dbPTM

BRCA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRCA1_MOUSE
UniProt AC	P48754
Protein Name	Breast cancer type 1 susceptibility protein homolog
Gene Name	Brca1
Organism	Mus musculus (Mouse).
Sequence Length	1812
Subcellular Localization	Nucleus . Chromosome . Cytoplasm . Localizes at sites of DNA damage at double-strand breaks (DSBs) recruitment to DNA damage sites is mediated by the BRCA1-A complex. Translocated to the cytoplasm during UV-induced apoptosis.
Protein Description	E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (By similarity). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation..
Protein Sequence	MDLSAVQIQEVQNVLHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSTRFSQLAEELLRIMAAFELDTGMQLTNGFSFSKKRNNSCERLNEEASIIQSVGYRNRVRRLPQVEPGNATLKDSLGVQLSNLGIVRSVKKNRQTQPRKKSVYIELDSDSSEETVTKPGDCSVRDQELLQTAPQEAGDEGKLHSAEEAACEFSEGIRNIEHHQCSDDLNPTENHATERHPEKCQSISISNVCVEPCGTDAHASSLQPETSSLLLIEDRMNAEKAEFCNKSKQPGIAVSQQSRWAASKGTCNDRQVPSTGEKVGPNADSLSDREKWTHPQSLCPENSGATTDVPWITLNSSVQKVNEWFSRTGEMLTSDSASARRHESNAEAAVVLEVSNEVDGGFSSSRKTDLVTPDPHHTLMCKSGRDFSKPVEDNISDKIFGKSYQRKGSRPHLNHVTEIIGTFITEPQITQEQPFTNKLKRKRSTSLQPEDFIKKADSAGVQRTPDNINQGTDLMEPNEQAVSTTSNCQENKIAGSNLQKEKSAHPTESLRKEPASTAGAKSISNSVSDLEVELNVHSSKAPKKNRLRRKSSIRCALPLEPISRNPSPPTCAELQIDSCGSSEETKKNHSNQQPAGHLREPQLIEDTEPAADAKKNEPNEHIRKRRASDAFPEEKLMNKAGLLTSCSSPRKSQGPVNPSPQRTGTEQLETRQMSDSAKELGDRVLGGEPSGKTTDRSEESTSVSLVSDTDYDTQNSVSVLDAHTVRYARTGSAQCMTQFVASENPKELVHGSNNAGSGTEGLKPPLRHALNLSQEKVEMEDSELDTQYLQNTFQVSKRQSFALFSKPRSPQKDCAHSVPSKELSPKVTAKGKQKERQGQEEFEISHVQAVAATVGLPVPCQEGKLAADTMCDRGCRLCPSSHYRSGENGLSATGKSGISQNSHFKQSVSPIRSSIKTDNRKPLTEGRFERHTSSTEMAVGNENILQSTVHTVSLNNRGNACQEAGSGSIHEVCSTGDSFPGQLGRNRGPKVNTVPPLDSMQPGVCQQSVPVSDKYLEIKKQEGEAVCADFSPCLFSDHLEQSMSGKVFQVCSETPDDLLDDVEIQGHTSFGEGDIMERSAVFNGSILRRESSRSPSPVTHASKSQSLHRASRKLESSEESDSTEDEDLPCFQHLLSRISNTPELTRCSSAVTQRMPEKAEGTQAPWKGSSSDCNNEVIMIEASQEHQFSEDPRCSGSMFSSQHSAAQGSTANANSQDSNFIPPSKQRSHQCGNEEAFLSDKELISDNEEMATCLEEDNDQEEDSIIPDSEASGYESETNLSEDCSQSDILTTQQRATMKYNLIKLQQEMAHLEAVLEQRGNQPSGHSPSLLADPCALEDLPDLEPNMSGAAILTSKNINENPVSQNLKSACDDKFQLQHLEGPTSGDDESGMGRPSPFKSPLAGSRGSAHGCSRHLQKRNSPSQEELLQPAGSEASSEPHNSTGQSCLPRRELEGTPYLGSGISLFSSRDPESESPKEPAHIGTTPASTSALKIPQGQVAFRSAAAAGADKAVVGIVSKIKPELTSSEERADRDISMVVSGLTPKEVMTVQKFAEKYRLTLTDAITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVVRSIQERRLLNVHEFEVKGDVVTGRNHQGPRRSRESREKLFKGLQVYCCEPFTNMPKDELERMLQLCGASVVKELPSLTHDTGAHLVVIVQPSAWTEDSNCPDIGQLCKARLVMWDWVLDSLSSYRCRDLDAYLVQNITCDSSEPQDSND

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDLSAVQI -------CCCCHHHH	48.19	-
114	Phosphorylation	FSKKRNNSCERLNEE CCHHCCCCHHHHHHH	22.39	25266776
163	Phosphorylation	SNLGIVRSVKKNRQT HHHHHHEEHHHCCCC	27.65	27600695
183	Phosphorylation	SVYIELDSDSSEETV EEEEEECCCCCCCCC	52.60	21149613
185	Phosphorylation	YIELDSDSSEETVTK EEEECCCCCCCCCCC	43.53	21149613
186	Phosphorylation	IELDSDSSEETVTKP EEECCCCCCCCCCCC	44.43	21149613
189	Phosphorylation	DSDSSEETVTKPGDC CCCCCCCCCCCCCCC	29.44	21149613
219	Phosphorylation	GDEGKLHSAEEAACE CCCCCCCCHHHHHHH	48.05	28066266
240	Phosphorylation	NIEHHQCSDDLNPTE CCCCCCCCCCCCCCC	27.82	28418008
305	Phosphorylation	KAEFCNKSKQPGIAV HHHHCCCCCCCCCCC	22.41	-
313	Phosphorylation	KQPGIAVSQQSRWAA CCCCCCCCCCCHHHH	17.30	-
343	Phosphorylation	KVGPNADSLSDREKW CCCCCCCCCCCHHHC	27.62	28066266
345	Phosphorylation	GPNADSLSDREKWTH CCCCCCCCCHHHCCC	38.28	25266776
392	Phosphorylation	RTGEMLTSDSASARR HHCCCCCCCCHHHHH	26.13	-
454	Phosphorylation	KPVEDNISDKIFGKS CCCCCCCCHHHCCHH	38.82	25266776
502	Phosphorylation	NKLKRKRSTSLQPED HHHHHHCCCCCCHHH	25.94	27566939
503	Phosphorylation	KLKRKRSTSLQPEDF HHHHHCCCCCCHHHH	37.17	26824392
504	Phosphorylation	LKRKRSTSLQPEDFI HHHHCCCCCCHHHHH	26.67	22942356
625	Phosphorylation	EPISRNPSPPTCAEL CCCCCCCCCCCCEEE	47.24	25619855
628	Phosphorylation	SRNPSPPTCAELQID CCCCCCCCCEEEEEE	27.94	25619855
636	Phosphorylation	CAELQIDSCGSSEET CEEEEEECCCCCHHH	23.23	25619855
643	Phosphorylation	SCGSSEETKKNHSNQ CCCCCHHHHHHCCCC	43.18	25619855
686	Phosphorylation	HIRKRRASDAFPEEK HHHHHHHHHCCCHHH	27.88	26824392
702	Phosphorylation	MNKAGLLTSCSSPRK HCHHCHHCCCCCCCC	32.50	27600695
703	Phosphorylation	NKAGLLTSCSSPRKS CHHCHHCCCCCCCCC	16.39	24453211
705	Phosphorylation	AGLLTSCSSPRKSQG HCHHCCCCCCCCCCC	43.05	26824392
706	Phosphorylation	GLLTSCSSPRKSQGP CHHCCCCCCCCCCCC	32.81	26824392
710	Phosphorylation	SCSSPRKSQGPVNPS CCCCCCCCCCCCCCC	41.47	27087446
717	Phosphorylation	SQGPVNPSPQRTGTE CCCCCCCCCCCCCHH	28.58	27087446
721	Phosphorylation	VNPSPQRTGTEQLET CCCCCCCCCHHHHHH	43.11	23984901
723	Phosphorylation	PSPQRTGTEQLETRQ CCCCCCCHHHHHHHH	21.68	23984901
728	Phosphorylation	TGTEQLETRQMSDSA CCHHHHHHHHCHHHH	34.49	23984901
788	Phosphorylation	HTVRYARTGSAQCMT HHHEEEECCCHHHHH	27.58	25266776
790	Phosphorylation	VRYARTGSAQCMTQF HEEEECCCHHHHHHH	17.98	26643407
831	Phosphorylation	LRHALNLSQEKVEME HHHHHCCCHHHHCCC	34.91	17525332
858	Phosphorylation	FQVSKRQSFALFSKP HCCCCCHHEEEECCC	19.27	25266776
867	Phosphorylation	ALFSKPRSPQKDCAH EEECCCCCCCCCCCC	39.96	25266776
875	Phosphorylation	PQKDCAHSVPSKELS CCCCCCCCCCCCCCC	19.73	28066266
882	Phosphorylation	SVPSKELSPKVTAKG CCCCCCCCCCCCCCC	24.62	27149854
943	Phosphorylation	CPSSHYRSGENGLSA CCCCCCCCCCCCCCC	43.20	24719451
949	Phosphorylation	RSGENGLSATGKSGI CCCCCCCCCCCCCCC	25.78	24719451
957	Phosphorylation	ATGKSGISQNSHFKQ CCCCCCCCCCHHHCC	27.17	17525332
965	Phosphorylation	QNSHFKQSVSPIRSS CCHHHCCCCCCCHHC	25.75	29514104
967	Phosphorylation	SHFKQSVSPIRSSIK HHHCCCCCCCHHCCC	21.61	24453211
971	Phosphorylation	QSVSPIRSSIKTDNR CCCCCCHHCCCCCCC	36.82	26745281
972	Phosphorylation	SVSPIRSSIKTDNRK CCCCCHHCCCCCCCC	20.46	26745281
991	Phosphorylation	GRFERHTSSTEMAVG CCEEECCCCCEEECC	29.19	25266776
992	Phosphorylation	RFERHTSSTEMAVGN CEEECCCCCEEECCC	29.55	-
1126	Phosphorylation	DVEIQGHTSFGEGDI CCEEECCCCCCCCCH	32.35	21149613
1127	Phosphorylation	VEIQGHTSFGEGDIM CEEECCCCCCCCCHH	26.11	21149613
1137	Phosphorylation	EGDIMERSAVFNGSI CCCHHHHHEEECCHH	18.58	27566939
1143	Phosphorylation	RSAVFNGSILRRESS HHEEECCHHHCCCCC	21.39	21743459
1149	Phosphorylation	GSILRRESSRSPSPV CHHHCCCCCCCCCCC	29.28	25159016
1150	Phosphorylation	SILRRESSRSPSPVT HHHCCCCCCCCCCCC	31.83	25159016
1152	Phosphorylation	LRRESSRSPSPVTHA HCCCCCCCCCCCCHH	31.51	19996295
1154	Phosphorylation	RESSRSPSPVTHASK CCCCCCCCCCCHHHH	33.00	25159016
1157	Phosphorylation	SRSPSPVTHASKSQS CCCCCCCCHHHHHHH	18.33	29514104
1160	Phosphorylation	PSPVTHASKSQSLHR CCCCCHHHHHHHHHH	25.82	29514104
1174	Phosphorylation	RASRKLESSEESDST HHHHHHHCCCCCCCC	54.19	-
1180	Phosphorylation	ESSEESDSTEDEDLP HCCCCCCCCCCCCCH	42.87	-
1197	Phosphorylation	QHLLSRISNTPELTR HHHHHHHCCCHHHHH	33.28	26745281
1199	Phosphorylation	LLSRISNTPELTRCS HHHHHCCCHHHHHCC	16.02	26824392
1203	Phosphorylation	ISNTPELTRCSSAVT HCCCHHHHHCCHHHH	28.15	21743459
1207	Phosphorylation	PELTRCSSAVTQRMP HHHHHCCHHHHHCCC	30.31	-
1241	Phosphorylation	EVIMIEASQEHQFSE CEEEEEECCCCCCCC	24.26	-
1297	Phosphorylation	GNEEAFLSDKELISD CCHHHHHCCHHHCCC	39.93	25619855
1303	Phosphorylation	LSDKELISDNEEMAT HCCHHHCCCCHHHHH	47.19	-
1343	Phosphorylation	TNLSEDCSQSDILTT CCCCCCCCCCHHCHH	45.07	-
1350	Phosphorylation	SQSDILTTQQRATMK CCCHHCHHHHHHHHH	35.49	-
1382	Phosphorylation	EQRGNQPSGHSPSLL HHCCCCCCCCCHHHH	30.66	26643407
1385	Phosphorylation	GNQPSGHSPSLLADP CCCCCCCCHHHHCCC	21.51	26643407
1387	Phosphorylation	QPSGHSPSLLADPCA CCCCCCHHHHCCCCC	38.96	26745281
1413	Phosphorylation	SGAAILTSKNINENP CCCEEEECCCCCCCC	21.91	-
1422	Phosphorylation	NINENPVSQNLKSAC CCCCCCCCHHHHHHC	18.01	25266776
1442	Phosphorylation	LQHLEGPTSGDDESG CCCCCCCCCCCCCCC	57.08	21149613
1443	Phosphorylation	QHLEGPTSGDDESGM CCCCCCCCCCCCCCC	43.27	21149613
1448	Phosphorylation	PTSGDDESGMGRPSP CCCCCCCCCCCCCCC	40.86	28066266
1454	Phosphorylation	ESGMGRPSPFKSPLA CCCCCCCCCCCCCCC	41.42	21149613
1458	Phosphorylation	GRPSPFKSPLAGSRG CCCCCCCCCCCCCCC	26.06	-
1479	Phosphorylation	RHLQKRNSPSQEELL HHHHHCCCCCHHHHH	29.93	25619855
1481	Phosphorylation	LQKRNSPSQEELLQP HHHCCCCCHHHHHCC	50.47	25619855
1491	Phosphorylation	ELLQPAGSEASSEPH HHHCCCCCCCCCCCC	31.90	25619855
1494	Phosphorylation	QPAGSEASSEPHNST CCCCCCCCCCCCCCC	31.05	25619855
1495	Phosphorylation	PAGSEASSEPHNSTG CCCCCCCCCCCCCCC	63.29	25619855
1500	Phosphorylation	ASSEPHNSTGQSCLP CCCCCCCCCCCCCCC	34.45	25619855
1501	Phosphorylation	SSEPHNSTGQSCLPR CCCCCCCCCCCCCCH	50.73	25619855
1504	Phosphorylation	PHNSTGQSCLPRREL CCCCCCCCCCCHHHH	23.46	25619855
1531	Phosphorylation	FSSRDPESESPKEPA ECCCCCCCCCCCCCC	49.08	28066266
1533	Phosphorylation	SRDPESESPKEPAHI CCCCCCCCCCCCCCC	51.02	28066266
1542	Phosphorylation	KEPAHIGTTPASTSA CCCCCCCCCCCCCCC	29.07	-
1543	Phosphorylation	EPAHIGTTPASTSAL CCCCCCCCCCCCCCC	16.19	-
1548	Phosphorylation	GTTPASTSALKIPQG CCCCCCCCCCCCCCC	23.98	-
1594	Phosphorylation	ERADRDISMVVSGLT HHHHCCHHHHHCCCC	15.15	29550500
1598	Phosphorylation	RDISMVVSGLTPKEV CCHHHHHCCCCHHHH	19.37	28059163
1603	Acetylation	VVSGLTPKEVMTVQK HHCCCCHHHHHHHHH	58.67	7713539
1610	Acetylation	KEVMTVQKFAEKYRL HHHHHHHHHHHHHCC	42.05	7713549
1614	Acetylation	TVQKFAEKYRLTLTD HHHHHHHHHCCCHHH	32.04	7713557
1665	Phosphorylation	SYSWVVRSIQERRLL EEHHHHHHHHHHHCC	19.60	20139300
1805	Phosphorylation	QNITCDSSEPQDSND EEEECCCCCCCCCCC	39.79	25293948
1810	Phosphorylation	DSSEPQDSND----- CCCCCCCCCC-----	37.34	25293948

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
971	S	Phosphorylation	Kinase	CHEK2	Q9Z265	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
971	S	Phosphorylation		-
Phosphorylation at Ser-971 by CHEK2 regulates mitotic spindle assembly.

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 BRCA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRCA2_MOUSE	Brca2	physical	20211142
EWS_MOUSE	Ewsr1	physical	20211142
HXA2_MOUSE	Hoxa2	physical	20211142
HXC12_MOUSE	Hoxc12	physical	20211142
TFE2_MOUSE	Tcf3	physical	20211142
OLIG1_MOUSE	Olig1	physical	20211142
SMCA2_MOUSE	Smarca2	physical	15574597
NBN_MOUSE	Nbn	physical	12792649
BACH_MOUSE	Acot7	physical	22034435
BRCA1_MOUSE	Brca1	physical	19088202
UB2D3_HUMAN	UBE2D3	physical	19088202
ESR1_MOUSE	Esr1	physical	16807234
JUN_MOUSE	Jun	physical	16807234
ETV4_MOUSE	Etv4	physical	16807234
UBC_HUMAN	UBC	physical	10500182
EZH2_MOUSE	Ezh2	physical	23624935
SUZ12_MOUSE	Suz12	physical	23624935
PO2F1_MOUSE	Pou2f1	physical	17700520
ACACA_MOUSE	Acaca	physical	24565757
BAD_HUMAN	BAD	physical	26496610
BARD1_HUMAN	BARD1	physical	26496610
BLMH_HUMAN	BLMH	physical	26496610
CETN2_HUMAN	CETN2	physical	26496610
NDST1_HUMAN	NDST1	physical	26496610
MSH5_HUMAN	MSH5	physical	26496610
MYH6_HUMAN	MYH6	physical	26496610
ABCE1_HUMAN	ABCE1	physical	26496610
UXT_HUMAN	UXT	physical	26496610
DNPH1_HUMAN	DNPH1	physical	26496610
SMHD1_HUMAN	SMCHD1	physical	26496610
PR38A_HUMAN	PRPF38A	physical	26496610
SCLT1_HUMAN	SCLT1	physical	26496610
TP53B_MOUSE	Trp53bp1	genetic	23657012

Drug and Disease Associations

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

Regulatory Network of BRCA1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831 AND SER-957, ANDMASS SPECTROMETRY.	17525332 [Abstract]

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