dbPTM

BRCA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRCA2_MOUSE
UniProt AC	P97929
Protein Name	Breast cancer type 2 susceptibility protein homolog
Gene Name	Brca2
Organism	Mus musculus (Mouse).
Sequence Length	3329
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus.
Protein Description	Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity)..
Protein Sequence	MPVEYKRRPTFWEIFKARCSTADLGPISLNWFEELSSEAPPYNSEPPEESEYKPHGYEPQLFKTPQRNPPYHQFASTPIMFKERSQTLPLDQSPFRELGKVVASSKHKTHSKKKTKVDPVVDVASPPLKSCLSESPLTLRCTQAVLQREKPVVSGSLFYTPKLKEGQTPKPISESLGVEVDPDMSWTSSLATPPTLSSTVLIARDEEARSSVTPADSPATLKSCFSNHNESPQKNDRSVPSVIDSENKNQQEAFSQGLGKMLGDSSGKRNSFKDCLRKPIPNILEDGETAVDTSEEDSFSLCFPKRRTRNLQKMRMGKTRKKIFSETRTDELSEEARRQTDDKNSFVFEMELRESDPLDPGVTSQKPFYSQNEEICNEAVQCSDSRWSQSNLSGLNETQTGKITLPHISSHSQNISEDFIDMKKEGTGSITSEKSLPHISSLPEPEKMFSEETVVDKEHEGQHFESLEDSIAGKQMVSRTSQAACLSPSIRKSIFKMREPLDETLGTVFSDSMTNSTFTEEHEASACGLGILTACSQREDSICPSSVDTGSWPTTLTDTSATVKNAGLISTLKNKKRKFIYSVSDDASLQGKKLQTHRQLELTNLSAQLEASAFEVPLTFTNVNSGIPDSSDKKRCLPNDPEEPSLTNSFGTATSKEISYIHALISQDLNDKEAIVIEEKPQPYTAREADFLLCLPERTCENDQKSPKVSNGKEKVLVSACLPSAVQLSSISFESQENPLGDHNGTSTLKLTPSSKLPLSKADMVSREKMCKMPEKLQCESCKVNIELSKNILEVNEICILSENSKTPGLLPPGENIIEVASSMKSQFNQNAKIVIQKDQKGSPFISEVAVNMNSEELFPDSGNNFAFQVTNKCNKPDLGSSVELQEEDLSHTQGPSLKNSPMAVDEDVDDAHAAQVLITKDSDSLAVVHDYTEKSRNNIEQHQKGTEDKDFKSNSSLNMKSDGNSDCSDKWSEFLDPVLNHNFGGSFRTASNKEIKLSEHNVKKSKMFFKDIEEQYPTRLACIDIVNTLPLANQKKLSEPHIFDLKSVTTVSTQSHNQSSVSHEDTDTAPQMLSSKQDFHSNNLTTSQKAEITELSTILEESGSQFEFTQFRKPSHIAQNTSEVPGNQMVVLSTASKEWKDTDLHLPVDPSVGQTDHSKQFEGSAGVKQSFPHLLEDTCNKNTSCFLPNINEMEFGGFCSALGTKLSVSNEALRKAMKLFSDIENSEEPSAKVGPRGFSSSAHHDSVASVFKIKKQNTEKSFDEKSSKCQVTLQNNIEMTTCIFVGRNPEKYIKNTKHEDSYTSSQRNNLENSDGSMSSTSGPVYIHKGDSDLPADQGSKCPESCTQYAREENTQIKENISDLTCLEIMKAEETCMKSSDKKQLPSDKMEQNIKEFNISFQTASGKNTRVSKESLNKSVNIFNRETDELTVISDSLNSKILHGINKDKMHTSCHKKAISIKKVFEDHFPIVTVSQLPAQQHPEYEIESTKEPTLLSFHTASGKKVKIMQESLDKVKNLFDETQYVRKTASFSQGSKPLKDSKKELTLAYEKIEVTASKCEEMQNFVSKETEMLPQQNYHMYRQTENLKTSNGTSSKVQENIENNVEKNPRICCICQSSYPVTEDSALAYYTEDSRKTCVRESSLSKGRKWLREQGDKLGTRNTIKIECVKEHTEDFAGNASYEHSLVIIRTEIDTNHVSENQVSTLLSDPNVCHSYLSQSSFCHCDDMHNDSGYFLKNKIDSDVPPDMKNAEGNTISPRVSATKERNLHPQTINEYCVQKLETNTSPHANKDVAIDPSLLDSRNCKVGSLVFITAHSQETERTKEIVTDNCYKIVEQNRQSKPDTCQTSCHKVLDDSKDFICPSSSGDVCINSRKDSFCPHNEQILQHNQSMSGLKKAATPPVGLETWDTSKSIREPPQAAHPSRTYGIFSTASGKAIQVSDASLEKARQVFSEMDGDAKQLSSMVSLEGNEKPHHSVKRENSVVHSTQGVLSLPKPLPGNVNSSVFSGFSTAGGKLVTVSESALHKVKGMLEEFDLIRTEHTLQHSPIPEDVSKILPQPCAEIRTPEYPVNSKLQKTYNDKSSLPSNYKESGSSGNTQSIEVSLQLSQMERNQDTQLVLGTKVSHSKANLLGKEQTLPQNIKVKTDEMKTFSDVPVKTNVGEYYSKESENYFETEAVESAKAFMEDDELTDSEQTHAKCSLFTCPQNETLFNSRTRKRGGVTVDAVGQPPIKRSLLNEFDRIIESKGKSLTPSKSTPDGTVKDRSLFTHHMSLEPVTCGPFCSSKERQGAQRPHLTSPAQELLSKGHPWRHSALEKSPSSPIVSILPAHDVSATRTERTRHSGKSTKVFVPPFKMKSQFHGDEHFNSKNVNLEGKNQKSTDGDREDGNDSHVRQFNKDLMSSLQSARDLQDMRIKNKERRHLRLQPGSLYLTKSSTLPRISLQAAVGDRAPSACSPKQLYIYGVSKECINVNSKNAEYFQFDIQDHFGKEDLCAGKGFQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISSIWVANHYRWIVWKLAAMEFAFPKEFANRCLNPERVLLQLKYRYDVEIDNSRRSALKKILERDDTAAKTLVLCISDIISPSTKVSETSGGKTSGEDANKVDTIELTDGWYAVRAQLDPPLMALVKSGKLTVGQKIITQGAELVGSPDACAPLEAPDSLRLKISANSTRPARWHSRLGFFRDPRPFPLPLSSLFSDGGNVGCVDIIVQRVYPLQWVEKTVSGLYIFRSEREEEKEALRFAEAQQKKLEALFTKVHTEFKDHEEDTTQRCVLSRTLTRQQVHALQDGAELYAAVQYASDPDHLEACFSEEQLRALNNYRQMLNDKKQARIQSEFRKALESAEKEEGLSRDVTTVWKLRVTSYKKKEKSALLSIWRPSSDLSSLLTEGKRYRIYHLAVSKSKSKFERPSIQLTATKRTQYQQLPVSSETLLQVYQPRESLHFSRLSDPAFQPPCSEVDVVGVVVSVVKPIGLAPLVYLSDECLNLLVVKFGIDLNEDIKPRVLIAASNLQCQPESTSGVPTLFAGHFSIFSASPKEAYFQEKVNNLKHAIENIDTFYKEAEKKLIHVLEGDSPKWSTPNKDPTREPHAASTCCASDLLGSGGQFLRISPTGQQSYQSPLSHCTLKGKSMPLAHSAQMAAKSWSGENEIDDPKTCRKRRALDFLSRLPLPSPVSPICTFVSPAAQKAFQPPRSCGTKYATPIKKEPSSPRRRTPFQKTSGVSLPDCDSVADEELALLSTQALTPDSVGGNEQAFPGDSTRNPQPAQRPDQQVGPRSRKESLRDCRGDSSEKLAVES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
85	Phosphorylation	PIMFKERSQTLPLDQ CEECCCCCCCCCCCC	28.71	28066266
87	Phosphorylation	MFKERSQTLPLDQSP ECCCCCCCCCCCCCH	31.43	28066266
93	Phosphorylation	QTLPLDQSPFRELGK CCCCCCCCHHHHHHH	26.18	28066266
125	Phosphorylation	DPVVDVASPPLKSCL CCCCCCCCCCHHHHC	27.22	21149613
135	Phosphorylation	LKSCLSESPLTLRCT HHHHCCCCCHHHHHH	23.10	29514104
213	Phosphorylation	EEARSSVTPADSPAT HHHHHCCCCCCCHHH	18.08	22817900
217	Phosphorylation	SSVTPADSPATLKSC HCCCCCCCHHHHHHH	20.67	25266776
220	Phosphorylation	TPADSPATLKSCFSN CCCCCHHHHHHHHHC	37.80	24759943
223	Phosphorylation	DSPATLKSCFSNHNE CCHHHHHHHHHCCCC	24.41	25777480
226	Phosphorylation	ATLKSCFSNHNESPQ HHHHHHHHCCCCCCC	41.32	23984901
231	Phosphorylation	CFSNHNESPQKNDRS HHHCCCCCCCCCCCC	37.64	29895711
388	Phosphorylation	QCSDSRWSQSNLSGL HCCCCCCCCCCCCCC	23.71	21183079
400	Phosphorylation	SGLNETQTGKITLPH CCCCCCCCCCEECCC	48.11	21183079
429	Phosphorylation	MKKEGTGSITSEKSL CHHCCCCCCCCCCCC	23.64	27841257
431	Phosphorylation	KEGTGSITSEKSLPH HCCCCCCCCCCCCCC	32.31	27841257
432	Phosphorylation	EGTGSITSEKSLPHI CCCCCCCCCCCCCCC	41.16	27841257
435	Phosphorylation	GSITSEKSLPHISSL CCCCCCCCCCCCCCC	42.98	-
481	Phosphorylation	KQMVSRTSQAACLSP HHHHCHHHHHHHHCH	19.40	-
487	Phosphorylation	TSQAACLSPSIRKSI HHHHHHHCHHHHHHH	19.24	25266776
489	Phosphorylation	QAACLSPSIRKSIFK HHHHHCHHHHHHHHH	31.48	28066266
735	Phosphorylation	LSSISFESQENPLGD HHHCCEECCCCCCCC	40.56	-
760	Phosphorylation	PSSKLPLSKADMVSR CCCCCCCCHHHHCCH	24.69	28059163
901	Phosphorylation	QGPSLKNSPMAVDED CCCCCCCCCCCCCCC	17.92	26370283
1222	Phosphorylation	RKAMKLFSDIENSEE HHHHHHHHHCCCCCC	48.38	22006019
1255	Acetylation	VASVFKIKKQNTEKS HHHHEEECCCCCCCC	49.23	6569923
1256	Acetylation	ASVFKIKKQNTEKSF HHHEEECCCCCCCCC	52.86	6569863
1266	Acetylation	TEKSFDEKSSKCQVT CCCCCCCCCCCCEEE	62.97	6569899
1531	Phosphorylation	QYVRKTASFSQGSKP HHHHHHCCCCCCCCC	30.57	23684622
1542	Phosphorylation	GSKPLKDSKKELTLA CCCCCCCCHHHHHHE	44.00	-
1547	Phosphorylation	KDSKKELTLAYEKIE CCCHHHHHHEEEEEE	15.50	30482847
1550	Phosphorylation	KKELTLAYEKIEVTA HHHHHHEEEEEECCH	22.37	30482847
1756	Phosphorylation	MKNAEGNTISPRVSA CCCCCCCCCCCCCCC	33.42	28066266
1758	Phosphorylation	NAEGNTISPRVSATK CCCCCCCCCCCCCCC	12.48	25266776
1786	Phosphorylation	VQKLETNTSPHANKD HHHHHCCCCCCCCCC	51.56	28066266
1787	Phosphorylation	QKLETNTSPHANKDV HHHHCCCCCCCCCCE	19.43	25266776
1901	Phosphorylation	SGLKKAATPPVGLET CCHHHCCCCCCCCCC	32.74	28066266
2022	Phosphorylation	GGKLVTVSESALHKV CCEEEEECHHHHHHH	19.23	23140645
2024	Phosphorylation	KLVTVSESALHKVKG EEEEECHHHHHHHHH	28.73	23140645
2044	Phosphorylation	DLIRTEHTLQHSPIP CCCCCCCHHCCCCCC	23.14	25159016
2048	Phosphorylation	TEHTLQHSPIPEDVS CCCHHCCCCCCHHHH	16.15	25159016
2165	Phosphorylation	VKTNVGEYYSKESEN CCCCCCCCCCCCCCC	13.70	28576409
2192	Phosphorylation	FMEDDELTDSEQTHA HHCCCCCCHHHHHHC	35.12	30482847
2264	Ubiquitination	STPDGTVKDRSLFTH CCCCCCCCCCCCCEE	47.46	-
2319	Phosphorylation	RHSALEKSPSSPIVS HHHHHHCCCCCCCEE	22.19	27841257
2454	Phosphorylation	AVGDRAPSACSPKQL HHCCCCCCCCCCCEE	40.71	26745281
2457	Phosphorylation	DRAPSACSPKQLYIY CCCCCCCCCCEEEEE	34.54	26745281
2810	Phosphorylation	QRCVLSRTLTRQQVH HHHHHCCCCCHHHHH	29.16	25619855
2924	Dimethylation	SLLTEGKRYRIYHLA HHHHCCCCEEEEEEE	36.50	-
3072	Phosphorylation	SASPKEAYFQEKVNN CCCHHHHHHHHHHHH	13.59	25338131
3142	Phosphorylation	GGQFLRISPTGQQSY CCCEEEECCCCCCCC	15.24	26370283
3151	Phosphorylation	TGQQSYQSPLSHCTL CCCCCCCCCCCCCEE	21.41	26370283
3214	Phosphorylation	SPICTFVSPAAQKAF CCCCEEECHHHHHHH	12.48	-
3240	Phosphorylation	TPIKKEPSSPRRRTP CCCCCCCCCCCCCCC	54.81	29895711
3241	Phosphorylation	PIKKEPSSPRRRTPF CCCCCCCCCCCCCCC	32.89	29895711
3309	Phosphorylation	DQQVGPRSRKESLRD CCCCCCCCHHHHHHH	51.33	22006019

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
3214	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
3214	S	Phosphorylation	Kinase	CDK2	P97377	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3291	S	Phosphorylation		-
Phosphorylation at Ser-3291 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding.

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 BRCA2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAD51_MOUSE	Rad51	physical	20211142
RA51B_MOUSE	Rad51b	physical	20211142
FACD2_MOUSE	Fancd2	physical	16127665
RAD51_MOUSE	Rad51	physical	15359272
BRCA1_MOUSE	Brca1	physical	11477095
RAD51_MOUSE	Rad51	physical	12893777
TP53B_MOUSE	Trp53bp1	genetic	23657012

Drug and Disease Associations

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

Regulatory Network of BRCA2_MOUSE

Related Literatures of Post-Translational Modification

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