dbPTM

MRE11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MRE11_HUMAN
UniProt AC	P49959
Protein Name	Double-strand break repair protein MRE11
Gene Name	MRE11 {ECO:0000312\|HGNC:HGNC:7230}
Organism	Homo sapiens (Human).
Sequence Length	708
Subcellular Localization	Nucleus . Chromosome, telomere . Localizes to discrete nuclear foci after treatment with genotoxic agents.
Protein Description	Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity 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. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. [PubMed: 9651580]
Protein Sequence	MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSTADALDD ------CCHHHHCCC	32.10	22223895
2	Phosphorylation	------MSTADALDD ------CCHHHHCCC	32.10	30108239
3	Phosphorylation	-----MSTADALDDE -----CCHHHHCCCC	27.53	30108239
12	Phosphorylation	DALDDENTFKILVAT HHCCCCCCEEEEEEE	25.02	25159151
70	Ubiquitination	HENKPSRKTLHTCLE CCCCCCHHHHHHHHH	60.83	-
73	Ubiquitination	KPSRKTLHTCLELLR CCCHHHHHHHHHHHH	21.55	-
74	Phosphorylation	PSRKTLHTCLELLRK CCHHHHHHHHHHHHH	23.15	22817900
156	Phosphorylation	FVNHFGRSMSVEKID HHHHCCCCCCEEECC	18.78	24719451
158	Phosphorylation	NHFGRSMSVEKIDIS HHCCCCCCEEECCCC	28.50	29083192
161	Ubiquitination	GRSMSVEKIDISPVL CCCCCEEECCCCHHE	43.45	-
164	Ubiquitination	MSVEKIDISPVLLQK CCEEECCCCHHEECC	5.97	-
165	Phosphorylation	SVEKIDISPVLLQKG CEEECCCCHHEECCC	12.76	25850435
171	Ubiquitination	ISPVLLQKGSTKIAL CCHHEECCCCCEEEE	55.59	-
174	Ubiquitination	VLLQKGSTKIALYGL HEECCCCCEEEEECC	34.83	-
183	Phosphorylation	IALYGLGSIPDERLY EEEECCCCCCCHHHH	35.67	-
190	Phosphorylation	SIPDERLYRMFVNKK CCCCHHHHHHHCCCE	13.27	-
196	Acetylation	LYRMFVNKKVTMLRP HHHHHCCCEEEEECC	43.23	7305589
197	Acetylation	YRMFVNKKVTMLRPK HHHHCCCEEEEECCC	37.42	7305601
197	Ubiquitination	YRMFVNKKVTMLRPK HHHHCCCEEEEECCC	37.42	-
254	Phosphorylation	HECKIAPTKNEQQLF CEEEECCCCCCEEEE	37.16	25002506
255	Sumoylation	ECKIAPTKNEQQLFY EEEECCCCCCEEEEE	58.38	28112733
255	Ubiquitination	ECKIAPTKNEQQLFY EEEECCCCCCEEEEE	58.38	-
258	Ubiquitination	IAPTKNEQQLFYISQ ECCCCCCEEEEEECC	55.46	-
262	Phosphorylation	KNEQQLFYISQPGSS CCCEEEEEECCCCCE	14.30	23186163
264	Phosphorylation	EQQLFYISQPGSSVV CEEEEEECCCCCEEE	20.95	19709933
268	Phosphorylation	FYISQPGSSVVTSLS EEECCCCCEEEEECC	27.00	28450419
269	Phosphorylation	YISQPGSSVVTSLSP EECCCCCEEEEECCC	26.90	28450419
272	Phosphorylation	QPGSSVVTSLSPGEA CCCCEEEEECCCHHH	23.07	28450419
273	Phosphorylation	PGSSVVTSLSPGEAV CCCEEEEECCCHHHH	18.42	28450419
275	Phosphorylation	SSVVTSLSPGEAVKK CEEEEECCCHHHHHH	30.53	25159151
282	Ubiquitination	SPGEAVKKHVGLLRI CCHHHHHHHHCEEEE	36.60	-
298	Ubiquitination	GRKMNMHKIPLHTVR CCCCCCCCCCHHHHH	34.94	-
329	Phosphorylation	NPDNPKVTQAIQSFC CCCCHHHHHHHHHHH	20.57	19709933
334	Phosphorylation	KVTQAIQSFCLEKIE HHHHHHHHHHHHHHH	16.29	28555341
339	Ubiquitination	IQSFCLEKIEEMLEN HHHHHHHHHHHHHHH	42.33	-
355	Phosphorylation	ERERLGNSHQPEKPL HHHHHCCCCCCCCCE	23.00	20873877
360	Ubiquitination	GNSHQPEKPLVRLRV CCCCCCCCCEEEEEE	50.78	-
363	Ubiquitination	HQPEKPLVRLRVDYS CCCCCCEEEEEEECC	8.00	-
382	Phosphorylation	PFSVLRFSQKFVDRV CEEEEEEHHHHHHHH	26.48	19709933
384	Acetylation	SVLRFSQKFVDRVAN EEEEEHHHHHHHHCC	46.27	25953088
384	Ubiquitination	SVLRFSQKFVDRVAN EEEEEHHHHHHHHCC	46.27	21890473
384 (in isoform 1)	Ubiquitination	-	46.27	21890473
384 (in isoform 2)	Ubiquitination	-	46.27	21890473
388	Methylation	FSQKFVDRVANPKDI EHHHHHHHHCCHHHH	24.93	115483665
393	Ubiquitination	VDRVANPKDIIHFFR HHHHCCHHHHHHHHH	62.46	21890473
393 (in isoform 1)	Ubiquitination	-	62.46	21890473
393 (in isoform 2)	Ubiquitination	-	62.46	21890473
407	Ubiquitination	RHREQKEKTGEEINF HCHHHHHHCCCCCCC	69.71	-
410	Ubiquitination	EQKEKTGEEINFGKL HHHHHCCCCCCCCCC	62.02	-
416	Acetylation	GEEINFGKLITKPSE CCCCCCCCCEECCCC	32.36	23954790
416	Sumoylation	GEEINFGKLITKPSE CCCCCCCCCEECCCC	32.36	28112733
416	Ubiquitination	GEEINFGKLITKPSE CCCCCCCCCEECCCC	32.36	21890473
416 (in isoform 1)	Ubiquitination	-	32.36	21890473
416 (in isoform 2)	Ubiquitination	-	32.36	21890473
419	Acetylation	INFGKLITKPSEGTT CCCCCCEECCCCCCE	47.54	-
419	Phosphorylation	INFGKLITKPSEGTT CCCCCCEECCCCCCE	47.54	20068231
420	Acetylation	NFGKLITKPSEGTTL CCCCCEECCCCCCEE	39.28	25953088
420	Ubiquitination	NFGKLITKPSEGTTL CCCCCEECCCCCCEE	39.28	-
423	Ubiquitination	KLITKPSEGTTLRVE CCEECCCCCCEEEHH	69.91	-
425	Phosphorylation	ITKPSEGTTLRVEDL EECCCCCCEEEHHHH	20.71	20068231
426	Phosphorylation	TKPSEGTTLRVEDLV ECCCCCCEEEHHHHH	24.35	20068231
434	Ubiquitination	LRVEDLVKQYFQTAE EEHHHHHHHHHHHHH	46.72	21890473
434 (in isoform 1)	Ubiquitination	-	46.72	21890473
434 (in isoform 2)	Ubiquitination	-	46.72	21890473
436	Phosphorylation	VEDLVKQYFQTAEKN HHHHHHHHHHHHHHH	7.61	-
442	Ubiquitination	QYFQTAEKNVQLSLL HHHHHHHHHHHHHHH	61.01	21890473
442 (in isoform 1)	Ubiquitination	-	61.01	21890473
442 (in isoform 2)	Ubiquitination	-	61.01	21890473
447	Phosphorylation	AEKNVQLSLLTERGM HHHHHHHHHHHHCCC	12.30	21406692
450	Phosphorylation	NVQLSLLTERGMGEA HHHHHHHHHCCCHHH	29.00	21406692
464	Ubiquitination	AVQEFVDKEEKDAIE HHHHHCCHHHHHHHH	63.57	-
475	Ubiquitination	DAIEELVKYQLEKTQ HHHHHHHHHHHHHHH	39.65	21890473
475 (in isoform 1)	Ubiquitination	-	39.65	21890473
475 (in isoform 2)	Ubiquitination	-	39.65	21890473
480	Acetylation	LVKYQLEKTQRFLKE HHHHHHHHHHHHHHH	59.56	20167786
480	Ubiquitination	LVKYQLEKTQRFLKE HHHHHHHHHHHHHHH	59.56	-
481	Phosphorylation	VKYQLEKTQRFLKER HHHHHHHHHHHHHHH	18.66	19709933
483	Ubiquitination	YQLEKTQRFLKERHI HHHHHHHHHHHHHHH	44.06	-
486	Ubiquitination	EKTQRFLKERHIDAL HHHHHHHHHHHHHHH	50.41	-
496	Ubiquitination	HIDALEDKIDEEVRR HHHHHHHHHHHHHHH	42.56	-
512	Phosphorylation	RETRQKNTNEEDDEV HHHHHHCCCCHHHHH	51.55	29214152
531	Phosphorylation	TRARALRSQSEESAS HHHHHHHCCCHHHHH	38.62	19709933
533	Phosphorylation	ARALRSQSEESASAF HHHHHCCCHHHHHCC	44.57	26126808
536	Phosphorylation	LRSQSEESASAFSAD HHCCCHHHHHCCCHH	24.38	27251275
538	Phosphorylation	SQSEESASAFSADDL CCCHHHHHCCCHHHH	38.84	27251275
541	Phosphorylation	EESASAFSADDLMSI HHHHHCCCHHHHHCC	30.42	27732954
547	Phosphorylation	FSADDLMSIDLAEQM CCHHHHHCCHHHHHH	21.90	27732954
558	Phosphorylation	AEQMANDSDDSISAA HHHHCCCCCCCHHHH	43.03	30278072
561	Phosphorylation	MANDSDDSISAATNK HCCCCCCCHHHHCCC	24.35	25137130
563	Phosphorylation	NDSDDSISAATNKGR CCCCCCHHHHCCCCC	18.79	30278072
566	Phosphorylation	DDSISAATNKGRGRG CCCHHHHCCCCCCCC	36.86	30278072
570	Methylation	SAATNKGRGRGRGRR HHHCCCCCCCCCCCC	32.99	4689435
572	Methylation	ATNKGRGRGRGRRGG HCCCCCCCCCCCCCC	30.21	4689429
574	Methylation	NKGRGRGRGRRGGRG CCCCCCCCCCCCCCC	33.80	4689439
576	Methylation	GRGRGRGRRGGRGQN CCCCCCCCCCCCCCC	32.48	4689437
577	Methylation	RGRGRGRRGGRGQNS CCCCCCCCCCCCCCC	55.53	4689427
580	Methylation	GRGRRGGRGQNSASR CCCCCCCCCCCCCCC	46.47	4689443
587	Methylation	RGQNSASRGGSQRGR CCCCCCCCCCCCCCC	53.89	4689433
590	Phosphorylation	NSASRGGSQRGRADT CCCCCCCCCCCCCCC	21.38	19709933
590 (in isoform 2)	Phosphorylation	-	21.38	27174698
592	Methylation	ASRGGSQRGRADTGL CCCCCCCCCCCCCCC	37.96	4689431
594	Methylation	RGGSQRGRADTGLET CCCCCCCCCCCCCCC	31.32	4689441
597	Phosphorylation	SQRGRADTGLETSTR CCCCCCCCCCCCCCC	42.56	18212344
598 (in isoform 2)	Phosphorylation	-	23.28	27174698
599 (in isoform 2)	Phosphorylation	-	7.62	27174698
601	Phosphorylation	RADTGLETSTRSRNS CCCCCCCCCCCCCCC	40.20	26434776
602	Phosphorylation	ADTGLETSTRSRNSK CCCCCCCCCCCCCCC	16.67	23401153
603	Phosphorylation	DTGLETSTRSRNSKT CCCCCCCCCCCCCCC	39.83	26434776
604	Methylation	TGLETSTRSRNSKTA CCCCCCCCCCCCCCC	33.13	80701739
609	Acetylation	STRSRNSKTAVSASR CCCCCCCCCCHHHCC	44.01	25953088
613	Phosphorylation	RNSKTAVSASRNMSI CCCCCCHHHCCCHHH	20.33	-
616	Methylation	KTAVSASRNMSIIDA CCCHHHCCCHHHHHH	42.46	115483673
619	Phosphorylation	VSASRNMSIIDAFKS HHHCCCHHHHHHHHH	21.68	25159151
625	Sumoylation	MSIIDAFKSTRQQPS HHHHHHHHHHCCCCC	53.27	-
625	Acetylation	MSIIDAFKSTRQQPS HHHHHHHHHHCCCCC	53.27	26051181
625	Sumoylation	MSIIDAFKSTRQQPS HHHHHHHHHHCCCCC	53.27	28112733
640	Phosphorylation	RNVTTKNYSEVIEVD CCCCCCCHHHEEEEC	14.04	20068231
641	Phosphorylation	NVTTKNYSEVIEVDE CCCCCCHHHEEEECH	34.48	20068231
645 (in isoform 2)	Ubiquitination	-	49.44	21890473
649	Phosphorylation	EVIEVDESDVEEDIF HEEEECHHHCCCCCC	42.36	19664994
658	Phosphorylation	VEEDIFPTTSKTDQR CCCCCCCCCCCCCCC	32.71	29978859
659	Phosphorylation	EEDIFPTTSKTDQRW CCCCCCCCCCCCCCC	28.59	20873877
660	Phosphorylation	EDIFPTTSKTDQRWS CCCCCCCCCCCCCCC	35.72	28176443
662	Phosphorylation	IFPTTSKTDQRWSST CCCCCCCCCCCCCCC	36.81	20068231
667	Phosphorylation	SKTDQRWSSTSSSKI CCCCCCCCCCCCHHH	26.40	20068231
668	Phosphorylation	KTDQRWSSTSSSKIM CCCCCCCCCCCHHHH	25.91	20068231
669	Phosphorylation	TDQRWSSTSSSKIMS CCCCCCCCCCHHHHC	27.41	20068231
670	Phosphorylation	DQRWSSTSSSKIMSQ CCCCCCCCCHHHHCH	34.26	20068231
671	Phosphorylation	QRWSSTSSSKIMSQS CCCCCCCCHHHHCHH	35.42	20068231
672	Phosphorylation	RWSSTSSSKIMSQSQ CCCCCCCHHHHCHHH	26.43	20068231
673	Acetylation	WSSTSSSKIMSQSQV CCCCCCHHHHCHHHH	44.36	25953088
673	Ubiquitination	WSSTSSSKIMSQSQV CCCCCCHHHHCHHHH	44.36	2189047
673 (in isoform 1)	Ubiquitination	-	44.36	21890473
676	Phosphorylation	TSSSKIMSQSQVSKG CCCHHHHCHHHHHCC	30.10	30266825
678	Phosphorylation	SSKIMSQSQVSKGVD CHHHHCHHHHHCCCC	25.83	17525332
681	Phosphorylation	IMSQSQVSKGVDFES HHCHHHHHCCCCCCC	18.96	20164059
688	Phosphorylation	SKGVDFESSEDDDDD HCCCCCCCCCCCCCC	38.73	22167270
689	Phosphorylation	KGVDFESSEDDDDDP CCCCCCCCCCCCCCC	37.54	22167270
700	Phosphorylation	DDDPFMNTSSLRRNR CCCCCCCHHHHHHCC	14.12	22167270
701	Phosphorylation	DDPFMNTSSLRRNRR CCCCCCHHHHHHCCC	23.52	22167270
702	Phosphorylation	DPFMNTSSLRRNRR- CCCCCHHHHHHCCC-	24.69	22167270

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
264	S	Phosphorylation	Kinase	ATM	Q13315	PSP
558	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
561	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
597	T	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
649	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
649	S	Phosphorylation	Kinase	PLK1	P53350	PSP
676	S	Phosphorylation	Kinase	ATM	Q13315	PSP
678	S	Phosphorylation	Kinase	ATM	Q13315	PSP
688	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
688	S	Phosphorylation	Kinase	PLK1	P53350	PSP
689	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	N/A#E4	P03243#Q6VGT3	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MRE11_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 MRE11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	10508516
BLM_HUMAN	BLM	physical	10783165
RAD50_HUMAN	RAD50	physical	10783165
RAD50_HUMAN	RAD50	physical	11504724
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
RAD50_HUMAN	RAD50	physical	8756642
NBN_HUMAN	NBN	physical	9705271
TERF2_HUMAN	TERF2	physical	10888888
RAD50_HUMAN	RAD50	physical	10508516
RAD50_HUMAN	RAD50	physical	19270065
NBN_HUMAN	NBN	physical	19270065
RECQ5_HUMAN	RECQL5	physical	19270065
MDC1_HUMAN	MDC1	physical	12607003
RAD50_HUMAN	RAD50	physical	12607003
NBN_HUMAN	NBN	physical	12607003
ANM1_HUMAN	PRMT1	physical	18285453
NALP2_HUMAN	NLRP2	physical	18285453
RAD50_HUMAN	RAD50	physical	17500065
NBN_HUMAN	NBN	physical	17500065
RAD50_HUMAN	RAD50	physical	15734743
NBN_HUMAN	NBN	physical	15734743
MRE11_HUMAN	MRE11A	physical	15734743
NBN_HUMAN	NBN	physical	22939629
RAD50_HUMAN	RAD50	physical	22939629
TERF2_HUMAN	TERF2	physical	22939629
TE2IP_HUMAN	TERF2IP	physical	22939629
RNF8_HUMAN	RNF8	physical	23115235
CDC45_HUMAN	CDC45	genetic	23390603
DPOLA_HUMAN	POLA1	genetic	23390603
PSF1_HUMAN	GINS1	genetic	23390603
MCM2_HUMAN	MCM2	genetic	23390603
AIDA_HUMAN	AIDA	physical	26344197
CHAP1_HUMAN	CHAMP1	physical	26344197
DRC1_HUMAN	DRC1	physical	26344197
FEN1_HUMAN	FEN1	physical	26344197
GCC2_HUMAN	GCC2	physical	26344197
RAD50_HUMAN	RAD50	physical	26344197
TPR_HUMAN	TPR	physical	26344197
XRCC6_HUMAN	XRCC6	physical	26344197
UBP4_HUMAN	USP4	physical	26455393
RAD50_HUMAN	RAD50	physical	26455393
NBN_HUMAN	NBN	physical	26455393
H31T_HUMAN	HIST3H3	physical	25823024
FEN1_HUMAN	FEN1	genetic	28628639
FANCJ_HUMAN	BRIP1	physical	23530059
RAD50_HUMAN	RAD50	physical	23530059
NBN_HUMAN	NBN	physical	23530059
BRCA1_HUMAN	BRCA1	physical	23530059

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604391	Ataxia-telangiectasia-like disorder 1 (ATLD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MRE11_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-649; SER-688 ANDSER-689, 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 SER-688 AND SER-689, ANDMASS 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-649; SER-688 ANDSER-689, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-689, ANDMASS SPECTROMETRY.	18691976 [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-678, AND MASSSPECTROMETRY.	17525332 [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-688 AND SER-689, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND MASSSPECTROMETRY.	16083285 [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 THR-74; SER-688 AND SER-689,AND MASS SPECTROMETRY.	15302935 [Abstract]