dbPTM

TOPB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOPB1_HUMAN
UniProt AC	Q92547
Protein Name	DNA topoisomerase 2-binding protein 1
Gene Name	TOPBP1
Organism	Homo sapiens (Human).
Sequence Length	1522
Subcellular Localization	Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Chromosome. Detected on unpaired autosomes in meiotic prophase cells. Detected on X and Y chromosomes during later stages of prophase.
Protein Description	Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double-stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR. [PubMed: 16530042]
Protein Sequence	MSRNDKEPFFVKFLKSSDNSKCFFKALESIKEFQSEEYLQIITEEEALKIKENDRSLYICDPFSGVVFDHLKKLGCRIVGPQVVIFCMHHQRCVPRAEHPVYNMVMSDVTISCTSLEKEKREEVHKYVQMMGGRVYRDLNVSVTHLIAGEVGSKKYLVAANLKKPILLPSWIKTLWEKSQEKKITRYTDINMEDFKCPIFLGCIICVTGLCGLDRKEVQQLTVKHGGQYMGQLKMNECTHLIVQEPKGQKYECAKRWNVHCVTTQWFFDSIEKGFCQDESIYKTEPRPEAKTMPNSSTPTSQINTIDSRTLSDVSNISNINASCVSESICNSLNSKLEPTLENLENLDVSAFQAPEDLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDELKQFWNKSAHRPHVVGAKWLLECFSKGYMLSEEPYIHANYQPVEIPVSHKPESKAALLKKKNSSFSKKDFAPSEKHEQADEDLLSQYENGSSTVVEAKTSEARPFNDSTHAEPLNDSTHISLQEENQSSVSHCVPDVSTITEEGLFSQKSFLVLGFSNENESNIANIIKENAGKIMSLLSRTVADYAVVPLLGCEVEATVGEVVTNTWLVTCIDYQTLFDPKSNPLFTPVPVMTGMTPLEDCVISFSQCAGAEKESLTFLANLLGASVQEYFVRKSNAKKGMFASTHLILKERGGSKYEAAKKWNLPAVTIAWLLETARTGKRADESHFLIENSTKEERSLETEITNGINLNSDTAEHPGTRLQTHRKTVVTPLDMNRFQSKAFRAVVSQHARQVAASPAVGQPLQKEPSLHLDTPSKFLSKDKLFKPSFDVKDALAALETPGRPSQQKRKPSTPLSEVIVKNLQLALANSSRNAVALSASPQLKEAQSEKEEAPKPLHKVVVCVSKKLSKKQSELNGIAASLGADYRWSFDETVTHFIYQGRPNDTNREYKSVKERGVHIVSEHWLLDCAQECKHLPESLYPHTYNPKMSLDISAVQDGRLCNSRLLSAVSSTKDDEPDPLILEENDVDNMATNNKESAPSNGSGKNDSKGVLTQTLEMRENFQKQLQEIMSATSIVKPQGQRTSLSRSGCNSASSTPDSTRSARSGRSRVLEALRQSRQTVPDVNTEPSQNEQIIWDDPTAREERARLASNLQWPSCPTQYSELQVDIQNLEDSPFQKPLHDSEIAKQAVCDPGNIRVTEAPKHPISEELETPIKDSHLIPTPQAPSIAFPLANPPVAPHPREKIITIEETHEELKKQYIFQLSSLNPQERIDYCHLIEKLGGLVIEKQCFDPTCTHIVVGHPLRNEKYLASVAAGKWVLHRSYLEACRTAGHFVQEEDYEWGSSSILDVLTGINVQQRRLALAAMRWRKKIQQRQESGIVEGAFSGWKVILHVDQSREAGFKRLLQSGGAKVLPGHSVPLFKEATHLFSDLNKLKPDDSGVNIAEAAAQNVYCLRTEYIADYLMQESPPHVENYCLPEAISFIQNNKELGTGLSQKRKAPTEKNKIKRPRVH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MSRNDKEPFFVKF --CCCCCCCCCHHHH	71.48	25953088
6	Ubiquitination	--MSRNDKEPFFVKF --CCCCCCCCCHHHH	71.48	-
15	Ubiquitination	PFFVKFLKSSDNSKC CCHHHHHCCCCCCHH	51.55	-
16	Phosphorylation	FFVKFLKSSDNSKCF CHHHHHCCCCCCHHH	45.10	30387612
21	Acetylation	LKSSDNSKCFFKALE HCCCCCCHHHHHHHH	41.12	26051181
21	Ubiquitination	LKSSDNSKCFFKALE HCCCCCCHHHHHHHH	41.12	-
25	Acetylation	DNSKCFFKALESIKE CCCHHHHHHHHHHHH	31.63	25953088
31	Ubiquitination	FKALESIKEFQSEEY HHHHHHHHHHCCHHH	62.85	-
72	Acetylation	GVVFDHLKKLGCRIV CCHHHHHHHHCCEEE	42.40	25953088
72	Ubiquitination	GVVFDHLKKLGCRIV CCHHHHHHHHCCEEE	42.40	-
127	Phosphorylation	KREEVHKYVQMMGGR HHHHHHHHHHHHCCE	4.88	22817900
142	Phosphorylation	VYRDLNVSVTHLIAG EECCCCEEEEEEECC	21.89	20068231
144	Phosphorylation	RDLNVSVTHLIAGEV CCCCEEEEEEECCCC	11.94	20068231
153	Phosphorylation	LIAGEVGSKKYLVAA EECCCCCCCEEEEEC	31.02	-
155	Ubiquitination	AGEVGSKKYLVAANL CCCCCCCEEEEECCC	45.58	-
163	Ubiquitination	YLVAANLKKPILLPS EEEECCCCCCCCCHH	57.20	-
164	Ubiquitination	LVAANLKKPILLPSW EEECCCCCCCCCHHH	40.22	-
178	Ubiquitination	WIKTLWEKSQEKKIT HHHHHHHHHHHHCCE	45.95	-
185	Phosphorylation	KSQEKKITRYTDINM HHHHHCCEECCCCCH	26.88	27251275
187	Phosphorylation	QEKKITRYTDINMED HHHCCEECCCCCHHH	10.50	27251275
188	Phosphorylation	EKKITRYTDINMEDF HHCCEECCCCCHHHC	27.41	27251275
224	Ubiquitination	EVQQLTVKHGGQYMG HHHHHEEECCCEEEE	31.15	21890473
224	Ubiquitination	EVQQLTVKHGGQYMG HHHHHEEECCCEEEE	31.15	21890473
234	Ubiquitination	GQYMGQLKMNECTHL CEEEEEEECCCCCEE	31.62	-
247	Ubiquitination	HLIVQEPKGQKYECA EEEEECCCCCCEEHH	73.54	-
283	Acetylation	CQDESIYKTEPRPEA CCCCCCCCCCCCCCC	44.75	26051181
283	Ubiquitination	CQDESIYKTEPRPEA CCCCCCCCCCCCCCC	44.75	-
291	Ubiquitination	TEPRPEAKTMPNSST CCCCCCCCCCCCCCC	43.63	-
292	Phosphorylation	EPRPEAKTMPNSSTP CCCCCCCCCCCCCCC	44.93	28450419
296	Phosphorylation	EAKTMPNSSTPTSQI CCCCCCCCCCCHHHH	29.71	28450419
297	Phosphorylation	AKTMPNSSTPTSQIN CCCCCCCCCCHHHHC	45.08	28450419
298	Phosphorylation	KTMPNSSTPTSQINT CCCCCCCCCHHHHCC	30.33	17525332
300	Phosphorylation	MPNSSTPTSQINTID CCCCCCCHHHHCCCC	33.09	28450419
301	Phosphorylation	PNSSTPTSQINTIDS CCCCCCHHHHCCCCC	30.21	17525332
305	Phosphorylation	TPTSQINTIDSRTLS CCHHHHCCCCCCCHH	27.99	25850435
308	Phosphorylation	SQINTIDSRTLSDVS HHHCCCCCCCHHHHH	24.26	24247654
340	Phosphorylation	LNSKLEPTLENLENL HHHCCHHHHHHHHCC	37.01	28464451
350	Phosphorylation	NLENLDVSAFQAPED HHHCCCCCCCCCCHH	24.04	25159151
370	Phosphorylation	RIYLCGFSGRKLDKL EEEECCCCCCHHHHH	23.99	25159151
397	Phosphorylation	NQLNEDVTHVIVGDY HHCCCCCEEEEECCC	23.81	22210691
404	Phosphorylation	THVIVGDYDDELKQF EEEEECCCCHHHHHH	21.26	22210691
414	Ubiquitination	ELKQFWNKSAHRPHV HHHHHHHHCCCCCCC	39.35	-
471	Phosphorylation	LLKKKNSSFSKKDFA HHHHCCCCCCCCCCC	42.82	24719451
482	Acetylation	KDFAPSEKHEQADED CCCCCCHHHHHHCHH	57.70	26051181
492	Phosphorylation	QADEDLLSQYENGSS HHCHHHHHHHHCCCC	37.70	17525332
494	Phosphorylation	DEDLLSQYENGSSTV CHHHHHHHHCCCCEE	14.16	23186163
498	Phosphorylation	LSQYENGSSTVVEAK HHHHHCCCCEEEEEE	34.12	29523821
499	Phosphorylation	SQYENGSSTVVEAKT HHHHCCCCEEEEEEC	26.98	29523821
500	Phosphorylation	QYENGSSTVVEAKTS HHHCCCCEEEEEECC	30.21	23186163
554	Phosphorylation	ITEEGLFSQKSFLVL CCCCCCCCCCEEEEE	41.56	22817900
581	Acetylation	IIKENAGKIMSLLSR HHHHHHHHHHHHHHH	32.59	19608861
584	Phosphorylation	ENAGKIMSLLSRTVA HHHHHHHHHHHHHHC	29.63	24719451
587	Phosphorylation	GKIMSLLSRTVADYA HHHHHHHHHHHCCCC	31.06	24719451
618	Phosphorylation	VTNTWLVTCIDYQTL CCCEEEEEEEEHHHC	11.11	-
734	Phosphorylation	TGKRADESHFLIENS HCCCCCHHCEEEECC	21.78	28555341
741	Phosphorylation	SHFLIENSTKEERSL HCEEEECCCHHHHCC	28.24	-
742	Phosphorylation	HFLIENSTKEERSLE CEEEECCCHHHHCCH	54.80	-
743	Ubiquitination	FLIENSTKEERSLET EEEECCCHHHHCCHH	58.35	-
747	Phosphorylation	NSTKEERSLETEITN CCCHHHHCCHHHHCC	33.56	25159151
753	Phosphorylation	RSLETEITNGINLNS HCCHHHHCCCCCCCC	22.59	28555341
776	Phosphorylation	RLQTHRKTVVTPLDM CCEECCCEEECCCCH	21.84	22199227
779	Phosphorylation	THRKTVVTPLDMNRF ECCCEEECCCCHHHH	17.50	25159151
788	Phosphorylation	LDMNRFQSKAFRAVV CCHHHHHHHHHHHHH	24.20	26074081
789	Ubiquitination	DMNRFQSKAFRAVVS CHHHHHHHHHHHHHH	40.54	-
805	Phosphorylation	HARQVAASPAVGQPL HHHHHHCCCCCCCCC	12.03	25159151
817	Phosphorylation	QPLQKEPSLHLDTPS CCCCCCCCCCCCCCH	29.52	29255136
822	Phosphorylation	EPSLHLDTPSKFLSK CCCCCCCCCHHHCCC	35.50	29255136
824	Phosphorylation	SLHLDTPSKFLSKDK CCCCCCCHHHCCCCC	37.83	29255136
834	Acetylation	LSKDKLFKPSFDVKD CCCCCCCCCCCCHHH	50.63	25953088
836	Phosphorylation	KDKLFKPSFDVKDAL CCCCCCCCCCHHHHH	34.37	23186163
840	Ubiquitination	FKPSFDVKDALAALE CCCCCCHHHHHHHHC	38.84	-
848	Phosphorylation	DALAALETPGRPSQQ HHHHHHCCCCCCCCC	31.71	30266825
853	Phosphorylation	LETPGRPSQQKRKPS HCCCCCCCCCCCCCC	43.83	30266825
856	Ubiquitination	PGRPSQQKRKPSTPL CCCCCCCCCCCCCCH	55.54	-
860	Phosphorylation	SQQKRKPSTPLSEVI CCCCCCCCCCHHHHH	45.77	25159151
861	Phosphorylation	QQKRKPSTPLSEVIV CCCCCCCCCHHHHHH	36.45	25159151
864	Phosphorylation	RKPSTPLSEVIVKNL CCCCCCHHHHHHHHH	30.90	25159151
878	Phosphorylation	LQLALANSSRNAVAL HHHHHHCCCCCCHHH	25.68	25159151
879	Phosphorylation	QLALANSSRNAVALS HHHHHCCCCCCHHHC	29.39	25159151
886	Phosphorylation	SRNAVALSASPQLKE CCCCHHHCCCHHHHH	19.57	30266825
888	Phosphorylation	NAVALSASPQLKEAQ CCHHHCCCHHHHHHH	15.14	22167270
921	Phosphorylation	KKLSKKQSELNGIAA HHHCHHHHHHHHHHH	53.59	22210691
998	Phosphorylation	HTYNPKMSLDISAVQ CCCCCCCCEECHHHC	29.08	29396449
1002	Phosphorylation	PKMSLDISAVQDGRL CCCCEECHHHCCCCC	23.27	25159151
1012	Phosphorylation	QDGRLCNSRLLSAVS CCCCCCCHHHHHHHH	24.25	18491316
1016	Phosphorylation	LCNSRLLSAVSSTKD CCCHHHHHHHHCCCC	31.08	25159151
1019	Phosphorylation	SRLLSAVSSTKDDEP HHHHHHHHCCCCCCC	31.82	28674419
1020	Phosphorylation	RLLSAVSSTKDDEPD HHHHHHHCCCCCCCC	32.64	26270265
1021	Phosphorylation	LLSAVSSTKDDEPDP HHHHHHCCCCCCCCC	30.87	26270265
1058	Sumoylation	GSGKNDSKGVLTQTL CCCCCCCCCHHHHHH	56.77	-
1058	Sumoylation	GSGKNDSKGVLTQTL CCCCCCCCCHHHHHH	56.77	-
1058	Ubiquitination	GSGKNDSKGVLTQTL CCCCCCCCCHHHHHH	56.77	-
1062	Phosphorylation	NDSKGVLTQTLEMRE CCCCCHHHHHHHHHH	19.66	17525332
1064	Phosphorylation	SKGVLTQTLEMRENF CCCHHHHHHHHHHHH	21.32	28188228
1082	Phosphorylation	LQEIMSATSIVKPQG HHHHHHHHCCCCCCC	16.22	28555341
1083	Phosphorylation	QEIMSATSIVKPQGQ HHHHHHHCCCCCCCC	25.71	28555341
1093	Phosphorylation	KPQGQRTSLSRSGCN CCCCCCCCCCCCCCC	26.91	-
1095	Phosphorylation	QGQRTSLSRSGCNSA CCCCCCCCCCCCCCC	24.94	22798277
1126	Phosphorylation	VLEALRQSRQTVPDV HHHHHHHHCCCCCCC	21.66	20860994
1129	Phosphorylation	ALRQSRQTVPDVNTE HHHHHCCCCCCCCCC	32.66	23312004
1135	Phosphorylation	QTVPDVNTEPSQNEQ CCCCCCCCCCCCCCC	49.47	29523821
1138	Phosphorylation	PDVNTEPSQNEQIIW CCCCCCCCCCCCCCC	39.13	17525332
1149	Phosphorylation	QIIWDDPTAREERAR CCCCCCCCHHHHHHH	45.39	23312004
1159	Phosphorylation	EERARLASNLQWPSC HHHHHHHHHCCCCCC	42.54	19477925
1170	Phosphorylation	WPSCPTQYSELQVDI CCCCCCCCEEEEEEH	13.44	28122231
1171	Phosphorylation	PSCPTQYSELQVDIQ CCCCCCCEEEEEEHH	23.24	28122231
1183	Phosphorylation	DIQNLEDSPFQKPLH EHHCCCCCCCCCCCC	20.45	26074081
1192	Phosphorylation	FQKPLHDSEIAKQAV CCCCCCCHHHHHHHH	21.83	25159151
1216	Phosphorylation	EAPKHPISEELETPI CCCCCCCCCCCCCCC	29.48	22199227
1221	Phosphorylation	PISEELETPIKDSHL CCCCCCCCCCCCCCC	42.83	25159151
1226	Phosphorylation	LETPIKDSHLIPTPQ CCCCCCCCCCCCCCC	18.39	29523821
1231	Phosphorylation	KDSHLIPTPQAPSIA CCCCCCCCCCCCCEE	22.50	25159151
1236	Phosphorylation	IPTPQAPSIAFPLAN CCCCCCCCEEEECCC	29.57	29523821
1253	Ubiquitination	VAPHPREKIITIEET CCCCCCHHCEEEHHH	40.46	-
1256	Phosphorylation	HPREKIITIEETHEE CCCHHCEEEHHHHHH	26.30	23403867
1260	Phosphorylation	KIITIEETHEELKKQ HCEEEHHHHHHHHHH	23.07	23403867
1265	Ubiquitination	EETHEELKKQYIFQL HHHHHHHHHHHHHHH	40.90	-
1283	Phosphorylation	NPQERIDYCHLIEKL CHHHHHHHHHHHHHH	4.57	29396449
1289	Ubiquitination	DYCHLIEKLGGLVIE HHHHHHHHHCCEEEE	45.50	-
1297	Acetylation	LGGLVIEKQCFDPTC HCCEEEEEECCCCCC	41.04	26051181
1297	Ubiquitination	LGGLVIEKQCFDPTC HCCEEEEEECCCCCC	41.04	-
1317	Ubiquitination	GHPLRNEKYLASVAA CCCCCCHHHHHHHHC	49.46	-
1412	Methylation	QSREAGFKRLLQSGG CCHHHHHHHHHHCCC	41.02	-
1421	Ubiquitination	LLQSGGAKVLPGHSV HHHCCCCEECCCCCC	47.80	21890473
1421	Ubiquitination	LLQSGGAKVLPGHSV HHHCCCCEECCCCCC	47.80	21890473
1432	Ubiquitination	GHSVPLFKEATHLFS CCCCCHHHHHHHHHH	54.87	-
1439	Phosphorylation	KEATHLFSDLNKLKP HHHHHHHHHHHHCCC	47.77	29507054
1443	Ubiquitination	HLFSDLNKLKPDDSG HHHHHHHHCCCCCCC	66.25	-
1445	Ubiquitination	FSDLNKLKPDDSGVN HHHHHHCCCCCCCCC	48.27	-
1449	Phosphorylation	NKLKPDDSGVNIAEA HHCCCCCCCCCHHHH	52.61	28555341
1501	Phosphorylation	QNNKELGTGLSQKRK HCCCCCCCCCCCCCC	47.80	29255136
1504	Phosphorylation	KELGTGLSQKRKAPT CCCCCCCCCCCCCCC	34.69	29255136
1506	Ubiquitination	LGTGLSQKRKAPTEK CCCCCCCCCCCCCCC	53.11	-

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
492	S	Phosphorylation	Kinase	ATM	Q13315	PSP
554	S	Phosphorylation	Kinase	ATM	Q13315	PSP
848	T	Phosphorylation	Kinase	CDK2	P24941	PSP
853	S	Phosphorylation	Kinase	ATM	Q13315	PSP
1062	T	Phosphorylation	Kinase	ATM	Q13315	PSP
1138	S	Phosphorylation	Kinase	ATM	Q13315	PSP
1159	S	Phosphorylation	Kinase	AKT1	P31749	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	UBR5	O95071	PMID:11714696

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TOPB1_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 TOPB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TOP2B_HUMAN	TOP2B	physical	9461304
E2F1_HUMAN	E2F1	physical	12697828
E2F1_HUMAN	E2F1	physical	14576433
PML_HUMAN	PML	physical	12773567
UBR5_HUMAN	UBR5	physical	11714696
ZBT17_HUMAN	ZBTB17	physical	12408820
RAD9A_HUMAN	RAD9A	physical	11395493
DPOE1_HUMAN	POLE	physical	11395493
RAD9A_HUMAN	RAD9A	physical	17575048
PMS2_HUMAN	PMS2	physical	20029092
MSH6_HUMAN	MSH6	physical	20029092
ABL1_HUMAN	ABL1	physical	15961388
FANCJ_HUMAN	BRIP1	physical	20159562
RFA1_HUMAN	RPA1	physical	20159562
NBN_HUMAN	NBN	physical	17765870
MDC1_HUMAN	MDC1	physical	21482717
E2F1_HUMAN	E2F1	physical	17006541
AKT1_HUMAN	AKT1	physical	17006541
TOPB1_HUMAN	TOPBP1	physical	17006541
ATRIP_HUMAN	ATRIP	physical	17616665
PML_HUMAN	PML	physical	19023333
VIGLN_HUMAN	HDLBP	physical	22939629
CHK1_HUMAN	CHEK1	physical	17686975
DTD1_HUMAN	DTD1	physical	20065034
CDC45_HUMAN	CDC45	physical	20065034
TICRR_HUMAN	TICRR	physical	21700459
HSP7C_HUMAN	HSPA8	physical	24239288
MDC1_HUMAN	MDC1	physical	24239288
GRP78_HUMAN	HSPA5	physical	24239288
ACTG_HUMAN	ACTG1	physical	24239288
BLM_HUMAN	BLM	physical	24239288
DDB1_HUMAN	DDB1	physical	24239288
DCAF1_HUMAN	VPRBP	physical	24239288
SMC4_HUMAN	SMC4	physical	24239288
RMI1_HUMAN	RMI1	physical	24239288
PSF1_HUMAN	GINS1	physical	23629628
ERCC2_HUMAN	ERCC2	physical	26344197
SMRCD_HUMAN	SMARCAD1	physical	28063255
FANCJ_HUMAN	BRIP1	physical	23157317
BRCA1_HUMAN	BRCA1	physical	23157317

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 TOPB1_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-581, AND MASS SPECTROMETRY.	19608861 [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-888, 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 THR-779; THR-848; SER-860;THR-861; SER-864; SER-888 AND SER-1002, 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-805; SER-888 ANDSER-1002, AND MASS SPECTROMETRY.	19007248 [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-298; SER-301; SER-492;THR-1062 AND SER-1138, AND MASS 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-805 AND SER-888, ANDMASS SPECTROMETRY.	16964243 [Abstract]