dbPTM

NBN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NBN_HUMAN
UniProt AC	O60934
Protein Name	Nibrin
Gene Name	NBN
Organism	Homo sapiens (Human).
Sequence Length	754
Subcellular Localization	Nucleus . Nucleus, PML body . Chromosome, telomere. Localizes to discrete nuclear foci after treatment with genotoxic agents.
Protein Description	Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex..
Protein Sequence	MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNTTTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNTLAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKSARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSHAAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETNDTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFRSLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MWKLLPAAGP -----CCCCCCCCCC	38.56	7825953
3	Ubiquitination	-----MWKLLPAAGP -----CCCCCCCCCC	38.56	-
16	Phosphorylation	GPAGGEPYRLLTGVE CCCCCCCCEEECCCE	15.02	21406692
24	Phosphorylation	RLLTGVEYVVGRKNC EEECCCEEEECCCCE	9.68	-
49	Phosphorylation	SRNHAVLTANFSVTN CCCCEEEEEEEEEEC	16.98	27732954
53	Phosphorylation	AVLTANFSVTNLSQT EEEEEEEEEECCCCC	28.04	27732954
55	Phosphorylation	LTANFSVTNLSQTDE EEEEEEEECCCCCCC	29.28	27732954
58	Phosphorylation	NFSVTNLSQTDEIPV EEEEECCCCCCCCCE	32.86	25159151
60	Phosphorylation	SVTNLSQTDEIPVLT EEECCCCCCCCCEEE	32.02	20068231
67	Phosphorylation	TDEIPVLTLKDNSKY CCCCCEEEECCCCCC	31.81	20068231
73	Acetylation	LTLKDNSKYGTFVNE EEECCCCCCCCCCCH	54.69	25953088
73	Malonylation	LTLKDNSKYGTFVNE EEECCCCCCCCCCCH	54.69	26320211
73	Ubiquitination	LTLKDNSKYGTFVNE EEECCCCCCCCCCCH	54.69	-
82	Ubiquitination	GTFVNEEKMQNGFSR CCCCCHHHHHHCCCC	39.34	-
188	Ubiquitination	LKAVESKKQPPQIES HHHHHHCCCCCCCHH	76.84	-
195	Phosphorylation	KQPPQIESFYPPLDE CCCCCCHHCCCCCCC	31.54	19835603
197	Phosphorylation	PPQIESFYPPLDEPS CCCCHHCCCCCCCCC	17.14	19835603
208	Acetylation	DEPSIGSKNVDLSGR CCCCCCCCCCCCCCH	56.64	26051181
208	Ubiquitination	DEPSIGSKNVDLSGR CCCCCCCCCCCCCCH	56.64	-
233	Acetylation	TFIFLNAKQHKKLSS EEEEEEHHHHCCCCE	52.43	25953088
233	Malonylation	TFIFLNAKQHKKLSS EEEEEEHHHHCCCCE	52.43	26320211
273	Phosphorylation	PGTCVVDTGITNSQT CCEEEEECCCCCCCC	20.90	28348404
276	Phosphorylation	CVVDTGITNSQTLIP EEEECCCCCCCCCCH	30.11	28348404
278	Phosphorylation	VDTGITNSQTLIPDC EECCCCCCCCCCHHH	18.85	12433983
280	Phosphorylation	TGITNSQTLIPDCQK CCCCCCCCCCHHHHH	26.86	28348404
292	Phosphorylation	CQKKWIQSIMDMLQR HHHHHHHHHHHHHHH	15.67	-
334	Acetylation	GHPSTGLKTTTPGPS CCCCCCCCCCCCCCC	45.21	25953088
334	Ubiquitination	GHPSTGLKTTTPGPS CCCCCCCCCCCCCCC	45.21	-
335	Phosphorylation	HPSTGLKTTTPGPSL CCCCCCCCCCCCCCH	40.73	23401153
336	Phosphorylation	PSTGLKTTTPGPSLS CCCCCCCCCCCCCHH	29.43	30266825
337	Phosphorylation	STGLKTTTPGPSLSQ CCCCCCCCCCCCHHC	31.32	17525332
341	Phosphorylation	KTTTPGPSLSQGVSV CCCCCCCCHHCCCCC	46.71	30266825
343	Phosphorylation	TTPGPSLSQGVSVDE CCCCCCHHCCCCCCC	29.26	29255136
347	Phosphorylation	PSLSQGVSVDEKLMP CCHHCCCCCCCCCCC	30.58	30266825
361	Phosphorylation	PSAPVNTTTYVADTE CCCCCCCEEEEECCC	15.78	28348404
362	Phosphorylation	SAPVNTTTYVADTES CCCCCCEEEEECCCC	17.60	28348404
367	Phosphorylation	TTTYVADTESEQADT CEEEEECCCCCCCCC	31.50	29759185
369	Phosphorylation	TYVADTESEQADTWD EEEECCCCCCCCCCC	36.78	28348404
388	Methylation	PKEIKVSKMEQKFRM CCCCCCCHHHHHHHH	49.82	-
395	Sulfoxidation	KMEQKFRMLSQDAPT HHHHHHHHHCCCCCC	4.80	21406390
397	Phosphorylation	EQKFRMLSQDAPTVK HHHHHHHCCCCCCHH	19.37	25159151
402	Phosphorylation	MLSQDAPTVKESCKT HHCCCCCCHHHHHCC	46.03	30266825
406	Phosphorylation	DAPTVKESCKTSSNN CCCCHHHHHCCCCCC	18.39	20068231
409	Phosphorylation	TVKESCKTSSNNNSM CHHHHHCCCCCCCCC	41.54	25159151
410	Phosphorylation	VKESCKTSSNNNSMV HHHHHCCCCCCCCCC	19.30	25159151
411	Phosphorylation	KESCKTSSNNNSMVS HHHHCCCCCCCCCCH	49.13	25159151
415	Phosphorylation	KTSSNNNSMVSNTLA CCCCCCCCCCHHHHH	23.76	21406692
416	Sulfoxidation	TSSNNNSMVSNTLAK CCCCCCCCCHHHHHH	4.10	21406390
418	Phosphorylation	SNNNSMVSNTLAKMR CCCCCCCHHHHHHCC	18.56	21406692
420	Phosphorylation	NNSMVSNTLAKMRIP CCCCCHHHHHHCCCC	22.16	25954137
423	Ubiquitination	MVSNTLAKMRIPNYQ CCHHHHHHCCCCCCC	31.65	-
429	Phosphorylation	AKMRIPNYQLSPTKL HHCCCCCCCCCCCCC	12.89	30278072
432	Phosphorylation	RIPNYQLSPTKLPSI CCCCCCCCCCCCCCC	18.26	29255136
434	Phosphorylation	PNYQLSPTKLPSINK CCCCCCCCCCCCCCC	41.66	29255136
438	Phosphorylation	LSPTKLPSINKSKDR CCCCCCCCCCCCCCH	49.59	30266825
441	Acetylation	TKLPSINKSKDRASQ CCCCCCCCCCCHHHH	58.16	189145
442	Phosphorylation	KLPSINKSKDRASQQ CCCCCCCCCCHHHHH	34.99	25394399
447	Phosphorylation	NKSKDRASQQQQTNS CCCCCHHHHHHHHHH	29.43	25159151
452	Phosphorylation	RASQQQQTNSIRNYF HHHHHHHHHHHHHHH	26.96	28555341
454	Phosphorylation	SQQQQTNSIRNYFQP HHHHHHHHHHHHHCC	26.72	24505115
462	Phosphorylation	IRNYFQPSTKKRERD HHHHHCCCCCCCHHH	41.92	25159151
463	Phosphorylation	RNYFQPSTKKRERDE HHHHCCCCCCCHHHH	47.47	25159151
485	Phosphorylation	CKSARIETSCSLLEQ HHHHHHHHHHHHHHH	32.44	28450419
486	Phosphorylation	KSARIETSCSLLEQT HHHHHHHHHHHHHHH	6.74	28450419
488	Phosphorylation	ARIETSCSLLEQTQP HHHHHHHHHHHHHCC	35.44	25159151
493	Phosphorylation	SCSLLEQTQPATPSL HHHHHHHHCCCCHHH	27.43	28450419
497	Phosphorylation	LEQTQPATPSLWKNK HHHHCCCCHHHHHCH	21.79	25159151
499	Phosphorylation	QTQPATPSLWKNKEQ HHCCCCHHHHHCHHH	42.37	20068231
504	Acetylation	TPSLWKNKEQHLSEN CHHHHHCHHHHCCCC	55.83	189149
509	Phosphorylation	KNKEQHLSENEPVDT HCHHHHCCCCCCCCC	35.93	30266825
516	Phosphorylation	SENEPVDTNSDNNLF CCCCCCCCCCCCCCC	36.53	20164059
518	Phosphorylation	NEPVDTNSDNNLFTD CCCCCCCCCCCCCCH	43.75	25159151
524	Phosphorylation	NSDNNLFTDTDLKSI CCCCCCCCHHHHHHH	40.95	23663014
526	Phosphorylation	DNNLFTDTDLKSIVK CCCCCCHHHHHHHHH	39.93	28450419
529	Sumoylation	LFTDTDLKSIVKNSA CCCHHHHHHHHHCHH	40.73	28112733
529	Ubiquitination	LFTDTDLKSIVKNSA CCCHHHHHHHHHCHH	40.73	-
535	Phosphorylation	LKSIVKNSASKSHAA HHHHHHCHHCHHHHH	28.35	24732914
537	Phosphorylation	SIVKNSASKSHAAEK HHHHCHHCHHHHHHH	34.22	24732914
544	Acetylation	SKSHAAEKLRSNKKR CHHHHHHHHHHCCCC	44.46	23954790
550	Acetylation	EKLRSNKKREMDDVA HHHHHCCCCCHHHHH	58.82	19822001
568	Acetylation	EVLEQLFKDTKPELE HHHHHHHCCCCCCEE	73.42	19822007
571	Sumoylation	EQLFKDTKPELEIDV HHHHCCCCCCEEEEE	46.78	28112733
582	Sumoylation	EIDVKVQKQEEDVNV EEEEEEECCHHHCCC	63.77	-
582	Sumoylation	EIDVKVQKQEEDVNV EEEEEEECCHHHCCC	63.77	28112733
599	Phosphorylation	RPRMDIETNDTFSDE CCCCCCCCCCCCCCC	38.43	24732914
602	Phosphorylation	MDIETNDTFSDEAVP CCCCCCCCCCCCCCC	27.40	30278072
604	Phosphorylation	IETNDTFSDEAVPES CCCCCCCCCCCCCCC	36.31	30278072
611	Phosphorylation	SDEAVPESSKISQEN CCCCCCCCCCCCCCC	30.75	28102081
612	Phosphorylation	DEAVPESSKISQENE CCCCCCCCCCCCCCC	32.14	28102081
615	Phosphorylation	VPESSKISQENEIGK CCCCCCCCCCCCCCC	34.87	25159151
627	Ubiquitination	IGKKRELKEDSLWSA CCCCCCCCHHHCCCH	55.51	-
630	Phosphorylation	KRELKEDSLWSAKEI CCCCCHHHCCCHHHH	32.59	26714015
635	Ubiquitination	EDSLWSAKEISNNDK HHHCCCHHHHCCCCC	50.49	-
638	Phosphorylation	LWSAKEISNNDKLQD CCCHHHHCCCCCCCC	30.58	26714015
642	Acetylation	KEISNNDKLQDDSEM HHHCCCCCCCCCHHH	50.61	26051181
647	Phosphorylation	NDKLQDDSEMLPKKL CCCCCCCHHHHCHHH	32.94	26714015
657	Phosphorylation	LPKKLLLTEFRSLVI HCHHHHHHHHHHHHH	32.80	20068231
661	Phosphorylation	LLLTEFRSLVIKNST HHHHHHHHHHHCCCC	32.10	20068231
665	Acetylation	EFRSLVIKNSTSRNP HHHHHHHCCCCCCCC	37.05	189157
665	Ubiquitination	EFRSLVIKNSTSRNP HHHHHHHCCCCCCCC	37.05	21890473
667	Phosphorylation	RSLVIKNSTSRNPSG HHHHHCCCCCCCCCC	23.82	20068231
668	Phosphorylation	SLVIKNSTSRNPSGI HHHHCCCCCCCCCCC	40.89	20068231
669	Phosphorylation	LVIKNSTSRNPSGIN HHHCCCCCCCCCCCC	29.85	20068231
673	Phosphorylation	NSTSRNPSGINDDYG CCCCCCCCCCCCCCH	56.72	16188882
679	Phosphorylation	PSGINDDYGQLKNFK CCCCCCCCHHHHCHH	15.05	27642862
683	Ubiquitination	NDDYGQLKNFKKFKK CCCCHHHHCHHHCCC	53.07	21890473
690	Acetylation	KNFKKFKKVTYPGAG HCHHHCCCCCCCCCC	42.83	189161
693	Phosphorylation	KKFKKVTYPGAGKLP HHCCCCCCCCCCCCC	11.58	-
698	Acetylation	VTYPGAGKLPHIIGG CCCCCCCCCCEEECC	59.31	189165
706	Phosphorylation	LPHIIGGSDLIAHHA CCEEECCCHHHHHHH	24.83	-
715	Acetylation	LIAHHARKNTELEEW HHHHHHHCCCHHHHH	69.84	189169
715	Methylation	LIAHHARKNTELEEW HHHHHHHCCCHHHHH	69.84	189169
715	Ubiquitination	LIAHHARKNTELEEW HHHHHHHCCCHHHHH	69.84	-
738	Phosphorylation	NQHAKEESLADDLFR HHHHCHHHHHHHHHH	29.92	30266825
751	Methylation	FRYNPYLKRRR---- HHHCHHHHHCC----	37.71	115973713
751	Ubiquitination	FRYNPYLKRRR---- HHHCHHHHHCC----	37.71	-

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
278	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
343	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
343	S	Phosphorylation	Kinase	ATR	Q13535	PSP
397	S	Phosphorylation	Kinase	ATM	Q13315	PSP
432	S	Phosphorylation	Kinase	CDK2	P24941	PSP
615	S	Phosphorylation	Kinase	ATM	Q13315	PSP
615	S	Phosphorylation	Kinase	ATR	Q13535	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:23115235
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NBN_HUMAN !!

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 NBN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BLM_HUMAN	BLM	physical	10783165
MRE11_HUMAN	MRE11A	physical	10783165
RAD50_HUMAN	RAD50	physical	10783165
H2AX_HUMAN	H2AFX	physical	12419185
MRE11_HUMAN	MRE11A	physical	12679336
RAD50_HUMAN	RAD50	physical	12679336
ATM_HUMAN	ATM	physical	10783165
MLH1_HUMAN	MLH1	physical	10783165
MSH2_HUMAN	MSH2	physical	10783165
MSH6_HUMAN	MSH6	physical	10783165
RFC1_HUMAN	RFC1	physical	10783165
TERF1_HUMAN	TERF1	physical	10913111
XRCC4_HUMAN	XRCC4	physical	18458108
MRE11_HUMAN	MRE11A	physical	18458108
MRE11_HUMAN	MRE11A	physical	11238951
RAD50_HUMAN	RAD50	physical	11238951
TERF2_HUMAN	TERF2	physical	10888888
RAD50_HUMAN	RAD50	physical	12607003
MRE11_HUMAN	MRE11A	physical	12607003
MDC1_HUMAN	MDC1	physical	12607003
ATF2_HUMAN	ATF2	physical	15916964
ATM_HUMAN	ATM	physical	17507690
TOPB1_HUMAN	TOPBP1	physical	17765870
MRE11_HUMAN	MRE11A	physical	12447395
RAD50_HUMAN	RAD50	physical	12447395
WRN_HUMAN	WRN	physical	20600238
TBG1_HUMAN	TUBG1	physical	19244116
MRE11_HUMAN	MRE11A	physical	19244116
BRCA1_HUMAN	BRCA1	physical	19244116
RAD18_HUMAN	RAD18	physical	21884979
MRE11_HUMAN	MRE11A	physical	21884979
UBE2A_HUMAN	UBE2A	physical	21884979
UBE2B_HUMAN	UBE2B	physical	21884979
RPA34_HUMAN	CD3EAP	physical	21884979
ATM_HUMAN	ATM	physical	15758953
RAD50_HUMAN	RAD50	physical	15758953
MRE11_HUMAN	MRE11A	physical	15758953
ATR_HUMAN	ATR	physical	15758953
PRKDC_HUMAN	PRKDC	physical	15758953
DNLI3_HUMAN	LIG3	physical	15758953
HSP74_HUMAN	HSPA4	physical	15758953
IPO5_HUMAN	IPO5	physical	15758953
RAD50_HUMAN	RAD50	physical	22464731
MRE11_HUMAN	MRE11A	physical	22464731
ATM_HUMAN	ATM	physical	22464731
SKP2_HUMAN	SKP2	physical	22464731
MDC1_HUMAN	MDC1	physical	12607005
CTIP_HUMAN	RBBP8	physical	18171670
RAD50_HUMAN	RAD50	physical	22939629
TERF2_HUMAN	TERF2	physical	22939629
TE2IP_HUMAN	TERF2IP	physical	22939629
RNF8_HUMAN	RNF8	physical	23115235
MDC1_HUMAN	MDC1	physical	23115235
MDC1_HUMAN	MDC1	physical	18678890
MTOR_HUMAN	MTOR	physical	23762398
RICTR_HUMAN	RICTOR	physical	23762398
SIN1_HUMAN	MAPKAP1	physical	23762398
PHRF1_HUMAN	PHRF1	physical	25855964
RAD50_HUMAN	RAD50	physical	26344197
BAP1_HUMAN	BAP1	physical	25640309
CASC3_HUMAN	CASC3	physical	25640309
ARY2_HUMAN	NAT2	physical	25640309
SNAI1_HUMAN	SNAI1	physical	25640309
ATM_HUMAN	ATM	physical	25088203
VRK1_HUMAN	VRK1	physical	26869104
BRCA1_HUMAN	BRCA1	physical	25939603
CTIP_HUMAN	RBBP8	physical	26387952
H31T_HUMAN	HIST3H3	physical	25823024
FANCJ_HUMAN	BRIP1	physical	23530059
MRE11_HUMAN	MRE11A	physical	23530059
RAD50_HUMAN	RAD50	physical	23530059
CHK1_HUMAN	CHEK1	genetic	14988723

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
251260	Nijmegen breakage syndrome (NBS)
114480	Breast cancer (BC)
609135	Aplastic anemia (AA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NBN_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-337; SER-341; SER-343AND THR-602, 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-397 AND SER-432, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-343 AND SER-397, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND MASSSPECTROMETRY.	15302935 [Abstract]
"ATM phosphorylation of Nijmegen breakage syndrome protein is requiredin a DNA damage response."; Wu X., Ranganathan V., Weisman D.S., Heine W.F., Ciccone D.N.,O'Neill T.B., Crick K.E., Pierce K.A., Lane W.S., Rathbun G.,Livingston D.M., Weaver D.T.; Nature 405:477-482(2000). Cited for: PHOSPHORYLATION AT SER-343; SER-397 AND SER-615, AND MUTAGENESIS OFSER-343; SER-397 AND SER-615.	10839545 [Abstract]
"Functional link between ataxia-telangiectasia and Nijmegen breakagesyndrome gene products."; Zhao S., Weng Y.-C., Yuan S.-S.F., Lin Y.-T., Hsu H.-C., Lin S.-C.,Gerbino E., Song M.-H., Zdzienicka M.Z., Gatti R.A., Shay J.W.,Ziv Y., Shiloh Y., Lee E.Y.-H.P.; Nature 405:473-477(2000). Cited for: PHOSPHORYLATION AT SER-278.	10839544 [Abstract]
"ATM-dependent phosphorylation of nibrin in response to radiationexposure."; Gatei M., Young D., Cerosaletti K.M., Desai-Mehta A., Spring K.,Kozlov S., Lavin M.F., Gatti R.A., Concannon P., Khanna K.K.; Nat. Genet. 25:115-119(2000). Cited for: PHOSPHORYLATION AT SER-343, AND MUTAGENESIS OF ARG-28; HIS-45;136-GLY-GLY-137 AND TYR-176.	10802669 [Abstract]