BRE1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BRE1A_MOUSE
• UniProt AC: Q5DTM8
• Protein Name: E3 ubiquitin-protein ligase BRE1A
• Gene Name: Rnf20
• Organism: Mus musculus (Mouse).
• Sequence Length: 973
• 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. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of PA2G4 leading to its proteasome-mediated degradation..
• Protein Sequence: MSGIGNKRAAGEPGTSMPPEKKTAVEDSGTTVETIKLGGVSSTEELDIRTLQSKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLDQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGDGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVDLLSRKLNSGDNLIVEEAVQELNSFLAQENVRLQELTDLLQEKHHTMSQEFCKLQGKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRHCELEKLRQDFEEVTTQNEKLKVELRSAVEEVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTHQRQVELIERDEVSLHKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPTELKQDSEDLATHSSALKASQEDEVKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSVKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDLFNFKRAQEDISRLRRKLETTKKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG

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
15	Phosphorylation	RAAGEPGTSMPPEKK CCCCCCCCCCCCCCC	32.35	28576409
21	Ubiquitination	GTSMPPEKKTAVEDS CCCCCCCCCCCCCCC	62.29	-
21	Acetylation	GTSMPPEKKTAVEDS CCCCCCCCCCCCCCC	62.29	-
41	Phosphorylation	TIKLGGVSSTEELDI EEEECCCCCCCHHHH	34.51	28066266
42	Phosphorylation	IKLGGVSSTEELDIR EEECCCCCCCHHHHH	37.11	26239621
43	Phosphorylation	KLGGVSSTEELDIRT EECCCCCCCHHHHHH	26.44	26239621
50	Phosphorylation	TEELDIRTLQSKNRK CCHHHHHHHHHHHHH	29.50	26239621
136	Phosphorylation	VPEPEPDSDSNQERK CCCCCCCCCCCCCCC	54.37	27087446
138	Phosphorylation	EPEPDSDSNQERKDD CCCCCCCCCCCCCCH	44.35	27087446
245	Phosphorylation	LLQEKHHTMSQEFCK HHHHHHHHHCHHHHH	20.45	-
247	Phosphorylation	QEKHHTMSQEFCKLQ HHHHHHHCHHHHHHH	27.93	-
348	Acetylation	NRHCELEKLRQDFEE HCCHHHHHHHHHHHH	62.69	-
510	Acetylation	EAQSDLNKTRLRSGS HHHHHHCHHHHHHHH	42.17	-
515	Phosphorylation	LNKTRLRSGSALLQS HCHHHHHHHHHHHHC	41.51	26160508
517	Phosphorylation	KTRLRSGSALLQSQS HHHHHHHHHHHHCCC	19.59	30372032
522	Phosphorylation	SGSALLQSQSSTEDP HHHHHHHCCCCCCCC	31.81	22942356
524	Phosphorylation	SALLQSQSSTEDPKD HHHHHCCCCCCCCCC	44.46	25521595
525	Phosphorylation	ALLQSQSSTEDPKDE HHHHCCCCCCCCCCC	28.33	25521595
526	Phosphorylation	LLQSQSSTEDPKDEP HHHCCCCCCCCCCCC	50.05	22942356
534	Phosphorylation	EDPKDEPTELKQDSE CCCCCCCCCHHHCHH	52.48	23737553
540	Phosphorylation	PTELKQDSEDLATHS CCCHHHCHHHHHHHH	30.43	21659605
545	Phosphorylation	QDSEDLATHSSALKA HCHHHHHHHHHHHHH	29.59	25777480
547	Phosphorylation	SEDLATHSSALKASQ HHHHHHHHHHHHHHH	16.98	25777480
548	Phosphorylation	EDLATHSSALKASQE HHHHHHHHHHHHHHH	29.98	25777480
553	Phosphorylation	HSSALKASQEDEVKS HHHHHHHHHHHHHHH	32.30	27841257
560	Phosphorylation	SQEDEVKSKRDEEER HHHHHHHHHHHHHHH	37.79	-
610	Ubiquitination	DSVKDKEKGKHDDGR HHHHHHHCCCCCCCC	78.12	-
855	Ubiquitination	QLELAQKKLHDFQDE HHHHHHHHHHHCHHH	38.69	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BRE1A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BRE1A_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BRE1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AP2A_MOUSE	Tfap2a	physical	24374663
SRBP1_MOUSE	Srebf1	physical	24425205

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.
PubMed: 19367708