dbPTM

BRD4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRD4_HUMAN
UniProt AC	O60885
Protein Name	Bromodomain-containing protein 4
Gene Name	BRD4
Organism	Homo sapiens (Human).
Sequence Length	1362
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.
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. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo. [PubMed: 22509028 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.; Isoform B: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AFX/H2A.x phosphorylation.]
Protein Sequence	MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Phosphorylation	RQTNQLQYLLRVVLK HHHHHHHHHHHHHHH	19.12	-
72	Acetylation	YLLRVVLKTLWKHQF HHHHHHHHHHHHHCC	29.93	25953088
91	Sumoylation	QQPVDAVKLNLPDYY CCCCCCHHCCCCCHH	33.12	-
91	Ubiquitination	QQPVDAVKLNLPDYY CCCCCCHHCCCCCHH	33.12	-
99	Sumoylation	LNLPDYYKIIKTPMD CCCCCHHHHHCCCCC	31.55	28112733
99	Ubiquitination	LNLPDYYKIIKTPMD CCCCCHHHHHCCCCC	31.55	21890473
99 (in isoform 1)	Ubiquitination	-	31.55	21890473
99 (in isoform 2)	Ubiquitination	-	31.55	21890473
99	Ubiquitination	LNLPDYYKIIKTPMD CCCCCHHHHHCCCCC	31.55	21890473
103	Phosphorylation	DYYKIIKTPMDMGTI CHHHHHCCCCCHHHH	17.28	29507054
109	Phosphorylation	KTPMDMGTIKKRLEN CCCCCHHHHHHHHHH	24.00	29507054
111	Acetylation	PMDMGTIKKRLENNY CCCHHHHHHHHHHCC	31.51	24887501
111	Ubiquitination	PMDMGTIKKRLENNY CCCHHHHHHHHHHCC	31.51	-
112	Ubiquitination	MDMGTIKKRLENNYY CCHHHHHHHHHHCCC	59.36	-
155	Ubiquitination	LMAEALEKLFLQKIN HHHHHHHHHHHHHHH	45.44	-
172	Sulfoxidation	PTEETEIMIVQAKGR CCCCCEEEEEEECCC	1.68	21406390
177	Acetylation	EIMIVQAKGRGRGRK EEEEEEECCCCCCCC	31.86	25953088
177	Methylation	EIMIVQAKGRGRGRK EEEEEEECCCCCCCC	31.86	-
179	Methylation	MIVQAKGRGRGRKET EEEEECCCCCCCCCC	30.81	-
181	Methylation	VQAKGRGRGRKETGT EEECCCCCCCCCCCC	40.14	-
183	Methylation	AKGRGRGRKETGTAK ECCCCCCCCCCCCCC	32.07	-
200	Phosphorylation	VSTVPNTTQASTPPQ CCCCCCCCCCCCCCC	28.86	26657352
204	Phosphorylation	PNTTQASTPPQTQTP CCCCCCCCCCCCCCC	41.84	-
294	Phosphorylation	GVKRKADTTTPTTID CCCCCCCCCCCCCCC	37.11	25159151
295	Phosphorylation	VKRKADTTTPTTIDP CCCCCCCCCCCCCCC	31.18	25159151
296	Phosphorylation	KRKADTTTPTTIDPI CCCCCCCCCCCCCCC	22.26	25159151
298	Phosphorylation	KADTTTPTTIDPIHE CCCCCCCCCCCCCCC	34.00	24732914
299	Phosphorylation	ADTTTPTTIDPIHEP CCCCCCCCCCCCCCC	25.29	28348404
308	Phosphorylation	DPIHEPPSLPPEPKT CCCCCCCCCCCCCCC	65.31	24732914
315	Phosphorylation	SLPPEPKTTKLGQRR CCCCCCCCCCCCCCC	39.62	-
316	Phosphorylation	LPPEPKTTKLGQRRE CCCCCCCCCCCCCCC	30.33	-
317	Acetylation	PPEPKTTKLGQRRES CCCCCCCCCCCCCCC	56.71	23749302
324	Phosphorylation	KLGQRRESSRPVKPP CCCCCCCCCCCCCCC	29.81	30206219
325	Phosphorylation	LGQRRESSRPVKPPK CCCCCCCCCCCCCCC	35.53	20068231
325 (in isoform 2)	Phosphorylation	-	35.53	-
333	Acetylation	RPVKPPKKDVPDSQQ CCCCCCCCCCCCHHC	70.50	30586091
338	Phosphorylation	PKKDVPDSQQHPAPE CCCCCCCHHCCCCCC	26.18	23663014
346	Acetylation	QQHPAPEKSSKVSEQ HCCCCCCHHHHHHHH	59.99	23749302
347	O-linked_Glycosylation	QHPAPEKSSKVSEQL CCCCCCHHHHHHHHH	33.46	30059200
348	O-linked_Glycosylation	HPAPEKSSKVSEQLK CCCCCHHHHHHHHHH	48.41	30059200
351	Phosphorylation	PEKSSKVSEQLKCCS CCHHHHHHHHHHHHH	24.30	20860994
358	Phosphorylation	SEQLKCCSGILKEMF HHHHHHHHHHHHHHH	38.04	20860994
362	Acetylation	KCCSGILKEMFAKKH HHHHHHHHHHHHHHC	45.25	20167786
367	Acetylation	ILKEMFAKKHAAYAW HHHHHHHHHCHHHCC	33.55	20167786
368	Acetylation	LKEMFAKKHAAYAWP HHHHHHHHCHHHCCC	34.74	20167786
404	"N6,N6-dimethyllysine"	PMDMSTIKSKLEARE CCCHHHHHHHHHHHH	41.44	-
404	Methylation	PMDMSTIKSKLEARE CCCHHHHHHHHHHHH	41.44	-
404	Ubiquitination	PMDMSTIKSKLEARE CCCHHHHHHHHHHHH	41.44	-
406	"N6,N6-dimethyllysine"	DMSTIKSKLEAREYR CHHHHHHHHHHHHHH	45.40	-
406	Methylation	DMSTIKSKLEAREYR CHHHHHHHHHHHHHH	45.40	-
431	Acetylation	LMFSNCYKYNPPDHE EHHCCCHHCCCCCHH	40.53	26051181
452	Sulfoxidation	KLQDVFEMRFAKMPD HHHHHHHHHHCCCCC	2.65	21406390
453	Methylation	LQDVFEMRFAKMPDE HHHHHHHHHCCCCCC	22.60	-
456	Acetylation	VFEMRFAKMPDEPEE HHHHHHCCCCCCCCC	48.53	25953088
469	Phosphorylation	EEPVVAVSSPAVPPP CCCEEEEECCCCCCC	22.37	29255136
469 (in isoform 2)	Phosphorylation	-	22.37	-
470	Phosphorylation	EPVVAVSSPAVPPPT CCEEEEECCCCCCCC	15.41	29255136
470 (in isoform 2)	Phosphorylation	-	15.41	-
477	Phosphorylation	SPAVPPPTKVVAPPS CCCCCCCCEEECCCC	42.09	29255136
484	Phosphorylation	TKVVAPPSSSDSSSD CEEECCCCCCCCCCC	41.22	23317504
488	Phosphorylation	APPSSSDSSSDSSSD CCCCCCCCCCCCCCC	33.42	23317504
492	Phosphorylation	SSDSSSDSSSDSDSS CCCCCCCCCCCCCCC	33.42	27174698
493	Phosphorylation	SDSSSDSSSDSDSST CCCCCCCCCCCCCCC	43.06	27174698
494	Phosphorylation	DSSSDSSSDSDSSTD CCCCCCCCCCCCCCC	45.12	27174698
496	Phosphorylation	SSDSSSDSDSSTDDS CCCCCCCCCCCCCCC	41.14	27174698
498	Phosphorylation	DSSSDSDSSTDDSEE CCCCCCCCCCCCCHH	38.80	27174698
499	Phosphorylation	SSSDSDSSTDDSEEE CCCCCCCCCCCCHHH	40.63	27174698
500	Phosphorylation	SSDSDSSTDDSEEER CCCCCCCCCCCHHHH	48.02	27174698
503	Phosphorylation	SDSSTDDSEEERAQR CCCCCCCCHHHHHHH	50.12	27174698
578	Phosphorylation	KKTKKNNSSNSNVSK CCCCCCCCCCCCCCC	40.05	21712546
579	Phosphorylation	KTKKNNSSNSNVSKK CCCCCCCCCCCCCCC	46.53	21712546
581	Phosphorylation	KKNNSSNSNVSKKEP CCCCCCCCCCCCCCC	40.32	21712546
584	Phosphorylation	NSSNSNVSKKEPAPM CCCCCCCCCCCCCCC	42.11	-
585	Sumoylation	SSNSNVSKKEPAPMK CCCCCCCCCCCCCCC	57.80	28112733
593	Phosphorylation	KEPAPMKSKPPPTYE CCCCCCCCCCCCCCC	44.11	23403867
598	Phosphorylation	MKSKPPPTYESEEED CCCCCCCCCCCCCCC	45.77	23927012
599	Phosphorylation	KSKPPPTYESEEEDK CCCCCCCCCCCCCCC	24.19	23927012
601	Phosphorylation	KPPPTYESEEEDKCK CCCCCCCCCCCCCCC	39.64	23927012
601 (in isoform 2)	Phosphorylation	-	39.64	-
611	Phosphorylation	EDKCKPMSYEEKRQL CCCCCCCCHHHHHHH	37.61	23403867
612	Phosphorylation	DKCKPMSYEEKRQLS CCCCCCCHHHHHHHH	23.12	23403867
619	Phosphorylation	YEEKRQLSLDINKLP HHHHHHHHCCHHHCC	18.69	25159151
624	Ubiquitination	QLSLDINKLPGEKLG HHHCCHHHCCHHHHH	57.29	-
629	Acetylation	INKLPGEKLGRVVHI HHHCCHHHHHHEEEE	63.26	25953088
629	Ubiquitination	INKLPGEKLGRVVHI HHHCCHHHHHHEEEE	63.26	-
645	Sumoylation	QSREPSLKNSNPDEI HCCCCCCCCCCCCCE	63.77	28112733
658	O-linked_Glycosylation	EIEIDFETLKPSTLR CEEECHHHCCHHHHH	39.82	30059200
658	Phosphorylation	EIEIDFETLKPSTLR CEEECHHHCCHHHHH	39.82	-
660	Acetylation	EIDFETLKPSTLREL EECHHHCCHHHHHHH	44.32	26051181
660	Ubiquitination	EIDFETLKPSTLREL EECHHHCCHHHHHHH	44.32	-
673	Phosphorylation	ELERYVTSCLRKKRK HHHHHHHHHHHHCCC	10.91	25159151
685	Acetylation	KRKPQAEKVDVIAGS CCCCCHHHCEEEECC	46.91	23749302
692	Phosphorylation	KVDVIAGSSKMKGFS HCEEEECCCCCCCCC	20.12	30001349
693	Phosphorylation	VDVIAGSSKMKGFSS CEEEECCCCCCCCCC	35.53	30001349
694	Sumoylation	DVIAGSSKMKGFSSS EEEECCCCCCCCCCC	46.45	-
694	Acetylation	DVIAGSSKMKGFSSS EEEECCCCCCCCCCC	46.45	25953088
694	Sumoylation	DVIAGSSKMKGFSSS EEEECCCCCCCCCCC	46.45	28112733
694	Ubiquitination	DVIAGSSKMKGFSSS EEEECCCCCCCCCCC	46.45	-
701	Phosphorylation	KMKGFSSSESESSSE CCCCCCCCCCCCCCC	43.90	-
701 (in isoform 2)	Phosphorylation	-	43.90	-
705	Phosphorylation	FSSSESESSSESSSS CCCCCCCCCCCCCCC	48.74	-
706	Phosphorylation	SSSESESSSESSSSD CCCCCCCCCCCCCCC	33.79	28348404
706 (in isoform 2)	Phosphorylation	-	33.79	-
707	Phosphorylation	SSESESSSESSSSDS CCCCCCCCCCCCCCC	51.26	28348404
709	Phosphorylation	ESESSSESSSSDSED CCCCCCCCCCCCCCC	37.15	28348404
710	Phosphorylation	SESSSESSSSDSEDS CCCCCCCCCCCCCCC	29.79	28348404
711	Phosphorylation	ESSSESSSSDSEDSE CCCCCCCCCCCCCCC	47.66	28348404
711 (in isoform 2)	Phosphorylation	-	47.66	-
712	Phosphorylation	SSSESSSSDSEDSET CCCCCCCCCCCCCCC	47.29	28348404
714	Phosphorylation	SESSSSDSEDSETEM CCCCCCCCCCCCCCC	45.30	28348404
726	Acetylation	TEMAPKSKKKGHPGR CCCCCCHHCCCCCCH	65.71	11793911
727	Acetylation	EMAPKSKKKGHPGRE CCCCCHHCCCCCCHH	71.70	11793921
795	Phosphorylation	QAAPAMKSSPPPFIA CCCHHHHCCCCCEEE	34.68	20068231
796	Phosphorylation	AAPAMKSSPPPFIAT CCHHHHCCCCCEEEE	35.59	26657352
803	Phosphorylation	SPPPFIATQVPVLEP CCCCEEEEECCCCCC	25.86	20068231
815	Phosphorylation	LEPQLPGSVFDPIGH CCCCCCCCCCCCCCC	20.05	20068231
858	Phosphorylation	LNQHAVVSPPALHNA CCCCCCCCCHHHHHC	20.68	17001009
942	Phosphorylation	LQKVQPPTPLLPSVK HHHCCCCCCCCCCCC	33.00	22322096
947	Phosphorylation	PPTPLLPSVKVQSQP CCCCCCCCCCCCCCC	34.24	27251275
1045	Phosphorylation	QVIQHHHSPRHHKSD HHHCCCCCCCCCCCC	21.19	30631047
1050	Sumoylation	HHSPRHHKSDPYSTG CCCCCCCCCCCCCCC	50.89	-
1050	Sumoylation	HHSPRHHKSDPYSTG CCCCCCCCCCCCCCC	50.89	28112733
1051	Phosphorylation	HSPRHHKSDPYSTGH CCCCCCCCCCCCCCC	39.19	25159151
1054	Phosphorylation	RHHKSDPYSTGHLRE CCCCCCCCCCCCCCC	24.69	27642862
1055	Phosphorylation	HHKSDPYSTGHLREA CCCCCCCCCCCCCCC	33.04	28152594
1064	Phosphorylation	GHLREAPSPLMIHSP CCCCCCCCCEEECCC	37.40	23401153
1070	Phosphorylation	PSPLMIHSPQMSQFQ CCCEEECCCCHHHHH	13.10	23401153
1074	Phosphorylation	MIHSPQMSQFQSLTH EECCCCHHHHHHHCC	23.69	30278072
1078	Phosphorylation	PQMSQFQSLTHQSPP CCHHHHHHHCCCCCC	36.20	23401153
1080	Phosphorylation	MSQFQSLTHQSPPQQ HHHHHHHCCCCCCCC	24.10	23401153
1083	Phosphorylation	FQSLTHQSPPQQNVQ HHHHCCCCCCCCCCC	30.83	30278072
1100	Phosphorylation	KQELRAASVVQPQPL HHHHHHHCCCCCCCE	23.10	25159151
1111	Sumoylation	PQPLVVVKEEKIHSP CCCEEEEECCCCCCC	48.85	-
1111	Acetylation	PQPLVVVKEEKIHSP CCCEEEEECCCCCCC	48.85	19608861
1111	Sumoylation	PQPLVVVKEEKIHSP CCCEEEEECCCCCCC	48.85	19608861
1114	Acetylation	LVVVKEEKIHSPIIR EEEEECCCCCCCCCC	46.97	30586085
1117	Phosphorylation	VKEEKIHSPIIRSEP EECCCCCCCCCCCCC	22.67	29255136
1122	Phosphorylation	IHSPIIRSEPFSPSL CCCCCCCCCCCCCCC	38.93	30266825
1126	Phosphorylation	IIRSEPFSPSLRPEP CCCCCCCCCCCCCCC	25.05	23401153
1128	Phosphorylation	RSEPFSPSLRPEPPK CCCCCCCCCCCCCCC	35.49	30266825
1139	Phosphorylation	EPPKHPESIKAPVHL CCCCCCCCCCCCCCC	33.56	24732914
1153	Acetylation	LPQRPEMKPVDVGRP CCCCCCCCCCCCCCC	39.98	26051181
1177	Acetylation	PPPGAPDKDKQKQEP CCCCCCCHHHCCCCC	66.81	23236377
1186	Phosphorylation	KQKQEPKTPVAPKKD HCCCCCCCCCCCCCC	33.44	28985074
1197	Sumoylation	PKKDLKIKNMGSWAS CCCCCCCCCCCHHHH	39.02	-
1197	Sumoylation	PKKDLKIKNMGSWAS CCCCCCCCCCCHHHH	39.02	28112733
1201	Phosphorylation	LKIKNMGSWASLVQK CCCCCCCHHHHHHHH	14.54	25159151
1204	Phosphorylation	KNMGSWASLVQKHPT CCCCHHHHHHHHCCC	23.86	25218447
1208	Acetylation	SWASLVQKHPTTPSS HHHHHHHHCCCCCCC	44.03	25953088
1211	O-linked_Glycosylation	SLVQKHPTTPSSTAK HHHHHCCCCCCCCCC	51.57	30059200
1211	Phosphorylation	SLVQKHPTTPSSTAK HHHHHCCCCCCCCCC	51.57	29396449
1212	O-linked_Glycosylation	LVQKHPTTPSSTAKS HHHHCCCCCCCCCCC	26.14	30059200
1212	Phosphorylation	LVQKHPTTPSSTAKS HHHHCCCCCCCCCCC	26.14	25627689
1214	O-linked_Glycosylation	QKHPTTPSSTAKSSS HHCCCCCCCCCCCCC	37.92	30059200
1214	Phosphorylation	QKHPTTPSSTAKSSS HHCCCCCCCCCCCCC	37.92	29396449
1215	O-linked_Glycosylation	KHPTTPSSTAKSSSD HCCCCCCCCCCCCCH	33.32	30059200
1215	O-linked_Glycosylation	KHPTTPSSTAKSSSD HCCCCCCCCCCCCCH	33.32	20068230
1215	Phosphorylation	KHPTTPSSTAKSSSD HCCCCCCCCCCCCCH	33.32	30576142
1216	O-linked_Glycosylation	HPTTPSSTAKSSSDS CCCCCCCCCCCCCHH	42.30	30059200
1216	Phosphorylation	HPTTPSSTAKSSSDS CCCCCCCCCCCCCHH	42.30	30576142
1218	Ubiquitination	TTPSSTAKSSSDSFE CCCCCCCCCCCHHHH	51.46	-
1219	O-linked_Glycosylation	TPSSTAKSSSDSFEQ CCCCCCCCCCHHHHH	32.39	30059200
1221	Phosphorylation	SSTAKSSSDSFEQFR CCCCCCCCHHHHHHH	44.35	28555341
1223	O-linked_Glycosylation	TAKSSSDSFEQFRRA CCCCCCHHHHHHHHH	32.41	30059200
1223	Phosphorylation	TAKSSSDSFEQFRRA CCCCCCHHHHHHHHH	32.41	21815630
1262	Phosphorylation	LRQERMRSREDEDAL HHHHHHHHHHHHHHH	30.58	30624053
1309	Phosphorylation	AAVAAAATPQAQSSQ HHHHHHHCHHHHHCC	15.94	26425664

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
484	S	Phosphorylation	Kinase	CK2	-	Uniprot
488	S	Phosphorylation	Kinase	CK2	-	Uniprot
492	S	Phosphorylation	Kinase	CK2	-	Uniprot
494	S	Phosphorylation	Kinase	CK2	-	Uniprot
498	S	Phosphorylation	Kinase	CK2	-	Uniprot
499	S	Phosphorylation	Kinase	CK2	-	Uniprot
503	S	Phosphorylation	Kinase	CK2	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	SPOP	O43791	PMID:28805820:28805822

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BRD4_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 BRD4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFC1_HUMAN	RFC1	physical	12192049
RFC2_HUMAN	RFC2	physical	12192049
RFC3_HUMAN	RFC3	physical	12192049
RFC4_HUMAN	RFC4	physical	12192049
RFC5_HUMAN	RFC5	physical	12192049
SIPA1_HUMAN	SIPA1	physical	15456879
MED12_HUMAN	MED12	physical	16109376
MED14_HUMAN	MED14	physical	16109376
MED24_HUMAN	MED24	physical	16109376
MED17_HUMAN	MED17	physical	16109376
CCNT1_HUMAN	CCNT1	physical	16109376
CDK9_HUMAN	CDK9	physical	16109376
CCNT2_HUMAN	CCNT2	physical	16109376
CCNT1_HUMAN	CCNT1	physical	18039861
CDK9_HUMAN	CDK9	physical	18039861
HEXI1_HUMAN	HEXIM1	physical	18039861
H32_HUMAN	HIST2H3C	physical	18500820
EP300_HUMAN	EP300	physical	20676058
H31_HUMAN	HIST1H3A	physical	19766566
CDK9_HUMAN	CDK9	physical	19766566
MED1_HUMAN	MED1	physical	19766566
CHD4_HUMAN	CHD4	physical	21555454
JMJD6_HUMAN	JMJD6	physical	21555454
BAIP2_HUMAN	BAIAP2	physical	21555454
BI2L1_HUMAN	BAIAP2L1	physical	21555454
RBM25_HUMAN	RBM25	physical	21555454
CCNT1_HUMAN	CCNT1	physical	21555454
CDK9_HUMAN	CDK9	physical	21555454
BRD3_HUMAN	BRD3	physical	21555454
BRD2_HUMAN	BRD2	physical	21555454
NSD2_HUMAN	WHSC1	physical	21555454
BICRA_HUMAN	GLTSCR1	physical	21555454
ATAD5_HUMAN	ATAD5	physical	21555454
SMCA4_HUMAN	SMARCA4	physical	21555454
ZN592_HUMAN	ZNF592	physical	21555454
BRD9_HUMAN	BRD9	physical	21555454
NSD3_HUMAN	WHSC1L1	physical	21555454
SIR1_HUMAN	SIRT1	physical	21555454
SIR5_HUMAN	SIRT5	physical	21555454
KAD1_HUMAN	AK1	physical	21555454
PGAM2_HUMAN	PGAM2	physical	21555454
LDHC_HUMAN	LDHC	physical	21555454
KCRM_HUMAN	CKM	physical	21555454
ENL_HUMAN	MLLT1	physical	21964340
RL6_HUMAN	RPL6	physical	22939629
CCNT1_HUMAN	CCNT1	physical	17690245
CDK9_HUMAN	CDK9	physical	17690245
CCNT1_HUMAN	CCNT1	physical	16109377
CDK9_HUMAN	CDK9	physical	16109377
HEXI1_HUMAN	HEXIM1	physical	16109377
JMJD6_HUMAN	JMJD6	physical	23455924
CCNT1_HUMAN	CCNT1	physical	24367103
AFF1_HUMAN	AFF1	physical	24367103
CDK9_HUMAN	CDK9	physical	24367103
NSD3_HUMAN	WHSC1L1	physical	24875858
BRD3_HUMAN	BRD3	physical	26344197
DMAP1_HUMAN	DMAP1	physical	26344197
RTF1_HUMAN	RTF1	physical	26344197
ZCH18_HUMAN	ZC3H18	physical	26344197
NSD3_HUMAN	WHSC1L1	physical	26626481
CHD8_HUMAN	CHD8	physical	26626481
PTEN_HUMAN	PTEN	genetic	28319113
FGFR3_HUMAN	FGFR3	genetic	28319113
KDM5C_HUMAN	KDM5C	genetic	28319113
DYR_HUMAN	DHFR	genetic	28319113
RB_HUMAN	RB1	genetic	28319113
MP2K1_HUMAN	MAP2K1	genetic	28319113
CUL1_HUMAN	CUL1	physical	28805820
CUL3_HUMAN	CUL3	physical	28805820
SPOP_HUMAN	SPOP	physical	28805820
ANDR_HUMAN	AR	physical	28805820
ERG_HUMAN	ERG	physical	28805820

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 BRD4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-1111, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-469; SER-470 ANDSER-601, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND SER-1117, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND MASSSPECTROMETRY.	17924679 [Abstract]
"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-1045 AND SER-1117, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND MASSSPECTROMETRY.	15302935 [Abstract]