BEGIN_HUMAN - dbPTM
BEGIN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BEGIN_HUMAN
UniProt AC Q9BUH8
Protein Name Brain-enriched guanylate kinase-associated protein
Gene Name BEGAIN
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description May sustain the structure of the postsynaptic density (PSD)..
Protein Sequence MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQERVSLHMEKHGCSLPSPLCHPAYADSVPTCVIAKVLEKPDPASLSSRLSDASARDLAFCDGVEKPGPRPPYKGDIYCSDTALYCPEERRRDRRPSVDAPVTDVGFLRAQNSTDSAAEEEEEAEAAAFPAGFQHEAFPSYAGSLPTSSSYSSFSATSEEKEHAQASTLTASQQAIYLNSRDELFDRKPPATTYEGSPRFAKATAAVAAPLEAEVAPGFGRTMSPYPAETFRFPASPGPQQALMPPNLWSLRAKPGTARLPGEDMRGQWRPLSVEDIGAYSYPVSAAGRASPCSFSERYYGGAGGSPGKKADGRASPLYASYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPGRSADPLPGYAPSEGGDGDRLGVQLCGTASSPEPEQGSRDSLEPSSMEASPEMHPAARLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN
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		10.3922814378
5Phosphorylation---MEKLSALQEQKG
---CHHHHHHHHHHH		37.6928509920
11UbiquitinationLSALQEQKGELRKRL
HHHHHHHHHHHHHHH		54.3129967540
20PhosphorylationELRKRLSYTTHKLEK
HHHHHHHHHHHHHHH		21.9029214152
27UbiquitinationYTTHKLEKLETEFDS
HHHHHHHHHHCHHHH		63.1629967540
77UbiquitinationINQELEDKLYRMGQH
HHHHHHHHHHHCHHH		37.7329967540
79PhosphorylationQELEDKLYRMGQHYE
HHHHHHHHHCHHHHH		12.3228985074
112UbiquitinationEAKVTIDKLSEDNEL
HEEEEHHHHHHCCHH		50.4929967540
122UbiquitinationEDNELYRKDCNLAAQ
HCCHHHHHHCHHHHH		53.7429967540
137PhosphorylationLLQCSQTYGRVHKVS
HHHHHHHHCCCEEHH		8.6927196784
142UbiquitinationQTYGRVHKVSELPSD
HHHCCCEEHHHCCCC		44.6029967540
148PhosphorylationHKVSELPSDFQERVS
EEHHHCCCCHHHHHH		64.7828555341
155PhosphorylationSDFQERVSLHMEKHG
CCHHHHHHHHHHHHC		20.8328555341
167PhosphorylationKHGCSLPSPLCHPAY
HHCCCCCCCCCCHHH		35.4825159151
174PhosphorylationSPLCHPAYADSVPTC
CCCCCHHHCCCCCEE		18.5227642862
176UbiquitinationLCHPAYADSVPTCVI
CCCHHHCCCCCEEEE		37.1822817900
180UbiquitinationAYADSVPTCVIAKVL
HHCCCCCEEEEEHHH		19.7622817900
185UbiquitinationVPTCVIAKVLEKPDP
CCEEEEEHHHCCCCH		35.9122817900
189UbiquitinationVIAKVLEKPDPASLS
EEEHHHCCCCHHHHH		51.0321906983
194PhosphorylationLEKPDPASLSSRLSD
HCCCCHHHHHHHCCC		33.8829214152
196PhosphorylationKPDPASLSSRLSDAS
CCCHHHHHHHCCCCC		15.7725159151
197UbiquitinationPDPASLSSRLSDASA
CCHHHHHHHCCCCCH		42.4022817900
197PhosphorylationPDPASLSSRLSDASA
CCHHHHHHHCCCCCH		42.4025159151
198UbiquitinationDPASLSSRLSDASAR
CHHHHHHHCCCCCHH		34.5322817900
200PhosphorylationASLSSRLSDASARDL
HHHHHHCCCCCHHHH		29.9825159151
201UbiquitinationSLSSRLSDASARDLA
HHHHHCCCCCHHHHH		49.4822817900
202UbiquitinationLSSRLSDASARDLAF
HHHHCCCCCHHHHHC		11.1722817900
203PhosphorylationSSRLSDASARDLAFC
HHHCCCCCHHHHHCC		28.9123186163
204UbiquitinationSRLSDASARDLAFCD
HHCCCCCHHHHHCCC		15.6622817900
208UbiquitinationDASARDLAFCDGVEK
CCCHHHHHCCCCCCC		13.8122817900
215UbiquitinationAFCDGVEKPGPRPPY
HCCCCCCCCCCCCCC		53.5229967540
227PhosphorylationPPYKGDIYCSDTALY
CCCCCCEEECCCEEE		7.2227642862
229PhosphorylationYKGDIYCSDTALYCP
CCCCEEECCCEEECC		22.4828674419
231PhosphorylationGDIYCSDTALYCPEE
CCEEECCCEEECCHH		11.4129449344
234PhosphorylationYCSDTALYCPEERRR
EECCCEEECCHHHHC		11.9627642862
246PhosphorylationRRRDRRPSVDAPVTD
HHCCCCCCCCCCCCC		30.7122167270
252PhosphorylationPSVDAPVTDVGFLRA
CCCCCCCCCHHHHHC		24.7323663014
265PhosphorylationRAQNSTDSAAEEEEE
HCCCCCCCHHHHHHH		29.48-
321PhosphorylationQASTLTASQQAIYLN
HHHHCCHHHHHHHHC		20.0028555341
326PhosphorylationTASQQAIYLNSRDEL
CHHHHHHHHCCCHHH		11.6627642862
341PhosphorylationFDRKPPATTYEGSPR
HCCCCCCCCCCCCHH		35.3729396449
342PhosphorylationDRKPPATTYEGSPRF
CCCCCCCCCCCCHHH		22.9829396449
343PhosphorylationRKPPATTYEGSPRFA
CCCCCCCCCCCHHHH		17.5929396449
346PhosphorylationPATTYEGSPRFAKAT
CCCCCCCCHHHHHHH		10.8525159151
371PhosphorylationVAPGFGRTMSPYPAE
ECCCCCCCCCCCCCC		23.5220068231
373PhosphorylationPGFGRTMSPYPAETF
CCCCCCCCCCCCCCC		22.2220068231
375PhosphorylationFGRTMSPYPAETFRF
CCCCCCCCCCCCCCC		14.0420068231
379PhosphorylationMSPYPAETFRFPASP
CCCCCCCCCCCCCCC		23.4020068231
381MethylationPYPAETFRFPASPGP
CCCCCCCCCCCCCCC		44.02-
381Asymmetric dimethylargininePYPAETFRFPASPGP
CCCCCCCCCCCCCCC		44.02-
385PhosphorylationETFRFPASPGPQQAL
CCCCCCCCCCCCCCC		30.5420068231
399PhosphorylationLMPPNLWSLRAKPGT
CCCCCHHHCCCCCCC		15.9020068231
422PhosphorylationRGQWRPLSVEDIGAY
CCCEECCCHHHHCCE		26.5827642862
429PhosphorylationSVEDIGAYSYPVSAA
CHHHHCCEECCCCCC		11.9723917254
440PhosphorylationVSAAGRASPCSFSER
CCCCCCCCCCCCCCC		25.6921815630
443PhosphorylationAGRASPCSFSERYYG
CCCCCCCCCCCCCCC		34.8822210691
445PhosphorylationRASPCSFSERYYGGA
CCCCCCCCCCCCCCC		12.60-
449PhosphorylationCSFSERYYGGAGGSP
CCCCCCCCCCCCCCC		18.4623186163
455PhosphorylationYYGGAGGSPGKKADG
CCCCCCCCCCCCCCC		29.5725159151
465PhosphorylationKKADGRASPLYASYK
CCCCCCCCCCHHHCC		17.6825159151
468PhosphorylationDGRASPLYASYKADS
CCCCCCCHHHCCCCC		9.2625159151
470PhosphorylationRASPLYASYKADSFS
CCCCCHHHCCCCCCC		17.38-
475PhosphorylationYASYKADSFSEGDDL
HHHCCCCCCCCCCCC		35.2223663014
477PhosphorylationSYKADSFSEGDDLSQ
HCCCCCCCCCCCCCC		44.6225159151
483PhosphorylationFSEGDDLSQGHLAEP
CCCCCCCCCCCCCCC		40.9017525332
500PhosphorylationLRAGGDLSLSPGRSA
EEECCCCCCCCCCCC		31.3822167270
502PhosphorylationAGGDLSLSPGRSADP
ECCCCCCCCCCCCCC		23.1822167270
506PhosphorylationLSLSPGRSADPLPGY
CCCCCCCCCCCCCCC		42.8326055452
516PhosphorylationPLPGYAPSEGGDGDR
CCCCCCCCCCCCCCE		40.4723186163
531PhosphorylationLGVQLCGTASSPEPE
EEEEECCCCCCCCCC		23.5221815630
533PhosphorylationVQLCGTASSPEPEQG
EEECCCCCCCCCCCC		46.3823312004
534PhosphorylationQLCGTASSPEPEQGS
EECCCCCCCCCCCCC		30.7121815630
544PhosphorylationPEQGSRDSLEPSSME
CCCCCCCCCCCCCCC		33.2623186163
548PhosphorylationSRDSLEPSSMEASPE
CCCCCCCCCCCCCCC		32.7027732954
549PhosphorylationRDSLEPSSMEASPEM
CCCCCCCCCCCCCCC		31.2127732954
553PhosphorylationEPSSMEASPEMHPAA
CCCCCCCCCCCCCCH		14.2123403867
563PhosphorylationMHPAARLSPQQAFPR
CCCCHHCCHHHCCCC		18.3422167270
581PhosphorylationSGLSRKDSLTKAQLY
CCCCCHHHCCHHHHH		40.7624719451
588PhosphorylationSLTKAQLYGTLLN--
HCCHHHHHHHHCC--		8.9327196784
590PhosphorylationTKAQLYGTLLN----
CHHHHHHHHCC----		17.95-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BEGIN_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HID1_HUMANHID1physical
16189514
ZN250_HUMANZNF250physical
16189514
CTSR1_HUMANCATSPER1physical
16189514
ZN417_HUMANZNF417physical
16189514
ENKD1_HUMANENKD1physical
16189514
BEGIN_HUMANBEGAINphysical
12097487
A4_HUMANAPPphysical
21832049
QSOX1_HUMANQSOX1physical
21988832
ZN774_HUMANZNF774physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BEGIN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-465; SER-502AND SER-563, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-563, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 AND SER-502, ANDMASS SPECTROMETRY.

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