dbPTM

MCM6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM6_HUMAN
UniProt AC	Q14566
Protein Name	DNA replication licensing factor MCM6
Gene Name	MCM6
Organism	Homo sapiens (Human).
Sequence Length	821
Subcellular Localization	Nucleus. Binds to chromatin during G1 and detach from it during S phase.
Protein Description	Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity..
Protein Sequence	MDLAAAAEPGAGSQHLEVRDEVAEKCQKLFLDFLEEFQSSDGEIKYLQLAEELIRPERNTLVVSFVDLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPLAKDFYVAFQDLPTRHKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIRDVEQQFKYTQPNICRNPVCANRRRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGDKCDFTGTLIVVPDVSKLSTPGARAETNSRVSGVDGYETEGIRGLRALGVRDLSYRLVFLACCVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDVRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPISGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKHLRQRDGSGVTKSSWRITVRQLESMIRLSEAMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMEVDEGAGGINGHADSPAPVNGINGYNEDINQESAPKASLRLGFSEYCRISNLIVLHLRKVEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVIHRLTHYDHVLIELTQAGLKGSTEGSESYEEDPYLVVNPNYLLED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDLAAAAE -------CCHHHHCC	9.57	20068231
13	Phosphorylation	AAEPGAGSQHLEVRD HCCCCCCCCCHHHHH	17.56	29255136
25	Acetylation	VRDEVAEKCQKLFLD HHHHHHHHHHHHHHH	32.03	25953088
25	Ubiquitination	VRDEVAEKCQKLFLD HHHHHHHHHHHHHHH	32.03	33845483
28	Ubiquitination	EVAEKCQKLFLDFLE HHHHHHHHHHHHHHH	51.15	-
46	Phosphorylation	SSDGEIKYLQLAEEL CCCCCEEHHHHHHHH	12.82	28152594
77	Phosphorylation	QFNQQLSTTIQEEFY HHHHHHHHHHHHHHH	36.19	24719451
95	Acetylation	PYLCRALKTFVKDRK HHHHHHHHHHHCCCC	38.64	25953088
95	Ubiquitination	PYLCRALKTFVKDRK HHHHHHHHHHHCCCC	38.64	24816145
102	2-Hydroxyisobutyrylation	KTFVKDRKEIPLAKD HHHHCCCCCCCCCCC	70.86	-
102	Ubiquitination	KTFVKDRKEIPLAKD HHHHCCCCCCCCCCC	70.86	33845483
108	Ubiquitination	RKEIPLAKDFYVAFQ CCCCCCCCCEEEEHH	56.93	21906983
111	Phosphorylation	IPLAKDFYVAFQDLP CCCCCCEEEEHHCCC	10.87	28152594
119	Phosphorylation	VAFQDLPTRHKIREL EEHHCCCCHHHHHHH	53.34	21406692
127	Phosphorylation	RHKIRELTSSRIGLL HHHHHHHHHCHHHHH	21.65	-
153	Phosphorylation	PVHPELVSGTFLCLD CCCHHHCCCCEEEEE	44.75	-
173	Acetylation	RDVEQQFKYTQPNIC HHHHHHHCCCCCCCC	42.95	26051181
173	Ubiquitination	RDVEQQFKYTQPNIC HHHHHHHCCCCCCCC	42.95	21906983
174	Phosphorylation	DVEQQFKYTQPNICR HHHHHHCCCCCCCCC	16.34	28152594
175	Phosphorylation	VEQQFKYTQPNICRN HHHHHCCCCCCCCCC	37.83	28152594
195	Phosphorylation	RRRFLLDTNKSRFVD CCEEEEECCCCCCCC	44.51	-
197	2-Hydroxyisobutyrylation	RFLLDTNKSRFVDFQ EEEEECCCCCCCCEE	45.13	-
197	Acetylation	RFLLDTNKSRFVDFQ EEEEECCCCCCCCEE	45.13	25953088
197	Ubiquitination	RFLLDTNKSRFVDFQ EEEEECCCCCCCCEE	45.13	21906983
198	Phosphorylation	FLLDTNKSRFVDFQK EEEECCCCCCCCEEE	32.78	29457462
205	Acetylation	SRFVDFQKVRIQETQ CCCCCEEEEEEEEHH	33.21	25953088
205	Methylation	SRFVDFQKVRIQETQ CCCCCEEEEEEEEHH	33.21	21680603
205	Ubiquitination	SRFVDFQKVRIQETQ CCCCCEEEEEEEEHH	33.21	21906983
211	Phosphorylation	QKVRIQETQAELPRG EEEEEEEHHHCCCCC	19.39	22210691
217	Methylation	ETQAELPRGSIPRSL EHHHCCCCCCCCCHH	65.20	115482923
219	Phosphorylation	QAELPRGSIPRSLEV HHCCCCCCCCCHHHH	30.60	25159151
235	Phosphorylation	LRAEAVESAQAGDKC HHHHHHHHHHCCCCC	21.05	29214152
241	Acetylation	ESAQAGDKCDFTGTL HHHHCCCCCCCCCEE	34.48	26051181
241	Ubiquitination	ESAQAGDKCDFTGTL HHHHCCCCCCCCCEE	34.48	-
242	Glutathionylation	SAQAGDKCDFTGTLI HHHCCCCCCCCCEEE	6.56	22555962
245	Phosphorylation	AGDKCDFTGTLIVVP CCCCCCCCCEEEEEC	18.92	30576142
247	Phosphorylation	DKCDFTGTLIVVPDV CCCCCCCEEEEECCH	15.39	30576142
255	Phosphorylation	LIVVPDVSKLSTPGA EEEECCHHHCCCCCC	34.95	30576142
256	Ubiquitination	IVVPDVSKLSTPGAR EEECCHHHCCCCCCC	46.43	-
258	Phosphorylation	VPDVSKLSTPGARAE ECCHHHCCCCCCCHH	35.97	24719451
259	Phosphorylation	PDVSKLSTPGARAET CCHHHCCCCCCCHHC	35.86	20068231
266	Phosphorylation	TPGARAETNSRVSGV CCCCCHHCCCCCCCC	37.19	30266825
268	Phosphorylation	GARAETNSRVSGVDG CCCHHCCCCCCCCCC	41.29	30266825
271	Phosphorylation	AETNSRVSGVDGYET HHCCCCCCCCCCCCC	31.80	23401153
276	Phosphorylation	RVSGVDGYETEGIRG CCCCCCCCCCCCCHH	18.40	23927012
278	Phosphorylation	SGVDGYETEGIRGLR CCCCCCCCCCCHHHH	30.91	30266825
282	Methylation	GYETEGIRGLRALGV CCCCCCCHHHHHCCC	49.29	115482931
294	Phosphorylation	LGVRDLSYRLVFLAC CCCCCCCHHHHHHHH	18.44	-
313	Acetylation	TNPRFGGKELRDEEQ CCCCCCCHHCCCHHH	54.69	26051181
313	Ubiquitination	TNPRFGGKELRDEEQ CCCCCCCHHCCCHHH	54.69	21906983
316	Methylation	RFGGKELRDEEQTAE CCCCHHCCCHHHHHH	50.84	115482907
324	Phosphorylation	DEEQTAESIKNQMTV CHHHHHHHHHHHCCH	36.08	25849741
326	2-Hydroxyisobutyrylation	EQTAESIKNQMTVKE HHHHHHHHHHCCHHH	50.86	-
326	Acetylation	EQTAESIKNQMTVKE HHHHHHHHHHCCHHH	50.86	26051181
326	Ubiquitination	EQTAESIKNQMTVKE HHHHHHHHHHCCHHH	50.86	23000965
332	Ubiquitination	IKNQMTVKEWEKVFE HHHHCCHHHHHHHHH	48.20	23000965
336	Ubiquitination	MTVKEWEKVFEMSQD CCHHHHHHHHHHHCC	53.98	23000965
344	Acetylation	VFEMSQDKNLYHNLC HHHHHCCCCHHHHHH	41.01	25953088
344	Ubiquitination	VFEMSQDKNLYHNLC HHHHHCCCCHHHHHH	41.01	32015554
365	2-Hydroxyisobutyrylation	IHGNDEVKRGVLLML CCCCCHHHHCEEEEE	41.19	-
365	Ubiquitination	IHGNDEVKRGVLLML CCCCCHHHHCEEEEE	41.19	-
379	Phosphorylation	LFGGVPKTTGEGTSL EECCCCCCCCCCCCC	33.68	21406692
380	Phosphorylation	FGGVPKTTGEGTSLR ECCCCCCCCCCCCCC	39.09	20068231
384	Phosphorylation	PKTTGEGTSLRGDIN CCCCCCCCCCCCCEE	21.93	21406692
385	Phosphorylation	KTTGEGTSLRGDINV CCCCCCCCCCCCEEE	27.25	20068231
393	Glutathionylation	LRGDINVCIVGDPST CCCCEEEEEECCHHH	1.48	22555962
402	Ubiquitination	VGDPSTAKSQFLKHV ECCHHHHHHHHHHHH	44.90	22817900
407	Acetylation	TAKSQFLKHVEEFSP HHHHHHHHHHHHHCC	47.06	26822725
407	Ubiquitination	TAKSQFLKHVEEFSP HHHHHHHHHHHHHCC	47.06	21906983
413	Phosphorylation	LKHVEEFSPRAVYTS HHHHHHHCCCEEEEC	19.43	30266825
422	Ubiquitination	RAVYTSGKASSAAGL CEEEECCCCCCCCCC	44.88	23000965
424	Phosphorylation	VYTSGKASSAAGLTA EEECCCCCCCCCCEE	24.81	21406692
425	Phosphorylation	YTSGKASSAAGLTAA EECCCCCCCCCCEEE	27.31	21406692
430	Phosphorylation	ASSAAGLTAAVVRDE CCCCCCCEEEEECCC	16.20	21406692
483	Phosphorylation	AMEQQTISITKAGVK HHHHCCEEEEHHHHH	27.82	24719451
486	Acetylation	QQTISITKAGVKATL HCCEEEEHHHHHHHH	41.28	25953088
486	Ubiquitination	QQTISITKAGVKATL HCCEEEEHHHHHHHH	41.28	21906983
490	Ubiquitination	SITKAGVKATLNART EEEHHHHHHHHHHHH	34.43	21906983
497	Phosphorylation	KATLNARTSILAAAN HHHHHHHHHHHHHHC	20.08	27080861
498	Phosphorylation	ATLNARTSILAAANP HHHHHHHHHHHHHCC	15.28	27080861
507	Phosphorylation	LAAANPISGHYDRSK HHHHCCCCCCCCCCH	22.30	22210691
510	Phosphorylation	ANPISGHYDRSKSLK HCCCCCCCCCCHHHH	19.31	27642862
513	Phosphorylation	ISGHYDRSKSLKQNI CCCCCCCCHHHHHHC	24.57	24719451
514	Ubiquitination	SGHYDRSKSLKQNIN CCCCCCCHHHHHHCC	61.78	23000965
517	Acetylation	YDRSKSLKQNINLSA CCCCHHHHHHCCCCC	48.68	7378595
517	Ubiquitination	YDRSKSLKQNINLSA CCCCHHHHHHCCCCC	48.68	23000965
523	Phosphorylation	LKQNINLSAPIMSRF HHHHCCCCCCHHHHC	27.75	20068231
527	Sulfoxidation	INLSAPIMSRFDLFF CCCCCCHHHHCCEEE	1.98	21406390
528	Phosphorylation	NLSAPIMSRFDLFFI CCCCCHHHHCCEEEE	30.43	20068231
546	Phosphorylation	ECNEVTDYAIARRIV CCCCCCHHHHHHHHH	7.19	-
557	Phosphorylation	RRIVDLHSRIEESID HHHHHHHHHHHHHHH	42.10	21406692
562	Phosphorylation	LHSRIEESIDRVYSL HHHHHHHHHHHCCCH	19.59	23186163
565	Methylation	RIEESIDRVYSLDDI HHHHHHHHCCCHHHH	27.83	115482915
567	Phosphorylation	EESIDRVYSLDDIRR HHHHHHCCCHHHHHH	12.38	23186163
568	Phosphorylation	ESIDRVYSLDDIRRY HHHHHCCCHHHHHHH	23.59	21815630
573	Methylation	VYSLDDIRRYLLFAR CCCHHHHHHHHHHHH	28.34	115482939
583	Ubiquitination	LLFARQFKPKISKES HHHHHHHCCCCCCCC	36.74	22817900
585	Ubiquitination	FARQFKPKISKESED HHHHHCCCCCCCCCC	61.27	22817900
588	Ubiquitination	QFKPKISKESEDFIV HHCCCCCCCCCCHHH	69.59	21906983
590	Phosphorylation	KPKISKESEDFIVEQ CCCCCCCCCCHHHHH	46.32	21712546
598	Nitration	EDFIVEQYKHLRQRD CCHHHHHHHHHHHCC	6.20	-
599	Acetylation	DFIVEQYKHLRQRDG CHHHHHHHHHHHCCC	35.54	23749302
599	Ubiquitination	DFIVEQYKHLRQRDG CHHHHHHHHHHHCCC	35.54	23000965
611	Acetylation	RDGSGVTKSSWRITV CCCCCCCHHHHEEEH	39.83	25953088
611	Ubiquitination	RDGSGVTKSSWRITV CCCCCCCHHHHEEEH	39.83	21906983
617	Phosphorylation	TKSSWRITVRQLESM CHHHHEEEHHHHHHH	10.89	27251275
643	Acetylation	CCDEVQPKHVKEAFR CCCCCCHHHHHHHHH	43.89	23749302
643	Ubiquitination	CCDEVQPKHVKEAFR CCCCCCHHHHHHHHH	43.89	22817900
646	Acetylation	EVQPKHVKEAFRLLN CCCHHHHHHHHHHHH	42.94	23749302
646	Ubiquitination	EVQPKHVKEAFRLLN CCCHHHHHHHHHHHH	42.94	22817900
654	Acetylation	EAFRLLNKSIIRVET HHHHHHHCCCEEEEC	42.89	25953088
654	Ubiquitination	EAFRLLNKSIIRVET HHHHHHHCCCEEEEC	42.89	27667366
661	Phosphorylation	KSIIRVETPDVNLDQ CCCEEEECCCCCCCH	23.18	-
689	Phosphorylation	GINGHADSPAPVNGI CCCCCCCCCCCCCCC	24.60	29496963
699	Phosphorylation	PVNGINGYNEDINQE CCCCCCCCCCCCCCC	15.76	26074081
718	Phosphorylation	ASLRLGFSEYCRISN HHHHCCHHHHHHHHC	26.34	28152594
720	Phosphorylation	LRLGFSEYCRISNLI HHCCHHHHHHHHCEE	5.94	28152594
733	Ubiquitination	LIVLHLRKVEEEEDE EEEEEEECCCHHHCH	61.43	21906983
744	Ubiquitination	EEDESALKRSELVNW HHCHHHHHHHHHHHH	54.30	21906983
752	Phosphorylation	RSELVNWYLKEIESE HHHHHHHHHHHHHHC	11.59	28152594
754	Ubiquitination	ELVNWYLKEIESEID HHHHHHHHHHHHCCC	40.73	-
758	Phosphorylation	WYLKEIESEIDSEEE HHHHHHHHCCCCHHH	45.58	30266825
762	Phosphorylation	EIESEIDSEEELINK HHHHCCCCHHHHHCH	53.20	29255136
769	2-Hydroxyisobutyrylation	SEEELINKKRIIEKV CHHHHHCHHHHHHHH	36.11	-
769	Ubiquitination	SEEELINKKRIIEKV CHHHHHCHHHHHHHH	36.11	23000965
770	Ubiquitination	EEELINKKRIIEKVI HHHHHCHHHHHHHHH	44.32	23000965
775	Acetylation	NKKRIIEKVIHRLTH CHHHHHHHHHHHHCC	35.76	19608861
775	Ubiquitination	NKKRIIEKVIHRLTH CHHHHHHHHHHHHCC	35.76	23000965
781	Phosphorylation	EKVIHRLTHYDHVLI HHHHHHHCCCHHHHH	20.53	28152594
783	Phosphorylation	VIHRLTHYDHVLIEL HHHHHCCCHHHHHHH	11.51	28152594
791	Phosphorylation	DHVLIELTQAGLKGS HHHHHHHHHHCCCCC	12.00	17525332
796	Ubiquitination	ELTQAGLKGSTEGSE HHHHHCCCCCCCCCC	50.31	21906983
798	Phosphorylation	TQAGLKGSTEGSESY HHHCCCCCCCCCCCC	23.00	28176443
799	Phosphorylation	QAGLKGSTEGSESYE HHCCCCCCCCCCCCC	53.70	28464451
802	Phosphorylation	LKGSTEGSESYEEDP CCCCCCCCCCCCCCC	19.69	29116813
804	Phosphorylation	GSTEGSESYEEDPYL CCCCCCCCCCCCCEE	39.27	29116813
810	Phosphorylation	ESYEEDPYLVVNPNY CCCCCCCEEEECCCC	25.17	17360941
817	Phosphorylation	YLVVNPNYLLED--- EEEECCCCCCCC---	17.58	26074081

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 MCM6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM6_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 MCM6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM6_HUMAN	MCM6	physical	12694531
I36RA_HUMAN	IL36RN	physical	16189514
C2CD6_HUMAN	ALS2CR11	physical	16189514
PSA1_HUMAN	PSMA1	physical	16189514
SCNM1_HUMAN	SCNM1	physical	16189514
ING5_HUMAN	ING5	physical	16189514
AF9_HUMAN	MLLT3	physical	16189514
MCM6_HUMAN	MCM6	physical	16189514
MCM10_HUMAN	MCM10	physical	16189514
MCM8_HUMAN	MCM8	physical	12771218
MCM2_HUMAN	MCM2	physical	12694531
MCM7_HUMAN	MCM7	physical	12694531
MCM2_HUMAN	MCM2	physical	12614612
MCM4_HUMAN	MCM4	physical	12614612
MCM6_HUMAN	MCM6	physical	12614612
MCM7_HUMAN	MCM7	physical	12614612
ORC1_HUMAN	ORC1	physical	12614612
ORC2_HUMAN	ORC2	physical	12614612
ORC4_HUMAN	ORC4	physical	12614612
CDC45_HUMAN	CDC45	physical	12614612
RFA1_HUMAN	RPA1	physical	12614612
MCM4_HUMAN	MCM4	physical	12207017
MCM7_HUMAN	MCM7	physical	12207017
MCM2_HUMAN	MCM2	physical	12207017
CDN2A_HUMAN	CDKN2A	physical	17955473
ARF_HUMAN	CDKN2A	physical	17955473
MCM7_HUMAN	MCM7	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
SF3B1_HUMAN	SF3B1	physical	22939629
ORC6_HUMAN	ORC6	physical	15232106
MCM10_HUMAN	MCM10	physical	15232106
MCM6_HUMAN	MCM6	physical	15232106
SMC1A_HUMAN	SMC1A	physical	16438930
MCM7_HUMAN	MCM7	physical	16438930
HS90B_HUMAN	HSP90AB1	physical	22863883
MCM3_HUMAN	MCM3	physical	22863883
RU2B_HUMAN	SNRPB2	physical	25416956
MCM10_HUMAN	MCM10	physical	25416956
F161A_HUMAN	FAM161A	physical	25416956
ZBTB9_HUMAN	ZBTB9	physical	25416956
MCM3_HUMAN	MCM3	physical	26344197
MCM5_HUMAN	MCM5	physical	26344197
MCM7_HUMAN	MCM7	physical	26344197
MCMBP_HUMAN	MCMBP	physical	26344197
MCM2_HUMAN	MCM2	physical	26496610
MCM3_HUMAN	MCM3	physical	26496610
MCM4_HUMAN	MCM4	physical	26496610
MCM7_HUMAN	MCM7	physical	26496610
TRPS1_HUMAN	TRPS1	physical	26496610
MCM10_HUMAN	MCM10	physical	26496610
MCMBP_HUMAN	MCMBP	physical	26496610
MCM2_HUMAN	MCM2	physical	27173435
MCM4_HUMAN	MCM4	physical	27173435
UBP15_HUMAN	USP15	physical	27173435
NS1BP_HUMAN	IVNS1ABP	physical	27173435
SMC1A_HUMAN	SMC1A	physical	27173435
SMC3_HUMAN	SMC3	physical	27173435
GAPD1_HUMAN	GAPVD1	physical	27173435
ANK3_HUMAN	ANK3	physical	27173435
SBNO1_HUMAN	SBNO1	physical	27173435
SF3A1_HUMAN	SF3A1	physical	27173435
SOX4_HUMAN	SOX4	physical	27173435
HSF1_HUMAN	HSF1	physical	27173435
K1468_HUMAN	KIAA1468	physical	27173435
PLK1_HUMAN	PLK1	physical	27173435

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 MCM6_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-762, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-599 AND LYS-775, AND MASSSPECTROMETRY.	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-271 AND SER-762, ANDMASS 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-762, 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-271 AND SER-762, ANDMASS SPECTROMETRY.	18669648 [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-271 AND SER-762, ANDMASS SPECTROMETRY.	16964243 [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-791, AND MASSSPECTROMETRY.	17525332 [Abstract]