BRD3_MOUSE - dbPTM
BRD3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD3_MOUSE
UniProt AC Q8K2F0
Protein Name Bromodomain-containing protein 3
Gene Name Brd3
Organism Mus musculus (Mouse).
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: 21536911 Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets]
Protein Sequence MSTTAAAPTGIPAVPGPVNPPPPEVSNPSKPGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPMDMGTIKKRLENNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMPQEEVELLPPAPKGKGRKPAAGAQNAGSQQVAAVSSVSPATPFQNIPPTVSQTPVIAATPVPTITANVTSVPVPPPAAPPPPATPIVPVVPPTPPVVKKKGVKRKADTTTPTTSAITASRSESPPPLSEPKQAKVVARRESGGRPIKPPKKDLEDGEVPQHAGKKGKLSEHLRHCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKRKMDSREYPDAQGFAADIRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPMEAPALPAPTAPIVSKGAESSRSSEESSSDSGSSDSEEERATRLAELQEQLKAVHEQLAALSQAPVNKPKKKKEKKEKEKKKKDKDKDKEKEKHKAKSEEEKKAKAAPAAKQAQQKKAPTKKANSTTTASRQLKKGGKQASASYDSEEEEEGLPMSYDEKRQLSLDINRLPGEKLGRVVHIIQSREPSLRDSNPDEIEIDFETLKPTTLRELERYVKSCLQKKQRKPLSTSGKKQAAKSKEELAQEKKKELEKRLQDVSGQLNSKKPTKKEKSGSAPSGGPSRLSSSSSSESASSSSSGSSSDSSDSE
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
35PhosphorylationPSKPGRKTNQLQYMQ
CCCCCCCCCHHHHHH
27.1720531401
118PhosphorylationCYIYNKPTDDIVLMA
CEECCCCCCHHHHHH
48.16-
247PhosphorylationGVKRKADTTTPTTSA
CCCCCCCCCCCCCHH
37.1128066266
248PhosphorylationVKRKADTTTPTTSAI
CCCCCCCCCCCCHHH
31.1826239621
249PhosphorylationKRKADTTTPTTSAIT
CCCCCCCCCCCHHHC
22.2626643407
251PhosphorylationKADTTTPTTSAITAS
CCCCCCCCCHHHCCC
31.1524453211
252PhosphorylationADTTTPTTSAITASR
CCCCCCCCHHHCCCC
19.8426643407
253PhosphorylationDTTTPTTSAITASRS
CCCCCCCHHHCCCCC
21.8327087446
256PhosphorylationTPTTSAITASRSESP
CCCCHHHCCCCCCCC
20.4926643407
258PhosphorylationTTSAITASRSESPPP
CCHHHCCCCCCCCCC
27.9126643407
260PhosphorylationSAITASRSESPPPLS
HHHCCCCCCCCCCCC
39.6727087446
262PhosphorylationITASRSESPPPLSEP
HCCCCCCCCCCCCCC
43.9127087446
267PhosphorylationSESPPPLSEPKQAKV
CCCCCCCCCCCCCEE
58.5925619855
280PhosphorylationKVVARRESGGRPIKP
EEEEEHHHCCCCCCC
44.7421183079
303AcetylationEVPQHAGKKGKLSEH
CCCCCCCCCCCHHHH
60.17130625
304AcetylationVPQHAGKKGKLSEHL
CCCCCCCCCCHHHHH
61.437428769
306AcetylationQHAGKKGKLSEHLRH
CCCCCCCCHHHHHHH
58.6923806337
548PhosphorylationANSTTTASRQLKKGG
CCCCHHHHHHHHHCC
20.61-
559PhosphorylationKKGGKQASASYDSEE
HHCCCCCCCCCCCHH
18.4325521595
561PhosphorylationGGKQASASYDSEEEE
CCCCCCCCCCCHHHH
27.2925521595
562PhosphorylationGKQASASYDSEEEEE
CCCCCCCCCCHHHHC
24.1725521595
564PhosphorylationQASASYDSEEEEEGL
CCCCCCCCHHHHCCC
38.3825521595
582PhosphorylationYDEKRQLSLDINRLP
HHHHHCCEEEHHCCC
18.6928059163
657PhosphorylationGKKQAAKSKEELAQE
HHHHHHHCHHHHHHH
40.3430387612
677PhosphorylationEKRLQDVSGQLNSKK
HHHHHHHHHHHCCCC
29.16-
691PhosphorylationKPTKKEKSGSAPSGG
CCCCCCCCCCCCCCC
38.79-
696PhosphorylationEKSGSAPSGGPSRLS
CCCCCCCCCCCCCCC
56.98-
703PhosphorylationSGGPSRLSSSSSSES
CCCCCCCCCCCCCCC
27.3629895711
704PhosphorylationGGPSRLSSSSSSESA
CCCCCCCCCCCCCCC
38.5429895711
705PhosphorylationGPSRLSSSSSSESAS
CCCCCCCCCCCCCCC
30.7529895711
706PhosphorylationPSRLSSSSSSESASS
CCCCCCCCCCCCCCC
39.5729895711
707PhosphorylationSRLSSSSSSESASSS
CCCCCCCCCCCCCCC
39.8229895711
708PhosphorylationRLSSSSSSESASSSS
CCCCCCCCCCCCCCC
37.2029895711
710PhosphorylationSSSSSSESASSSSSG
CCCCCCCCCCCCCCC
35.0829895711
712PhosphorylationSSSSESASSSSSGSS
CCCCCCCCCCCCCCC
39.7829895711
713PhosphorylationSSSESASSSSSGSSS
CCCCCCCCCCCCCCC
33.6829895711
714PhosphorylationSSESASSSSSGSSSD
CCCCCCCCCCCCCCC
26.4829895711
715PhosphorylationSESASSSSSGSSSDS
CCCCCCCCCCCCCCC
40.4429895711
716PhosphorylationESASSSSSGSSSDSS
CCCCCCCCCCCCCCC
44.6429895711
718PhosphorylationASSSSSGSSSDSSDS
CCCCCCCCCCCCCCC
28.7229895711
719PhosphorylationSSSSSGSSSDSSDSE
CCCCCCCCCCCCCCC
41.5129895711
720PhosphorylationSSSSGSSSDSSDSE-
CCCCCCCCCCCCCC-
43.1229895711

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 BRD3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD3_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 BRD3_MOUSE !!

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

Oops, there are no PPI records of BRD3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRD3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASSSPECTROMETRY.
"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-262, AND MASSSPECTROMETRY.

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