BRD8_MOUSE - dbPTM
BRD8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD8_MOUSE
UniProt AC Q8R3B7
Protein Name Bromodomain-containing protein 8
Gene Name Brd8
Organism Mus musculus (Mouse).
Sequence Length 951
Subcellular Localization Nucleus.
Protein Description May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome..
Protein Sequence MATGTGKHKLLSTGPTEPWSIREKLCLASSVMRSGDQNWVSVSRAIKPFAEPGRPPDWFSQKHCASQYSELLETTETPKRKRGEKGEVVETVEDVIVRKLTAERVEELKKVIKETQERYRRLKRDAELIQAGHMDSRLDELCNDIAMKKKLEEEEAEVKRKATDAAYQARQAVKTPPRRLPTVMVRSPVDSASPGGDYPLGDLTPTTMEEATSGVTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPITDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLVNESEMPVPPGHLNSTGVLLEVGGVLPMIHGGEIQPTTSAVAASPAASGAPTLSRLLEAGPTQFTTPLPSFTTVASEPPVKLVPPPVESVSQATIVMMPALPAPSSAAAVSTSESGAPVSQPEPCVPLEAVGDPHTVTVSMDSNEISMIINSIKEECFRSGVAEAPGGSKAPSIDGKEDLDLAEKMDIAVSYTGEELDFETVGDIIAIIEDKVDDHPEVLDVAAVEAALSFCEENDDPQSLPGPWEHPIQQERDKPVPLPAPEMTVKQERLDFEESENKGLHDLVDIRDSGVEIKVEPTEPEPGMSGAEIVAGVGPVPSMEPPELRSQDSDEEPRSSAAGDIGEADGSSGKGDERPLSAVKTEASPESMLSPSHGSNLIEDPLEAETQHKFEMSDSLKEESGTIFGSQIKDAPGDDEEEDGVSEAASLEEPKEEDQGEGYLSEMDNEPPVSESDDGFSIHNATLQSHTLADSIPSSPASSQFSVCSEDQEAIQAQKIWKKAIMLVWRAAANHRYANVFLQPVTDDIAPGYHSIVQRPMDLSTIKKNIENGLIRSTAEFQRDIMLMFQNAVMYNSSDHDVYHMAVEMQRDVLEQIQQFLATQLIMQTSESGISAKSLRGRDSTRKQDASEKDSVPMGSPAFLLSLFDGGTRGRRCAIEADMKMKK
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
5Phosphorylation---MATGTGKHKLLS
---CCCCCCCCCCCC		38.4128576409
7Acetylation-MATGTGKHKLLSTG
-CCCCCCCCCCCCCC		37.0923806337
9AcetylationATGTGKHKLLSTGPT
CCCCCCCCCCCCCCC		55.3923806337
12PhosphorylationTGKHKLLSTGPTEPW
CCCCCCCCCCCCCCC		41.5821149613
13PhosphorylationGKHKLLSTGPTEPWS
CCCCCCCCCCCCCCC		47.3421149613
16PhosphorylationKLLSTGPTEPWSIRE
CCCCCCCCCCCCHHH		56.9021149613
85AcetylationPKRKRGEKGEVVETV
CCCCCCCCCCEEEEH		64.2923806337
136PhosphorylationIQAGHMDSRLDELCN
HHCCCHHHHHHHHHH		27.4525266776
175PhosphorylationQARQAVKTPPRRLPT
HHHHHHCCCCCCCCE		31.7429472430
264PhosphorylationKMLGQKATPPPSPLL
HHCCCCCCCCCCHHH		43.2827087446
268PhosphorylationQKATPPPSPLLSELL
CCCCCCCCHHHHHHH		33.6727087446
272PhosphorylationPPPSPLLSELLKKGS
CCCCHHHHHHHHCCC		33.6021082442
279PhosphorylationSELLKKGSLLPTSPR
HHHHHCCCCCCCCCC		35.3026060331
283PhosphorylationKKGSLLPTSPRLVNE
HCCCCCCCCCCCCCC		51.8627566939
284PhosphorylationKGSLLPTSPRLVNES
CCCCCCCCCCCCCCC		13.1926824392
456PhosphorylationVAEAPGGSKAPSIDG
CCCCCCCCCCCCCCC		31.4023375375
460PhosphorylationPGGSKAPSIDGKEDL
CCCCCCCCCCCHHCC		37.8725521595
554AcetylationPAPEMTVKQERLDFE
CCCCCEEEHHHCCHH		36.9623806337
614PhosphorylationMEPPELRSQDSDEEP
CCCCHHHCCCCCCCC		51.4627087446
617PhosphorylationPELRSQDSDEEPRSS
CHHHCCCCCCCCCHH		39.0125521595
623PhosphorylationDSDEEPRSSAAGDIG
CCCCCCCHHCCCCCC		34.7430635358
624PhosphorylationSDEEPRSSAAGDIGE
CCCCCCHHCCCCCCC		24.3430635358
635PhosphorylationDIGEADGSSGKGDER
CCCCCCCCCCCCCCC		36.1425619855
636PhosphorylationIGEADGSSGKGDERP
CCCCCCCCCCCCCCC		50.4825619855
638AcetylationEADGSSGKGDERPLS
CCCCCCCCCCCCCCH		66.2019860189
645PhosphorylationKGDERPLSAVKTEAS
CCCCCCCHHCCCCCC		33.4325619855
649PhosphorylationRPLSAVKTEASPESM
CCCHHCCCCCCHHHH		30.1325159016
652PhosphorylationSAVKTEASPESMLSP
HHCCCCCCHHHHCCC		23.9827087446
655PhosphorylationKTEASPESMLSPSHG
CCCCCHHHHCCCCCC		28.5427087446
658PhosphorylationASPESMLSPSHGSNL
CCHHHHCCCCCCCCC		18.7321082442
660PhosphorylationPESMLSPSHGSNLIE
HHHHCCCCCCCCCCC		36.7821659605
663PhosphorylationMLSPSHGSNLIEDPL
HCCCCCCCCCCCCCH		24.0425159016
674PhosphorylationEDPLEAETQHKFEMS
CCCHHHHHHHHCCCC		42.9225293948
683PhosphorylationHKFEMSDSLKEESGT
HHCCCCHHHHHHCCC		33.7527841257
688PhosphorylationSDSLKEESGTIFGSQ
CHHHHHHCCCEECCC		42.1828066266
690PhosphorylationSLKEESGTIFGSQIK
HHHHHCCCEECCCCC		23.5528066266
694PhosphorylationESGTIFGSQIKDAPG
HCCCEECCCCCCCCC		20.2728066266
710PhosphorylationDEEEDGVSEAASLEE
CCCCCCCCCCCCCCC		27.3519367708
714PhosphorylationDGVSEAASLEEPKEE
CCCCCCCCCCCCCCH		43.2819367708
832MalonylationMDLSTIKKNIENGLI
CCHHHHHHHHHCCCC		60.3426320211
924PhosphorylationKDSVPMGSPAFLLSL
CCCCCCCCCHHHHHH		13.5525367039
936PhosphorylationLSLFDGGTRGRRCAI
HHHHCCCCCHHCCHH		35.1625367039
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 BRD8_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD8_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 BRD8_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BRD8_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRD8_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 SER-710 AND SER-714, ANDMASS SPECTROMETRY.

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