BRD2_MOUSE - dbPTM
BRD2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD2_MOUSE
UniProt AC Q7JJ13
Protein Name Bromodomain-containing protein 2
Gene Name Brd2
Organism Mus musculus (Mouse).
Sequence Length 798
Subcellular Localization Nucleus . Detected on chromatin and nucleosomes..
Protein Description Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly (By similarity). May play a role in spermatogenesis or folliculogenesis..
Protein Sequence MLQNVTPHKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLAPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSITSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVSAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTALPPGLTKSSSESSSEESSSESSSEEEEEEEEDEDEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRIGIDEDDKGPRAPRPPQPKKSKKAGGGGSNATTLSHPGFGTSGGSSNKLPKKSQKTAPPVLPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIRKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKASEKTESSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG
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-------MLQNVTPH
-------CCCCCCCC
8.62-
6Phosphorylation--MLQNVTPHKLPGE
--CCCCCCCCCCCCC
27.5026239621
9AcetylationLQNVTPHKLPGEGNA
CCCCCCCCCCCCCCC
58.5488611
30AcetylationPEAAAPGKRIRKPSL
HHHCCCCCCCCCHHH
43.5288615
36PhosphorylationGKRIRKPSLLYEGFE
CCCCCCHHHHCCCCC
33.7626160508
39PhosphorylationIRKPSLLYEGFESPT
CCCHHHHCCCCCCCC
21.2126160508
44PhosphorylationLLYEGFESPTMASVP
HHCCCCCCCCCCCCC
24.3326160508
46PhosphorylationYEGFESPTMASVPAL
CCCCCCCCCCCCCHH
34.3525266776
49PhosphorylationFESPTMASVPALQLA
CCCCCCCCCCHHHCC
20.1526160508
112PhosphorylationVKLGLPDYHKIIKQP
HHCCCCCHHHHHCCC
11.76-
124PhosphorylationKQPMDMGTIKRRLEN
CCCCCHHHHHHHHHH
19.38-
133PhosphorylationKRRLENNYYWAASEC
HHHHHHCCEEEHHHH
16.3822802335
134PhosphorylationRRLENNYYWAASECM
HHHHHCCEEEHHHHH
7.2422802335
138PhosphorylationNNYYWAASECMQDFN
HCCEEEHHHHHHHHH
24.4722802335
158PhosphorylationCYIYNKPTDDIVLMA
EEECCCCCCHHHHHH
48.1622802335
167PhosphorylationDIVLMAQTLEKIFLQ
HHHHHHHHHHHHHHH
27.6122802335
284PhosphorylationGVKRKADTTTPTPTA
CCCCCCCCCCCCCCE
37.1125619855
285PhosphorylationVKRKADTTTPTPTAI
CCCCCCCCCCCCCEE
31.1825619855
286PhosphorylationKRKADTTTPTPTAIL
CCCCCCCCCCCCEEE
27.5325619855
288PhosphorylationKADTTTPTPTAILAP
CCCCCCCCCCEEECC
31.0525619855
290PhosphorylationDTTTPTPTAILAPGS
CCCCCCCCEEECCCC
28.8925619855
297PhosphorylationTAILAPGSPASPPGS
CEEECCCCCCCCCCC
19.0827087446
300PhosphorylationLAPGSPASPPGSLEP
ECCCCCCCCCCCCCC
34.7027087446
304PhosphorylationSPASPPGSLEPKAAR
CCCCCCCCCCCHHHC
35.0222942356
319PhosphorylationLPPMRRESGRPIKPP
CCCCCCCCCCCCCCC
37.9928725479
333PhosphorylationPRKDLPDSQQQHQSS
CCCCCCHHHHHHHHH
28.1322817900
339PhosphorylationDSQQQHQSSKKGKLS
HHHHHHHHHHHHHHH
41.8422817900
340PhosphorylationSQQQHQSSKKGKLSE
HHHHHHHHHHHHHHH
31.6422817900
361PhosphorylationGILKELLSKKHAAYA
HHHHHHHHHCCHHHC
52.8922817900
585PhosphorylationRPPQPKKSKKAGGGG
CCCCCCCCCCCCCCC
45.5824704852
620PhosphorylationLPKKSQKTAPPVLPT
CCCCCCCCCCCCCCC
36.4425619855
627PhosphorylationTAPPVLPTGYDSEEE
CCCCCCCCCCCCHHH
44.1825619855
629PhosphorylationPPVLPTGYDSEEEEE
CCCCCCCCCCHHHHH
20.8327087446
631PhosphorylationVLPTGYDSEEEEESR
CCCCCCCCHHHHHHC
38.1227087446
637PhosphorylationDSEEEEESRPMSYDE
CCHHHHHHCCCCHHH
44.9925619855
641PhosphorylationEEESRPMSYDEKRQL
HHHHCCCCHHHHHHH
31.9225619855
642PhosphorylationEESRPMSYDEKRQLS
HHHCCCCHHHHHHHH
23.1325619855
649PhosphorylationYDEKRQLSLDINKLP
HHHHHHHHCCHHHCC
18.6926824392
747PhosphorylationDVSGQLNSTKKPPKK
HHHHHCCCCCCCCCC
50.6328066266
748PhosphorylationVSGQLNSTKKPPKKA
HHHHCCCCCCCCCCC
41.8528066266
769PhosphorylationSAQQVAVSRLSASSS
HHHHHHHHHHHCCCC
20.1228059163
775PhosphorylationVSRLSASSSSSDSSS
HHHHHCCCCCCCCCC
33.68-
786PhosphorylationDSSSSSSSSSSSDTS
CCCCCCCCCCCCCCC
35.87-
788PhosphorylationSSSSSSSSSSDTSDS
CCCCCCCCCCCCCCC
35.49-
789PhosphorylationSSSSSSSSSDTSDSD
CCCCCCCCCCCCCCC
33.89-
790PhosphorylationSSSSSSSSDTSDSDS
CCCCCCCCCCCCCCC
47.02-
797PhosphorylationSDTSDSDSG------
CCCCCCCCC------
50.80-

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 BRD2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD2_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 BRD2_MOUSE !!

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

Oops, there are no PPI records of BRD2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRD2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-297 AND SER-300, ANDMASS SPECTROMETRY.

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