dbPTM

LC7L2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LC7L2_HUMAN
UniProt AC	Q9Y383
Protein Name	Putative RNA-binding protein Luc7-like 2
Gene Name	LUC7L2
Organism	Homo sapiens (Human).
Sequence Length	392
Subcellular Localization	Nucleus speckle. Nucleus, nucleoplasm. Colocalizes with SCNM1 and SNRNP70 in nuclear speckles..
Protein Description	May bind to RNA via its Arg/Ser-rich domain..
Protein Sequence	MSAQAQMRAMLDQLMGTSRDGDTTRQRIKFSDDRVCKSHLLNCCPHDVLSGTRMDLGECLKVHDLALRADYEIASKEQDFFFELDAMDHLQSFIADCDRRTEVAKKRLAETQEEISAEVAAKAERVHELNEEIGKLLAKVEQLGAEGNVEESQKVMDEVEKARAKKREAEEVYRNSMPASSFQQQKLRVCEVCSAYLGLHDNDRRLADHFGGKLHLGFIEIREKLEELKRVVAEKQEKRNQERLKRREEREREEREKLRRSRSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSRERSKRRSSKERFRDQDLASCDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Sulfoxidation	AQAQMRAMLDQLMGT HHHHHHHHHHHHHCC	2.75	21406390
15	Sulfoxidation	RAMLDQLMGTSRDGD HHHHHHHHCCCCCCC	4.59	30846556
17	Phosphorylation	MLDQLMGTSRDGDTT HHHHHHCCCCCCCCH	13.46	29255136
17 (in isoform 2)	Phosphorylation	-	13.46	23322592
18	Phosphorylation	LDQLMGTSRDGDTTR HHHHHCCCCCCCCHH	23.73	29255136
23	Phosphorylation	GTSRDGDTTRQRIKF CCCCCCCCHHHHEEC	29.43	26846344
24	Phosphorylation	TSRDGDTTRQRIKFS CCCCCCCHHHHEECC	29.55	26846344
26	Ubiquitination	RDGDTTRQRIKFSDD CCCCCHHHHEECCCC	49.73	32015554
28	Ubiquitination	GDTTRQRIKFSDDRV CCCHHHHEECCCCHH	3.90	32015554
29	Acetylation	DTTRQRIKFSDDRVC CCHHHHEECCCCHHH	40.79	25953088
29	Ubiquitination	DTTRQRIKFSDDRVC CCHHHHEECCCCHHH	40.79	33845483
31	Phosphorylation	TRQRIKFSDDRVCKS HHHHEECCCCHHHHH	33.33	20873877
34	Methylation	RIKFSDDRVCKSHLL HEECCCCHHHHHHHH	40.50	115482421
34	Ubiquitination	RIKFSDDRVCKSHLL HEECCCCHHHHHHHH	40.50	29967540
36	Ubiquitination	KFSDDRVCKSHLLNC ECCCCHHHHHHHHCC	3.79	29967540
37	Ubiquitination	FSDDRVCKSHLLNCC CCCCHHHHHHHHCCC	37.74	29967540
38	Phosphorylation	SDDRVCKSHLLNCCP CCCHHHHHHHHCCCC	17.78	24247654
40	Ubiquitination	DRVCKSHLLNCCPHD CHHHHHHHHCCCCCC	4.79	21890473
40 (in isoform 1)	Ubiquitination	-	4.79	21890473
43	Glutathionylation	CKSHLLNCCPHDVLS HHHHHHCCCCCCHHC	3.73	22555962
54	Sulfoxidation	DVLSGTRMDLGECLK CHHCCCCCCHHHHHH	5.11	21406390
58	Ubiquitination	GTRMDLGECLKVHDL CCCCCHHHHHHHHHH	43.93	32015554
60	Ubiquitination	RMDLGECLKVHDLAL CCCHHHHHHHHHHHH	5.89	32015554
61	Acetylation	MDLGECLKVHDLALR CCHHHHHHHHHHHHH	49.54	25953088
61	Ubiquitination	MDLGECLKVHDLALR CCHHHHHHHHHHHHH	49.54	32015554
102	Ubiquitination	ADCDRRTEVAKKRLA HHCHHHHHHHHHHHH	38.37	24816145
104	Ubiquitination	CDRRTEVAKKRLAET CHHHHHHHHHHHHHH	12.86	24816145
105	Ubiquitination	DRRTEVAKKRLAETQ HHHHHHHHHHHHHHH	43.53	24816145
111	Phosphorylation	AKKRLAETQEEISAE HHHHHHHHHHHHHHH	35.36	17525332
119	Acetylation	QEEISAEVAAKAERV HHHHHHHHHHHHHHH	6.67	19608861
119	Ubiquitination	QEEISAEVAAKAERV HHHHHHHHHHHHHHH	6.67	32015554
121	Acetylation	EISAEVAAKAERVHE HHHHHHHHHHHHHHH	19.43	19608861
121	Ubiquitination	EISAEVAAKAERVHE HHHHHHHHHHHHHHH	19.43	32015554
122	Acetylation	ISAEVAAKAERVHEL HHHHHHHHHHHHHHH	40.83	19608861
122	Ubiquitination	ISAEVAAKAERVHEL HHHHHHHHHHHHHHH	40.83	32015554
132	Acetylation	RVHELNEEIGKLLAK HHHHHHHHHHHHHHH	56.84	19608861
132	Ubiquitination	RVHELNEEIGKLLAK HHHHHHHHHHHHHHH	56.84	29967540
134	Acetylation	HELNEEIGKLLAKVE HHHHHHHHHHHHHHH	20.17	19608861
134	Ubiquitination	HELNEEIGKLLAKVE HHHHHHHHHHHHHHH	20.17	29967540
135	Acetylation	ELNEEIGKLLAKVEQ HHHHHHHHHHHHHHH	46.09	19608861
135	Ubiquitination	ELNEEIGKLLAKVEQ HHHHHHHHHHHHHHH	46.09	19608861
136	Ubiquitination	LNEEIGKLLAKVEQL HHHHHHHHHHHHHHH	4.79	32015554
138	Ubiquitination	EEIGKLLAKVEQLGA HHHHHHHHHHHHHCC	25.04	32015554
138 (in isoform 2)	Ubiquitination	-	25.04	21906983
139	Sumoylation	EIGKLLAKVEQLGAE HHHHHHHHHHHHCCC	46.39	-
139	Acetylation	EIGKLLAKVEQLGAE HHHHHHHHHHHHCCC	46.39	26051181
139	Sumoylation	EIGKLLAKVEQLGAE HHHHHHHHHHHHCCC	46.39	-
139	Ubiquitination	EIGKLLAKVEQLGAE HHHHHHHHHHHHCCC	46.39	32015554
152	Phosphorylation	AEGNVEESQKVMDEV CCCCHHHHHHHHHHH	23.07	21601212
156	Sulfoxidation	VEESQKVMDEVEKAR HHHHHHHHHHHHHHH	4.72	21406390
161	Acetylation	KVMDEVEKARAKKRE HHHHHHHHHHHHHHH	48.63	23749302
161	Ubiquitination	KVMDEVEKARAKKRE HHHHHHHHHHHHHHH	48.63	-
166	Methylation	VEKARAKKREAEEVY HHHHHHHHHHHHHHH	55.26	23748837
176	Phosphorylation	AEEVYRNSMPASSFQ HHHHHHHCCCCHHHH	19.69	28555341
183	Ubiquitination	SMPASSFQQQKLRVC CCCCHHHHHHHHHHH	46.90	24816145
185	Ubiquitination	PASSFQQQKLRVCEV CCHHHHHHHHHHHHH	35.65	24816145
186	Sumoylation	ASSFQQQKLRVCEVC CHHHHHHHHHHHHHH	33.64	-
186	Acetylation	ASSFQQQKLRVCEVC CHHHHHHHHHHHHHH	33.64	82979627
186	Sumoylation	ASSFQQQKLRVCEVC CHHHHHHHHHHHHHH	33.64	-
186	Ubiquitination	ASSFQQQKLRVCEVC CHHHHHHHHHHHHHH	33.64	24816145
205 (in isoform 1)	Ubiquitination	-	36.77	21890473
213	Acetylation	LADHFGGKLHLGFIE HHHHHCCCEEECHHH	32.86	25953088
221	Ubiquitination	LHLGFIEIREKLEEL EEECHHHHHHHHHHH	6.19	24816145
223	Ubiquitination	LGFIEIREKLEELKR ECHHHHHHHHHHHHH	68.59	24816145
224	Ubiquitination	GFIEIREKLEELKRV CHHHHHHHHHHHHHH	51.88	24816145
226	Acetylation	IEIREKLEELKRVVA HHHHHHHHHHHHHHH	72.80	19413330
228	Acetylation	IREKLEELKRVVAEK HHHHHHHHHHHHHHH	2.91	19413330
229	Acetylation	REKLEELKRVVAEKQ HHHHHHHHHHHHHHH	46.56	19413330
232	Ubiquitination	LEELKRVVAEKQEKR HHHHHHHHHHHHHHH	7.08	24816145
234	Ubiquitination	ELKRVVAEKQEKRNQ HHHHHHHHHHHHHHH	43.60	24816145
235	Ubiquitination	LKRVVAEKQEKRNQE HHHHHHHHHHHHHHH	54.76	24816145
237	Ubiquitination	RVVAEKQEKRNQERL HHHHHHHHHHHHHHH	66.12	24816145
238	Ubiquitination	VVAEKQEKRNQERLK HHHHHHHHHHHHHHH	54.90	24816145
261	Phosphorylation	EREKLRRSRSHSKNP HHHHHHHHHHCCCCC	31.53	23532336
266	Hydroxylation	RRSRSHSKNPKRSRS HHHHHCCCCCCHHHH	72.37	19574390
269	Hydroxylation	RSHSKNPKRSRSREH HHCCCCCCHHHHHHH	72.84	19574390
271	Phosphorylation	HSKNPKRSRSREHRR CCCCCCHHHHHHHHH	40.51	20068231
273	Phosphorylation	KNPKRSRSREHRRHR CCCCHHHHHHHHHHH	43.18	27422710
281	Phosphorylation	REHRRHRSRSMSRER HHHHHHHHHHHHHHH	23.68	30576142
283	Phosphorylation	HRRHRSRSMSRERKR HHHHHHHHHHHHHHH	23.50	30576142
285	Phosphorylation	RHRSRSMSRERKRRT HHHHHHHHHHHHHHH	32.03	20068231
305	Phosphorylation	EKRHRHRSRSSSRSR HHHHHHHHCCHHHHH	30.32	20068231
307	Phosphorylation	RHRHRSRSSSRSRSR HHHHHHCCHHHHHHH	33.63	20068231
308	Phosphorylation	HRHRSRSSSRSRSRS HHHHHCCHHHHHHHH	28.76	20068231
309	Phosphorylation	RHRSRSSSRSRSRSH HHHHCCHHHHHHHHH	35.21	20068231
322	Phosphorylation	SHQRSRHSSRDRSRE HHHHHHHHHHHHHHH	26.42	20068231
323	Phosphorylation	HQRSRHSSRDRSRER HHHHHHHHHHHHHHH	31.88	20068231
327	Phosphorylation	RHSSRDRSRERSKRR HHHHHHHHHHHHHHH	42.66	20068231
331	Phosphorylation	RDRSRERSKRRSSKE HHHHHHHHHHHHHHH	26.26	26074081
335	Phosphorylation	RERSKRRSSKERFRD HHHHHHHHHHHHHHH	50.20	26074081
336	Phosphorylation	ERSKRRSSKERFRDQ HHHHHHHHHHHHHHH	36.40	26074081
344	Phosphorylation	KERFRDQDLASCDRD HHHHHHHHHHHCCCC	48.79	32645325
346	Phosphorylation	RFRDQDLASCDRDRS HHHHHHHHHCCCCCC	19.19	32645325
347	Phosphorylation	FRDQDLASCDRDRSS HHHHHHHHCCCCCCC	24.69	29255136
348	Glutathionylation	RDQDLASCDRDRSSR HHHHHHHCCCCCCCC	4.07	22555962
353	Phosphorylation	ASCDRDRSSRDRSPR HHCCCCCCCCCCCCC	33.73	23401153
354	Phosphorylation	SCDRDRSSRDRSPRD HCCCCCCCCCCCCCC	38.81	29255136
358	Phosphorylation	DRSSRDRSPRDRDRK CCCCCCCCCCCCCHH	28.69	30576142
370	Phosphorylation	DRKDKKRSYESANGR CHHHHHHHHHHCCCC	41.97	30576142
371	Phosphorylation	RKDKKRSYESANGRS HHHHHHHHHHCCCCC	20.24	26074081
373	Phosphorylation	DKKRSYESANGRSED HHHHHHHHCCCCCCC	20.85	26074081
378	Phosphorylation	YESANGRSEDRRSSE HHHCCCCCCCCCCHH	45.29	23911959
381	Phosphorylation	ANGRSEDRRSSEERE CCCCCCCCCCHHHHH	36.01	33259812
383	Phosphorylation	GRSEDRRSSEEREAG CCCCCCCCHHHHHHC	42.89	25159151
384	Phosphorylation	RSEDRRSSEEREAGE CCCCCCCHHHHHHCC	41.48	25159151

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
Oops, there are no upstream regulatory protein records of LC7L2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LC7L2_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 LC7L2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTCD3_HUMAN	PTCD3	physical	16169070
LC7L2_HUMAN	LUC7L2	physical	16169070
PEA15_HUMAN	PEA15	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
PTN_HUMAN	PTN	physical	16169070
HAP1_HUMAN	HAP1	physical	15383276
A4_HUMAN	APP	physical	21832049
RL19_HUMAN	RPL19	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
SYCC_HUMAN	CARS	physical	22863883
HS74L_HUMAN	HSPA4L	physical	22863883
GLYM_HUMAN	SHMT2	physical	22863883
LARP7_HUMAN	LARP7	physical	26186194
ZCH18_HUMAN	ZC3H18	physical	26186194
NKAP_HUMAN	NKAP	physical	26186194
BCLF1_HUMAN	BCLAF1	physical	26186194
TR150_HUMAN	THRAP3	physical	26186194
PRP4B_HUMAN	PRPF4B	physical	26186194
CCDC9_HUMAN	CCDC9	physical	26186194
ACINU_HUMAN	ACIN1	physical	26186194
NCBP3_HUMAN	C17orf85	physical	26186194
C1QBP_HUMAN	C1QBP	physical	26186194
SRPK1_HUMAN	SRPK1	physical	26186194
SRPK2_HUMAN	SRPK2	physical	26186194
PABP4_HUMAN	PABPC4	physical	26186194
GPTC8_HUMAN	GPATCH8	physical	26186194
U2AF2_HUMAN	U2AF2	physical	26186194
PAIP1_HUMAN	PAIP1	physical	26186194
UBE2O_HUMAN	UBE2O	physical	26186194
RBM22_HUMAN	RBM22	physical	26186194
MEPCE_HUMAN	MEPCE	physical	26186194
PININ_HUMAN	PNN	physical	26186194
LARP1_HUMAN	LARP1	physical	26186194
LAR1B_HUMAN	LARP1B	physical	26186194
SRSF1_HUMAN	SRSF1	physical	26186194
RNPS1_HUMAN	RNPS1	physical	26186194
SNW1_HUMAN	SNW1	physical	26186194
CLASR_HUMAN	CLASRP	physical	26186194
JMJD6_HUMAN	JMJD6	physical	26186194
PAI2B_HUMAN	PAIP2B	physical	26186194
SRRT_HUMAN	SRRT	physical	26186194
CSK21_HUMAN	CSNK2A1	physical	26186194
CCD12_HUMAN	CCDC12	physical	26186194
LC7L3_HUMAN	LUC7L3	physical	26186194
MOV10_HUMAN	MOV10	physical	26186194
PRP17_HUMAN	CDC40	physical	26186194
DDX46_HUMAN	DDX46	physical	26186194
SF3A1_HUMAN	SF3A1	physical	26186194
ZC3HE_HUMAN	ZC3H14	physical	26186194
CPSF6_HUMAN	CPSF6	physical	26186194
SNR27_HUMAN	SNRNP27	physical	26186194
CLK3_HUMAN	CLK3	physical	26186194
RED_HUMAN	IK	physical	26186194
CASC3_HUMAN	CASC3	physical	26186194
FA98A_HUMAN	FAM98A	physical	26186194
FRIL_HUMAN	FTL	physical	26186194
RU17_HUMAN	SNRNP70	physical	26186194
MKRN2_HUMAN	MKRN2	physical	26186194
SCAFB_HUMAN	SCAF11	physical	26186194
MKRN1_HUMAN	MKRN1	physical	26186194
TRA2B_HUMAN	TRA2B	physical	26186194
SRSF8_HUMAN	SRSF8	physical	26186194
SRSF7_HUMAN	SRSF7	physical	26186194
SRS12_HUMAN	SRSF12	physical	26186194
SRS10_HUMAN	SRSF10	physical	26186194
SREK1_HUMAN	SREK1	physical	26186194
CLK2_HUMAN	CLK2	physical	26186194
HNRPR_HUMAN	HNRNPR	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
U520_HUMAN	SNRNP200	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
RUXE_HUMAN	SNRPE	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
U2AF1_HUMAN	U2AF1	physical	26344197
JMJD6_HUMAN	JMJD6	physical	28514442
GPTC8_HUMAN	GPATCH8	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
CCDC9_HUMAN	CCDC9	physical	28514442
PAI2B_HUMAN	PAIP2B	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
PININ_HUMAN	PNN	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
ZCH18_HUMAN	ZC3H18	physical	28514442
CLK3_HUMAN	CLK3	physical	28514442
SRSF8_HUMAN	SRSF8	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
ZC3HE_HUMAN	ZC3H14	physical	28514442
CLK2_HUMAN	CLK2	physical	28514442
DDX46_HUMAN	DDX46	physical	28514442
PRP17_HUMAN	CDC40	physical	28514442
SCAFB_HUMAN	SCAF11	physical	28514442
MEPCE_HUMAN	MEPCE	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
FRIL_HUMAN	FTL	physical	28514442
SRSF1_HUMAN	SRSF1	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
SRPK2_HUMAN	SRPK2	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
MKRN1_HUMAN	MKRN1	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
RED_HUMAN	IK	physical	28514442
MOV10_HUMAN	MOV10	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
SRPK1_HUMAN	SRPK1	physical	28514442
SNW1_HUMAN	SNW1	physical	28514442
UBE2O_HUMAN	UBE2O	physical	28514442
TRA2B_HUMAN	TRA2B	physical	28514442
PPIL4_HUMAN	PPIL4	physical	28514442
ISY1_HUMAN	ISY1	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442

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 LC7L2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND MASS SPECTROMETRY.	19608861 [Abstract]
Hydroxylation
Reference	PubMed
"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associatedwith RNA splicing."; Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,Boettger A.; Science 325:90-93(2009). Cited for: HYDROXYLATION AT LYS-266 AND LYS-269, AND MUTAGENESIS OF LYS-266 ANDLYS-269.	19574390 [Abstract]
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-18, AND MASSSPECTROMETRY.	19690332 [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-18; SER-383 AND SER-384,AND MASS SPECTROMETRY.	18669648 [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 THR-17; SER-18; SER-354 ANDSER-358, AND MASS SPECTROMETRY.	17287340 [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-358, AND MASSSPECTROMETRY.	17081983 [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 THR-111, AND MASSSPECTROMETRY.	17525332 [Abstract]