCCCCCCCCCCCEE
31.0626192747
623UbiquitinationSLGNIHHKPGGGQVE
CCCCCCCCCCCCCEE
31.0626192747
635AcetylationQVEVKSEKLDFKDRV
CEEEEEEECCHHHHH
61.5226192747
635UbiquitinationQVEVKSEKLDFKDRV
CEEEEEEECCHHHHH
61.5226192747
639AcetylationKSEKLDFKDRVQSKI
EEEECCHHHHHHHHH
44.2726192747
639UbiquitinationKSEKLDFKDRVQSKI
EEEECCHHHHHHHHH
44.2726192747
641MethylationEKLDFKDRVQSKIGS
EECCHHHHHHHHHCC
29.0326192747
644PhosphorylationDFKDRVQSKIGSLDN
CHHHHHHHHHCCCCC
24.31-
645UbiquitinationFKDRVQSKIGSLDNI
HHHHHHHHHCCCCCC
33.7126192747
648PhosphorylationRVQSKIGSLDNITHV
HHHHHHCCCCCCEEC
35.7025521595
653PhosphorylationIGSLDNITHVPGGGN
HCCCCCCEECCCCCC
24.0729472430
661AcetylationHVPGGGNKKIETHKL
ECCCCCCCCCEEEEC
59.4026192747
661UbiquitinationHVPGGGNKKIETHKL
ECCCCCCCCCEEEEC
59.4026192747
665PhosphorylationGGNKKIETHKLTFRE
CCCCCCEEEECCHHH
27.9928059163
667UbiquitinationNKKIETHKLTFRENA
CCCCEEEECCHHHHC
57.5526192747
669PhosphorylationKIETHKLTFRENAKA
CCEEEECCHHHHCCC
26.0029899451
677AcetylationFRENAKAKTDHGAEI
HHHHCCCCCCCCCEE
54.5026192747
677UbiquitinationFRENAKAKTDHGAEI
HHHHCCCCCCCCCEE
54.5026192747
678PhosphorylationRENAKAKTDHGAEIV
HHHCCCCCCCCCEEE
37.7824925903
686PhosphorylationDHGAEIVYKSPVVSG
CCCCEEEEECCCCCC
16.0625521595
688PhosphorylationGAEIVYKSPVVSGDT
CCEEEEECCCCCCCC
12.7718388127
692O-linked_GlycosylationVYKSPVVSGDTSPRH
EEECCCCCCCCCCCH
31.0530059200
692PhosphorylationVYKSPVVSGDTSPRH
EEECCCCCCCCCCCH
31.0525521595
695PhosphorylationSPVVSGDTSPRHLSN
CCCCCCCCCCCHHCC
44.1225521595
696PhosphorylationPVVSGDTSPRHLSNV
CCCCCCCCCCHHCCC
25.3625521595
701PhosphorylationDTSPRHLSNVSSTGS
CCCCCHHCCCCCCCC
29.1218388127
704PhosphorylationPRHLSNVSSTGSIDM
CCHHCCCCCCCCCCC
26.8318388127
705PhosphorylationRHLSNVSSTGSIDMV
CHHCCCCCCCCCCCC
32.2918388127
706PhosphorylationHLSNVSSTGSIDMVD
HHCCCCCCCCCCCCC
27.6918388127
708PhosphorylationSNVSSTGSIDMVDSP
CCCCCCCCCCCCCCH
18.5918388127
714PhosphorylationGSIDMVDSPQLATLA
CCCCCCCCHHHHHHH
11.7926239621
719PhosphorylationVDSPQLATLADEVSA
CCCHHHHHHHHHHHH
30.9422324799

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
18YPhosphorylationKinaseFYNP39688
Uniprot
491SPhosphorylationKinaseCDK5P49615
PSP
491SPhosphorylationKinaseGSK3BQ9WV60
PSP
494SPhosphorylationKinaseGSK3BQ9WV60
PSP
494SPhosphorylationKinaseCK1-FAMILY-GPS
494SPhosphorylationKinaseTTBK1Q3UVR3
GPS
494SPhosphorylationKinasePDPK1Q9Z2A0
GPS
497TPhosphorylationKinaseCK1-FAMILY-GPS
497TPhosphorylationKinaseCDK5P49615
PSP
497TPhosphorylationKinaseGSK3BQ9WV60
PSP
497TPhosphorylationKinasePDPK1Q9Z2A0
GPS
506SPhosphorylationKinasePRKACAP17612
GPS
554SPhosphorylationKinasePHK-Uniprot
554SPhosphorylationKinaseBRSK1Q5RJI5
Uniprot
554SPhosphorylationKinaseMARK2Q7KZI7
PSP
554SPhosphorylationKinaseMARK1Q8VHJ5
Uniprot
554SPhosphorylationKinaseGSK3BQ9WV60
PSP
554SPhosphorylationKinaseBRSK2Q69Z98
Uniprot
688SPhosphorylationKinaseGSK3BQ9WV60
PSP
688SPhosphorylationKinasePDPK1Q9Z2A0
GPS
688SPhosphorylationKinaseCK1-FAMILY-GPS
688SPhosphorylationKinaseCDK5P49615
PSP
696SPhosphorylationKinasePDPK1Q9Z2A0
GPS
696SPhosphorylationKinaseGSK3BQ9WV60
PSP
696SPhosphorylationKinaseCK1-FAMILY-GPS
701SPhosphorylationKinasePRKACAP17612
GPS
-KUbiquitinationE3 ubiquitin ligaseStub1Q9WUD1
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
188SPhosphorylation

21183079
554SPhosphorylation

15705853

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_MOUSEHspa8physical
17954934
BAG1_MOUSEBag1physical
17954934
HDAC6_MOUSEHdac6physical
19457097
HSP7C_MOUSEHspa8physical
18346207
SYVN1_MOUSESyvn1physical
23719816
TERA_MOUSEVcpphysical
23719816

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523; SER-688; SER-692AND SER-701, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-688; SER-692AND SER-696, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-470; THR-473;TYR-489; SER-494; THR-497; SER-688; SER-692 AND THR-695, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-457; SER-490; SER-491;SER-494; THR-497; SER-688; SER-692; THR-695 AND SER-696, AND MASSSPECTROMETRY.
"LKB1 and SAD kinases define a pathway required for the polarizationof cortical neurons.";
Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W.,Raines A.N., Sanes J.R., Polleux F.;
Cell 129:549-563(2007).
Cited for: PHOSPHORYLATION AT SER-554.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523 AND SER-527, ANDMASS SPECTROMETRY.
"Mammalian SAD kinases are required for neuronal polarization.";
Kishi M., Pan Y.A., Crump J.G., Sanes J.R.;
Science 307:929-932(2005).
Cited for: PHOSPHORYLATION AT SER-554.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-491; SER-494;SER-688; SER-692; THR-695; SER-696; SER-704 AND THR-706, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-701; THR-706AND SER-708, AND MASS SPECTROMETRY.

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