dbPTM

CAF1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAF1A_HUMAN
UniProt AC	Q13111
Protein Name	Chromatin assembly factor 1 subunit A
Gene Name	CHAF1A
Organism	Homo sapiens (Human).
Sequence Length	956
Subcellular Localization	Nucleus . DNA replication foci.
Protein Description	Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci (By similarity)..
Protein Sequence	MLEELECGAPGARGAATAMDCKDRPAFPVKKLIQARLPFKRLNLVPKGKADDMSDDQGTSVQSKSPDLEASLDTLENNCHVGSDIDFRPKLVNGKGPLDNFLRNRIETSIGQSTVIIDLTEDSNEQPDSLVDHNKLNSEASPSREAINGQREDTGDQQGLLKAIQNDKLAFPGETLSDIPCKTEEEGVGCGGAGRRGDSQECSPRSCPELTSGPRMCPRKEQDSWSEAGGILFKGKVPMVVLQDILAVRPPQIKSLPATPQGKNMTPESEVLESFPEEDSVLSHSSLSSPSSTSSPEGPPAPPKQHSSTSPFPTSTPLRRITKKFVKGSTEKNKLRLQRDQERLGKQLKLRAEREEKEKLKEEAKRAKEEAKKKKEEEKELKEKERREKREKDEKEKAEKQRLKEERRKERQEALEAKLEEKRKKEEEKRLREEEKRIKAEKAEITRFFQKPKTPQAPKTLAGSCGKFAPFEIKEHMVLAPRRRTAFHPDLCSQLDQLLQQQSGEFSFLKDLKGRQPLRSGPTHVSTRNADIFNSDVVIVERGKGDGVPERRKFGRMKLLQFCENHRPAYWGTWNKKTALIRARDPWAQDTKLLDYEVDSDEEWEEEEPGESLSHSEGDDDDDMGEDEDEDDGFFVPHGYLSEDEGVTEECADPENHKVRQKLKAKEWDEFLAKGKRFRVLQPVKIGCVWAADRDCAGDDLKVLQQFAACFLETLPAQEEQTPKASKRERRDEQILAQLLPLLHGNVNGSKVIIREFQEHCRRGLLSNHTGSPRSPSTTYLHTPTPSEDAAIPSKSRLKRLISENSVYEKRPDFRMCWYVHPQVLQSFQQEHLPVPCQWSYVTSVPSAPKEDSGSVPSTGPSQGTPISLKRKSAGSMCITQFMKKRRHDGQIGAEDMDGFQADTEEEEEEEGDCMIVDVPDAAEVQAPCGAASGAGGGVGVDTGKATLTASPLGAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Acetylation	AATAMDCKDRPAFPV CHHHCCCCCCCCCCH	53.13	12436423
22	Ubiquitination	AATAMDCKDRPAFPV CHHHCCCCCCCCCCH	53.13	-
30	Acetylation	DRPAFPVKKLIQARL CCCCCCHHHHHHHCC	41.94	12436435
49	Ubiquitination	LNLVPKGKADDMSDD CCCCCCCCCCCCCCC	55.56	27667366
54	Phosphorylation	KGKADDMSDDQGTSV CCCCCCCCCCCCCCC	45.06	25159151
59	Phosphorylation	DMSDDQGTSVQSKSP CCCCCCCCCCCCCCC	21.79	29978859
60	Phosphorylation	MSDDQGTSVQSKSPD CCCCCCCCCCCCCCC	25.61	29496963
63	Phosphorylation	DQGTSVQSKSPDLEA CCCCCCCCCCCCHHH	32.71	30576142
65	Phosphorylation	GTSVQSKSPDLEASL CCCCCCCCCCHHHHH	28.97	23927012
71	Phosphorylation	KSPDLEASLDTLENN CCCCHHHHHHHHHHC	19.87	30266825
74	Phosphorylation	DLEASLDTLENNCHV CHHHHHHHHHHCCCC	41.06	30266825
83	Phosphorylation	ENNCHVGSDIDFRPK HHCCCCCCCCCCCCH	30.24	23927012
108	Phosphorylation	FLRNRIETSIGQSTV HHHHHHHHHCCCEEE	24.23	20068231
109	Phosphorylation	LRNRIETSIGQSTVI HHHHHHHHCCCEEEE	16.36	23663014
113	Phosphorylation	IETSIGQSTVIIDLT HHHHCCCEEEEEECC	21.30	23663014
114	Phosphorylation	ETSIGQSTVIIDLTE HHHCCCEEEEEECCC	14.08	23663014
120	Phosphorylation	STVIIDLTEDSNEQP EEEEEECCCCCCCCC	33.72	23663014
123	Phosphorylation	IIDLTEDSNEQPDSL EEECCCCCCCCCCCC	35.71	30278072
129	Phosphorylation	DSNEQPDSLVDHNKL CCCCCCCCCCCHHHC	36.65	23663014
138	Phosphorylation	VDHNKLNSEASPSRE CCHHHCCCCCCCCHH	45.00	25159151
141	Phosphorylation	NKLNSEASPSREAIN HHCCCCCCCCHHHHC	21.25	29255136
143	Phosphorylation	LNSEASPSREAINGQ CCCCCCCCHHHHCCC	40.01	30266825
154	Phosphorylation	INGQREDTGDQQGLL HCCCCCCCCCCHHHH	37.59	22617229
162	Ubiquitination	GDQQGLLKAIQNDKL CCCHHHHHHHHCCCC	48.78	32015554
168	Acetylation	LKAIQNDKLAFPGET HHHHHCCCCCCCCCC	49.63	26051181
168	Ubiquitination	LKAIQNDKLAFPGET HHHHHCCCCCCCCCC	49.63	32015554
177	Phosphorylation	AFPGETLSDIPCKTE CCCCCCHHCCCCCCC	40.70	25159151
181	Phosphorylation	ETLSDIPCKTEEEGV CCHHCCCCCCCCCCC	9.71	17525332
182	Sumoylation	TLSDIPCKTEEEGVG CHHCCCCCCCCCCCC	54.33	-
182	Acetylation	TLSDIPCKTEEEGVG CHHCCCCCCCCCCCC	54.33	26051181
182	Sumoylation	TLSDIPCKTEEEGVG CHHCCCCCCCCCCCC	54.33	25114211
182	Ubiquitination	TLSDIPCKTEEEGVG CHHCCCCCCCCCCCC	54.33	32015554
185	Phosphorylation	DIPCKTEEEGVGCGG CCCCCCCCCCCCCCC	66.34	17525332
188	Phosphorylation	CKTEEEGVGCGGAGR CCCCCCCCCCCCCCC	6.93	18669648
199	Phosphorylation	GAGRRGDSQECSPRS CCCCCCCCCCCCCCC	30.61	17525332
203	Phosphorylation	RGDSQECSPRSCPEL CCCCCCCCCCCCCCC	23.69	17525332
206	Phosphorylation	SQECSPRSCPELTSG CCCCCCCCCCCCCCC	37.09	19664994
211	Phosphorylation	PRSCPELTSGPRMCP CCCCCCCCCCCCCCC	29.94	22167270
212	Phosphorylation	RSCPELTSGPRMCPR CCCCCCCCCCCCCCC	60.47	23927012
224	Phosphorylation	CPRKEQDSWSEAGGI CCCCCCCCHHHHCCE	32.00	25159151
226	Phosphorylation	RKEQDSWSEAGGILF CCCCCCHHHHCCEEC	22.86	30576142
234	Ubiquitination	EAGGILFKGKVPMVV HHCCEECCCCCCEEE	55.14	29967540
237	Phosphorylation	GILFKGKVPMVVLQD CEECCCCCCEEEEEH	5.15	16964243
241	Phosphorylation	KGKVPMVVLQDILAV CCCCCEEEEEHHHHC	3.02	16964243
255	Phosphorylation	VRPPQIKSLPATPQG CCCCCCCCCCCCCCC	41.01	30266825
259	Phosphorylation	QIKSLPATPQGKNMT CCCCCCCCCCCCCCC	17.76	30266825
266	Phosphorylation	TPQGKNMTPESEVLE CCCCCCCCCHHHHHH	33.04	29116813
269	Phosphorylation	GKNMTPESEVLESFP CCCCCCHHHHHHHCC	33.92	26074081
274	Phosphorylation	PESEVLESFPEEDSV CHHHHHHHCCCCCCC	41.77	29978859
280	Phosphorylation	ESFPEEDSVLSHSSL HHCCCCCCCCCCCCC	28.39	29978859
283	Phosphorylation	PEEDSVLSHSSLSSP CCCCCCCCCCCCCCC	21.11	25159151
285	Phosphorylation	EDSVLSHSSLSSPSS CCCCCCCCCCCCCCC	29.60	29978859
286	Phosphorylation	DSVLSHSSLSSPSST CCCCCCCCCCCCCCC	27.18	25159151
288	Phosphorylation	VLSHSSLSSPSSTSS CCCCCCCCCCCCCCC	41.99	29978859
289	Phosphorylation	LSHSSLSSPSSTSSP CCCCCCCCCCCCCCC	33.81	30576142
291	Phosphorylation	HSSLSSPSSTSSPEG CCCCCCCCCCCCCCC	48.47	25159151
292	Phosphorylation	SSLSSPSSTSSPEGP CCCCCCCCCCCCCCC	35.37	29978859
293	Phosphorylation	SLSSPSSTSSPEGPP CCCCCCCCCCCCCCC	37.25	29978859
294	Phosphorylation	LSSPSSTSSPEGPPA CCCCCCCCCCCCCCC	45.93	29978859
295	Phosphorylation	SSPSSTSSPEGPPAP CCCCCCCCCCCCCCC	27.36	29978859
307	Phosphorylation	PAPPKQHSSTSPFPT CCCCCCCCCCCCCCC	32.58	25159151
308	Phosphorylation	APPKQHSSTSPFPTS CCCCCCCCCCCCCCC	30.68	25159151
309	Phosphorylation	PPKQHSSTSPFPTST CCCCCCCCCCCCCCC	43.35	25159151
310	Phosphorylation	PKQHSSTSPFPTSTP CCCCCCCCCCCCCCH	26.87	25159151
314	Phosphorylation	SSTSPFPTSTPLRRI CCCCCCCCCCHHHHH	45.68	23403867
315	Phosphorylation	STSPFPTSTPLRRIT CCCCCCCCCHHHHHH	28.41	25159151
316	Phosphorylation	TSPFPTSTPLRRITK CCCCCCCCHHHHHHH	28.90	25159151
327	Ubiquitination	RITKKFVKGSTEKNK HHHHHHHCCCHHHCC	50.72	27667366
329	Phosphorylation	TKKFVKGSTEKNKLR HHHHHCCCHHHCCHH	27.89	30576142
330	Phosphorylation	KKFVKGSTEKNKLRL HHHHCCCHHHCCHHH	60.70	29496963
378	Ubiquitination	AKKKKEEEKELKEKE HHHHHHHHHHHHHHH	53.58	24816145
397	Ubiquitination	REKDEKEKAEKQRLK HHHHHHHHHHHHHHH	73.28	24816145
399	Ubiquitination	KDEKEKAEKQRLKEE HHHHHHHHHHHHHHH	61.87	24816145
418	Ubiquitination	RQEALEAKLEEKRKK HHHHHHHHHHHHHHH	47.24	24816145
423	Ubiquitination	EAKLEEKRKKEEEKR HHHHHHHHHHHHHHH	59.57	24816145
442	Ubiquitination	EKRIKAEKAEITRFF HHHHHHHHHHHHHHH	57.06	24816145
454	Phosphorylation	RFFQKPKTPQAPKTL HHHCCCCCCCCCCCC	29.21	25159151
467	Acetylation	TLAGSCGKFAPFEIK CCCCCCCCCCCCEEE	42.55	21339330
467	Ubiquitination	TLAGSCGKFAPFEIK CCCCCCCCCCCCEEE	42.55	29967540
507	Phosphorylation	QQQSGEFSFLKDLKG HHCCCCCCHHHCCCC	25.93	24719451
513	Sumoylation	FSFLKDLKGRQPLRS CCHHHCCCCCCCCCC	63.28	-
513	Sumoylation	FSFLKDLKGRQPLRS CCHHHCCCCCCCCCC	63.28	-
520	Phosphorylation	KGRQPLRSGPTHVST CCCCCCCCCCCCEEC	57.73	22210691
523	Phosphorylation	QPLRSGPTHVSTRNA CCCCCCCCCEECCCC	38.13	22210691
527	Phosphorylation	SGPTHVSTRNADIFN CCCCCEECCCCCCCC	27.18	22210691
535	Phosphorylation	RNADIFNSDVVIVER CCCCCCCCCEEEEEC	22.49	21712546
544	Sumoylation	VVIVERGKGDGVPER EEEEECCCCCCCCHH	61.11	-
544	Sumoylation	VVIVERGKGDGVPER EEEEECCCCCCCCHH	61.11	-
640	Phosphorylation	GFFVPHGYLSEDEGV CEECCCCCCCCCCCC	12.20	26074081
642	Phosphorylation	FVPHGYLSEDEGVTE ECCCCCCCCCCCCCH	34.22	26657352
666	Acetylation	VRQKLKAKEWDEFLA HHHHHHHHHHHHHHH	58.72	26051181
666	Ubiquitination	VRQKLKAKEWDEFLA HHHHHHHHHHHHHHH	58.72	29967540
674	Acetylation	EWDEFLAKGKRFRVL HHHHHHHCCCCEEEE	68.09	25953088
674	Ubiquitination	EWDEFLAKGKRFRVL HHHHHHHCCCCEEEE	68.09	32015554
714	Phosphorylation	FAACFLETLPAQEEQ HHHHHHHHCCCCCHH	39.94	24732914
722	Phosphorylation	LPAQEEQTPKASKRE CCCCCHHCCCCCHHH	30.00	25159151
731 (in isoform 2)	Phosphorylation	-	47.25	23322592
750	Phosphorylation	LHGNVNGSKVIIREF HHCCCCCCEEHHHHH	20.67	24247654
767	Phosphorylation	HCRRGLLSNHTGSPR HHHHCCCCCCCCCCC	31.44	23401153
770	Phosphorylation	RGLLSNHTGSPRSPS HCCCCCCCCCCCCCC	43.54	30266825
772	Phosphorylation	LLSNHTGSPRSPSTT CCCCCCCCCCCCCCC	20.49	29255136
775	Phosphorylation	NHTGSPRSPSTTYLH CCCCCCCCCCCCEEC	26.96	23927012
777	Phosphorylation	TGSPRSPSTTYLHTP CCCCCCCCCCEECCC	34.33	23927012
778	Phosphorylation	GSPRSPSTTYLHTPT CCCCCCCCCEECCCC	23.89	23927012
779	Phosphorylation	SPRSPSTTYLHTPTP CCCCCCCCEECCCCC	28.55	23927012
780	Phosphorylation	PRSPSTTYLHTPTPS CCCCCCCEECCCCCC	9.14	23927012
783	Phosphorylation	PSTTYLHTPTPSEDA CCCCEECCCCCCCCC	26.68	25159151
785	Phosphorylation	TTYLHTPTPSEDAAI CCEECCCCCCCCCCC	40.37	25159151
787	Phosphorylation	YLHTPTPSEDAAIPS EECCCCCCCCCCCCC	51.06	23927012
794	Phosphorylation	SEDAAIPSKSRLKRL CCCCCCCCHHHHHHH	36.83	23927012
795	Sumoylation	EDAAIPSKSRLKRLI CCCCCCCHHHHHHHH	33.95	-
795	Sumoylation	EDAAIPSKSRLKRLI CCCCCCCHHHHHHHH	33.95	-
796	Phosphorylation	DAAIPSKSRLKRLIS CCCCCCHHHHHHHHH	47.37	-
803	Phosphorylation	SRLKRLISENSVYEK HHHHHHHHCCCCCCC	35.00	25159151
806	Phosphorylation	KRLISENSVYEKRPD HHHHHCCCCCCCCCC	23.25	28152594
808	Phosphorylation	LISENSVYEKRPDFR HHHCCCCCCCCCCCE	18.63	28152594
837	Phosphorylation	QEHLPVPCQWSYVTS HHCCCCCCCEEEEEE	7.06	18669648
853	Phosphorylation	PSAPKEDSGSVPSTG CCCCCCCCCCCCCCC	33.78	20068231
855	Phosphorylation	APKEDSGSVPSTGPS CCCCCCCCCCCCCCC	34.50	18669648
858	Phosphorylation	EDSGSVPSTGPSQGT CCCCCCCCCCCCCCC	43.79	25850435
859	Phosphorylation	DSGSVPSTGPSQGTP CCCCCCCCCCCCCCC	47.22	25850435
862	Phosphorylation	SVPSTGPSQGTPISL CCCCCCCCCCCCCCC	42.46	29255136
865	Phosphorylation	STGPSQGTPISLKRK CCCCCCCCCCCCCCC	15.15	29255136
868	Phosphorylation	PSQGTPISLKRKSAG CCCCCCCCCCCCCCC	29.10	29255136
870	Methylation	QGTPISLKRKSAGSM CCCCCCCCCCCCCCC	51.49	-
870	Ubiquitination	QGTPISLKRKSAGSM CCCCCCCCCCCCCCC	51.49	29967540
872	Methylation	TPISLKRKSAGSMCI CCCCCCCCCCCCCHH	42.97	-
873	Phosphorylation	PISLKRKSAGSMCIT CCCCCCCCCCCCHHH	41.73	25159151
876	Phosphorylation	LKRKSAGSMCITQFM CCCCCCCCCHHHHHH	15.36	25159151
880	Phosphorylation	SAGSMCITQFMKKRR CCCCCHHHHHHHHCC	15.72	20068231
933	Phosphorylation	QAPCGAASGAGGGVG CCCCCCCCCCCCCCC	28.74	16964243
947	Phosphorylation	GVDTGKATLTASPLG CCCCCCEEEEECCCC	33.77	26074081
949	Phosphorylation	DTGKATLTASPLGAS CCCCEEEEECCCCCC	23.86	20068231
950	Phosphorylation	TGKATLTASPLGAS- CCCEEEEECCCCCC-	32.83	20363803
951	Phosphorylation	GKATLTASPLGAS-- CCEEEEECCCCCC--	20.93	16964243
956	Phosphorylation	TASPLGAS------- EECCCCCC-------	38.67	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 CAF1A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAF1A_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 CAF1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MBD1_HUMAN	MBD1	physical	12697822
PCNA_HUMAN	PCNA	physical	10648606
CBX5_HUMAN	CBX5	physical	10938122
ASF1A_HUMAN	ASF1A	physical	11897662
ASF1B_HUMAN	ASF1B	physical	11897662
SUMO3_HUMAN	SUMO3	physical	19919826
WRN_HUMAN	WRN	physical	17173071
PCNA_HUMAN	PCNA	physical	19822659
RFA1_HUMAN	RPA1	physical	19059499
XPC_HUMAN	XPC	physical	19059499
RFOX2_HUMAN	RBFOX2	physical	20211142
PHS2_HUMAN	PCBD2	physical	20211142
SETB1_HUMAN	SETDB1	physical	19498464
CAF1A_HUMAN	CHAF1A	physical	16826239
PCNA_HUMAN	PCNA	physical	16826239
CAF1A_HUMAN	CHAF1A	physical	11296234
CA1AB_XENLA	chaf1a	physical	11296234
MBD1_HUMAN	MBD1	physical	15327775
SETB1_HUMAN	SETDB1	physical	15327775
H31_HUMAN	HIST1H3A	physical	15327775
AN32A_HUMAN	ANP32A	physical	21209461
AN32B_HUMAN	ANP32B	physical	21209461
CBX5_HUMAN	CBX5	physical	21209461
DDX41_HUMAN	DDX41	physical	21209461
EIF3C_HUMAN	EIF3C	physical	21209461
GTF2I_HUMAN	GTF2I	physical	21209461
HMGB2_HUMAN	HMGB2	physical	21209461
NONO_HUMAN	NONO	physical	21209461
PCNA_HUMAN	PCNA	physical	21209461
PAF1_HUMAN	PAF1	physical	21209461
PRKDC_HUMAN	PRKDC	physical	21209461
PRP31_HUMAN	PRPF31	physical	21209461
RBM3_HUMAN	RBM3	physical	21209461
RS3_HUMAN	RPS3	physical	21209461
RS9_HUMAN	RPS9	physical	21209461
SET_HUMAN	SET	physical	21209461
XRCC5_HUMAN	XRCC5	physical	21209461
1433Z_HUMAN	YWHAZ	physical	21209461
1433B_HUMAN	YWHAB	physical	21209461
XRCC6_HUMAN	XRCC6	physical	21209461
H31_HUMAN	HIST1H3A	physical	22228774
H32_HUMAN	HIST2H3C	physical	21724829
CAF1B_HUMAN	CHAF1B	physical	22939629
GFI1_HUMAN	GFI1	physical	21570500
SQSTM_HUMAN	SQSTM1	physical	17065558
RBBP4_HUMAN	RBBP4	physical	17065558
PCNA_HUMAN	PCNA	physical	17065558
CBX3_HUMAN	CBX3	physical	17065558
BECN1_HUMAN	BECN1	physical	18843052
BAKOR_HUMAN	ATG14	physical	18843052

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 CAF1A_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-775, AND MASSSPECTROMETRY.	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-206; THR-259 ANDTHR-865, 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-224; THR-722; SER-772;SER-775; SER-873 AND SER-951, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-206, AND MASSSPECTROMETRY.	18220336 [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-199; SER-203 ANDSER-206, 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-255; THR-259 ANDSER-951, AND MASS SPECTROMETRY.	16964243 [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-65; SER-141 AND SER-772,AND MASS SPECTROMETRY.	17081983 [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-141 AND SER-206, ANDMASS SPECTROMETRY.	15302935 [Abstract]