dbPTM

BRD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRD1_HUMAN
UniProt AC	O95696
Protein Name	Bromodomain-containing protein 1
Gene Name	BRD1
Organism	Homo sapiens (Human).
Sequence Length	1058
Subcellular Localization	Nucleus .
Protein Description	Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity..
Protein Sequence	MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEALPSAHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIVNEKRKGDCVPAVSQSMFEFLMDRFEKESHCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGGTTFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKALAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRSSQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQVAMELRLTPLTVLLRSVLDQLQDKDPARIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHEFEEDFDLIIDNCMKYNARDTVFYRAAVRLRDQGGVVLRQARREVDSIGLEEASGMHLPERPAAAPRRPFSWEDVDRLLDPANRAHLGLEEQLRELLDMLDLTCAMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQPLPTGPGLEGFEEDGAALGPEAGEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDAGLTNGFGGARSEQEPGGGLGRKATPRRRCASESSISSSNSPLCDSSFNAPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSSMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSDEKLFLVLFFDNKRSWQWLPKSKMVPLGIDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPTSDLSDID

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	KGRCHRGSAARHPSS CCCCCCCCCCCCCCC	20.79	23312004
17	Phosphorylation	GSAARHPSSPCSVKH CCCCCCCCCCCCCCC	40.56	22167270
18	Phosphorylation	SAARHPSSPCSVKHS CCCCCCCCCCCCCCC	34.08	23401153
21	Phosphorylation	RHPSSPCSVKHSPTR CCCCCCCCCCCCCCH	37.27	22167270
23	Acetylation	PSSPCSVKHSPTRET CCCCCCCCCCCCHHH	23.28	21466224
25	Phosphorylation	SPCSVKHSPTRETLT CCCCCCCCCCHHHEE	23.42	23401153
27	Phosphorylation	CSVKHSPTRETLTYA CCCCCCCCHHHEEHH	44.12	22167270
30	Phosphorylation	KHSPTRETLTYAQAQ CCCCCHHHEEHHHHH	22.55	24117733
32	Phosphorylation	SPTRETLTYAQAQRM CCCHHHEEHHHHHHH	25.00	30576142
33	Phosphorylation	PTRETLTYAQAQRMV CCHHHEEHHHHHHHE	10.38	30576142
33 (in isoform 2)	Phosphorylation	-	10.38	27642862
66	Phosphorylation	IILEDDLTAQEMSEC HHHCCCCCHHHHHHH	33.03	28348404
71	Phosphorylation	DLTAQEMSECNSNKE CCCHHHHHHHHCCCC	37.94	26074081
75	Phosphorylation	QEMSECNSNKENSER HHHHHHHCCCCCCCC	62.02	25849741
100	Acetylation	KNNRVKKKNEALPSA CCCCCCCCCCCCCCC	55.06	26051181
106	Phosphorylation	KKNEALPSAHGTPAS CCCCCCCCCCCCCCC	33.47	29496963
110	Phosphorylation	ALPSAHGTPASASAL CCCCCCCCCCCCCCC	13.05	29496963
113	Phosphorylation	SAHGTPASASALPEP CCCCCCCCCCCCCCC	24.78	27732954
115	Phosphorylation	HGTPASASALPEPKV CCCCCCCCCCCCCCE	28.04	27732954
127	Phosphorylation	PKVRIVEYSPPSAPR CCEEEEEECCCCCCC	18.64	28102081
128	Phosphorylation	KVRIVEYSPPSAPRR CEEEEEECCCCCCCC	19.48	29255136
131	Phosphorylation	IVEYSPPSAPRRPPV EEEECCCCCCCCCCC	55.05	25159151
277	Acetylation	DCVLCPNKGGAFKKT CEEECCCCCCCCCCC	43.81	26822725
324	Acetylation	NIPPARWKLTCYLCK CCCHHHHEEEEHHHC	28.50	23749302
328	Phosphorylation	ARWKLTCYLCKQKGV HHHEEEEHHHCCCCC	15.20	-
331	Acetylation	KLTCYLCKQKGVGAC EEEEHHHCCCCCCEE	53.07	23749302
333	Acetylation	TCYLCKQKGVGACIQ EEHHHCCCCCCEEEE	40.85	26051181
343	Acetylation	GACIQCHKANCYTAF CEEEEECCCCCEEEE	49.25	25953088
357	Acetylation	FHVTCAQKAGLYMKM EEHHHHHHCCEEEEE	26.37	25953088
361	Phosphorylation	CAQKAGLYMKMEPVK HHHHCCEEEEEEEEE	8.18	29759185
363	Acetylation	QKAGLYMKMEPVKEL HHCCEEEEEEEEEEC	26.93	25953088
368	Ubiquitination	YMKMEPVKELTGGGT EEEEEEEEECCCCCC	58.69	21890473
368	Acetylation	YMKMEPVKELTGGGT EEEEEEEEECCCCCC	58.69	19608861
368	Ubiquitination	YMKMEPVKELTGGGT EEEEEEEEECCCCCC	58.69	21890473
368 (in isoform 2)	Ubiquitination	-	58.69	-
407	Acetylation	IYGDVEMKNGVCRKE EECCEEEECCEECCC	36.72	23749302
413	Acetylation	MKNGVCRKESSVKTV EECCEECCCCCCCHH	57.74	23749302
415	Phosphorylation	NGVCRKESSVKTVRS CCEECCCCCCCHHHC	43.39	-
416	Phosphorylation	GVCRKESSVKTVRST CEECCCCCCCHHHCH	28.82	-
418	Acetylation	CRKESSVKTVRSTSK ECCCCCCCHHHCHHH	43.16	23749302
422	O-linked_Glycosylation	SSVKTVRSTSKVRKK CCCCHHHCHHHHHHH	32.47	30379171
422	Phosphorylation	SSVKTVRSTSKVRKK CCCCHHHCHHHHHHH	32.47	-
446	Phosphorylation	EPCAVLPTVCAPYIP CCCCCCCCCCCCCCC	24.85	-
451	Phosphorylation	LPTVCAPYIPPQRLN CCCCCCCCCCHHHHH	13.92	-
486	Phosphorylation	YWLLKRLSRNGAPLL HHHHHHHHHCCHHHH	27.94	26029660
498	Phosphorylation	PLLRRLQSSLQSQRS HHHHHHHHHHHHHHH	37.29	25884760
499	Phosphorylation	LLRRLQSSLQSQRSS HHHHHHHHHHHHHHH	19.91	30266825
502	Phosphorylation	RLQSSLQSQRSSQQR HHHHHHHHHHHHHHH	32.62	30266825
516	Acetylation	RENDEEMKAAKEKLK HHCHHHHHHHHHHHH	48.77	19608861
519	Acetylation	DEEMKAAKEKLKYWQ HHHHHHHHHHHHHHH	61.31	19608861
521	Acetylation	EMKAAKEKLKYWQRL HHHHHHHHHHHHHHH	49.96	26051181
523	Acetylation	KAAKEKLKYWQRLRH HHHHHHHHHHHHHHH	56.35	19608861
523	Ubiquitination	KAAKEKLKYWQRLRH HHHHHHHHHHHHHHH	56.35	-
523 (in isoform 2)	Ubiquitination	-	56.35	-
554	Acetylation	KLKREQVKVEQVAME HHHHHHCCHHHHHHH	39.48	23749302
554	Sumoylation	KLKREQVKVEQVAME HHHHHHCCHHHHHHH	39.48	28112733
554	Ubiquitination	KLKREQVKVEQVAME HHHHHHCCHHHHHHH	39.48	-
581	Acetylation	VLDQLQDKDPARIFA HHHHHCCCCHHHHHC	53.29	26051181
594	Acetylation	FAQPVSLKEVPDYLD HCCCCCHHHCCHHHH	49.51	26051181
594	Sumoylation	FAQPVSLKEVPDYLD HCCCCCHHHCCHHHH	49.51	28112733
594	Ubiquitination	FAQPVSLKEVPDYLD HCCCCCHHHCCHHHH	49.51	-
604	Acetylation	PDYLDHIKHPMDFAT CHHHHHCCCCCCHHH	37.93	25953088
614	Acetylation	MDFATMRKRLEAQGY CCHHHHHHHHHHCCC	50.98	19813111
622	Acetylation	RLEAQGYKNLHEFEE HHHHCCCCCHHHHHH	60.91	19813121
641	Phosphorylation	IIDNCMKYNARDTVF HHHCHHHCCCCCCEE	6.28	26074081
732	Acetylation	LDLTCAMKSSGSRSK HHHHHHHHCCCCHHH	23.97	25953088
754	Acetylation	EIALLRNKLSQQHSQ HHHHHHHHHHHHCCC	42.98	25953088
754	Ubiquitination	EIALLRNKLSQQHSQ HHHHHHHHHHHHCCC	42.98	-
756	Phosphorylation	ALLRNKLSQQHSQPL HHHHHHHHHHCCCCC	29.42	26714015
756 (in isoform 2)	Phosphorylation	-	29.42	22210691
760	Phosphorylation	NKLSQQHSQPLPTGP HHHHHHCCCCCCCCC	29.20	26714015
760 (in isoform 2)	Phosphorylation	-	29.20	22210691
790 (in isoform 2)	Phosphorylation	-	40.78	29507054
793	Phosphorylation	EVLPRLETLLQPRKR HHHHHHHHHHCCCCC	37.04	26074081
801	Phosphorylation	LLQPRKRSRSTCGDS HHCCCCCCCCCCCCC	33.35	23401153
803	Phosphorylation	QPRKRSRSTCGDSEV CCCCCCCCCCCCCCC	29.33	23401153
804	Phosphorylation	PRKRSRSTCGDSEVE CCCCCCCCCCCCCCC	21.28	23927012
808	Phosphorylation	SRSTCGDSEVEEESP CCCCCCCCCCCCCCC	28.91	20164059
814	Phosphorylation	DSEVEEESPGKRLDA CCCCCCCCCCCCCCC	42.08	23927012
817	Acetylation	VEEESPGKRLDAGLT CCCCCCCCCCCCCCC	53.85	25953088
832	Phosphorylation	NGFGGARSEQEPGGG CCCCCCCCCCCCCCC	43.00	-
837 (in isoform 2)	Phosphorylation	-	41.89	22210691
839 (in isoform 2)	Phosphorylation	-	30.76	22210691
845	Phosphorylation	GGLGRKATPRRRCAS CCCCCCCCCCCCCCC	21.99	27282143
852	Phosphorylation	TPRRRCASESSISSS CCCCCCCCCCCCCCC	41.45	27273156
854	Phosphorylation	RRRCASESSISSSNS CCCCCCCCCCCCCCC	30.40	27273156
855	Phosphorylation	RRCASESSISSSNSP CCCCCCCCCCCCCCC	23.57	27273156
857	Phosphorylation	CASESSISSSNSPLC CCCCCCCCCCCCCCC	29.66	28102081
858	Phosphorylation	ASESSISSSNSPLCD CCCCCCCCCCCCCCC	31.69	28102081
859	Phosphorylation	SESSISSSNSPLCDS CCCCCCCCCCCCCCC	34.24	27273156
861	Phosphorylation	SSISSSNSPLCDSSF CCCCCCCCCCCCCCC	22.61	23403867
866	Phosphorylation	SNSPLCDSSFNAPKC CCCCCCCCCCCCCCC	35.51	23403867
867	Phosphorylation	NSPLCDSSFNAPKCG CCCCCCCCCCCCCCC	14.85	23403867
875 (in isoform 2)	Phosphorylation	-	60.47	22210691
877	Acetylation	APKCGRGKPALVRRH CCCCCCCCCCHHCCC	26.25	23749302
881 (in isoform 2)	Phosphorylation	-	5.70	20860994
882 (in isoform 2)	Phosphorylation	-	26.05	25159151
885	Phosphorylation	PALVRRHTLEDRSEL CCHHCCCCCCCHHHH	29.99	27273156
888 (in isoform 2)	Phosphorylation	-	63.62	30177828
890	Phosphorylation	RHTLEDRSELISCIE CCCCCCHHHHHHHHH	49.42	29214152
890 (in isoform 2)	Phosphorylation	-	49.42	30177828
892 (in isoform 2)	Phosphorylation	-	3.54	30177828
894	Phosphorylation	EDRSELISCIENGNY CCHHHHHHHHHCCCH	22.97	23882029
900 (in isoform 2)	Phosphorylation	-	45.21	28111955
902 (in isoform 2)	Phosphorylation	-	10.06	30266825
903	Acetylation	IENGNYAKAARIAAE HHCCCHHHHHHHHHH	32.02	19608861
905 (in isoform 2)	Phosphorylation	-	11.60	30266825
906 (in isoform 2)	Phosphorylation	-	24.76	30266825
911 (in isoform 2)	Phosphorylation	-	7.88	27987026
915	Phosphorylation	AAEVGQSSMWISTDA HHHHCCCCEEECCHH	15.39	23532336
920	Phosphorylation	QSSMWISTDAAASVL CCCEEECCHHHHHHH	22.11	23532336
932 (in isoform 2)	Phosphorylation	-	5.98	25159151
936	Acetylation	PLKVVWAKCSGYPSY CHHHHEEECCCCCCC	17.14	25953088
951	Acetylation	PALIIDPKMPRVPGH CEEEECCCCCCCCCC	58.76	26051181
981	Acetylation	IGEHMQTKSDEKLFL ECCCCCCCCCCCEEE	38.73	23749302
995	Acetylation	LVLFFDNKRSWQWLP EEEEECCCCCEEECC	50.05	11925801
1003	Acetylation	RSWQWLPKSKMVPLG CCEEECCHHCCEECC	61.61	26051181
1005	Acetylation	WQWLPKSKMVPLGID EEECCHHCCEECCCC	50.47	25953088
1016 (in isoform 2)	Phosphorylation	-	58.62	-
1017	Ubiquitination	GIDETIDKLKMMEGR CCCHHHHHHHHHCCC	46.27	-
1026	Phosphorylation	KMMEGRNSSIRKAVR HHHCCCCHHHHHHHH	26.28	21406692
1027	Phosphorylation	MMEGRNSSIRKAVRI HHCCCCHHHHHHHHH	29.93	21406692
1051	Phosphorylation	SRVHGEPTSDLSDID HHHCCCCCCCCCCCC	30.48	22167270
1052	Phosphorylation	RVHGEPTSDLSDID- HHCCCCCCCCCCCC-	47.47	22167270
1055	Phosphorylation	GEPTSDLSDID---- CCCCCCCCCCC----	37.19	22167270
1126 (in isoform 2)	Acetylation	-		-

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 BRD1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BRD1_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 BRD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VIME_HUMAN	VIM	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
CREST_HUMAN	SS18L1	physical	20211142
H33_HUMAN	H3F3A	physical	21880731
H32_HUMAN	HIST2H3C	physical	21720545
ZC3HF_HUMAN	ZC3H15	physical	27142060
DRG1_HUMAN	DRG1	physical	27142060
C1QBP_HUMAN	C1QBP	physical	27142060
KAT7_HUMAN	KAT7	physical	27142060
KMT5B_HUMAN	SUV420H1	physical	27142060
EAF6_HUMAN	MEAF6	physical	27142060
1433E_HUMAN	YWHAE	physical	27142060
PB1_HUMAN	PBRM1	physical	27142060
ING4_HUMAN	ING4	physical	27142060
ING5_HUMAN	ING5	physical	27142060
NPM_HUMAN	NPM1	physical	27142060
1433Z_HUMAN	YWHAZ	physical	27142060
IMA5_HUMAN	KPNA1	physical	27142060
IMA1_HUMAN	KPNA2	physical	27142060
CHD3_HUMAN	CHD3	physical	27142060
CHD4_HUMAN	CHD4	physical	27142060
CHD5_HUMAN	CHD5	physical	27142060
1433B_HUMAN	YWHAB	physical	27142060
NP1L4_HUMAN	NAP1L4	physical	27142060
CLH1_HUMAN	CLTC	physical	27142060
DNMT1_HUMAN	DNMT1	physical	27142060
LYAR_HUMAN	LYAR	physical	27142060
RT14_HUMAN	MRPS14	physical	27142060
EIF3I_HUMAN	EIF3I	physical	27142060
PHB2_HUMAN	PHB2	physical	27142060
NSUN2_HUMAN	NSUN2	physical	27142060
1433G_HUMAN	YWHAG	physical	27142060
RT34_HUMAN	MRPS34	physical	27142060
QSER1_HUMAN	QSER1	physical	27142060
H33_HUMAN	H3F3A	physical	27142060
H31_HUMAN	HIST1H3A	physical	27142060
H31T_HUMAN	HIST3H3	physical	27142060
1433F_HUMAN	YWHAH	physical	27142060
RL22L_HUMAN	RPL22L1	physical	27142060

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BRD1_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-368; LYS-418; LYS-516;LYS-519; LYS-523 AND LYS-903, AND MASS SPECTROMETRY.	19608861 [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-128 AND SER-1055, ANDMASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; THR-1051 ANDSER-1055, 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-1052 AND SER-1055, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.	19007248 [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-25, AND MASSSPECTROMETRY.	17081983 [Abstract]