dbPTM

SF3A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SF3A1_HUMAN
UniProt AC	Q15459
Protein Name	Splicing factor 3A subunit 1
Gene Name	SF3A1
Organism	Homo sapiens (Human).
Sequence Length	793
Subcellular Localization	Nucleus.
Protein Description	Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex..
Protein Sequence	MPAGPVQAVPPPPPVPTEPKQPTEEEASSKEDSAPSKPVVGIIYPPPEVRNIVDKTASFVARNGPEFEARIRQNEINNPKFNFLNPNDPYHAYYRHKVSEFKEGKAQEPSAAIPKVMQQQQQTTQQQLPQKVQAQVIQETIVPKEPPPEFEFIADPPSISAFDLDVVKLTAQFVARNGRQFLTQLMQKEQRNYQFDFLRPQHSLFNYFTKLVEQYTKILIPPKGLFSKLKKEAENPREVLDQVCYRVEWAKFQERERKKEEEEKEKERVAYAQIDWHDFVVVETVDFQPNEQGNFPPPTTPEELGARILIQERYEKFGESEEVEMEVESDEEDDKQEKAEEPPSQLDQDTQVQDMDEGSDDEEEGQKVPPPPETPMPPPLPPTPDQVIVRKDYDPKASKPLPPAPAPDEYLVSPITGEKIPASKMQEHMRIGLLDPRWLEQRDRSIREKQSDDEVYAPGLDIESSLKQLAERRTDIFGVEETAIGKKIGEEEIQKPEEKVTWDGHSGSMARTQQAAQANITLQEQIEAIHKAKGLVPEDDTKEKIGPSKPNEIPQQPPPPSSATNIPSSAPPITSVPRPPTMPPPVRTTVVSAVPVMPRPPMASVVRLPPGSVIAPMPPIIHAPRINVVPMPPSAPPIMAPRPPPMIVPTAFVPAPPVAPVPAPAPMPPVHPPPPMEDEPTSKKLKTEDSLMPEEEFLRRNKGPVSIKVQVPNMQDKTEWKLNGQVLVFTLPLTDQVSVIKVKIHEATGMPAGKQKLQYEGIFIKDSNSLAYYNMANGAVIHLALKERGGRKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	PPPPPVPTEPKQPTE CCCCCCCCCCCCCCH	66.22	-
20	Sumoylation	PPVPTEPKQPTEEEA CCCCCCCCCCCHHHH	63.78	28112733
23	Phosphorylation	PTEPKQPTEEEASSK CCCCCCCCHHHHCCC	54.24	25367160
28	Phosphorylation	QPTEEEASSKEDSAP CCCHHHHCCCCCCCC	45.26	25627689
29	Phosphorylation	PTEEEASSKEDSAPS CCHHHHCCCCCCCCC	47.30	25627689
30	Acetylation	TEEEASSKEDSAPSK CHHHHCCCCCCCCCC	64.15	26051181
33	Phosphorylation	EASSKEDSAPSKPVV HHCCCCCCCCCCCEE	43.07	28555341
37	Ubiquitination	KEDSAPSKPVVGIIY CCCCCCCCCEEEEEE	40.55	-
44	Nitration	KPVVGIIYPPPEVRN CCEEEEEECCHHHHH	14.04	-
55	Acetylation	EVRNIVDKTASFVAR HHHHHHHHHHHHHHH	34.79	19608861
55	Ubiquitination	EVRNIVDKTASFVAR HHHHHHHHHHHHHHH	34.79	21890473
55	Acetylation	EVRNIVDKTASFVAR HHHHHHHHHHHHHHH	34.79	-
55	Ubiquitination	EVRNIVDKTASFVAR HHHHHHHHHHHHHHH	34.79	-
55	2-Hydroxyisobutyrylation	EVRNIVDKTASFVAR HHHHHHHHHHHHHHH	34.79	-
55	Malonylation	EVRNIVDKTASFVAR HHHHHHHHHHHHHHH	34.79	26320211
58	Phosphorylation	NIVDKTASFVARNGP HHHHHHHHHHHHCCH	26.03	28634120
70	Methylation	NGPEFEARIRQNEIN CCHHHHHHHHHCCCC	19.88	115916577
80	Acetylation	QNEINNPKFNFLNPN HCCCCCCCCCCCCCC	55.87	23954790
80	Ubiquitination	QNEINNPKFNFLNPN HCCCCCCCCCCCCCC	55.87	21890473
80	Sumoylation	QNEINNPKFNFLNPN HCCCCCCCCCCCCCC	55.87	-
80	Acetylation	QNEINNPKFNFLNPN HCCCCCCCCCCCCCC	55.87	-
80	Ubiquitination	QNEINNPKFNFLNPN HCCCCCCCCCCCCCC	55.87	-
90	Phosphorylation	FLNPNDPYHAYYRHK CCCCCCHHHHHHHHC	11.27	28152594
93	Phosphorylation	PNDPYHAYYRHKVSE CCCHHHHHHHHCHHH	6.42	28152594
94	Phosphorylation	NDPYHAYYRHKVSEF CCHHHHHHHHCHHHH	13.66	28152594
102	Acetylation	RHKVSEFKEGKAQEP HHCHHHHHCCCCCCC	62.60	25953088
110	Phosphorylation	EGKAQEPSAAIPKVM CCCCCCCCCHHHHHH	29.58	21406692
115	Ubiquitination	EPSAAIPKVMQQQQQ CCCCHHHHHHHHHHH	44.20	-
115	Acetylation	EPSAAIPKVMQQQQQ CCCCHHHHHHHHHHH	44.20	26051181
117	Sulfoxidation	SAAIPKVMQQQQQTT CCHHHHHHHHHHHHH	3.57	21406390
123	Phosphorylation	VMQQQQQTTQQQLPQ HHHHHHHHHHHHHCH	23.41	22210691
123	Ubiquitination	VMQQQQQTTQQQLPQ HHHHHHHHHHHHHCH	23.41	-
124	Phosphorylation	MQQQQQTTQQQLPQK HHHHHHHHHHHHCHH	21.75	17525332
131	Acetylation	TQQQLPQKVQAQVIQ HHHHHCHHHHHHHHH	34.08	25953088
131	Ubiquitination	TQQQLPQKVQAQVIQ HHHHHCHHHHHHHHH	34.08	21890473
131	Sumoylation	TQQQLPQKVQAQVIQ HHHHHCHHHHHHHHH	34.08	28112733
158	Phosphorylation	EFIADPPSISAFDLD EECCCCCCCCCCCCC	34.27	25338102
158	Acetylation	EFIADPPSISAFDLD EECCCCCCCCCCCCC	34.27	-
158	Ubiquitination	EFIADPPSISAFDLD EECCCCCCCCCCCCC	34.27	-
176	Methylation	LTAQFVARNGRQFLT HHHHHHHHCHHHHHH	40.61	115916565
183	Phosphorylation	RNGRQFLTQLMQKEQ HCHHHHHHHHHHHHH	22.42	-
186	Ubiquitination	RQFLTQLMQKEQRNY HHHHHHHHHHHHHHC	3.73	-
188	Ubiquitination	FLTQLMQKEQRNYQF HHHHHHHHHHHHCCC	41.68	21890473
188	Acetylation	FLTQLMQKEQRNYQF HHHHHHHHHHHHCCC	41.68	25953088
223	Acetylation	TKILIPPKGLFSKLK HHHHCCCCCHHHHHH	63.99	23749302
223	Ubiquitination	TKILIPPKGLFSKLK HHHHCCCCCHHHHHH	63.99	21890473
227	Phosphorylation	IPPKGLFSKLKKEAE CCCCCHHHHHHHHHC	41.96	24719451
228	Acetylation	PPKGLFSKLKKEAEN CCCCHHHHHHHHHCC	57.92	25953088
244	Glutathionylation	REVLDQVCYRVEWAK HHHHHHHHHHHHHHH	1.17	22555962
245	Phosphorylation	EVLDQVCYRVEWAKF HHHHHHHHHHHHHHH	20.88	21406692
251	Acetylation	CYRVEWAKFQERERK HHHHHHHHHHHHHHH	48.96	19608861
251	Ubiquitination	CYRVEWAKFQERERK HHHHHHHHHHHHHHH	48.96	21906983
251	2-Hydroxyisobutyrylation	CYRVEWAKFQERERK HHHHHHHHHHHHHHH	48.96	-
320	Phosphorylation	RYEKFGESEEVEMEV HHHHHCCCCEEEEEE	39.16	23927012
329	Phosphorylation	EVEMEVESDEEDDKQ EEEEEECCCCCCHHH	56.34	22167270
334	Ubiquitination	VESDEEDDKQEKAEE ECCCCCCHHHHHHCC	58.79	-
344	Phosphorylation	EKAEEPPSQLDQDTQ HHHCCCCCCCCCCCC	54.83	23403867
350	Phosphorylation	PSQLDQDTQVQDMDE CCCCCCCCCCCCCCC	25.63	23403867
354	Ubiquitination	DQDTQVQDMDEGSDD CCCCCCCCCCCCCCC	47.87	-
359	Phosphorylation	VQDMDEGSDDEEEGQ CCCCCCCCCCHHCCC	39.58	19664994
359	Acetylation	VQDMDEGSDDEEEGQ CCCCCCCCCCHHCCC	39.58	-
359	Ubiquitination	VQDMDEGSDDEEEGQ CCCCCCCCCCHHCCC	39.58	-
374	Phosphorylation	KVPPPPETPMPPPLP CCCCCCCCCCCCCCC	30.57	29496963
383	Phosphorylation	MPPPLPPTPDQVIVR CCCCCCCCCCCEEEC	37.24	29255136
384	Ubiquitination	PPPLPPTPDQVIVRK CCCCCCCCCCEEECC	35.49	-
398	Phosphorylation	KDYDPKASKPLPPAP CCCCCCCCCCCCCCC	40.72	24719451
399	Ubiquitination	DYDPKASKPLPPAPA CCCCCCCCCCCCCCC	56.27	21890473
399	Acetylation	DYDPKASKPLPPAPA CCCCCCCCCCCCCCC	56.27	26051181
402	Ubiquitination	PKASKPLPPAPAPDE CCCCCCCCCCCCCCC	31.38	-
410	Phosphorylation	PAPAPDEYLVSPITG CCCCCCCEEECCCCC	21.56	24732914
413	Phosphorylation	APDEYLVSPITGEKI CCCCEEECCCCCCCC	14.16	25159151
416	Phosphorylation	EYLVSPITGEKIPAS CEEECCCCCCCCCHH	42.55	25159151
419	Ubiquitination	VSPITGEKIPASKMQ ECCCCCCCCCHHHHH	56.16	21890473
419	Acetylation	VSPITGEKIPASKMQ ECCCCCCCCCHHHHH	56.16	26051181
421	Acetylation	PITGEKIPASKMQEH CCCCCCCCHHHHHHH	41.36	-
421	Ubiquitination	PITGEKIPASKMQEH CCCCCCCCHHHHHHH	41.36	-
422	Ubiquitination	ITGEKIPASKMQEHM CCCCCCCHHHHHHHH	25.84	-
423	Phosphorylation	TGEKIPASKMQEHMR CCCCCCHHHHHHHHH	24.25	-
424	Acetylation	GEKIPASKMQEHMRI CCCCCHHHHHHHHHH	46.86	23749302
424	Sumoylation	GEKIPASKMQEHMRI CCCCCHHHHHHHHHH	46.86	-
424	Sumoylation	GEKIPASKMQEHMRI CCCCCHHHHHHHHHH	46.86	28112733
424	Ubiquitination	GEKIPASKMQEHMRI CCCCCHHHHHHHHHH	46.86	-
430	Acetylation	SKMQEHMRIGLLDPR HHHHHHHHHCCCCHH	23.02	-
445	Phosphorylation	WLEQRDRSIREKQSD HHHHHHHHHHHHCCC	30.22	28102081
449	Ubiquitination	RDRSIREKQSDDEVY HHHHHHHHCCCCCCC	45.30	21890473
451	Phosphorylation	RSIREKQSDDEVYAP HHHHHHCCCCCCCCC	59.08	22167270
456	Phosphorylation	KQSDDEVYAPGLDIE HCCCCCCCCCCCCHH	12.67	30266825
456	Nitration	KQSDDEVYAPGLDIE HCCCCCCCCCCCCHH	12.67	-
464	Phosphorylation	APGLDIESSLKQLAE CCCCCHHHHHHHHHH	41.11	23403867
465	Phosphorylation	PGLDIESSLKQLAER CCCCHHHHHHHHHHH	27.13	23403867
467	Ubiquitination	LDIESSLKQLAERRT CCHHHHHHHHHHHCC	45.26	21890473
474	Phosphorylation	KQLAERRTDIFGVEE HHHHHHCCCCCCCCH	39.40	-
486	Acetylation	VEETAIGKKIGEEEI CCHHHHCCHHCHHHC	34.79	23954790
486	Ubiquitination	VEETAIGKKIGEEEI CCHHHHCCHHCHHHC	34.79	21890473
486	2-Hydroxyisobutyrylation	VEETAIGKKIGEEEI CCHHHHCCHHCHHHC	34.79	-
487	Ubiquitination	EETAIGKKIGEEEIQ CHHHHCCHHCHHHCC	51.21	-
495	Acetylation	IGEEEIQKPEEKVTW HCHHHCCCCHHHCCC	61.12	23749302
499	Acetylation	EIQKPEEKVTWDGHS HCCCCHHHCCCCCCC	43.21	7234929
499	Sumoylation	EIQKPEEKVTWDGHS HCCCCHHHCCCCCCC	43.21	28112733
506	Phosphorylation	KVTWDGHSGSMARTQ HCCCCCCCHHHHHHH	37.78	25159151
508	Phosphorylation	TWDGHSGSMARTQQA CCCCCCHHHHHHHHH	16.57	23401153
521	Phosphorylation	QAAQANITLQEQIEA HHHHHCCCHHHHHHH	23.38	28555341
531	Ubiquitination	EQIEAIHKAKGLVPE HHHHHHHHHCCCCCC	45.76	-
531	Acetylation	EQIEAIHKAKGLVPE HHHHHHHHHCCCCCC	45.76	25953088
533	Acetylation	IEAIHKAKGLVPEDD HHHHHHHCCCCCCCC	58.54	26051181
542	Sumoylation	LVPEDDTKEKIGPSK CCCCCCCCCCCCCCC	65.10	-
542	Sumoylation	LVPEDDTKEKIGPSK CCCCCCCCCCCCCCC	65.10	28112733
578	Methylation	PPITSVPRPPTMPPP CCCCCCCCCCCCCCC	47.91	115916569
587	Methylation	PTMPPPVRTTVVSAV CCCCCCCEEEEEEEE	30.38	115916573
588	Phosphorylation	TMPPPVRTTVVSAVP CCCCCCEEEEEEEEE	24.95	27690223
589	Phosphorylation	MPPPVRTTVVSAVPV CCCCCEEEEEEEEEC	14.35	27690223
592	Phosphorylation	PVRTTVVSAVPVMPR CCEEEEEEEEECCCC	21.15	27690223
599	Dimethylation	SAVPVMPRPPMASVV EEEECCCCCCCCEEE	29.83	-
599	Methylation	SAVPVMPRPPMASVV EEEECCCCCCCCEEE	29.83	115386603
604	Phosphorylation	MPRPPMASVVRLPPG CCCCCCCEEEECCCC	18.20	27690223
607	Dimethylation	PPMASVVRLPPGSVI CCCCEEEECCCCCEE	39.04	-
607	Methylation	PPMASVVRLPPGSVI CCCCEEEECCCCCEE	39.04	115390629
612	Phosphorylation	VVRLPPGSVIAPMPP EEECCCCCEEECCCC	19.00	27690223
643	Ubiquitination	PPIMAPRPPPMIVPT CCCCCCCCCCEECCC	35.97	-
686	Sumoylation	EPTSKKLKTEDSLMP CCCCCCCCCHHHCCC	59.76	-
686	Sumoylation	EPTSKKLKTEDSLMP CCCCCCCCCHHHCCC	59.76	28112733
687	Phosphorylation	PTSKKLKTEDSLMPE CCCCCCCCHHHCCCH	56.30	21406692
690	Phosphorylation	KKLKTEDSLMPEEEF CCCCCHHHCCCHHHH	21.97	20068231
692	Sulfoxidation	LKTEDSLMPEEEFLR CCCHHHCCCHHHHHH	4.55	21406390
702	Ubiquitination	EEFLRRNKGPVSIKV HHHHHCCCCCEEEEE	63.88	-
702	2-Hydroxyisobutyrylation	EEFLRRNKGPVSIKV HHHHHCCCCCEEEEE	63.88	-
708	Ubiquitination	NKGPVSIKVQVPNMQ CCCCEEEEEECCCCC	21.07	21890473
717	Malonylation	QVPNMQDKTEWKLNG ECCCCCCCCEEEECC	31.30	26320211
717	Acetylation	QVPNMQDKTEWKLNG ECCCCCCCCEEEECC	31.30	26051181
718	Phosphorylation	VPNMQDKTEWKLNGQ CCCCCCCCEEEECCE	56.20	-
743	Ubiquitination	QVSVIKVKIHEATGM CEEEEEEEEEEHHCC	33.09	-
743	2-Hydroxyisobutyrylation	QVSVIKVKIHEATGM CEEEEEEEEEEHHCC	33.09	-
754	Ubiquitination	ATGMPAGKQKLQYEG HHCCCCCCCEEEEEE	46.49	-
756	Acetylation	GMPAGKQKLQYEGIF CCCCCCCEEEEEEEE	40.83	25953088
756	Malonylation	GMPAGKQKLQYEGIF CCCCCCCEEEEEEEE	40.83	26320211
759	Phosphorylation	AGKQKLQYEGIFIKD CCCCEEEEEEEEECC	26.93	28112733

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 SF3A1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SF3A1_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 SF3A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRP11_YEAST	PRP11	physical	8718683
PRP9_YEAST	PRP9	physical	8718683
SF3A3_HUMAN	SF3A3	physical	11533230
SF3A3_HUMAN	SF3A3	physical	8022796
SF3A3_HUMAN	SF3A3	physical	22939629
SF3A2_HUMAN	SF3A2	physical	22939629
SF3B3_HUMAN	SF3B3	physical	22939629
SF3B1_HUMAN	SF3B1	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
SF3B4_HUMAN	SF3B4	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
SNUT2_HUMAN	USP39	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
SK2L2_HUMAN	SKIV2L2	physical	22939629
SYF1_HUMAN	XAB2	physical	22939629
SFPQ_HUMAN	SFPQ	physical	22939629
TRA2A_HUMAN	TRA2A	physical	22939629
TRI55_HUMAN	TRIM55	physical	22939629
TPBG_HUMAN	TPBG	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
SSBP_HUMAN	SSBP1	physical	22939629
TSKS_HUMAN	TSKS	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
SP16H_HUMAN	SUPT16H	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
TOX4_HUMAN	TOX4	physical	22939629
VASN_HUMAN	VASN	physical	22939629
TR112_HUMAN	TRMT112	physical	22939629
SRP54_HUMAN	SRP54	physical	22939629
PR40A_HUMAN	PRPF40A	physical	22365833
SF3A2_HUMAN	SF3A2	physical	22365833
SF3A3_HUMAN	SF3A3	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
SF01_HUMAN	SF1	physical	22365833
DDX42_HUMAN	DDX42	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
RFOX2_HUMAN	RBFOX2	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
SF3A3_HUMAN	SF3A3	physical	17098193
BRCC3_HUMAN	BRCC3	physical	22863883
CCDC6_HUMAN	CCDC6	physical	22863883
GAPD1_HUMAN	GAPVD1	physical	22863883
HDAC1_HUMAN	HDAC1	physical	22863883
HNRPR_HUMAN	HNRNPR	physical	22863883
GCR_HUMAN	NR3C1	physical	22863883
PP4R2_HUMAN	PPP4R2	physical	22863883
P4R3A_HUMAN	SMEK1	physical	22863883
ACTZ_HUMAN	ACTR1A	physical	26344197
DDX46_HUMAN	DDX46	physical	26344197
IF4G1_HUMAN	EIF4G1	physical	26344197
41_HUMAN	EPB41	physical	26344197
T2FA_HUMAN	GTF2F1	physical	26344197
MCM5_HUMAN	MCM5	physical	26344197
PRP19_HUMAN	PRPF19	physical	26344197
PRP6_HUMAN	PRPF6	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
SNUT1_HUMAN	SART1	physical	26344197
SMRC1_HUMAN	SMARCC1	physical	26344197
SMRC2_HUMAN	SMARCC2	physical	26344197
RU2A_HUMAN	SNRPA1	physical	26344197
SR140_HUMAN	U2SURP	physical	26344197
ZN830_HUMAN	ZNF830	physical	26344197
HSP7C_HUMAN	HSPA8	physical	28514442
CATH_HUMAN	CTSH	physical	28514442
SF3A3_HUMAN	SF3A3	physical	28514442
SAP3_HUMAN	GM2A	physical	28514442
CALL3_HUMAN	CALML3	physical	28514442
CYTM_HUMAN	CST6	physical	28514442
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	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 SF3A1_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-55 AND LYS-251, 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-320; SER-329; SER-359AND SER-451, 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-329; SER-359 ANDSER-413, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASSSPECTROMETRY.	18318008 [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-329; SER-413 ANDSER-451, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASSSPECTROMETRY.	19367720 [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 SER-320; SER-329 ANDSER-359, 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-329 AND SER-359, ANDMASS 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-359, AND MASSSPECTROMETRY.	15302935 [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-124, AND MASSSPECTROMETRY.	17525332 [Abstract]
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