BRD4_MOUSE - dbPTM
BRD4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD4_MOUSE
UniProt AC Q9ESU6
Protein Name Bromodomain-containing protein 4
Gene Name Brd4
Organism Mus musculus (Mouse).
Sequence Length 1400
Subcellular Localization Nucleus. Chromosome. Associates with acetylated chromatin. Released from chromatin upon deacetylation of histones that can be triggered by different signals such as activation of the JNK pathway or nocodazole treatment. Preferentially localizes to mi
Protein Description Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters: BRD4 is required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters..
Protein Sequence MSTESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGAAKPGVSTVPNTTQASTSPQTQTPQQNPPPPVQATTHPFPAVTPDLIAQPPVMTMVPPQPLQTPSPVPPQPPPPPAPVPQPVQSHPPIIATTPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLAPEPKTAKLGPRRESSRPVKPPKKDVPDSQQHPGPEKSSKISEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLESREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVTVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKKKEEVEENKKSKTKELPPKKTKKNNSSNSNVSKKEPVPTKTKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESTSESSSSDSEDSETEMAPKSKKKGHTGRDQKKHHHHHHPQMQPAPAPVPQQPPPPPQQPPPPPPPQQQQQQPPPPPPPPSMPQQTAPAMKSSPPPFITAQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPTRPPAVSPALAQPPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQQLQPQPPPPPPPQPQPPPQQQHQPPPRPVHLPSMPFSAHIQQPPPPPGQQPTHPPPGQQPPPPQPAKPQQVIQHHPSPRHHKSDPYSAGHLREAPSPLMIHSPQMPQFQSLTHQSPPQQNVQPKKQVKGRAEPQPPGPVMGQGQGCPPASPAAVPMLSQELRPPSVVQPQPLVVVKEEKIHSPIIRSEPFSTSLRPEPPKHPENIKAPVHLPQRPEMKPVDIGRPVIRPPEQSAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEHFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQQQQRQEQQQQQQQAAAVAAASAPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF
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------MSTESGPGT
------CCCCCCCCC		52.7929514104
99UbiquitinationLNLPDYYKIIKTPMD
CCCCCHHHHHCCCCC		31.55-
295PhosphorylationGVKRKADTTTPTTID
CCCCCCCCCCCCCCC		37.1129895711
296PhosphorylationVKRKADTTTPTTIDP
CCCCCCCCCCCCCCC		31.1825266776
297PhosphorylationKRKADTTTPTTIDPI
CCCCCCCCCCCCCCC		22.2629895711
299PhosphorylationKADTTTPTTIDPIHE
CCCCCCCCCCCCCCC		34.0025777480
300PhosphorylationADTTTPTTIDPIHEP
CCCCCCCCCCCCCCC		25.2926643407
325PhosphorylationKLGPRRESSRPVKPP
CCCCCCCCCCCCCCC		29.8125338131
326PhosphorylationLGPRRESSRPVKPPK
CCCCCCCCCCCCCCC		35.53-
339PhosphorylationPKKDVPDSQQHPGPE
CCCCCCCHHCCCCCC		26.1828059163
468PhosphorylationEPEEPVVTVSSPAVP
CCCCCCEEEECCCCC		18.2027087446
470PhosphorylationEEPVVTVSSPAVPPP
CCCCEEEECCCCCCC		22.6520469934
471PhosphorylationEPVVTVSSPAVPPPT
CCCEEEECCCCCCCC		16.7325521595
478PhosphorylationSPAVPPPTKVVAPPS
CCCCCCCCEEECCCC		42.0925619855
485PhosphorylationTKVVAPPSSSDSSSD
CEEECCCCCCCCCCC		41.22-
489PhosphorylationAPPSSSDSSSDSSSD
CCCCCCCCCCCCCCC		33.42-
493PhosphorylationSSDSSSDSSSDSDSS
CCCCCCCCCCCCCCC		33.42-
495PhosphorylationDSSSDSSSDSDSSTD
CCCCCCCCCCCCCCC		45.12-
499PhosphorylationDSSSDSDSSTDDSEE
CCCCCCCCCCCCCHH		38.80-
500PhosphorylationSSSDSDSSTDDSEEE
CCCCCCCCCCCCHHH		40.63-
504PhosphorylationSDSSTDDSEEERAQR
CCCCCCCCHHHHHHH		50.12-
579PhosphorylationKKTKKNNSSNSNVSK
CCCCCCCCCCCCCCC		40.0530635358
580PhosphorylationKTKKNNSSNSNVSKK
CCCCCCCCCCCCCCC		46.5330635358
582PhosphorylationKKNNSSNSNVSKKEP
CCCCCCCCCCCCCCC		40.3230635358
592PhosphorylationSKKEPVPTKTKPPPT
CCCCCCCCCCCCCCC		52.1328059163
594PhosphorylationKEPVPTKTKPPPTYE
CCCCCCCCCCCCCCC		51.7925619855
599PhosphorylationTKTKPPPTYESEEED
CCCCCCCCCCCCCCC		45.7723684622
600PhosphorylationKTKPPPTYESEEEDK
CCCCCCCCCCCCCCC		24.1925619855
602PhosphorylationKPPPTYESEEEDKCK
CCCCCCCCCCCCCCC		39.6425521595
612PhosphorylationEDKCKPMSYEEKRQL
CCCCCCCCHHHHHHH		37.6125777480
613PhosphorylationDKCKPMSYEEKRQLS
CCCCCCCHHHHHHHH		23.1225777480
620PhosphorylationYEEKRQLSLDINKLP
HHHHHHHHCCHHHCC		18.6926824392
693PhosphorylationKVDVIAGSSKMKGFS
HCEEEECCCCCCCCC		20.1225338131
715PhosphorylationSESSSSDSEDSETEM
CCCCCCCCCCCCCCC		45.30-
718PhosphorylationSSSDSEDSETEMAPK
CCCCCCCCCCCCCCC		42.22-
797PhosphorylationQTAPAMKSSPPPFIT
CCCCHHHCCCCCEEE		34.6825338131
944PhosphorylationLQKVQPPTPLLPSVK
HHHCCCCCCCCCCCC		33.00-
1048PhosphorylationQVIQHHPSPRHHKSD
HHHCCCCCCCCCCCC		30.1526824392
1054PhosphorylationPSPRHHKSDPYSAGH
CCCCCCCCCCCCCCC		39.1925266776
1058PhosphorylationHHKSDPYSAGHLREA
CCCCCCCCCCCCCCC		32.9126060331
1067PhosphorylationGHLREAPSPLMIHSP
CCCCCCCCCEEECCC		37.4027087446
1073PhosphorylationPSPLMIHSPQMPQFQ
CCCEEECCCCCCCHH		13.1027087446
1081PhosphorylationPQMPQFQSLTHQSPP
CCCCCHHHCCCCCCC		36.2027087446
1083PhosphorylationMPQFQSLTHQSPPQQ
CCCHHHCCCCCCCCC		24.1027087446
1086PhosphorylationFQSLTHQSPPQQNVQ
HHHCCCCCCCCCCCC		30.8327087446
1136PhosphorylationSQELRPPSVVQPQPL
CCCCCCCCCCCCCCE		37.2924453211
1147AcetylationPQPLVVVKEEKIHSP
CCCEEEEECCCCCCC		48.85-
1153PhosphorylationVKEEKIHSPIIRSEP
EECCCCCCCCCCCCC		22.6726824392
1162PhosphorylationIIRSEPFSTSLRPEP
CCCCCCCCCCCCCCC		28.00-
1222PhosphorylationKQKQEPKTPVAPKKD
HCCCCCCCCCCCCCC		33.4429514104
1237PhosphorylationLKIKNMGSWASLVQK
CCCCCCCHHHHHHHH		14.5426643407
1240PhosphorylationKNMGSWASLVQKHPT
CCCCHHHHHHHHCCC		23.86-
1247PhosphorylationSLVQKHPTTPSSTAK
HHHHHCCCCCCCCCC		51.5720139300
1248PhosphorylationLVQKHPTTPSSTAKS
HHHHCCCCCCCCCCC		26.1429550500
1250PhosphorylationQKHPTTPSSTAKSSS
HHCCCCCCCCCCCCC		37.9229550500
1251PhosphorylationKHPTTPSSTAKSSSD
HCCCCCCCCCCCCCC		33.3229550500
1252PhosphorylationHPTTPSSTAKSSSDS
CCCCCCCCCCCCCCH		42.3029550500
1298PhosphorylationLRQERMRSREDEDAL
HHHHHHHHHHHHHHH		30.5829514104
1357PhosphorylationAQSSQPQSMLDQQRE
HHHCCCHHHHHHHHH		28.1722802335
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
485SPhosphorylationKinaseCK2-Uniprot
489SPhosphorylationKinaseCK2-Uniprot
493SPhosphorylationKinaseCK2-Uniprot
499SPhosphorylationKinaseCK2-Uniprot
500SPhosphorylationKinaseCK2-Uniprot
504SPhosphorylationKinaseCK2-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD4_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 BRD4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BRD4_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRD4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-599; SER-602 ANDSER-1048, AND MASS SPECTROMETRY.

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