UIMC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UIMC1_MOUSE
• UniProt AC: Q5U5Q9
• Protein Name: BRCA1-A complex subunit RAP80
• Gene Name: Uimc1
• Organism: Mus musculus (Mouse).
• Sequence Length: 727
• Subcellular Localization: Nucleus . Localizes at sites of DNA damage at double-strand breaks (DSBs).
• Protein Description: Ubiquitin-binding protein. Specifically recognizes and binds 'Lys-63'-linked ubiquitin. [PubMed: 19536136 Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1 (By similarity]
• Protein Sequence: MPRRKKKIKEASESQNLEKKDLETSSCVSIKKKRRLEDLLIVISDSDGEETKEENGLQKTKTKQSNRSKCLAKRKVAHMSEEEQFALALKMSEQEAREVNNQEEKEEELLRKAIAESLNSCWSSAASATRSRPLAAELSSHSHQENTKDSGTTEGVWQLVPPSLCKGSHVSQGNEAEQRKEPWDHNENTEEEPVSGSSGSWDQSSQPVFENENVKCFDRCTGHLAEHTQCGKPQESTGSGYAFSKAVQGRGDTSRQCLPIPADTKGLQDTGGTVHYYWGIPFCPAGVDPNQYTNVILCQLEVYQKSLKMAQRQLVKKRGFGEPVLPRPPFLIQNECGQEDQTSDKNEGISEDMGDEAKEERQESRASVWHSETKDFQKSPIKSLKQKLLLEEEPTTSRGQSSQGLFVEETSEEGLKSSEGDNSVPTTQSIAALTSKRSLVLMPESSAEEITVCPETQLSFLEPLDLNREDSPDSRELPIEVRMAVGDKQVANREDCMKENPPPAVSSSTRVSCPLCNQDFPPTKIEQHAMYCNGLMEQETVLTRRRREAKNKSDGRTAAQPALDANRKEKCYLCKSLVPLGEYQCHVEACLQLAKVDREDGIEGTRRPRVCAPVEGKQQQRLKKSKDKGHSQGRLLSLLEQSEHRTTGVEKKPKYSEVRTFRMPSPEVEEASCSREMQSTLSQLNLNESPIKSFVPVSEATNCLVDFKEQFAFRSRTKSGRGRRRKS

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
29	Phosphorylation	LETSSCVSIKKKRRL CCCCCCEEHHHHCCH	32.77	-
31	Ubiquitination	TSSCVSIKKKRRLED CCCCEEHHHHCCHHH	44.74	-
44	Phosphorylation	EDLLIVISDSDGEET HHEEEEEECCCCCHH	21.84	22817900
46	Phosphorylation	LLIVISDSDGEETKE EEEEEECCCCCHHHH	40.50	22817900
51	Phosphorylation	SDSDGEETKEENGLQ ECCCCCHHHHHHCCC	39.18	21183079
105	Ubiquitination	EVNNQEEKEEELLRK HHCCHHHHHHHHHHH	70.45	-
131	Phosphorylation	SAASATRSRPLAAEL HHHHHHCCCCHHHHH	33.62	26160508
140	Phosphorylation	PLAAELSSHSHQENT CHHHHHHHCCCCCCC	41.45	-
168	Phosphorylation	PPSLCKGSHVSQGNE CHHHCCCCCCCCCCH	13.25	28066266
171	Phosphorylation	LCKGSHVSQGNEAEQ HCCCCCCCCCCHHHH	27.26	27087446
195	Phosphorylation	NTEEEPVSGSSGSWD CCCCCCCCCCCCCCC	43.61	25338131
197	Phosphorylation	EEEPVSGSSGSWDQS CCCCCCCCCCCCCCC	24.82	25338131
205	Phosphorylation	SGSWDQSSQPVFENE CCCCCCCCCCCCCCC	32.63	17621610
221	Phosphorylation	VKCFDRCTGHLAEHT CEEHHHHCCHHHHHC	28.64	20469934
228	Phosphorylation	TGHLAEHTQCGKPQE CCHHHHHCCCCCCCC	19.63	20469934
350	Phosphorylation	SDKNEGISEDMGDEA CCCCCCCCCCCCHHH	38.10	27841257
379	Phosphorylation	ETKDFQKSPIKSLKQ CCCCHHHCCCHHHHH	22.52	26824392
395	Phosphorylation	LLLEEEPTTSRGQSS HHCCCCCCCCCCCCC	40.46	26745281
396	Phosphorylation	LLEEEPTTSRGQSSQ HCCCCCCCCCCCCCC	27.43	26745281
397	Phosphorylation	LEEEPTTSRGQSSQG CCCCCCCCCCCCCCC	36.57	26745281
401	Phosphorylation	PTTSRGQSSQGLFVE CCCCCCCCCCCEEEE	27.70	28833060
402	Phosphorylation	TTSRGQSSQGLFVEE CCCCCCCCCCEEEEE	22.00	28833060
410	Phosphorylation	QGLFVEETSEEGLKS CCEEEEECCHHCCCC	28.12	28833060
411	Phosphorylation	GLFVEETSEEGLKSS CEEEEECCHHCCCCC	36.61	28833060
417	Phosphorylation	TSEEGLKSSEGDNSV CCHHCCCCCCCCCCC	38.37	26643407
418	Phosphorylation	SEEGLKSSEGDNSVP CHHCCCCCCCCCCCC	43.97	26643407
423	Phosphorylation	KSSEGDNSVPTTQSI CCCCCCCCCCHHHHH	33.93	25266776
426	Phosphorylation	EGDNSVPTTQSIAAL CCCCCCCHHHHHHHH	35.00	26643407
427	Phosphorylation	GDNSVPTTQSIAALT CCCCCCHHHHHHHHH	17.78	26643407
459	Phosphorylation	VCPETQLSFLEPLDL ECCCHHCHHCCCCCC	20.26	21149613
471	Phosphorylation	LDLNREDSPDSRELP CCCCCCCCCCCCCCC	26.34	21149613
474	Phosphorylation	NREDSPDSRELPIEV CCCCCCCCCCCCCEE	30.91	21149613
498	Ubiquitination	ANREDCMKENPPPAV CCHHHHHHHCCCCCC	61.75	-
637	Phosphorylation	HSQGRLLSLLEQSEH CCHHHHHHHHHHCCC	35.18	21183079
655	Phosphorylation	GVEKKPKYSEVRTFR CCCCCCCCCCCEEEE	20.70	25619855
656	Phosphorylation	VEKKPKYSEVRTFRM CCCCCCCCCCEEEEC	35.42	25619855
660	Phosphorylation	PKYSEVRTFRMPSPE CCCCCCEEEECCCHH	22.29	23984901
665	Phosphorylation	VRTFRMPSPEVEEAS CEEEECCCHHHHHHH	25.09	25521595
672	Phosphorylation	SPEVEEASCSREMQS CHHHHHHHCCHHHHH	18.86	25619855
674	Phosphorylation	EVEEASCSREMQSTL HHHHHHCCHHHHHHH	28.87	25619855
679	Phosphorylation	SCSREMQSTLSQLNL HCCHHHHHHHHHHCC	29.97	28066266
680	Phosphorylation	CSREMQSTLSQLNLN CCHHHHHHHHHHCCC	17.34	28066266
682	Phosphorylation	REMQSTLSQLNLNES HHHHHHHHHHCCCCC	32.48	25619855
689	Phosphorylation	SQLNLNESPIKSFVP HHHCCCCCCCCCCCC	30.74	26824392
693	Phosphorylation	LNESPIKSFVPVSEA CCCCCCCCCCCHHHH	32.00	25777480
698	Phosphorylation	IKSFVPVSEATNCLV CCCCCCHHHHHCCEE	18.55	25777480
701	Phosphorylation	FVPVSEATNCLVDFK CCCHHHHHCCEECHH	23.55	25777480

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
205	S	Phosphorylation	Kinase	ATM	Q13315	PSP
402	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UIMC1_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 UIMC1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC9_MOUSE	Ube2i	physical	17698038

Drug and Disease Associations

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