dbPTM

BRE1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRE1B_HUMAN
UniProt AC	O75150
Protein Name	E3 ubiquitin-protein ligase BRE1B
Gene Name	RNF40
Organism	Homo sapiens (Human).
Sequence Length	1001
Subcellular Localization	Nucleus .
Protein Description	Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes..
Protein Sequence	MSGPGNKRAAGDGGSGPPEKKLSREEKTTTTLIEPIRLGGISSTEEMDLKVLQFKNKKLAERLEQRQACEDELRERIEKLEKRQATDDATLLIVNRYWAQLDETVEALLRCHESQGELSSAPEAPGTQEGPTCDGTPLPEPGTSELRDPLLMQLRPPLSEPALAFVVALGASSSEEVELELQGRMEFSKAAVSRVVEASDRLQRRVEELCQRVYSRGDSEPLSEAAQAHTRELGRENRRLQDLATQLQEKHHRISLEYSELQDKVTSAETKVLEMETTVEDLQWDIEKLRKREQKLNKHLAEALEQLNSGYYVSGSSSGFQGGQITLSMQKFEMLNAELEENQELANSRMAELEKLQAELQGAVRTNERLKVALRSLPEEVVRETGEYRMLQAQFSLLYNESLQVKTQLDEARGLLLATKNSHLRHIEHMESDELGLQKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQNLAANEQAGPINREMRHLISSLQNHNHQLKGDAQRYKRKLREVQAEIGKLRAQASGSAHSTPNLGHPEDSGVSAPAPGKEEGGPGPVSTPDNRKEMAPVPGTTTTTTSVKKEELVPSEEDFQGITPGAQGPSSRGREPEARPKRELQEREGPSLGPPPVASALSRADREKAKVEETKRKESELLKGLRAELKKAQESQKEMKLLLDMYKSAPKEQRDKVQLMAAERKAKAEVDELRSRIRELEERDRRESKKIADEDALRRIRQAEEQIEHLQRKLGATKQEEEALLSEMDVTGQAFEDMQEQNGRLLQQLREKDDANFKLMSERIKANQIHKLLREEKDELGEQVLGLKSQVDAQLLTVQKLEEKERALQGSLGGVEKELTLRSQALELNKRKAVEAAQLAEDLKVQLEHVQTRLREIQPCLAESRAAREKESFNLKRAQEDISRLRRKLEKQRKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVRGRYEARQRKCPKCNAAFGAHDFHRIYIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MSGPGNKRAAGDGG -CCCCCCCCCCCCCC	49.70	-
20	Acetylation	GGSGPPEKKLSREEK CCCCCCHHHCCCCCC	65.86	23954790
21	Acetylation	GSGPPEKKLSREEKT CCCCCHHHCCCCCCC	50.46	7693009
27	Ubiquitination	KKLSREEKTTTTLIE HHCCCCCCCCCEEEE	46.55	-
28	Phosphorylation	KLSREEKTTTTLIEP HCCCCCCCCCEEEEC	32.43	21406692
29	Phosphorylation	LSREEKTTTTLIEPI CCCCCCCCCEEEECE	28.93	21406692
30	Phosphorylation	SREEKTTTTLIEPIR CCCCCCCCEEEECEE	25.49	21406692
31	Phosphorylation	REEKTTTTLIEPIRL CCCCCCCEEEECEEC	24.52	21406692
42	Phosphorylation	PIRLGGISSTEEMDL CEECCCCCCCHHHHH	34.19	-
50	Ubiquitination	STEEMDLKVLQFKNK CCHHHHHHHHHHCCH	36.31	-
55	Ubiquitination	DLKVLQFKNKKLAER HHHHHHHCCHHHHHH	55.70	-
114	Phosphorylation	ALLRCHESQGELSSA HHHHHHHHCCCCCCC	21.59	21362549
127	Phosphorylation	SAPEAPGTQEGPTCD CCCCCCCCCCCCCCC	23.53	18077418
189	Ubiquitination	QGRMEFSKAAVSRVV ECCHHHHHHHHHHHH	45.76	-
193	Phosphorylation	EFSKAAVSRVVEASD HHHHHHHHHHHHHHH	18.03	23401153
201	Methylation	RVVEASDRLQRRVEE HHHHHHHHHHHHHHH	30.17	115491431
219	Phosphorylation	RVYSRGDSEPLSEAA HHHHCCCCCHHHHHH	43.89	29214152
250	2-Hydroxyisobutyrylation	LATQLQEKHHRISLE HHHHHHHHHHHHCCC	31.58	-
250	Acetylation	LATQLQEKHHRISLE HHHHHHHHHHHHCCC	31.58	21466224
255	Phosphorylation	QEKHHRISLEYSELQ HHHHHHHCCCHHHHH	18.33	28555341
264	Ubiquitination	EYSELQDKVTSAETK CHHHHHHHHHHCHHH	34.16	-
277	Phosphorylation	TKVLEMETTVEDLQW HHHEEEECCHHHHHH	34.53	27794612
278	Phosphorylation	KVLEMETTVEDLQWD HHEEEECCHHHHHHH	14.48	27794612
314 (in isoform 4)	Phosphorylation	-	19.48	22210691
316 (in isoform 4)	Phosphorylation	-	17.52	22210691
318 (in isoform 4)	Phosphorylation	-	45.37	22210691
334	Sulfoxidation	LSMQKFEMLNAELEE EEHHHHHHHHHHHHH	3.83	21406390
355	Acetylation	SRMAELEKLQAELQG HHHHHHHHHHHHHHH	59.53	-
355	Ubiquitination	SRMAELEKLQAELQG HHHHHHHHHHHHHHH	59.53	-
385	O-linked_Glycosylation	PEEVVRETGEYRMLQ CHHHHHHHHCHHHHH	25.42	30379171
420	Ubiquitination	RGLLLATKNSHLRHI HHHHHHHCCHHHHHH	51.34	-
439	Ubiquitination	SDELGLQKKLRTEVI CCCHHHHHHHHHHHH	59.84	-
451	Phosphorylation	EVIQLEDTLAQVRKE HHHHHHHHHHHHHHH	18.02	-
457	Ubiquitination	DTLAQVRKEYEMLRI HHHHHHHHHHHHHHH	66.83	-
498	Acetylation	QNHNHQLKGDAQRYK HHCCCCCHHHHHHHH	48.45	26051181
498	Ubiquitination	QNHNHQLKGDAQRYK HHCCCCCHHHHHHHH	48.45	-
517	Ubiquitination	EVQAEIGKLRAQASG HHHHHHHHHHHHHCC	40.22	-
517	Acetylation	EVQAEIGKLRAQASG HHHHHHHHHHHHHCC	40.22	23954790
523	Phosphorylation	GKLRAQASGSAHSTP HHHHHHHCCCCCCCC	22.62	25159151
525	Phosphorylation	LRAQASGSAHSTPNL HHHHHCCCCCCCCCC	21.95	27050516
528	Phosphorylation	QASGSAHSTPNLGHP HHCCCCCCCCCCCCC	45.32	25159151
529	Phosphorylation	ASGSAHSTPNLGHPE HCCCCCCCCCCCCCC	13.31	25159151
538	Phosphorylation	NLGHPEDSGVSAPAP CCCCCCCCCCCCCCC	39.16	29978859
541	Phosphorylation	HPEDSGVSAPAPGKE CCCCCCCCCCCCCCC	31.87	29978859
556	Phosphorylation	EGGPGPVSTPDNRKE CCCCCCCCCCCCCCC	37.04	25159151
557	Phosphorylation	GGPGPVSTPDNRKEM CCCCCCCCCCCCCCC	34.59	25159151
562	Acetylation	VSTPDNRKEMAPVPG CCCCCCCCCCCCCCC	59.08	11920825
564	Sulfoxidation	TPDNRKEMAPVPGTT CCCCCCCCCCCCCCC	5.99	21406390
570	Phosphorylation	EMAPVPGTTTTTTSV CCCCCCCCCCCCCCE	18.20	23401153
571	Phosphorylation	MAPVPGTTTTTTSVK CCCCCCCCCCCCCEE	28.23	25159151
572	Phosphorylation	APVPGTTTTTTSVKK CCCCCCCCCCCCEEH	23.22	29396449
573	Phosphorylation	PVPGTTTTTTSVKKE CCCCCCCCCCCEEHH	26.45	23401153
574	Phosphorylation	VPGTTTTTTSVKKEE CCCCCCCCCCEEHHH	18.25	23401153
575	Phosphorylation	PGTTTTTTSVKKEEL CCCCCCCCCEEHHHC	29.45	23401153
576	Phosphorylation	GTTTTTTSVKKEELV CCCCCCCCEEHHHCC	29.82	23401153
578	Sumoylation	TTTTTSVKKEELVPS CCCCCCEEHHHCCCC	54.99	28112733
578	Sumoylation	TTTTTSVKKEELVPS CCCCCCEEHHHCCCC	54.99	-
579	Sumoylation	TTTTSVKKEELVPSE CCCCCEEHHHCCCCH	55.02	28112733
585	Phosphorylation	KKEELVPSEEDFQGI EHHHCCCCHHHCCCC	46.25	28985074
593	Phosphorylation	EEDFQGITPGAQGPS HHHCCCCCCCCCCCC	23.61	21815630
600	Phosphorylation	TPGAQGPSSRGREPE CCCCCCCCCCCCCCC	39.22	25159151
601	Phosphorylation	PGAQGPSSRGREPEA CCCCCCCCCCCCCCC	41.72	25159151
621	Phosphorylation	LQEREGPSLGPPPVA HHHCCCCCCCCCCHH	57.74	28555341
629	Phosphorylation	LGPPPVASALSRADR CCCCCHHHHHHHHHH	29.94	28555341
644	Phosphorylation	EKAKVEETKRKESEL HHHHHHHHHHHHHHH	23.73	20068231
653	Acetylation	RKESELLKGLRAELK HHHHHHHHHHHHHHH	69.40	25953088
653	Ubiquitination	RKESELLKGLRAELK HHHHHHHHHHHHHHH	69.40	-
676	Phosphorylation	MKLLLDMYKSAPKEQ HHHHHHHHHHCCHHH	11.06	29083192
677	2-Hydroxyisobutyrylation	KLLLDMYKSAPKEQR HHHHHHHHHCCHHHH	33.24	-
678	Phosphorylation	LLLDMYKSAPKEQRD HHHHHHHHCCHHHHH	32.11	29083192
686	Acetylation	APKEQRDKVQLMAAE CCHHHHHHHHHHHHH	33.79	25953088
688 (in isoform 4)	Ubiquitination	-	31.12	21890473
690	Sulfoxidation	QRDKVQLMAAERKAK HHHHHHHHHHHHHHH	1.53	21406390
697	Acetylation	MAAERKAKAEVDELR HHHHHHHHHHHHHHH	48.38	25953088
743	Ubiquitination	QIEHLQRKLGATKQE HHHHHHHHHCCCHHH	38.01	-
788	Ubiquitination	EKDDANFKLMSERIK HCCCCCHHHHHHHHH	42.99	-
788 (in isoform 3)	Ubiquitination	-	42.99	21890473
788 (in isoform 1)	Ubiquitination	-	42.99	21890473
795	Methylation	KLMSERIKANQIHKL HHHHHHHHHHHHHHH	47.72	-
795	Ubiquitination	KLMSERIKANQIHKL HHHHHHHHHHHHHHH	47.72	-
801	Ubiquitination	IKANQIHKLLREEKD HHHHHHHHHHHHHHH	51.34	-
807	Acetylation	HKLLREEKDELGEQV HHHHHHHHHHHHHHH	52.31	25953088
818	Ubiquitination	GEQVLGLKSQVDAQL HHHHHCCHHHHHHHH	36.72	-
819	Phosphorylation	EQVLGLKSQVDAQLL HHHHCCHHHHHHHHH	40.24	17478428
827	Phosphorylation	QVDAQLLTVQKLEEK HHHHHHHHHHHHHHH	29.50	20860994
830	Ubiquitination	AQLLTVQKLEEKERA HHHHHHHHHHHHHHH	54.23	-
847	Ubiquitination	GSLGGVEKELTLRSQ CCCCCHHHHHHHHHH	56.47	-
853	Phosphorylation	EKELTLRSQALELNK HHHHHHHHHHHHHHH	23.94	17478428
862	2-Hydroxyisobutyrylation	ALELNKRKAVEAAQL HHHHHHHHHHHHHHH	59.39	-
874	Ubiquitination	AQLAEDLKVQLEHVQ HHHHHHHHHHHHHHH	40.01	-
906	Methylation	EKESFNLKRAQEDIS HHHHHCHHHHHHHHH	46.95	115976811
985	Acetylation	ARQRKCPKCNAAFGA HHHCCCCCCCCCCCC	49.98	26051181

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
114	S	Phosphorylation	Kinase	ATM	Q13315	PSP
819	S	Phosphorylation	Kinase	ATM	Q13315	PSP
853	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BRE1B_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 BRE1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI51_HUMAN	TRIM51	physical	16189514
ZN451_HUMAN	ZNF451	physical	16189514
STX1A_HUMAN	STX1A	physical	12121982
UB2L6_HUMAN	UBE2L6	physical	12121982
BRE1A_HUMAN	RNF20	physical	22155569
ANDR_HUMAN	AR	physical	22155569
CDC73_HUMAN	CDC73	physical	22021426
BRE1A_HUMAN	RNF20	physical	21362549
ATM_HUMAN	ATM	physical	21362549
H2B2E_HUMAN	HIST2H2BE	physical	16307923
RB_HUMAN	RB1	physical	10944455
BRE1B_HUMAN	RNF40	physical	10944455
UB2E1_HUMAN	UBE2E1	physical	16307923
H2B2E_HUMAN	HIST2H2BE	physical	24837678
UBE2A_HUMAN	UBE2A	physical	24837678
MSL1_HUMAN	MSL1	physical	24837678
MSL2_HUMAN	MSL2	physical	24837678
PAF1_HUMAN	PAF1	physical	24837678
CDK9_HUMAN	CDK9	physical	24837678
UBE2A_HUMAN	UBE2A	physical	19410543
UBE2B_HUMAN	UBE2B	physical	19410543
BRE1B_HUMAN	RNF40	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
CC146_HUMAN	CCDC146	physical	25416956
SFR1_HUMAN	SFR1	physical	25416956
PLCG1_HUMAN	PLCG1	physical	26344197
XPP1_HUMAN	XPNPEP1	physical	26344197
SPT6H_HUMAN	SUPT6H	physical	24441044
BRE1A_HUMAN	RNF20	physical	25533843
KIF11_HUMAN	KIF11	physical	27557628
BRE1A_HUMAN	RNF20	physical	27557628
TRAIP_HUMAN	TRAIP	physical	26781088
BRE1B_HUMAN	RNF40	physical	27569044
UBE2B_HUMAN	UBE2B	physical	27569044

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 BRE1B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-644, AND MASSSPECTROMETRY.	17081983 [Abstract]