BEGIN_MOUSE - dbPTM
BEGIN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BEGIN_MOUSE
UniProt AC Q68EF6
Protein Name Brain-enriched guanylate kinase-associated protein
Gene Name Begain
Organism Mus musculus (Mouse).
Sequence Length 600
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description May sustain the structure of the postsynaptic density (PSD)..
Protein Sequence MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQQRVSLHMEKHGCSLPSALCHPAYADSVPTCVIAKVLEKPDPGSLSSRMSDASARDLGYRDGVEKSGPRPPYKGDIYCSDPALYCPDEREHARRPSVDTPVTDVGFLRAQNSTDSAAEEEEEAEAAAFPEAYRREAYQGYAASLPTSSSYSSFSATSEEKEHAQAGTLTASQQAIYLSSRDEFFNRKPSATYGSGPRFAKAASTLGSPLEAQVAPGFARTVSPYPAEPYRYPASPGPQQALMPPNLWSLRAKPSGNRLAGEDIRGQWRPVSVEDVGAYSYQAGAAAGRAASPCNYSERYYGGGGGGGAAGGGSPGDKAEGRASPLYATYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPSRSADALAGYAASDGDGDRLRVQLCGAGSSPEPEHGSRESLEPSSMEASPEMHPPTRLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN
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
1Acetylation-------MEKLSALQ
-------CHHHHHHH
10.39-
16PhosphorylationEQKGELRKRLSYTTH
HHHHHHHHHHHHHHH
71.02-
19PhosphorylationGELRKRLSYTTHKLE
HHHHHHHHHHHHHHH
25.1929899451
21PhosphorylationLRKRLSYTTHKLEKL
HHHHHHHHHHHHHHH
21.0325338131
62PhosphorylationEKLRRIQSNYMALQR
HHHHHHHHHHHHHHH
27.7930635358
64PhosphorylationLRRIQSNYMALQRIN
HHHHHHHHHHHHHHH
6.7630635358
77UbiquitinationINQELEDKLYRMGQH
HHHHHHHHHHHCHHH
37.73-
136PhosphorylationQLLQCSQTYGRVHKV
HHHHHHHHHCCCEEH
16.2029899451
137PhosphorylationLLQCSQTYGRVHKVS
HHHHHHHHCCCEEHH
8.6929899451
194PhosphorylationLEKPDPGSLSSRMSD
HCCCCCCCHHHHCCH
30.3920415495
196PhosphorylationKPDPGSLSSRMSDAS
CCCCCCHHHHCCHHH
20.0021183079
197PhosphorylationPDPGSLSSRMSDASA
CCCCCHHHHCCHHHH
36.9821183079
200PhosphorylationGSLSSRMSDASARDL
CCHHHHCCHHHHHHH
28.9921183079
227PhosphorylationPPYKGDIYCSDPALY
CCCCCCEEECCCCCC
7.2219060867
229PhosphorylationYKGDIYCSDPALYCP
CCCCEEECCCCCCCC
29.6525521595
234PhosphorylationYCSDPALYCPDEREH
EECCCCCCCCCHHHH
12.2129899451
246PhosphorylationREHARRPSVDTPVTD
HHHCCCCCCCCCCCH
30.7125521595
249PhosphorylationARRPSVDTPVTDVGF
CCCCCCCCCCCHHHH
19.9418056256
252PhosphorylationPSVDTPVTDVGFLRA
CCCCCCCCHHHHHHC
26.6021183079
262PhosphorylationGFLRAQNSTDSAAEE
HHHHCCCCCCCHHHH
22.8525521595
263PhosphorylationFLRAQNSTDSAAEEE
HHHCCCCCCCHHHHH
41.3319060867
265PhosphorylationRAQNSTDSAAEEEEE
HCCCCCCCHHHHHHH
29.4825521595
302PhosphorylationPTSSSYSSFSATSEE
CCCCCCCCCCCCHHH
18.2629899451
317PhosphorylationKEHAQAGTLTASQQA
HHHHHHCCCCHHHHH
24.7729899451
319PhosphorylationHAQAGTLTASQQAIY
HHHHCCCCHHHHHHH
24.8929899451
321PhosphorylationQAGTLTASQQAIYLS
HHCCCCHHHHHHHHH
20.0025521595
326PhosphorylationTASQQAIYLSSRDEF
CHHHHHHHHHCHHHH
11.9830635358
328PhosphorylationSQQAIYLSSRDEFFN
HHHHHHHHCHHHHHC
13.3230635358
329PhosphorylationQQAIYLSSRDEFFNR
HHHHHHHCHHHHHCC
40.9530635358
341PhosphorylationFNRKPSATYGSGPRF
HCCCCCCCCCCCHHH
32.52-
344PhosphorylationKPSATYGSGPRFAKA
CCCCCCCCCHHHHHH
34.90-
353PhosphorylationPRFAKAASTLGSPLE
HHHHHHHHHHCCCHH
29.0825521595
354PhosphorylationRFAKAASTLGSPLEA
HHHHHHHHHCCCHHH
30.3429899451
357PhosphorylationKAASTLGSPLEAQVA
HHHHHHCCCHHHHCC
29.4418056256
372PhosphorylationPGFARTVSPYPAEPY
CCCCCCCCCCCCCCC
20.36-
380Asymmetric dimethylargininePYPAEPYRYPASPGP
CCCCCCCCCCCCCCC
41.49-
380MethylationPYPAEPYRYPASPGP
CCCCCCCCCCCCCCC
41.4924129315
384PhosphorylationEPYRYPASPGPQQAL
CCCCCCCCCCCCCCC
26.36-
421PhosphorylationRGQWRPVSVEDVGAY
CCCEECCCHHHHCCE
23.5930635358
428PhosphorylationSVEDVGAYSYQAGAA
CHHHHCCEEEHHHCC
11.2821183079
429PhosphorylationVEDVGAYSYQAGAAA
HHHHCCEEEHHHCCC
15.3830635358
430PhosphorylationEDVGAYSYQAGAAAG
HHHCCEEEHHHCCCC
6.9530635358
441PhosphorylationAAAGRAASPCNYSER
CCCCCCCCCCCCCCC
29.0625521595
445PhosphorylationRAASPCNYSERYYGG
CCCCCCCCCCCCCCC
20.7330635358
446PhosphorylationAASPCNYSERYYGGG
CCCCCCCCCCCCCCC
11.1230635358
450PhosphorylationCNYSERYYGGGGGGG
CCCCCCCCCCCCCCC
18.6029899451
463PhosphorylationGGAAGGGSPGDKAEG
CCCCCCCCCCCCCCC
29.0522324799
473PhosphorylationDKAEGRASPLYATYK
CCCCCCCCCCEEEEE
17.6825521595
476PhosphorylationEGRASPLYATYKADS
CCCCCCCEEEEECCC
10.5725521595
478PhosphorylationRASPLYATYKADSFS
CCCCCEEEEECCCCC
16.4022324799
479PhosphorylationASPLYATYKADSFSE
CCCCEEEEECCCCCC
8.9422324799
483PhosphorylationYATYKADSFSEGDDL
EEEEECCCCCCCCCC
35.2222324799
485PhosphorylationTYKADSFSEGDDLSQ
EEECCCCCCCCCCCC
44.6225521595
491PhosphorylationFSEGDDLSQGHLAEP
CCCCCCCCCCCCCCC
40.9025521595
508PhosphorylationLRAGGDLSLSPSRSA
EECCCCCCCCCCCCH
31.3821743459
510PhosphorylationAGGDLSLSPSRSADA
CCCCCCCCCCCCHHH
19.9022324799
512PhosphorylationGDLSLSPSRSADALA
CCCCCCCCCCHHHHC
35.1820415495
514PhosphorylationLSLSPSRSADALAGY
CCCCCCCCHHHHCCC
34.53-
521PhosphorylationSADALAGYAASDGDG
CHHHHCCCCCCCCCC
8.0629899451
524PhosphorylationALAGYAASDGDGDRL
HHCCCCCCCCCCCEE
33.6725521595
540PhosphorylationVQLCGAGSSPEPEHG
EEECCCCCCCCCCCC
42.0322324799
541PhosphorylationQLCGAGSSPEPEHGS
EECCCCCCCCCCCCC
32.1522324799
548PhosphorylationSPEPEHGSRESLEPS
CCCCCCCCCCCCCCC
34.4825367039
551PhosphorylationPEHGSRESLEPSSME
CCCCCCCCCCCCCCC
36.6025367039
555PhosphorylationSRESLEPSSMEASPE
CCCCCCCCCCCCCCC
32.7025367039
556PhosphorylationRESLEPSSMEASPEM
CCCCCCCCCCCCCCC
31.2125367039
560PhosphorylationEPSSMEASPEMHPPT
CCCCCCCCCCCCCCC
14.2125367039
567PhosphorylationSPEMHPPTRLSPQQA
CCCCCCCCCCCHHHC
49.0125367039
570PhosphorylationMHPPTRLSPQQAFPR
CCCCCCCCHHHCCCC
19.8520415495
588PhosphorylationSGLSRKDSLTKAQLY
CCCCCHHHCCHHHHH
40.7629514104
595PhosphorylationSLTKAQLYGTLLN--
HCCHHHHHHHHCC--
8.9325521595
597PhosphorylationTKAQLYGTLLN----
CHHHHHHHHCC----
17.9520415495

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

Oops, there are no upstream regulatory protein records of BEGIN_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 BEGIN_MOUSE !!

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

Oops, there are no PPI records of BEGIN_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-265; SER-357 ANDSER-473, AND MASS SPECTROMETRY.
"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 SER-194 AND SER-246, ANDMASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, AND MASSSPECTROMETRY.

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