dbPTM

BRD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRD2_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	P25440
Protein Name	Bromodomain-containing protein 2
Gene Name	BRD2
Organism	Homo sapiens (Human).
Sequence Length	801
Subcellular Localization	Nucleus . Detected on chromatin and nucleosomes.
Protein Description	May play a role in spermatogenesis or folliculogenesis (By similarity). 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..
Protein Sequence	MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MLQNVTPH -------CCCCCCCC	8.62	20068231
6	Phosphorylation	--MLQNVTPHNKLPG --CCCCCCCCCCCCC	26.78	25159151
6 (in isoform 2)	Phosphorylation	-	26.78	24719451
10	Acetylation	QNVTPHNKLPGEGNA CCCCCCCCCCCCCCC	53.69	25953088
31	Acetylation	PEAAAPGKRIRKPSL HHHCCCCCCCCCHHH	43.52	23954790
37	Phosphorylation	GKRIRKPSLLYEGFE CCCCCCHHHHCCCCC	33.76	27273156
37 (in isoform 2)	Phosphorylation	-	33.76	27251275
40	Phosphorylation	IRKPSLLYEGFESPT CCCHHHHCCCCCCCC	21.21	28102081
45	Phosphorylation	LLYEGFESPTMASVP HHCCCCCCCCCCCCC	24.33	25159151
47	Phosphorylation	YEGFESPTMASVPAL CCCCCCCCCCCCCCC	34.35	23882029
50	Phosphorylation	FESPTMASVPALQLT CCCCCCCCCCCCCCC	20.15	23882029
57	Phosphorylation	SVPALQLTPANPPPP CCCCCCCCCCCCCCC	13.85	26055452
67	Phosphorylation	NPPPPEVSNPKKPGR CCCCCCCCCCCCCCC	45.83	23882029
115	Acetylation	LGLPDYHKIIKQPMD CCCCCHHHHHCCCCC	39.64	25953088
118	Ubiquitination	PDYHKIIKQPMDMGT CCHHHHHCCCCCHHH	52.39	-
125	Phosphorylation	KQPMDMGTIKRRLEN CCCCCHHHHHHHHHH	19.38	-
134	Phosphorylation	KRRLENNYYWAASEC HHHHHHCCEEEHHHH	16.38	24043423
135	Phosphorylation	RRLENNYYWAASECM HHHHHCCEEEHHHHH	7.24	24043423
139	Phosphorylation	NNYYWAASECMQDFN HCCEEEHHHHHHHHH	24.47	24043423
147	Phosphorylation	ECMQDFNTMFTNCYI HHHHHHHHHHCCEEE	17.41	24043423
150	Phosphorylation	QDFNTMFTNCYIYNK HHHHHHHCCEEECCC	17.35	24043423
153	Phosphorylation	NTMFTNCYIYNKPTD HHHHCCEEECCCCCC	14.44	24043423
155	Phosphorylation	MFTNCYIYNKPTDDI HHCCEEECCCCCCHH	7.23	24043423
179	Phosphorylation	IFLQKVASMPQEEQE HHHHHHHCCCHHHHE	33.70	26074081
208	O-linked_Glycosylation	KLAALQGSVTSAHQV HHHHHCCCCCCCHHC	14.84	32119511
211	O-linked_Glycosylation	ALQGSVTSAHQVPAV HHCCCCCCCHHCCCC	22.92	32119511
219	O-linked_Glycosylation	AHQVPAVSSVSHTAL CHHCCCCEEECCCEE	27.42	32119511
220	O-linked_Glycosylation	HQVPAVSSVSHTALY HHCCCCEEECCCEEC	22.50	32119511
227	Phosphorylation	SVSHTALYTPPPEIP EECCCEECCCCCCCC	18.09	29496963
235	O-linked_Glycosylation	TPPPEIPTTVLNIPH CCCCCCCCCCCCCCC	34.89	32119511
236	O-linked_Glycosylation	PPPEIPTTVLNIPHP CCCCCCCCCCCCCCH	20.03	32119511
248	Phosphorylation	PHPSVISSPLLKSLH CCHHHCCHHHHHHHH	14.40	29496963
253	Phosphorylation	ISSPLLKSLHSAGPP CCHHHHHHHHHCCCC	31.14	22322096
256	Phosphorylation	PLLKSLHSAGPPLLA HHHHHHHHCCCCEEE	39.97	28555341
275	Acetylation	PPAQPLAKKKGVKRK CCCCCCHHHCCCCCC	63.80	25953088
276	Acetylation	PAQPLAKKKGVKRKA CCCCCHHHCCCCCCC	49.50	25953088
285	Phosphorylation	GVKRKADTTTPTPTA CCCCCCCCCCCCCCE	37.11	23927012
286	Phosphorylation	VKRKADTTTPTPTAI CCCCCCCCCCCCCEE	31.18	23927012
287	Phosphorylation	KRKADTTTPTPTAIL CCCCCCCCCCCCEEE	27.53	23927012
289	Phosphorylation	KADTTTPTPTAILAP CCCCCCCCCCEEECC	31.05	23927012
291	Phosphorylation	DTTTPTPTAILAPGS CCCCCCCCEEECCCC	28.89	23927012
298	Phosphorylation	TAILAPGSPASPPGS CEEECCCCCCCCCCC	19.08	29255136
298 (in isoform 2)	Phosphorylation	-	19.08	24719451
301	Phosphorylation	LAPGSPASPPGSLEP ECCCCCCCCCCCCCC	34.70	29255136
301 (in isoform 2)	Phosphorylation	-	34.70	24719451
305	Phosphorylation	SPASPPGSLEPKAAR CCCCCCCCCCCHHHC	35.02	29255136
305 (in isoform 2)	Phosphorylation	-	35.02	21406692
320	Phosphorylation	LPPMRRESGRPIKPP CCCCCCCCCCCCCCC	37.99	27273156
325	Acetylation	RESGRPIKPPRKDLP CCCCCCCCCCCCCCC	52.21	25953088
334	Phosphorylation	PRKDLPDSQQQHQSS CCCCCCHHHHHHHHH	28.13	25849741
340	Phosphorylation	DSQQQHQSSKKGKLS HHHHHHHHHHHHHHH	41.84	22496350
341	Phosphorylation	SQQQHQSSKKGKLSE HHHHHHHHHHHHHHH	31.64	20068231
342	Acetylation	QQQHQSSKKGKLSEQ HHHHHHHHHHHHHHH	71.44	23749302
343	Acetylation	QQHQSSKKGKLSEQL HHHHHHHHHHHHHHH	64.32	25953088
345	Acetylation	HQSSKKGKLSEQLKH HHHHHHHHHHHHHHH	58.69	23749302
397	Phosphorylation	IKHPMDLSTVKRKME HHCCCCHHHHHHHHH	27.22	22210691
398	Phosphorylation	KHPMDLSTVKRKMEN HCCCCHHHHHHHHHC	37.03	22210691
400	2-Hydroxyisobutyrylation	PMDLSTVKRKMENRD CCCHHHHHHHHHCCC	46.52	-
400	Ubiquitination	PMDLSTVKRKMENRD CCCHHHHHHHHHCCC	46.52	-
449	Methylation	LQDVFEFRYAKMPDE HHHHHHHHCCCCCCC	24.25	-
450	Phosphorylation	QDVFEFRYAKMPDEP HHHHHHHCCCCCCCC	18.85	-
538	Phosphorylation	HEQLAALSQGPISKP HHHHHHHHCCCCCCC	28.50	23312004
543	Phosphorylation	ALSQGPISKPKRKRE HHHCCCCCCCHHHHH	46.14	23186163
544	Acetylation	LSQGPISKPKRKREK HHCCCCCCCHHHHHH	56.10	23749302
574	Acetylation	AGADEDDKGPRAPRP CCCCCCCCCCCCCCC	81.02	23749302
591	Phosphorylation	PKKSKKASGSGGGSA CCCCCCCCCCCCCCC	42.23	28152594
593	Phosphorylation	KSKKASGSGGGSAAL CCCCCCCCCCCCCCC	31.59	28152594
597	Phosphorylation	ASGSGGGSAALGPSG CCCCCCCCCCCCCCC	17.40	28152594
597 (in isoform 2)	Phosphorylation	-	17.40	27251275
603	Phosphorylation	GSAALGPSGFGPSGG CCCCCCCCCCCCCCC	44.98	24732914
608	Phosphorylation	GPSGFGPSGGSGTKL CCCCCCCCCCCCCCC	57.05	25159151
608 (in isoform 2)	Phosphorylation	-	57.05	20068231
611	Phosphorylation	GFGPSGGSGTKLPKK CCCCCCCCCCCCCCC	46.98	25159151
611 (in isoform 2)	Phosphorylation	-	46.98	28985074
613	Phosphorylation	GPSGGSGTKLPKKAT CCCCCCCCCCCCCCC	30.98	25159151
614	Acetylation	PSGGSGTKLPKKATK CCCCCCCCCCCCCCC	67.33	25953088
617	Acetylation	GSGTKLPKKATKTAP CCCCCCCCCCCCCCC	66.53	30583773
622	Phosphorylation	LPKKATKTAPPALPT CCCCCCCCCCCCCCC	39.79	23927012
629	Phosphorylation	TAPPALPTGYDSEEE CCCCCCCCCCCCHHH	49.58	23401153
631	Phosphorylation	PPALPTGYDSEEEEE CCCCCCCCCCHHHHH	20.83	23927012
633	Phosphorylation	ALPTGYDSEEEEESR CCCCCCCCHHHHHHC	38.12	23927012
639	Phosphorylation	DSEEEEESRPMSYDE CCHHHHHHCCCCHHH	44.99	23927012
643	Phosphorylation	EEESRPMSYDEKRQL HHHHCCCCHHHHHHH	31.92	23927012
644	Phosphorylation	EESRPMSYDEKRQLS HHHCCCCHHHHHHHH	23.13	23927012
651	Phosphorylation	YDEKRQLSLDINKLP HHHHHHHHCCHHHCC	18.69	25159151
656	Ubiquitination	QLSLDINKLPGEKLG HHHCCHHHCCHHHHH	57.29	-
661	2-Hydroxyisobutyrylation	INKLPGEKLGRVVHI HHHCCHHHHHHEEEE	63.26	-
661	Ubiquitination	INKLPGEKLGRVVHI HHHCCHHHHHHEEEE	63.26	-
664 (in isoform 2)	Phosphorylation	-	37.41	21406692
668 (in isoform 2)	Phosphorylation	-	1.36	27251275
678 (in isoform 2)	Phosphorylation	-	59.04	27251275
690	Phosphorylation	EIEIDFETLKPSTLR HEEECHHHCCHHHHH	39.82	19664995
705	Phosphorylation	ELERYVLSCLRKKPR HHHHHHHHHHHCCCC	10.89	21712546
713	Acetylation	CLRKKPRKPYTIKKP HHHCCCCCCCCCCCC	51.40	26051181
715	Phosphorylation	RKKPRKPYTIKKPVG HCCCCCCCCCCCCCC	24.92	-
716	Phosphorylation	KKPRKPYTIKKPVGK CCCCCCCCCCCCCCC	34.54	-
724	Phosphorylation	IKKPVGKTKEELALE CCCCCCCCHHHHHHH	37.45	17081983
725	Acetylation	KKPVGKTKEELALEK CCCCCCCHHHHHHHH	53.31	23749302
732	2-Hydroxyisobutyrylation	KEELALEKKRELEKR HHHHHHHHHHHHHHH	58.96	-
744	Phosphorylation	EKRLQDVSGQLNSTK HHHHHHHHHCCCCCC	29.16	24732914
749	Phosphorylation	DVSGQLNSTKKPPKK HHHHCCCCCCCCCCC	50.63	25159151
750	Phosphorylation	VSGQLNSTKKPPKKA HHHCCCCCCCCCCCC	41.85	21815630
760	Acetylation	PPKKANEKTESSSAQ CCCCCCCCCCCCHHH	58.35	26051181
761	Phosphorylation	PKKANEKTESSSAQQ CCCCCCCCCCCHHHH	34.61	22210691
763	Phosphorylation	KANEKTESSSAQQVA CCCCCCCCCHHHHHH	34.52	26503892
764	Phosphorylation	ANEKTESSSAQQVAV CCCCCCCCHHHHHHH	24.38	22210691
765	Phosphorylation	NEKTESSSAQQVAVS CCCCCCCHHHHHHHH	39.10	22210691
772	Phosphorylation	SAQQVAVSRLSASSS HHHHHHHHHHHCCCC	20.12	26503892
775	Phosphorylation	QVAVSRLSASSSSSD HHHHHHHHCCCCCCC	25.62	-
777	Phosphorylation	AVSRLSASSSSSDSS HHHHHHCCCCCCCCC	27.64	-
778	Phosphorylation	VSRLSASSSSSDSSS HHHHHCCCCCCCCCC	33.68	-
779	Phosphorylation	SRLSASSSSSDSSSS HHHHCCCCCCCCCCC	31.22	-
784	Phosphorylation	SSSSSDSSSSSSSSS CCCCCCCCCCCCCCC	38.95	-
785	Phosphorylation	SSSSDSSSSSSSSSS CCCCCCCCCCCCCCC	37.89	-
786	Phosphorylation	SSSDSSSSSSSSSSS CCCCCCCCCCCCCCC	35.87	-
787	Phosphorylation	SSDSSSSSSSSSSSD CCCCCCCCCCCCCCC	35.87	-
788	Phosphorylation	SDSSSSSSSSSSSDT CCCCCCCCCCCCCCC	35.87	-
789	Phosphorylation	DSSSSSSSSSSSDTS CCCCCCCCCCCCCCC	35.87	-
795	Phosphorylation	SSSSSSDTSDSDSG- CCCCCCCCCCCCCC-	36.06	-

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
-	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 BRD2_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 BRD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E2F2_HUMAN	E2F2	physical	12145330
E2F1_HUMAN	E2F1	physical	10965846
E2F2_HUMAN	E2F2	physical	10965846
BRD2_HUMAN	BRD2	physical	17148447
TBP_HUMAN	TBP	physical	17111193
E2F1_HUMAN	E2F1	physical	17111193
BRD7_HUMAN	BRD7	physical	16786191
BAG1_HUMAN	BAG1	physical	26496610
CSK21_HUMAN	CSNK2A1	physical	26496610
CSK22_HUMAN	CSNK2A2	physical	26496610
CSK2B_HUMAN	CSNK2B	physical	26496610
E41L1_HUMAN	EPB41L1	physical	26496610
RPB2_HUMAN	POLR2B	physical	26496610
BRPF1_HUMAN	BRPF1	physical	26496610
TAGL2_HUMAN	TAGLN2	physical	26496610
COX5A_HUMAN	COX5A	physical	26496610
FARP1_HUMAN	FARP1	physical	26496610
TADA3_HUMAN	TADA3	physical	26496610
NSD3_HUMAN	WHSC1L1	physical	26496610
PWP2B_HUMAN	PWWP2B	physical	26496610

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 BRD2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-298 AND SER-301, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-298 AND SER-301,AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-298 AND SER-301, 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-298; SER-301; SER-305AND SER-633, AND MASS SPECTROMETRY.	18669648 [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-320, AND MASSSPECTROMETRY.	17287340 [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-298 AND SER-301, ANDMASS SPECTROMETRY.	15302935 [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 THR-724, AND MASSSPECTROMETRY.	17081983 [Abstract]