BRD3_HUMAN - dbPTM
BRD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD3_HUMAN
UniProt AC Q15059
Protein Name Bromodomain-containing protein 3
Gene Name BRD3
Organism Homo sapiens (Human).
Sequence Length 726
Subcellular Localization Nucleus . Detected on chromatin.
Protein Description Chromatin reader that recognizes and binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. [PubMed: 18406326]
Protein Sequence MSTATTVAPAGIPATPGPVNPPPPEVSNPSKPGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPMDMGTIKKRLENNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMPQEEVELLPPAPKGKGRKPAAGAQSAGTQQVAAVSSVSPATPFQSVPPTVSQTPVIAATPVPTITANVTSVPVPPAAAPPPPATPIVPVVPPTPPVVKKKGVKRKADTTTPTTSAITASRSESPPPLSDPKQAKVVARRESGGRPIKPPKKDLEDGEVPQHAGKKGKLSEHLRYCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKRKMDGREYPDAQGFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPVEAPALPAPAAPMVSKGAESSRSSEESSSDSGSSDSEEERATRLAELQEQLKAVHEQLAALSQAPVNKPKKKKEKKEKEKKKKDKEKEKEKHKVKAEEEKKAKVAPPAKQAQQKKAPAKKANSTTTAGRQLKKGGKQASASYDSEEEEEGLPMSYDEKRQLSLDINRLPGEKLGRVVHIIQSREPSLRDSNPDEIEIDFETLKPTTLRELERYVKSCLQKKQRKPFSASGKKQAAKSKEELAQEKKKELEKRLQDVSGQLSSSKKPARKEKPGSAPSGGPSRLSSSSSSESGSSSSSGSSSDSSDSE
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
2Phosphorylation------MSTATTVAP
------CCCCCCCCC		27.0921406692
2Acetylation------MSTATTVAP
------CCCCCCCCC		27.0919413330
3Phosphorylation-----MSTATTVAPA
-----CCCCCCCCCC		27.0721406692
5Phosphorylation---MSTATTVAPAGI
---CCCCCCCCCCCC		23.1521406692
6Phosphorylation--MSTATTVAPAGIP
--CCCCCCCCCCCCC		16.5321406692
15PhosphorylationAPAGIPATPGPVNPP
CCCCCCCCCCCCCCC		24.3521406692
27PhosphorylationNPPPPEVSNPSKPGR
CCCCCCCCCCCCCCC		41.1621406692
30PhosphorylationPPEVSNPSKPGRKTN
CCCCCCCCCCCCCCC		56.5921406692
75UbiquitinationLNLPDYHKIIKNPMD
CCCCCHHHHCCCCCC		39.64-
85PhosphorylationKNPMDMGTIKKRLEN
CCCCCHHHHHHHHHH		24.00-
248PhosphorylationGVKRKADTTTPTTSA
CCCCCCCCCCCCCHH		37.1130266825
249PhosphorylationVKRKADTTTPTTSAI
CCCCCCCCCCCCHHH		31.1830266825
250PhosphorylationKRKADTTTPTTSAIT
CCCCCCCCCCCHHHC		22.2630266825
252PhosphorylationKADTTTPTTSAITAS
CCCCCCCCCHHHCCC		31.1530266825
253PhosphorylationADTTTPTTSAITASR
CCCCCCCCHHHCCCC		19.8430266825
254PhosphorylationDTTTPTTSAITASRS
CCCCCCCHHHCCCCC		21.8324732914
257PhosphorylationTPTTSAITASRSESP
CCCCHHHCCCCCCCC		20.4925159151
259PhosphorylationTTSAITASRSESPPP
CCHHHCCCCCCCCCC		27.9125159151
261PhosphorylationSAITASRSESPPPLS
HHHCCCCCCCCCCCC		39.6722167270
263PhosphorylationITASRSESPPPLSDP
HCCCCCCCCCCCCCH		43.9119664994
268PhosphorylationSESPPPLSDPKQAKV
CCCCCCCCCHHHCEE		58.6125159151
274UbiquitinationLSDPKQAKVVARRES
CCCHHHCEEEEEHHH		34.45-
281PhosphorylationKVVARRESGGRPIKP
EEEEEHHHCCCCCCC		44.7417287340
304TrimethylationEVPQHAGKKGKLSEH
CCCCCCCCCCCHHHH		60.17-
304AcetylationEVPQHAGKKGKLSEH
CCCCCCCCCCCHHHH		60.1723749302
304MethylationEVPQHAGKKGKLSEH
CCCCCCCCCCCHHHH		60.17-
305TrimethylationVPQHAGKKGKLSEHL
CCCCCCCCCCHHHHH		61.43-
305AcetylationVPQHAGKKGKLSEHL
CCCCCCCCCCHHHHH		61.437428765
305MethylationVPQHAGKKGKLSEHL
CCCCCCCCCCHHHHH		61.43-
307AcetylationQHAGKKGKLSEHLRY
CCCCCCCCHHHHHHH		58.6923749302
317PhosphorylationEHLRYCDSILREMLS
HHHHHHHHHHHHHHH		21.6924719451
359PhosphorylationIKHPMDLSTVKRKMD
HCCCCCHHHHHHHCC		27.2222210691
360PhosphorylationKHPMDLSTVKRKMDG
CCCCCHHHHHHHCCC		37.0322210691
362UbiquitinationPMDLSTVKRKMDGRE
CCCHHHHHHHCCCCC		46.52-
411MethylationLQDVFEMRFAKMPDE
HHHHHHHHHCCCCCC		22.60-
414SumoylationVFEMRFAKMPDEPVE
HHHHHHCCCCCCCCC		48.5328112733
434PhosphorylationAPAAPMVSKGAESSR
CCCCCCCCCCCCCCC		21.0826434552
439PhosphorylationMVSKGAESSRSSEES
CCCCCCCCCCCCCCC		30.4321118733
450PhosphorylationSEESSSDSGSSDSEE
CCCCCCCCCCCCCHH		42.3921118733
452PhosphorylationESSSDSGSSDSEEER
CCCCCCCCCCCHHHH		34.6221118733
453PhosphorylationSSSDSGSSDSEEERA
CCCCCCCCCCHHHHH		48.9921118733
455PhosphorylationSDSGSSDSEEERATR
CCCCCCCCHHHHHHH		49.1821118733
481PhosphorylationHEQLAALSQAPVNKP
HHHHHHHHCCCCCCC		21.4123312004
539UbiquitinationQKKAPAKKANSTTTA
HHCCCCCCCCCCCHH		55.71-
542PhosphorylationAPAKKANSTTTAGRQ
CCCCCCCCCCHHHHH		31.8029083192
543PhosphorylationPAKKANSTTTAGRQL
CCCCCCCCCHHHHHH		28.1529083192
544PhosphorylationAKKANSTTTAGRQLK
CCCCCCCCHHHHHHH		17.9229083192
545PhosphorylationKKANSTTTAGRQLKK
CCCCCCCHHHHHHHH		27.4829083192
558PhosphorylationKKGGKQASASYDSEE
HHCCCCCCCCCCCHH		18.4323401153
560PhosphorylationGGKQASASYDSEEEE
CCCCCCCCCCCHHHH		27.2922167270
561PhosphorylationGKQASASYDSEEEEE
CCCCCCCCCCHHHHC		24.1722167270
563PhosphorylationQASASYDSEEEEEGL
CCCCCCCCHHHHCCC		38.3822167270
573PhosphorylationEEEGLPMSYDEKRQL
HHCCCCCCHHHHHCC		27.7422167270
574PhosphorylationEEGLPMSYDEKRQLS
HCCCCCCHHHHHCCE		23.1322167270
581PhosphorylationYDEKRQLSLDINRLP
HHHHHCCEEEHHCCC		18.6923917254
591UbiquitinationINRLPGEKLGRVVHI
HHCCCHHHHHHEEEE		63.26-
609PhosphorylationREPSLRDSNPDEIEI
CCCCCCCCCCCCEEE		43.77-
632PhosphorylationTLRELERYVKSCLQK
HHHHHHHHHHHHHHH		11.6725367160
635PhosphorylationELERYVKSCLQKKQR
HHHHHHHHHHHHHCC		15.2625367160
655AcetylationSGKKQAAKSKEELAQ
HCHHHHHHCHHHHHH		66.147704273
656PhosphorylationGKKQAAKSKEELAQE
CHHHHHHCHHHHHHH		40.3425106551
657AcetylationKKQAAKSKEELAQEK
HHHHHHCHHHHHHHH		55.2723749302
666AcetylationELAQEKKKELEKRLQ
HHHHHHHHHHHHHHH		77.8219827531
676PhosphorylationEKRLQDVSGQLSSSK
HHHHHHHHHHHCCCC		29.1629396449
680PhosphorylationQDVSGQLSSSKKPAR
HHHHHHHCCCCCCCC		25.3625159151
681PhosphorylationDVSGQLSSSKKPARK
HHHHHHCCCCCCCCC		55.5625159151
682PhosphorylationVSGQLSSSKKPARKE
HHHHHCCCCCCCCCC		41.1225159151
683AcetylationSGQLSSSKKPARKEK
HHHHCCCCCCCCCCC		65.8025953088
703PhosphorylationSGGPSRLSSSSSSES
CCCCCCCCCCCCCCC		27.36-
705PhosphorylationGPSRLSSSSSSESGS
CCCCCCCCCCCCCCC		30.75-
706PhosphorylationPSRLSSSSSSESGSS
CCCCCCCCCCCCCCC		39.57-
707PhosphorylationSRLSSSSSSESGSSS
CCCCCCCCCCCCCCC		39.82-
708PhosphorylationRLSSSSSSESGSSSS
CCCCCCCCCCCCCCC		37.42-
710PhosphorylationSSSSSSESGSSSSSG
CCCCCCCCCCCCCCC		46.02-
712PhosphorylationSSSSESGSSSSSGSS
CCCCCCCCCCCCCCC		36.00-
716PhosphorylationESGSSSSSGSSSDSS
CCCCCCCCCCCCCCC		44.64-
718PhosphorylationGSSSSSGSSSDSSDS
CCCCCCCCCCCCCCC		28.72-
719PhosphorylationSSSSSGSSSDSSDSE
CCCCCCCCCCCCCCC		41.51-
720PhosphorylationSSSSGSSSDSSDSE-
CCCCCCCCCCCCCC-		43.12-
722PhosphorylationSSGSSSDSSDSE---
CCCCCCCCCCCC---		37.68-
723PhosphorylationSGSSSDSSDSE----
CCCCCCCCCCC----		50.58-
725PhosphorylationSSSDSSDSE------
CCCCCCCCC------		47.34-
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
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:28805821
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD3_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 BRD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
YETS4_HUMANYEATS4physical
22939629
RUVB2_HUMANRUVBL2physical
26344197
BRD2_HUMANBRD2physical
28514442
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 BRD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-563, ANDMASS SPECTROMETRY.
"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-263 AND SER-563, ANDMASS 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-680, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-263 ANDSER-281, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND MASSSPECTROMETRY.
"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-263, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-563, ANDMASS SPECTROMETRY.

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