dbPTM

XRCC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XRCC1_HUMAN
UniProt AC	P18887
Protein Name	DNA repair protein XRCC1
Gene Name	XRCC1
Organism	Homo sapiens (Human).
Sequence Length	633
Subcellular Localization	Nucleus . Moves from the nucleoli to the global nuclear chromatin upon DNA damage.
Protein Description	Involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Probably during DNA repair, negatively regulates ADP-ribose levels by modulating ADP-ribosyltransferase PARP1 activity..
Protein Sequence	MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRFHSPPDKDEAEAPSQKVTVTKLGQFRVKEEDESANSLRPGALFFSRINKTSPVTASDPAGPSYAAATLQASSAASSASPVSRAIGSTSKPQESPKGKRKLDLNQEEKKTPSKPPAQLSPSVPKRPKLPAPTRTPATAPVPARAQGAVTGKPRGEGTEPRRPRAGPEELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSRRYLMAGPGSSSEEDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQKPPTPEETKAASPVLQEDIDIEGVQSEGQDNGAEDSGDTEDELRRVAEQKEHRLPPGQEENGEDPYAGSTDENTDSEEHQEPPDLPVPELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDNMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	IRLRHVVSCSSQDST EEEEEEEECCCCCCH	13.75	27251275
13	Phosphorylation	LRHVVSCSSQDSTHC EEEEEECCCCCCHHH	24.43	27251275
14	Phosphorylation	RHVVSCSSQDSTHCA EEEEECCCCCCHHHH	42.19	20873877
17	Phosphorylation	VSCSSQDSTHCAENL EECCCCCCHHHHHHH	16.65	27251275
18	Phosphorylation	SCSSQDSTHCAENLL ECCCCCCHHHHHHHH	29.30	20873877
26	Acetylation	HCAENLLKADTYRKW HHHHHHHHHHHHHHH	47.59	26051181
42	Phosphorylation	AAKAGEKTISVVLQL HHHCCCCEEEEEEEE	17.74	22210691
44	Phosphorylation	KAGEKTISVVLQLEK HCCCCEEEEEEEECC	16.05	22210691
115	Acetylation	VRMFGPDKLVRAAAE CEEECHHHHHHHHHH	52.60	25953088
129	Ubiquitination	EKRWDRVKIVCSQPY HHHHCEEEEEECCCC	30.25	-
138	Ubiquitination	VCSQPYSKDSPFGLS EECCCCCCCCCCCCE	57.28	-
140	Phosphorylation	SQPYSKDSPFGLSFV CCCCCCCCCCCCEEE	26.35	21815630
145	Phosphorylation	KDSPFGLSFVRFHSP CCCCCCCEEEEECCC	23.29	28857561
151	Phosphorylation	LSFVRFHSPPDKDEA CEEEEECCCCCCCCC	35.10	25159151
155	Acetylation	RFHSPPDKDEAEAPS EECCCCCCCCCCCCC	64.34	26051181
162	Phosphorylation	KDEAEAPSQKVTVTK CCCCCCCCCEEEEEE	50.08	23312004
166	Phosphorylation	EAPSQKVTVTKLGQF CCCCCEEEEEECEEE	29.50	26714015
169	Acetylation	SQKVTVTKLGQFRVK CCEEEEEECEEEECC	46.41	23954790
169	Ubiquitination	SQKVTVTKLGQFRVK CCEEEEEECEEEECC	46.41	21890473
176	Sumoylation	KLGQFRVKEEDESAN ECEEEECCCCCCCCC	51.64	-
176	Sumoylation	KLGQFRVKEEDESAN ECEEEECCCCCCCCC	51.64	25114211
181	Phosphorylation	RVKEEDESANSLRPG ECCCCCCCCCCCCCC	45.10	28555341
184	Phosphorylation	EEDESANSLRPGALF CCCCCCCCCCCCEEE	26.02	26074081
193	Phosphorylation	RPGALFFSRINKTSP CCCEEEEECCCCCCC	25.56	26074081
198	Phosphorylation	FFSRINKTSPVTASD EEECCCCCCCCCCCC	33.50	25159151
199	Phosphorylation	FSRINKTSPVTASDP EECCCCCCCCCCCCC	20.98	25159151
202	Phosphorylation	INKTSPVTASDPAGP CCCCCCCCCCCCCCC	24.67	30266825
204	Phosphorylation	KTSPVTASDPAGPSY CCCCCCCCCCCCCCH	34.46	30266825
210	Phosphorylation	ASDPAGPSYAAATLQ CCCCCCCCHHHHHHH	26.87	30266825
211	Phosphorylation	SDPAGPSYAAATLQA CCCCCCCHHHHHHHH	11.91	30266825
215	Phosphorylation	GPSYAAATLQASSAA CCCHHHHHHHHHHHH	18.06	30266825
219	Phosphorylation	AAATLQASSAASSAS HHHHHHHHHHHHCCC	13.93	21955146
220	Phosphorylation	AATLQASSAASSASP HHHHHHHHHHHCCCH	30.76	28176443
223	Phosphorylation	LQASSAASSASPVSR HHHHHHHHCCCHHHH	26.59	21955146
224	Phosphorylation	QASSAASSASPVSRA HHHHHHHCCCHHHHH	28.21	25159151
226	Phosphorylation	SSAASSASPVSRAIG HHHHHCCCHHHHHHC	27.99	25159151
229	Phosphorylation	ASSASPVSRAIGSTS HHCCCHHHHHHCCCC	21.27	30278072
234	Phosphorylation	PVSRAIGSTSKPQES HHHHHHCCCCCCCCC	24.32	23927012
234	O-linked_Glycosylation	PVSRAIGSTSKPQES HHHHHHCCCCCCCCC	24.32	OGP
235	Phosphorylation	VSRAIGSTSKPQESP HHHHHCCCCCCCCCC	35.24	30278072
236	Phosphorylation	SRAIGSTSKPQESPK HHHHCCCCCCCCCCC	44.00	23401153
236	O-linked_Glycosylation	SRAIGSTSKPQESPK HHHHCCCCCCCCCCC	44.00	OGP
237	Acetylation	RAIGSTSKPQESPKG HHHCCCCCCCCCCCC	51.30	26051181
241	Phosphorylation	STSKPQESPKGKRKL CCCCCCCCCCCCCCC	27.02	29255136
241	O-linked_Glycosylation	STSKPQESPKGKRKL CCCCCCCCCCCCCCC	27.02	OGP
247	Sumoylation	ESPKGKRKLDLNQEE CCCCCCCCCCCCHHH	50.25	-
247	Sumoylation	ESPKGKRKLDLNQEE CCCCCCCCCCCCHHH	50.25	-
256	Acetylation	DLNQEEKKTPSKPPA CCCHHHCCCCCCCHH	69.79	25953088
256	Sumoylation	DLNQEEKKTPSKPPA CCCHHHCCCCCCCHH	69.79	-
256	Sumoylation	DLNQEEKKTPSKPPA CCCHHHCCCCCCCHH	69.79	-
257	Phosphorylation	LNQEEKKTPSKPPAQ CCHHHCCCCCCCHHH	43.81	25159151
259	Phosphorylation	QEEKKTPSKPPAQLS HHHCCCCCCCHHHCC	64.13	25159151
260	Acetylation	EEKKTPSKPPAQLSP HHCCCCCCCHHHCCC	57.11	88077
266	Phosphorylation	SKPPAQLSPSVPKRP CCCHHHCCCCCCCCC	11.75	23927012
268	Phosphorylation	PPAQLSPSVPKRPKL CHHHCCCCCCCCCCC	47.91	25159151
271	Acetylation	QLSPSVPKRPKLPAP HCCCCCCCCCCCCCC	78.25	88081
279	Phosphorylation	RPKLPAPTRTPATAP CCCCCCCCCCCCCCC	49.64	22617229
281	Phosphorylation	KLPAPTRTPATAPVP CCCCCCCCCCCCCCC	21.54	25159151
284	Phosphorylation	APTRTPATAPVPARA CCCCCCCCCCCCCCC	32.47	24732914
296	Phosphorylation	ARAQGAVTGKPRGEG CCCCCCCCCCCCCCC	38.67	22912867
296	O-linked_Glycosylation	ARAQGAVTGKPRGEG CCCCCCCCCCCCCCC	38.67	68722349
298	Acetylation	AQGAVTGKPRGEGTE CCCCCCCCCCCCCCC	23.36	23954790
310	Methylation	GTEPRRPRAGPEELG CCCCCCCCCCHHHHH	50.82	115920125
341	Ubiquitination	FRSELRDKALELGAK CHHHHHHHHHHHCCC	48.73	-
348	Ubiquitination	KALELGAKYRPDWTR HHHHHCCCCCCCCCC	39.74	-
348	Acetylation	KALELGAKYRPDWTR HHHHHCCCCCCCCCC	39.74	25953088
357	Phosphorylation	RPDWTRDSTHLICAF CCCCCCCCCEEEEEE	17.90	20068231
358	Phosphorylation	PDWTRDSTHLICAFA CCCCCCCCEEEEEEC	25.62	20873877
367	Phosphorylation	LICAFANTPKYSQVL EEEEECCCCCHHHHC	20.09	25159151
369	Ubiquitination	CAFANTPKYSQVLGL EEECCCCCHHHHCCC	56.34	-
370	Phosphorylation	AFANTPKYSQVLGLG EECCCCCHHHHCCCC	12.92	-
371	Phosphorylation	FANTPKYSQVLGLGG ECCCCCHHHHCCCCC	21.68	16397295
383	Ubiquitination	LGGRIVRKEWVLDCH CCCEEEEEEHHHHHH	45.06	-
383	Acetylation	LGGRIVRKEWVLDCH CCCEEEEEEHHHHHH	45.06	26051181
398	Phosphorylation	RMRRRLPSRRYLMAG HHHHHCCCCCEEECC	33.70	24719451
401	Phosphorylation	RRLPSRRYLMAGPGS HHCCCCCEEECCCCC	10.34	20068231
408	Phosphorylation	YLMAGPGSSSEEDEA EEECCCCCCCHHHHH	33.55	22115753
409	Phosphorylation	LMAGPGSSSEEDEAS EECCCCCCCHHHHHH	47.92	22115753
410	Phosphorylation	MAGPGSSSEEDEASH ECCCCCCCHHHHHHH	46.86	22115753
416	Phosphorylation	SSEEDEASHSGGSGD CCHHHHHHHCCCCCC	19.01	22115753
418	Phosphorylation	EEDEASHSGGSGDEA HHHHHHHCCCCCCCC	42.21	22115753
421	Phosphorylation	EASHSGGSGDEAPKL HHHHCCCCCCCCCCC	46.74	22115753
431	Ubiquitination	EAPKLPQKQPQTKTK CCCCCCCCCCCCCCC	63.10	-
431	Acetylation	EAPKLPQKQPQTKTK CCCCCCCCCCCCCCC	63.10	26051181
435	Phosphorylation	LPQKQPQTKTKPTQA CCCCCCCCCCCCCCC	47.57	21406692
437	Phosphorylation	QKQPQTKTKPTQAAG CCCCCCCCCCCCCCC	45.72	29209046
440	Phosphorylation	PQTKTKPTQAAGPSS CCCCCCCCCCCCCCC	32.18	23927012
440	O-linked_Glycosylation	PQTKTKPTQAAGPSS CCCCCCCCCCCCCCC	32.18	19664995
446	Phosphorylation	PTQAAGPSSPQKPPT CCCCCCCCCCCCCCC	54.45	25159151
446	O-linked_Glycosylation	PTQAAGPSSPQKPPT CCCCCCCCCCCCCCC	54.45	19664995
447	Phosphorylation	TQAAGPSSPQKPPTP CCCCCCCCCCCCCCH	34.19	20201521
447	O-linked_Glycosylation	TQAAGPSSPQKPPTP CCCCCCCCCCCCCCH	34.19	19664995
453	Phosphorylation	SSPQKPPTPEETKAA CCCCCCCCHHHHHCC	52.43	20201521
453	O-linked_Glycosylation	SSPQKPPTPEETKAA CCCCCCCCHHHHHCC	52.43	19664995
457	Phosphorylation	KPPTPEETKAASPVL CCCCHHHHHCCCCCC	25.07	23927012
461	Phosphorylation	PEETKAASPVLQEDI HHHHHCCCCCCHHCC	22.02	30278072
475	Phosphorylation	IDIEGVQSEGQDNGA CCCCCCCCCCCCCCC	41.09	30278072
485	Phosphorylation	QDNGAEDSGDTEDEL CCCCCCCCCCCHHHH	30.03	25159151
488	Phosphorylation	GAEDSGDTEDELRRV CCCCCCCCHHHHHHH	49.19	25159151
515	Phosphorylation	EENGEDPYAGSTDEN CCCCCCCCCCCCCCC	35.60	20873877
518	Phosphorylation	GEDPYAGSTDENTDS CCCCCCCCCCCCCCC	25.23	23909892
519	Phosphorylation	EDPYAGSTDENTDSE CCCCCCCCCCCCCCH	46.55	23909892
523	Phosphorylation	AGSTDENTDSEEHQE CCCCCCCCCCHHCCC	38.56	25218447
525	Phosphorylation	STDENTDSEEHQEPP CCCCCCCCHHCCCCC	42.73	20873877
578	Phosphorylation	GELEDNMSDRVQFVI CCCCCCCCCCEEEEE	28.64	-
618	Ubiquitination	WIYSCNEKQKLLPHQ EEEECCHHHHCCHHH	38.45	-
618	Acetylation	WIYSCNEKQKLLPHQ EEEECCHHHHCCHHH	38.45	26051181
620	Ubiquitination	YSCNEKQKLLPHQLY EECCHHHHCCHHHHC	64.16	-
620	Acetylation	YSCNEKQKLLPHQLY EECCHHHHCCHHHHC	64.16	26051181
627	Phosphorylation	KLLPHQLYGVVPQA- HCCHHHHCCCCCCC-	10.99	28152594

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
184	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
210	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
284	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
371	S	Phosphorylation	Kinase	DNAPK	P78527	PSP
408	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
408	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
409	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
409	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
410	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
410	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
416	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
418	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
421	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
421	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
475	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
475	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
485	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
485	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
485	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
488	T	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
488	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
488	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
515	Y	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
518	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
518	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
518	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
519	T	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
519	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
519	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
523	T	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
523	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
523	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
525	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
525	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
578	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RNF146	Q9NTX7	PMID:21825151

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
371	S	Phosphorylation		16397295
Phosphorylation of Ser-371 causes dimer dissociation.

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 XRCC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DNLI3_HUMAN	LIG3	physical	11163244
PNKP_HUMAN	PNKP	physical	11163244
APTX_HUMAN	APTX	physical	15555565
DNLI3_HUMAN	LIG3	physical	17353931
PNKP_HUMAN	PNKP	physical	17353931
NEIL1_HUMAN	NEIL1	physical	15260972
PCNA_HUMAN	PCNA	physical	15107487
DPOLB_HUMAN	POLB	physical	15107487
APTX_HUMAN	APTX	physical	15044383
P53_HUMAN	TP53	physical	15044383
PARP1_HUMAN	PARP1	physical	15044383
DPOLB_HUMAN	POLB	physical	8978692
DNLI3_HUMAN	LIG3	physical	8264637
DNLI3_HUMAN	LIG3	physical	9136882
PARP1_HUMAN	PARP1	physical	9584196
DNLI3_HUMAN	LIG3	physical	9705932
APEX1_HUMAN	APEX1	physical	11707423
PARP2_HUMAN	PARP2	physical	11948190
DNLI3_HUMAN	LIG3	physical	20227374
POLK_HUMAN	POLK	physical	20227374
DPOD1_HUMAN	POLD1	physical	20227374
PRAF3_HUMAN	ARL6IP5	physical	19208635
XPO1_HUMAN	XPO1	physical	21909257
POLI_HUMAN	POLI	physical	18923427
APTX_HUMAN	APTX	physical	15367657
PNKP_HUMAN	PNKP	physical	15367657
DPOLB_HUMAN	POLB	physical	15367657
APEX1_HUMAN	APEX1	physical	19934257
C1QBP_HUMAN	C1QBP	physical	26496610
DNLI3_HUMAN	LIG3	physical	26496610
DPOLB_HUMAN	POLB	physical	26496610
RAP1B_HUMAN	RAP1B	physical	26496610
BRPF1_HUMAN	BRPF1	physical	26496610
LIPA1_HUMAN	PPFIA1	physical	26496610
GT2D1_HUMAN	GTF2IRD1	physical	26496610
PPIH_HUMAN	PPIH	physical	26496610
XPOT_HUMAN	XPOT	physical	26496610
PNKP_HUMAN	PNKP	physical	26496610
SF3B6_HUMAN	SF3B6	physical	26496610
M3K20_HUMAN	ZAK	physical	26496610
APTX_HUMAN	APTX	physical	26496610
S39AA_HUMAN	SLC39A10	physical	26496610
GCC1_HUMAN	GCC1	physical	26496610
RUSD4_HUMAN	RPUSD4	physical	26496610
DPH7_HUMAN	DPH7	physical	26496610
DPOLB_HUMAN	POLB	physical	25423885
HS90A_HUMAN	HSP90AA1	physical	25423885
PRKDC_HUMAN	PRKDC	physical	18678286

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 XRCC1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Specific recognition of a multiply phosphorylated motif in the DNArepair scaffold XRCC1 by the FHA domain of human PNK."; Ali A.A., Jukes R.M., Pearl L.H., Oliver A.W.; Nucleic Acids Res. 37:1701-1712(2009). Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 515-522 IN COMPLEX WITHPNKP, AND PHOSPHORYLATION AT SER-518; THR-519 AND THR-523.	19155274 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198; SER-199; SER-226;SER-241; THR-453; SER-461; SER-485 AND THR-488, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; SER-226; SER-446;SER-447; THR-453 AND THR-457, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-226; SER-241;THR-257; SER-259; SER-266; SER-408; SER-409; SER-410; SER-418;SER-421; SER-447 AND THR-453, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-447 ANDTHR-453, AND MASS SPECTROMETRY.	17287340 [Abstract]
"XRCC1 is phosphorylated by DNA-dependent protein kinase in responseto DNA damage."; Levy N., Martz A., Bresson A., Spenlehauer C., de Murcia G.,Menissier-de Murcia J.; Nucleic Acids Res. 34:32-41(2006). Cited for: SUBUNIT, AND PHOSPHORYLATION AT SER-371.	16397295 [Abstract]
"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 SER-408; SER-409; SER-410;SER-416; SER-418 AND SER-421, AND MASS SPECTROMETRY.	17081983 [Abstract]

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