DDX24_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DDX24_HUMAN
• UniProt AC: Q9GZR7
• Protein Name: ATP-dependent RNA helicase DDX24
• Gene Name: DDX24
• Organism: Homo sapiens (Human).
• Sequence Length: 859
• Protein Description: ATP-dependent RNA helicase..
• Protein Sequence: MKLKDTKSRPKQSSCGKFQTKGIKVVGKWKEVKIDPNMFADGQMDDLVCFEELTDYQLVSPAKNPSSLFSKEAPKRKAQAVSEEEEEEEGKSSSPKKKIKLKKSKNVATEGTSTQKEFEVKDPELEAQGDDMVCDDPEAGEMTSENLVQTAPKKKKNKGKKGLEPSQSTAAKVPKKAKTWIPEVHDQKADVSAWKDLFVPRPVLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHAVLQWQKRNAAPPPSNTEAPPGETRTEAGAETRSPGKAEAESDALPDDTVIESEALPSDIAAEARAKTGGTVSDQALLFGDDDAGEGPSSLIREKPVPKQNENEEENLDKEQTGNLKQELDDKSATCKAYPKRPLLGLVLTPTRELAVQVKQHIDAVARFTGIKTAILVGGMSTQKQQRMLNRRPEIVVATPGRLWELIKEKHYHLRNLRQLRCLVVDEADRMVEKGHFAELSQLLEMLNDSQYNPKRQTLVFSATLTLVHQAPARILHKKHTKKMDKTAKLDLLMQKIGMRGKPKVIDLTRNEATVETLTETKIHCETDEKDFYLYYFLMQYPGRSLVFANSISCIKRLSGLLKVLDIMPLTLHACMHQKQRLRNLEQFARLEDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYVHRSGRTARATNEGLSLMLIGPEDVINFKKIYKTLKKDEDIPLFPVQTKYMDVVKERIRLARQIEKSEYRNFQACLHNSWIEQAAAALEIELEEDMYKGGKADQQEERRRQKQMKVLKKELRHLLSQPLFTESQKTKYPTQSGKPPLLVSAPSKSESALSCLSKQKKKKTKKPKEPQPEQPQPSTSAN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Ubiquitination	----MKLKDTKSRPK ----CCCCCCCCCCC	58.81	24816145
6	Phosphorylation	--MKLKDTKSRPKQS --CCCCCCCCCCCCC	29.36	-
17	Acetylation	PKQSSCGKFQTKGIK CCCCCCCCCCCCCEE	38.33	19608861
17	Ubiquitination	PKQSSCGKFQTKGIK CCCCCCCCCCCCCEE	38.33	19608861
21	Acetylation	SCGKFQTKGIKVVGK CCCCCCCCCEEEEEE	48.10	23749302
21	Ubiquitination	SCGKFQTKGIKVVGK CCCCCCCCCEEEEEE	48.10	33845483
24	Acetylation	KFQTKGIKVVGKWKE CCCCCCEEEEEECEE	39.27	25953088
28	Acetylation	KGIKVVGKWKEVKID CCEEEEEECEEEECC	43.41	26051181
54	Phosphorylation	LVCFEELTDYQLVSP EEEHHHCCCCCCCCC	35.62	28450419
56	Phosphorylation	CFEELTDYQLVSPAK EHHHCCCCCCCCCCC	9.86	28450419
60	Phosphorylation	LTDYQLVSPAKNPSS CCCCCCCCCCCCHHH	27.94	25159151
66	Phosphorylation	VSPAKNPSSLFSKEA CCCCCCHHHCCCCCC	49.41	28450419
67	Phosphorylation	SPAKNPSSLFSKEAP CCCCCHHHCCCCCCC	34.39	28450419
70	Phosphorylation	KNPSSLFSKEAPKRK CCHHHCCCCCCCHHH	34.57	28450419
71	Acetylation	NPSSLFSKEAPKRKA CHHHCCCCCCCHHHC	51.03	19608861
71	Ubiquitination	NPSSLFSKEAPKRKA CHHHCCCCCCCHHHC	51.03	32015554
82	Phosphorylation	KRKAQAVSEEEEEEE HHHCCCCCHHHHHHC	42.16	29255136
92	Phosphorylation	EEEEEGKSSSPKKKI HHHHCCCCCCCCHHH	47.07	23401153
93	Phosphorylation	EEEEGKSSSPKKKIK HHHCCCCCCCCHHHE	54.89	22167270
94	Phosphorylation	EEEGKSSSPKKKIKL HHCCCCCCCCHHHEE	48.07	22167270
104	Phosphorylation	KKIKLKKSKNVATEG HHHEECCCCCCCCCC	28.07	29083192
109	Phosphorylation	KKSKNVATEGTSTQK CCCCCCCCCCCCCCE	30.57	29083192
112	Phosphorylation	KNVATEGTSTQKEFE CCCCCCCCCCCEEEE	23.51	25159151
113	Phosphorylation	NVATEGTSTQKEFEV CCCCCCCCCCEEEEE	39.43	25159151
114	Phosphorylation	VATEGTSTQKEFEVK CCCCCCCCCEEEEEC	43.42	25159151
143	Phosphorylation	DPEAGEMTSENLVQT CCCCCCCCHHHHHHC	28.69	-
166	Phosphorylation	GKKGLEPSQSTAAKV CCCCCCCCCCCCCCC	27.64	17525332
172	Acetylation	PSQSTAAKVPKKAKT CCCCCCCCCCCCCCC	57.51	25953088
172	Ubiquitination	PSQSTAAKVPKKAKT CCCCCCCCCCCCCCC	57.51	29967540
178	Ubiquitination	AKVPKKAKTWIPEVH CCCCCCCCCCCCHHC	53.95	29967540
188	Acetylation	IPEVHDQKADVSAWK CCHHCCCCCCHHHHH	53.24	25953088
188	Ubiquitination	IPEVHDQKADVSAWK CCHHCCCCCCHHHHH	53.24	29967540
192	Phosphorylation	HDQKADVSAWKDLFV CCCCCCHHHHHHHCC	29.03	22817900
195	2-Hydroxyisobutyrylation	KADVSAWKDLFVPRP CCCHHHHHHHCCCHH	44.25	-
195	Acetylation	KADVSAWKDLFVPRP CCCHHHHHHHCCCHH	44.25	26051181
195	Ubiquitination	KADVSAWKDLFVPRP CCCHHHHHHHCCCHH	44.25	21890473
208	Phosphorylation	RPVLRALSFLGFSAP HHHHHHHHHHCCCCC	19.90	24114839
213	Phosphorylation	ALSFLGFSAPTPIQA HHHHHCCCCCCHHHH	31.38	24114839
230	2-Hydroxyisobutyrylation	LAPAIRDKLDILGAA HHHHHHHHCEEECEE	37.90	-
230	Acetylation	LAPAIRDKLDILGAA HHHHHHHHCEEECEE	37.90	25953088
230	Ubiquitination	LAPAIRDKLDILGAA HHHHHHHHCEEECEE	37.90	29967540
268	Phosphorylation	RNAAPPPSNTEAPPG HCCCCCCCCCCCCCC	63.26	20068231
270	Phosphorylation	AAPPPSNTEAPPGET CCCCCCCCCCCCCCC	37.55	21406692
277	Phosphorylation	TEAPPGETRTEAGAE CCCCCCCCCCCCCCC	49.13	21406692
279	Phosphorylation	APPGETRTEAGAETR CCCCCCCCCCCCCCC	37.29	23401153
285	Phosphorylation	RTEAGAETRSPGKAE CCCCCCCCCCCCCHH	35.59	25159151
287	Phosphorylation	EAGAETRSPGKAEAE CCCCCCCCCCCHHHH	45.48	29255136
290	Ubiquitination	AETRSPGKAEAESDA CCCCCCCCHHHHCCC	46.57	22817900
295	Phosphorylation	PGKAEAESDALPDDT CCCHHHHCCCCCCCC	34.92	29255136
302	Phosphorylation	SDALPDDTVIESEAL CCCCCCCCEEECCCC	30.66	29255136
306	Phosphorylation	PDDTVIESEALPSDI CCCCEEECCCCCHHH	19.62	29255136
311	Phosphorylation	IESEALPSDIAAEAR EECCCCCHHHHHHHH	42.36	23927012
320	Ubiquitination	IAAEARAKTGGTVSD HHHHHHHHHCCCCCC	41.99	21906983
342	Phosphorylation	DDAGEGPSSLIREKP CCCCCCCCCHHCCCC	48.94	25627689
343	Phosphorylation	DAGEGPSSLIREKPV CCCCCCCCHHCCCCC	30.83	25159151
370	Sumoylation	KEQTGNLKQELDDKS HHHHCCHHHHHCCCC	45.81	-
370	Sumoylation	KEQTGNLKQELDDKS HHHHCCHHHHHCCCC	45.81	28112733
381	Ubiquitination	DDKSATCKAYPKRPL CCCCCCCCCCCCCCC	46.75	29967540
394	Phosphorylation	PLLGLVLTPTRELAV CCEEEEEECCHHHHH	18.35	20068231
396	Phosphorylation	LGLVLTPTRELAVQV EEEEEECCHHHHHHH	31.38	20068231
404	2-Hydroxyisobutyrylation	RELAVQVKQHIDAVA HHHHHHHHHHHHHHH	21.04	-
404	Ubiquitination	RELAVQVKQHIDAVA HHHHHHHHHHHHHHH	21.04	33845483
414	Phosphorylation	IDAVARFTGIKTAIL HHHHHHHHCCCEEEE	32.23	20860994
425	Sulfoxidation	TAILVGGMSTQKQQR EEEECCCCCHHHHHH	3.01	21406390
429	Ubiquitination	VGGMSTQKQQRMLNR CCCCCHHHHHHHHCC	48.78	22505724
444	Phosphorylation	RPEIVVATPGRLWEL CCCEEEECCCHHHHH	18.05	28674419
453	Ubiquitination	GRLWELIKEKHYHLR CHHHHHHHHHCHHHC	73.64	29967540
455	2-Hydroxyisobutyrylation	LWELIKEKHYHLRNL HHHHHHHHCHHHCCH	44.45	-
475	Methylation	LVVDEADRMVEKGHF EEEEHHHHHHHHCCH	37.79	-
503	Phosphorylation	QYNPKRQTLVFSATL CCCCCCCCEEEEEEE	28.99	20068231
507	Phosphorylation	KRQTLVFSATLTLVH CCCCEEEEEEEEHHH	16.92	20068231
509	Phosphorylation	QTLVFSATLTLVHQA CCEEEEEEEEHHHHC	21.05	20068231
511	Phosphorylation	LVFSATLTLVHQAPA EEEEEEEEHHHHCCH	23.52	20068231
532	Phosphorylation	HTKKMDKTAKLDLLM HCCCCCHHHHHHHHH	25.43	20068231
534	Acetylation	KKMDKTAKLDLLMQK CCCCHHHHHHHHHHH	48.00	25953088
541	Acetylation	KLDLLMQKIGMRGKP HHHHHHHHHCCCCCC	27.54	25953088
541	Ubiquitination	KLDLLMQKIGMRGKP HHHHHHHHHCCCCCC	27.54	-
547	Ubiquitination	QKIGMRGKPKVIDLT HHHCCCCCCEEEECC	31.16	24816145
549	Ubiquitination	IGMRGKPKVIDLTRN HCCCCCCEEEECCCC	56.14	29967540
567	Ubiquitination	VETLTETKIHCETDE EEEEEECEEEEECCC	24.99	29967540
601	Acetylation	ANSISCIKRLSGLLK HHHHHHHHHHHHHHH	52.17	25953088
601	Ubiquitination	ANSISCIKRLSGLLK HHHHHHHHHHHHHHH	52.17	-
624	Acetylation	LHACMHQKQRLRNLE HHHHHHHHHHHHCHH	23.78	25953088
624	Sumoylation	LHACMHQKQRLRNLE HHHHHHHHHHHHCHH	23.78	28112733
624	Ubiquitination	LHACMHQKQRLRNLE HHHHHHHHHHHHCHH	23.78	-
655	Ubiquitination	ARGLDIPKVQHVIHY HCCCCCCCCEEEEEE	55.66	33845483
700	Acetylation	PEDVINFKKIYKTLK HHHHCCHHHHHHHHC	33.50	24431627
700	Ubiquitination	PEDVINFKKIYKTLK HHHHCCHHHHHHHHC	33.50	21906983
701	Ubiquitination	EDVINFKKIYKTLKK HHHCCHHHHHHHHCC	47.32	22817900
703	Phosphorylation	VINFKKIYKTLKKDE HCCHHHHHHHHCCCC	13.55	-
704	Ubiquitination	INFKKIYKTLKKDED CCHHHHHHHHCCCCC	51.35	22817900
705	Phosphorylation	NFKKIYKTLKKDEDI CHHHHHHHHCCCCCC	27.17	-
708	Ubiquitination	KIYKTLKKDEDIPLF HHHHHHCCCCCCCCC	70.26	29967540
719	Phosphorylation	IPLFPVQTKYMDVVK CCCCCCCCCHHHHHH	25.11	29978859
720	2-Hydroxyisobutyrylation	PLFPVQTKYMDVVKE CCCCCCCCHHHHHHH	22.83	-
720	Ubiquitination	PLFPVQTKYMDVVKE CCCCCCCCHHHHHHH	22.83	21906983
726	Ubiquitination	TKYMDVVKERIRLAR CCHHHHHHHHHHHHH	40.92	23503661
737	Ubiquitination	RLARQIEKSEYRNFQ HHHHHHHHHHHHCHH	50.66	24816145
769	Ubiquitination	ELEEDMYKGGKADQQ HCHHHHHCCCCHHHH	55.33	22817900
772	Ubiquitination	EDMYKGGKADQQEER HHHHCCCCHHHHHHH	58.41	22817900
786	Ubiquitination	RRRQKQMKVLKKELR HHHHHHHHHHHHHHH	41.75	24816145
797	Phosphorylation	KELRHLLSQPLFTES HHHHHHHCCCCCCCC	35.79	23312004
804	Phosphorylation	SQPLFTESQKTKYPT CCCCCCCCCCCCCCC	33.64	28555341
806	Ubiquitination	PLFTESQKTKYPTQS CCCCCCCCCCCCCCC	57.15	22817900
807	Phosphorylation	LFTESQKTKYPTQSG CCCCCCCCCCCCCCC	28.33	28152594
808	Sumoylation	FTESQKTKYPTQSGK CCCCCCCCCCCCCCC	57.16	-
808	Acetylation	FTESQKTKYPTQSGK CCCCCCCCCCCCCCC	57.16	25953088
808	Sumoylation	FTESQKTKYPTQSGK CCCCCCCCCCCCCCC	57.16	28112733
808	Ubiquitination	FTESQKTKYPTQSGK CCCCCCCCCCCCCCC	57.16	22817900
809	Phosphorylation	TESQKTKYPTQSGKP CCCCCCCCCCCCCCC	19.42	28152594
811	Phosphorylation	SQKTKYPTQSGKPPL CCCCCCCCCCCCCCE	32.07	28152594
813	Phosphorylation	KTKYPTQSGKPPLLV CCCCCCCCCCCCEEE	51.79	28152594
815	Acetylation	KYPTQSGKPPLLVSA CCCCCCCCCCEEEEC	49.02	25953088
815	Ubiquitination	KYPTQSGKPPLLVSA CCCCCCCCCCEEEEC	49.02	29967540
821	Phosphorylation	GKPPLLVSAPSKSES CCCCEEEECCCCCHH	34.14	27251275
824	Phosphorylation	PLLVSAPSKSESALS CEEEECCCCCHHHHH	48.83	28555341
825	Acetylation	LLVSAPSKSESALSC EEEECCCCCHHHHHH	58.12	26051181
825	Sumoylation	LLVSAPSKSESALSC EEEECCCCCHHHHHH	58.12	28112733
826	Phosphorylation	LVSAPSKSESALSCL EEECCCCCHHHHHHH	40.91	20068231
828	Phosphorylation	SAPSKSESALSCLSK ECCCCCHHHHHHHHH	41.42	20068231
831	Phosphorylation	SKSESALSCLSKQKK CCCHHHHHHHHHHHC	16.84	20068231
834	Phosphorylation	ESALSCLSKQKKKKT HHHHHHHHHHHCCCC	37.05	25159151
835	Acetylation	SALSCLSKQKKKKTK HHHHHHHHHHCCCCC	53.87	25953088
835	Ubiquitination	SALSCLSKQKKKKTK HHHHHHHHHHCCCCC	53.87	33845483
857	Phosphorylation	EQPQPSTSAN----- CCCCCCCCCC-----	30.10	25627689

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
82	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:24980433

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DDX24_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DDX24_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCS1_HUMAN	BCS1L	physical	16169070
TRDMT_HUMAN	TRDMT1	physical	16169070
EIF3E_HUMAN	EIF3E	physical	16169070
MKS1_HUMAN	MKS1	physical	16169070
HS90B_HUMAN	HSP90AB1	physical	16169070
CENPR_HUMAN	ITGB3BP	physical	16169070
PA1B3_HUMAN	PAFAH1B3	physical	16169070
TPIS_HUMAN	TPI1	physical	16169070
VDAC3_HUMAN	VDAC3	physical	16169070
IF4A2_MOUSE	Eif4a2	physical	16169070
GRP78_HUMAN	HSPA5	physical	16169070
PIN1_HUMAN	PIN1	physical	16169070
SPTN1_HUMAN	SPTAN1	physical	16169070
GIT1_HUMAN	GIT1	physical	16169070
DPOA2_HUMAN	POLA2	physical	16169070
RS25_HUMAN	RPS25	physical	22939629
RPAC1_HUMAN	POLR1C	physical	22939629
INO80_HUMAN	INO80	physical	22939629
DKC1_HUMAN	DKC1	physical	22939629
DDX31_HUMAN	DDX31	physical	22939629
GLRA2_HUMAN	GLRA2	physical	21988832
BCCIP_HUMAN	BCCIP	physical	26344197
BRX1_HUMAN	BRIX1	physical	26344197
DDX27_HUMAN	DDX27	physical	26344197
DDX55_HUMAN	DDX55	physical	26344197
DDX56_HUMAN	DDX56	physical	26344197
FBRL_HUMAN	FBL	physical	26344197
SPB1_HUMAN	FTSJ3	physical	26344197
GNL3_HUMAN	GNL3	physical	26344197
GRWD1_HUMAN	GRWD1	physical	26344197
NOG1_HUMAN	GTPBP4	physical	26344197
INT6_HUMAN	INTS6	physical	26344197
KRR1_HUMAN	KRR1	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
NOC2L_HUMAN	NOC2L	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
NOP2_HUMAN	NOP2	physical	26344197
NOP56_HUMAN	NOP56	physical	26344197
NSA2_HUMAN	NSA2	physical	26344197
PESC_HUMAN	PES1	physical	26344197
PWP1_HUMAN	PWP1	physical	26344197
RBBP6_HUMAN	RBBP6	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
TBL3_HUMAN	TBL3	physical	26344197
TSR2_HUMAN	TSR2	physical	26344197
WDR12_HUMAN	WDR12	physical	26344197
XRN1_HUMAN	XRN1	physical	26344197
MDM2_MOUSE	Mdm2	physical	24980433
NUCL_HUMAN	NCL	physical	24980433
NIP7_HUMAN	NIP7	physical	24980433
COR1A_HUMAN	CORO1A	physical	27173435
IFT57_HUMAN	IFT57	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-17 AND LYS-71, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-82; SER-94; SER-287 ANDSER-295, AND MASS SPECTROMETRY.
PubMed: 19690332

"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-82, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-82, AND MASSSPECTROMETRY.
PubMed: 18318008

"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-82; SER-94; SER-287;SER-295 AND THR-302, AND MASS SPECTROMETRY.
PubMed: 18669648

"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-82, AND MASSSPECTROMETRY.
PubMed: 19007248

"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-166, AND MASSSPECTROMETRY.
PubMed: 17525332

"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-82, AND MASSSPECTROMETRY.
PubMed: 16964243

"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-82 AND SER-192, AND MASSSPECTROMETRY.
PubMed: 17081983

"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-82 AND THR-302, AND MASSSPECTROMETRY.
PubMed: 15302935