BRD8_HUMAN - dbPTM
BRD8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD8_HUMAN
UniProt AC Q9H0E9
Protein Name Bromodomain-containing protein 8
Gene Name BRD8
Organism Homo sapiens (Human).
Sequence Length 1235
Subcellular Localization Nucleus.
Protein Description May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components 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 MATGTGKHKLLSTGPTEPWSIREKLCLASSVMRSGDQNWVSVSRAIKPFAEPGRPPDWFSQKHCASQYSELLETTETPKRKRGEKGEVVETVEDVIVRKLTAERVEELKKVIKETQERYRRLKRDAELIQAGHMDSRLDELCNDIATKKKLEEEEAEVKRKATDAAYQARQAVKTPPRRLPTVMVRSPIDSASPGGDYPLGDLTPTTMEEATSGVNESEMAVASGHLNSTGVLLEVGGVLPMIHGGEIQQTPNTVAASPAASGAPTLSRLLEAGPTQFTTPLASFTTVASEPPVKLVPPPVESVSQATIVMMPALPAPSSAPAVSTTESVAPVSQPDNCVPMEAVGDPHTVTVSMDSSEISMIINSIKEECFRSGVAEAPVGSKAPSIDGKEELDLAEKMDIAVSYTGEELDFETVGDIIAIIEDKVDDHPEVLDVAAVEAALSFCEENDDPQSLPGPWEHPIQQERDKPVPLPAPEMTVKQERLDFEETENKGIHELVDIREPSAEIKVEPAEPEPVISGAEIVAGVVPATSMEPPELRSQDLDEELGSTAAGEIVEADVAIGKGDETPLTNVKTEASPESMLSPSHGSNPIEDPLEAETQHKFEMSDSLKEESGTIFGSQIKDAPGEDEEEDGVSEAASLEEPKEEDQGEGYLSEMDNEPPVSESDDGFSIHNATLQSHTLADSIPSSPASSQFSVCSEDQEAIQAQKIWKKAIMLVWRAAANHRYANVFLQPVTDDIAPGYHSIVQRPMDLSTIKKNIENGLIRSTAEFQRDIMLMFQNAVMYNSSDHDVYHMAVEMQRDVLEQIQQFLATQLIMQTSESGISAKSLRGRDSTRKQDASEKDSVPMGSPAFLLSLFMGHEWVWLDSEQDHPNDSELSNDCRSLFSSWDSSLDLDVGNWRETEDPEAEELEESSPEREPSELLVGDGGSEESQEAARKASHQNLLHFLSEVAYLMEPLCISSNESSEGCCPPSGTRQEGREIKASEGERELCRETEELSAKGDPLVAEKPLGENGKPEVASAPSVICTVQGLLTESEEGEAQQESKGEDQGEVYVSEMEDQPPSGECDDAFNIKETPLVDTLFSHATSSKLTDLSQDDPVQDHLLFKKTLLPVWKMIASHRFSSPFLKPVSERQAPGYKDVVKRPMDLTSLKRNLSKGRIRTMAQFLRDLMLMFQNAVMYNDSDHHVYHMAVEMRQEVLEQIQVLNIWLDKRKGSSSLEGEPANPVDDGKPVF
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
3Phosphorylation-----MATGTGKHKL
-----CCCCCCCCCC		47.32-
5Phosphorylation---MATGTGKHKLLS
---CCCCCCCCCCCC		38.41-
7Acetylation-MATGTGKHKLLSTG
-CCCCCCCCCCCCCC		37.0925953088
9AcetylationATGTGKHKLLSTGPT
CCCCCCCCCCCCCCC		55.3925953088
16PhosphorylationKLLSTGPTEPWSIRE
CCCCCCCCCCCCHHH		56.90-
20PhosphorylationTGPTEPWSIREKLCL
CCCCCCCCHHHHHHH		23.60-
30PhosphorylationEKLCLASSVMRSGDQ
HHHHHHHHHHHCCCC		17.8328555341
47AcetylationVSVSRAIKPFAEPGR
EEHHHCCCCCCCCCC		32.8526051181
66PhosphorylationFSQKHCASQYSELLE
HCHHHHHHHHHHHHH		34.7427251275
68PhosphorylationQKHCASQYSELLETT
HHHHHHHHHHHHHCC		11.1327251275
69PhosphorylationKHCASQYSELLETTE
HHHHHHHHHHHHCCC		17.7129978859
74PhosphorylationQYSELLETTETPKRK
HHHHHHHCCCCCCCC		29.8722199227
75PhosphorylationYSELLETTETPKRKR
HHHHHHCCCCCCCCC		28.6122199227
77PhosphorylationELLETTETPKRKRGE
HHHHCCCCCCCCCCC		31.8325159151
79AcetylationLETTETPKRKRGEKG
HHCCCCCCCCCCCCC		77.3526051181
85AcetylationPKRKRGEKGEVVETV
CCCCCCCCCCEEEEH		64.2923954790
109AcetylationAERVEELKKVIKETQ
HHHHHHHHHHHHHHH		48.5523236377
124 (in isoform 3)Phosphorylation-53.6222167270
128 (in isoform 3)Phosphorylation-3.6422167270
132 (in isoform 3)Phosphorylation-10.5623927012
136PhosphorylationIQAGHMDSRLDELCN
HHCCCHHHHHHHHHH		27.4520068231
139 (in isoform 3)Phosphorylation-45.7922167270
143 (in isoform 3)Phosphorylation-57.2430266825
144 (in isoform 3)Phosphorylation-30.7919664994
1482-HydroxyisobutyrylationLCNDIATKKKLEEEE
HHHHHHHHHHHHHHH		38.60-
148UbiquitinationLCNDIATKKKLEEEE
HHHHHHHHHHHHHHH		38.60-
163PhosphorylationAEVKRKATDAAYQAR
HHHHHHHHHHHHHHH		29.25-
167PhosphorylationRKATDAAYQARQAVK
HHHHHHHHHHHHHHC		12.3926074081
174AcetylationYQARQAVKTPPRRLP
HHHHHHHCCCCCCCC		59.3325953088
175PhosphorylationQARQAVKTPPRRLPT
HHHHHHCCCCCCCCE		31.7430266825
182PhosphorylationTPPRRLPTVMVRSPI
CCCCCCCEEEEECCC		26.3126074081
187PhosphorylationLPTVMVRSPIDSASP
CCEEEEECCCCCCCC		18.1326074081
251PhosphorylationHGGEIQQTPNTVAAS
ECCCCCCCCCCCCCC		11.3526074081
254PhosphorylationEIQQTPNTVAASPAA
CCCCCCCCCCCCCCC		16.8426074081
258PhosphorylationTPNTVAASPAASGAP
CCCCCCCCCCCCCCC		12.8226074081
262O-linked_GlycosylationVAASPAASGAPTLSR
CCCCCCCCCCCCHHH		37.2823301498
262PhosphorylationVAASPAASGAPTLSR
CCCCCCCCCCCCHHH		37.2826074081
264 (in isoform 2)Phosphorylation-7.4522167270
264 (in isoform 4)Phosphorylation-7.4522167270
266PhosphorylationPAASGAPTLSRLLEA
CCCCCCCCHHHHHHH		36.5116964243
266 (in isoform 2)Phosphorylation-36.5116964243
268PhosphorylationASGAPTLSRLLEAGP
CCCCCCHHHHHHHCC		24.3020230923
268 (in isoform 2)Phosphorylation-24.3022167270
268 (in isoform 4)Phosphorylation-24.3022167270
272 (in isoform 2)Phosphorylation-57.0523927012
272 (in isoform 4)Phosphorylation-57.0523927012
276O-linked_GlycosylationRLLEAGPTQFTTPLA
HHHHHCCCCCCCCCC		35.0823301498
276PhosphorylationRLLEAGPTQFTTPLA
HHHHHCCCCCCCCCC		35.0828122231
279PhosphorylationEAGPTQFTTPLASFT
HHCCCCCCCCCCCEE		20.0728122231
279 (in isoform 2)Phosphorylation-20.0722167270
279 (in isoform 4)Phosphorylation-20.0722167270
280O-linked_GlycosylationAGPTQFTTPLASFTT
HCCCCCCCCCCCEEE		20.0023301498
280PhosphorylationAGPTQFTTPLASFTT
HCCCCCCCCCCCEEE		20.0021815630
283 (in isoform 2)Phosphorylation-12.1030266825
283 (in isoform 4)Phosphorylation-12.1030266825
284O-linked_GlycosylationQFTTPLASFTTVASE
CCCCCCCCEEECCCC		30.7023301498
284PhosphorylationQFTTPLASFTTVASE
CCCCCCCCEEECCCC		30.7019664994
284 (in isoform 2)Phosphorylation-30.7019664994
284 (in isoform 4)Phosphorylation-30.7019664994
286O-linked_GlycosylationTTPLASFTTVASEPP
CCCCCCEEECCCCCC		20.1923301498
286PhosphorylationTTPLASFTTVASEPP
CCCCCCEEECCCCCC		20.1928122231
287O-linked_GlycosylationTPLASFTTVASEPPV
CCCCCEEECCCCCCC		16.4423301498
290O-linked_GlycosylationASFTTVASEPPVKLV
CCEEECCCCCCCEEC		46.4223301498
374PhosphorylationIKEECFRSGVAEAPV
HHHHHHHHCCCCCCC		19.8423403867
375AcetylationKEECFRSGVAEAPVG
HHHHHHHCCCCCCCC		20.5619608861
383PhosphorylationVAEAPVGSKAPSIDG
CCCCCCCCCCCCCCC		26.3623401153
384AcetylationAEAPVGSKAPSIDGK
CCCCCCCCCCCCCCH		59.3925953088
384UbiquitinationAEAPVGSKAPSIDGK
CCCCCCCCCCCCCCH		59.39-
387PhosphorylationPVGSKAPSIDGKEEL
CCCCCCCCCCCHHHH		37.8725159151
391AcetylationKAPSIDGKEELDLAE
CCCCCCCHHHHCHHH		44.2426051181
469AcetylationPIQQERDKPVPLPAP
CCCCCCCCCCCCCCC		54.8825953088
469SumoylationPIQQERDKPVPLPAP
CCCCCCCCCCCCCCC		54.8828112733
479PhosphorylationPLPAPEMTVKQERLD
CCCCCCCEEEHHHCC		23.92-
481AcetylationPAPEMTVKQERLDFE
CCCCCEEEHHHCCHH		36.9619608861
481SumoylationPAPEMTVKQERLDFE
CCCCCEEEHHHCCHH		36.9619608861
484AcetylationEMTVKQERLDFEETE
CCEEEHHHCCHHHHC		36.7419608861
502MethylationIHELVDIREPSAEIK
CCEEEECCCCCCEEE		45.36-
505PhosphorylationLVDIREPSAEIKVEP
EEECCCCCCEEEECC		33.5128555341
509SumoylationREPSAEIKVEPAEPE
CCCCCEEEECCCCCC		31.8628112733
541PhosphorylationMEPPELRSQDLDEEL
CCCCHHHCCCHHHHH		40.4427690223
550PhosphorylationDLDEELGSTAAGEIV
CHHHHHCCCHHHEEE		27.7427690223
551PhosphorylationLDEELGSTAAGEIVE
HHHHHCCCHHHEEEE		20.8027690223
554AcetylationELGSTAAGEIVEADV
HHCCCHHHEEEEEEE		23.7719608861
569PhosphorylationAIGKGDETPLTNVKT
EECCCCCCCCCCCCC		28.4729255136
572PhosphorylationKGDETPLTNVKTEAS
CCCCCCCCCCCCCCC		38.8919691289
575SumoylationETPLTNVKTEASPES
CCCCCCCCCCCCHHH		42.5928112733
576PhosphorylationTPLTNVKTEASPESM
CCCCCCCCCCCHHHH		32.2830278072
579PhosphorylationTNVKTEASPESMLSP
CCCCCCCCHHHHCCC		23.9830278072
582PhosphorylationKTEASPESMLSPSHG
CCCCCHHHHCCCCCC		28.5430278072
585PhosphorylationASPESMLSPSHGSNP
CCHHHHCCCCCCCCC		18.7330278072
587PhosphorylationPESMLSPSHGSNPIE
HHHHCCCCCCCCCCC		36.7823927012
590PhosphorylationMLSPSHGSNPIEDPL
HCCCCCCCCCCCCCH		33.7330278072
601PhosphorylationEDPLEAETQHKFEMS
CCCHHHHHCHHCCCC		42.9220873877
608PhosphorylationTQHKFEMSDSLKEES
HCHHCCCCHHHHHCC		19.4921815630
610PhosphorylationHKFEMSDSLKEESGT
HHCCCCHHHHHCCCC		33.7521815630
612SumoylationFEMSDSLKEESGTIF
CCCCHHHHHCCCCEE		64.4928112733
615O-linked_GlycosylationSDSLKEESGTIFGSQ
CHHHHHCCCCEECCC		42.1823301498
615PhosphorylationSDSLKEESGTIFGSQ
CHHHHHCCCCEECCC		42.1823663014
617PhosphorylationSLKEESGTIFGSQIK
HHHHCCCCEECCCCC		23.5525159151
621PhosphorylationESGTIFGSQIKDAPG
CCCCEECCCCCCCCC		20.2725159151
637PhosphorylationDEEEDGVSEAASLEE
CCCCCCCCCCCCCCC		27.3528355574
641PhosphorylationDGVSEAASLEEPKEE
CCCCCCCCCCCCCCH		43.2828355574
656PhosphorylationDQGEGYLSEMDNEPP
HCCCCCCCCCCCCCC		23.53-
694PhosphorylationIPSSPASSQFSVCSE
CCCCCCHHCCEECCC		37.0320068231
842PhosphorylationSTRKQDASEKDSVPM
CCCCCCCCHHCCCCC		54.17-
846PhosphorylationQDASEKDSVPMGSPA
CCCCHHCCCCCCCHH		38.9122199227
851PhosphorylationKDSVPMGSPAFLLSL
HCCCCCCCHHHHHHH		13.5520068231
915 (in isoform 2)Phosphorylation-41.6420068231
919 (in isoform 2)Phosphorylation-65.5920068231
924 (in isoform 2)Phosphorylation-5.7222199227
930 (in isoform 2)Phosphorylation-36.3020068231
936 (in isoform 2)Phosphorylation-54.2820068231
1001O-linked_GlycosylationCRETEELSAKGDPLV
HHHHHHHHHCCCCCE		31.0823301498
1110AcetylationQDHLLFKKTLLPVWK
HHHHHHHHHHHHHHH		36.7526210075
1117AcetylationKTLLPVWKMIASHRF
HHHHHHHHHHHHHCC		22.2126210075
1126PhosphorylationIASHRFSSPFLKPVS
HHHHCCCCCCCCCCC		19.5724719451
1151PhosphorylationVKRPMDLTSLKRNLS
HCCCCCHHHHHHHHC		27.9620068231
1152PhosphorylationKRPMDLTSLKRNLSK
CCCCCHHHHHHHHCH		38.9120068231
1182PhosphorylationMFQNAVMYNDSDHHV
HHHHCCEECCCCCHH		14.82-
1190PhosphorylationNDSDHHVYHMAVEMR
CCCCCHHHHHHHHHH		4.98-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD8_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 BRD8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RXRA_HUMANRXRAphysical
10517671
THB_HUMANTHRBphysical
9368056
MRGBP_HUMANMRGBPphysical
20051959
MS18A_HUMANMIS18Aphysical
25416956
FSD2_HUMANFSD2physical
25416956
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 BRD8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-641, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, 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-637; SER-641; THR-1151AND SER-1152 (ISOFORM 1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATTHR-264; SER-268 AND SER-284 (ISOFORM 4), AND MASS SPECTROMETRY.

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