dbPTM

GEMI5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GEMI5_HUMAN
UniProt AC	Q8TEQ6
Protein Name	Gem-associated protein 5
Gene Name	GEMIN5
Organism	Homo sapiens (Human).
Sequence Length	1508
Subcellular Localization	Nucleus, nucleoplasm . Nucleus, gem . Cytoplasm . Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
Protein Description	Required for the assembly of the SMN complex that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. [PubMed: 16857593]
Protein Sequence	MGQEPRTLPPSPNWYCARCSDAVPGGLFGFAARTSVFLVRVGPGAGESPGTPPFRVIGELVGHTERVSGFTFSHHPGQYNLCATSSDDGTVKIWDVETKTVVTEHALHQHTISTLHWSPRVKDLIVSGDEKGVVFCYWFNRNDSQHLFIEPRTIFCLTCSPHHEDLVAIGYKDGIVVIIDISKKGEVIHRLRGHDDEIHSIAWCPLPGEDCLSINQEETSEEAEITNGNAVAQAPVTKGCYLATGSKDQTIRIWSCSRGRGVMILKLPFLKRRGGGIDPTVKERLWLTLHWPSNQPTQLVSSCFGGELLQWDLTQSWRRKYTLFSASSEGQNHSRIVFNLCPLQTEDDKQLLLSTSMDRDVKCWDIATLECSWTLPSLGGFAYSLAFSSVDIGSLAIGVGDGMIRVWNTLSIKNNYDVKNFWQGVKSKVTALCWHPTKEGCLAFGTDDGKVGLYDTYSNKPPQISSTYHKKTVYTLAWGPPVPPMSLGGEGDRPSLALYSCGGEGIVLQHNPWKLSGEAFDINKLIRDTNSIKYKLPVHTEISWKADGKIMALGNEDGSIEIFQIPNLKLICTIQQHHKLVNTISWHHEHGSQPELSYLMASGSNNAVIYVHNLKTVIESSPESPVTITEPYRTLSGHTAKITSVAWSPHHDGRLVSASYDGTAQVWDALREEPLCNFRGHRGRLLCVAWSPLDPDCIYSGADDFCVHKWLTSMQDHSRPPQGKKSIELEKKRLSQPKAKPKKKKKPTLRTPVKLESIDGNEEESMKENSGPVENGVSDQEGEEQAREPELPCGLAPAVSREPVICTPVSSGFEKSKVTINNKVILLKKEPPKEKPETLIKKRKARSLLPLSTSLDHRSKEELHQDCLVLATAKHSRELNEDVSADVEERFHLGLFTDRATLYRMIDIEGKGHLENGHPELFHQLMLWKGDLKGVLQTAAERGELTDNLVAMAPAAGYHVWLWAVEAFAKQLCFQDQYVKAASHLLSIHKVYEAVELLKSNHFYREAIAIAKARLRPEDPVLKDLYLSWGTVLERDGHYAVAAKCYLGATCAYDAAKVLAKKGDAASLRTAAELAAIVGEDELSASLALRCAQELLLANNWVGAQEALQLHESLQGQRLVFCLLELLSRHLEEKQLSEGKSSSSYHTWNTGTEGPFVERVTAVWKSIFSLDTPEQYQEAFQKLQNIKYPSATNNTPAKQLLLHICHDLTLAVLSQQMASWDEAVQALLRAVVRSYDSGSFTIMQEVYSAFLPDGCDHLRDKLGDHQSPATPAFKSLEAFFLYGRLYEFWWSLSRPCPNSSVWVRAGHRTLSVEPSQQLDTASTEETDPETSQPEPNRPSELDLRLTEEGERMLSTFKELFSEKHASLQNSQRTVAEVQETLAEMIRQHQKSQLCKSTANGPDKNEPEVEAEQPLCSSQSQCKEEKNEPLSLPELTKRLTEANQRMAKFPESIKAWPFPDVLECCLVLLLIRSHFPGCLAQEMQQQAQELLQKYGNTKTYRRHCQTFCM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Phosphorylation	VGPGAGESPGTPPFR ECCCCCCCCCCCCCE	27.93	29255136
51	Phosphorylation	GAGESPGTPPFRVIG CCCCCCCCCCCEEHH	31.04	29255136
118	Phosphorylation	TISTLHWSPRVKDLI CHHHCCCCCHHHEEE	7.65	24719451
122	Ubiquitination	LHWSPRVKDLIVSGD CCCCCHHHEEEEECC	48.36	-
127	Phosphorylation	RVKDLIVSGDEKGVV HHHEEEEECCCCEEE	33.27	-
144	Phosphorylation	YWFNRNDSQHLFIEP EEECCCCCCCEEECC	24.05	20873877
247	Acetylation	CYLATGSKDQTIRIW CEEECCCCCCEEEEE	56.02	26051181
247	Ubiquitination	CYLATGSKDQTIRIW CEEECCCCCCEEEEE	56.02	-
260	Methylation	IWSCSRGRGVMILKL EEEECCCCCEEEEEC	33.16	-
273	Methylation	KLPFLKRRGGGIDPT ECCCHHHCCCCCCCH	46.66	-
282	Acetylation	GGIDPTVKERLWLTL CCCCCHHHHEEEEEE	39.33	26051181
282	Ubiquitination	GGIDPTVKERLWLTL CCCCCHHHHEEEEEE	39.33	21906983
320	Acetylation	LTQSWRRKYTLFSAS CCHHHHHHEEEEECC	33.73	26051181
345	Phosphorylation	FNLCPLQTEDDKQLL EEECCCCCCCHHHHH	49.41	22817900
354	Phosphorylation	DDKQLLLSTSMDRDV CHHHHHHHCCCCCCC	20.57	25072903
355	Phosphorylation	DKQLLLSTSMDRDVK HHHHHHHCCCCCCCC	28.21	25072903
356	Phosphorylation	KQLLLSTSMDRDVKC HHHHHHCCCCCCCCC	18.47	25072903
413	Ubiquitination	VWNTLSIKNNYDVKN EEEEEEECCCCCCCH	35.45	-
419	Acetylation	IKNNYDVKNFWQGVK ECCCCCCCHHHHHHH	43.46	26051181
419	Ubiquitination	IKNNYDVKNFWQGVK ECCCCCCCHHHHHHH	43.46	-
426	Acetylation	KNFWQGVKSKVTALC CHHHHHHHHHHEEEE	51.92	25953088
428	Malonylation	FWQGVKSKVTALCWH HHHHHHHHHEEEEEC	37.58	26320211
437	Phosphorylation	TALCWHPTKEGCLAF EEEEECCCCCCCEEE	28.92	25599653
438	Acetylation	ALCWHPTKEGCLAFG EEEECCCCCCCEEEE	57.47	26051181
450	Acetylation	AFGTDDGKVGLYDTY EEECCCCCEECEECC	39.87	26051181
450	Ubiquitination	AFGTDDGKVGLYDTY EEECCCCCEECEECC	39.87	-
460	Acetylation	LYDTYSNKPPQISST CEECCCCCCCCCCEE	52.73	26051181
460	Ubiquitination	LYDTYSNKPPQISST CEECCCCCCCCCCEE	52.73	-
470	Ubiquitination	QISSTYHKKTVYTLA CCCEEECCCEEEEEE	39.46	-
474	Phosphorylation	TYHKKTVYTLAWGPP EECCCEEEEEEECCC	10.98	25884760
516	Phosphorylation	QHNPWKLSGEAFDIN ECCCCCCCCCEECHH	30.75	23312004
524	Acetylation	GEAFDINKLIRDTNS CCEECHHHHHCCCCC	45.70	26051181
524	Ubiquitination	GEAFDINKLIRDTNS CCEECHHHHHCCCCC	45.70	-
531	Phosphorylation	KLIRDTNSIKYKLPV HHHCCCCCCEEECCC	23.66	28857561
533	Acetylation	IRDTNSIKYKLPVHT HCCCCCCEEECCCCC	35.83	26051181
535	Acetylation	DTNSIKYKLPVHTEI CCCCCEEECCCCCEE	41.11	26051181
535	Ubiquitination	DTNSIKYKLPVHTEI CCCCCEEECCCCCEE	41.11	-
616	O-linked_Glycosylation	IYVHNLKTVIESSPE EEEEEEEEEEECCCC	29.86	30059200
620	O-linked_Glycosylation	NLKTVIESSPESPVT EEEEEEECCCCCCCE	39.82	30059200
620	Phosphorylation	NLKTVIESSPESPVT EEEEEEECCCCCCCE	39.82	23186163
621	Phosphorylation	LKTVIESSPESPVTI EEEEEECCCCCCCEE	21.64	25850435
624	O-linked_Glycosylation	VIESSPESPVTITEP EEECCCCCCCEECCC	28.23	30059200
624	Phosphorylation	VIESSPESPVTITEP EEECCCCCCCEECCC	28.23	21815630
627	Phosphorylation	SSPESPVTITEPYRT CCCCCCCEECCCEEE	26.09	23186163
643	Phosphorylation	SGHTAKITSVAWSPH CCCEEEEEEEEECCC	19.22	20873877
644	Phosphorylation	GHTAKITSVAWSPHH CCEEEEEEEEECCCC	17.20	20873877
648	Phosphorylation	KITSVAWSPHHDGRL EEEEEEECCCCCCCE	12.48	20873877
657	Phosphorylation	HHDGRLVSASYDGTA CCCCCEEEEEECCCH	18.98	27050516
724	Ubiquitination	HSRPPQGKKSIELEK CCCCCCCCCCHHHHH	37.79	-
726	Phosphorylation	RPPQGKKSIELEKKR CCCCCCCCHHHHHHH	25.44	21815630
735	Phosphorylation	ELEKKRLSQPKAKPK HHHHHHHCCCCCCCC	48.77	28176443
748	Phosphorylation	PKKKKKPTLRTPVKL CCCCCCCCCCCCEEE	37.44	30576142
751	Phosphorylation	KKKPTLRTPVKLESI CCCCCCCCCEEEEEC	35.23	25159151
754	Sumoylation	PTLRTPVKLESIDGN CCCCCCEEEEECCCC	47.98	-
754	Acetylation	PTLRTPVKLESIDGN CCCCCCEEEEECCCC	47.98	23236377
754	Sumoylation	PTLRTPVKLESIDGN CCCCCCEEEEECCCC	47.98	28112733
754	Ubiquitination	PTLRTPVKLESIDGN CCCCCCEEEEECCCC	47.98	-
757	Phosphorylation	RTPVKLESIDGNEEE CCCEEEEECCCCCHH	36.09	28355574
765	Phosphorylation	IDGNEEESMKENSGP CCCCCHHHHHCCCCC	38.13	21815630
770	Phosphorylation	EESMKENSGPVENGV HHHHHCCCCCCCCCC	45.63	28731282
778	Phosphorylation	GPVENGVSDQEGEEQ CCCCCCCCCHHHHHH	34.67	19664994
800	Phosphorylation	CGLAPAVSREPVICT CCCCCCCCCCCEEEE	32.79	20068231
806	Glutathionylation	VSREPVICTPVSSGF CCCCCEEEECCCCCC	3.42	22555962
807	Phosphorylation	SREPVICTPVSSGFE CCCCEEEECCCCCCC	18.66	25159151
810	O-linked_Glycosylation	PVICTPVSSGFEKSK CEEEECCCCCCCCCE	26.41	30059200
810	Phosphorylation	PVICTPVSSGFEKSK CEEEECCCCCCCCCE	26.41	21815630
811	Phosphorylation	VICTPVSSGFEKSKV EEEECCCCCCCCCEE	47.97	24732914
815	Acetylation	PVSSGFEKSKVTINN CCCCCCCCCEEEECC	54.00	26051181
815	Methylation	PVSSGFEKSKVTINN CCCCCCCCCEEEECC	54.00	-
838	Phosphorylation	PPKEKPETLIKKRKA CCCCCCCHHHHHHHH	42.16	29214152
847	Phosphorylation	IKKRKARSLLPLSTS HHHHHHHHHCCCCCC	38.83	25159151
852	Phosphorylation	ARSLLPLSTSLDHRS HHHHCCCCCCCCCCC	17.63	20873877
853	Phosphorylation	RSLLPLSTSLDHRSK HHHCCCCCCCCCCCH	40.78	21712546
854	Phosphorylation	SLLPLSTSLDHRSKE HHCCCCCCCCCCCHH	28.55	25159151
859	Phosphorylation	STSLDHRSKEELHQD CCCCCCCCHHHHHHH	40.79	20873877
860	Acetylation	TSLDHRSKEELHQDC CCCCCCCHHHHHHHH	55.98	26051181
860	Malonylation	TSLDHRSKEELHQDC CCCCCCCHHHHHHHH	55.98	32601280
860	Ubiquitination	TSLDHRSKEELHQDC CCCCCCCHHHHHHHH	55.98	-
867	Glutathionylation	KEELHQDCLVLATAK HHHHHHHHHHHHHHH	1.97	22555962
897	Phosphorylation	RFHLGLFTDRATLYR HHHHCCCCCCHHEEE	29.62	-
911	Acetylation	RMIDIEGKGHLENGH EEEECCCCCCHHCCC	30.30	19824993
933	Ubiquitination	MLWKGDLKGVLQTAA HHCCCCHHHHHHHHH	52.27	21906983
978	Phosphorylation	QLCFQDQYVKAASHL HHHCCHHHHHHHHHH	16.53	28152594
983	Phosphorylation	DQYVKAASHLLSIHK HHHHHHHHHHHHHHH	21.37	20860994
1012	2-Hydroxyisobutyrylation	REAIAIAKARLRPED HHHHHHHHHCCCCCC	28.11	-
1012	Ubiquitination	REAIAIAKARLRPED HHHHHHHHHCCCCCC	28.11	-
1026	Phosphorylation	DPVLKDLYLSWGTVL CCHHHHHHCCCCCEE	14.60	-
1039	Phosphorylation	VLERDGHYAVAAKCY EEEECCCEEEEEEEE	14.32	27642862
1053	Phosphorylation	YLGATCAYDAAKVLA ECCCHHHHHHHHHHH	14.30	22817900
1057	Acetylation	TCAYDAAKVLAKKGD HHHHHHHHHHHHCCC	39.23	26051181
1122	S-palmitoylation	QGQRLVFCLLELLSR HHHHHHHHHHHHHHH	3.10	29575903
1128	Phosphorylation	FCLLELLSRHLEEKQ HHHHHHHHHHHHHHH	30.22	24719451
1134	2-Hydroxyisobutyrylation	LSRHLEEKQLSEGKS HHHHHHHHHHCCCCC	47.35	-
1134	Acetylation	LSRHLEEKQLSEGKS HHHHHHHHHHCCCCC	47.35	26051181
1165	Ubiquitination	ERVTAVWKSIFSLDT HHHHHHHHHHHCCCC	27.37	-
1182	Ubiquitination	QYQEAFQKLQNIKYP HHHHHHHHHHCCCCC	45.66	-
1187	Acetylation	FQKLQNIKYPSATNN HHHHHCCCCCCCCCC	59.67	26051181
1187	Ubiquitination	FQKLQNIKYPSATNN HHHHHCCCCCCCCCC	59.67	21906983
1188	Phosphorylation	QKLQNIKYPSATNNT HHHHCCCCCCCCCCC	9.91	24114839
1190	Phosphorylation	LQNIKYPSATNNTPA HHCCCCCCCCCCCHH	44.64	28152594
1192	Phosphorylation	NIKYPSATNNTPAKQ CCCCCCCCCCCHHHH	33.08	30622161
1195	Phosphorylation	YPSATNNTPAKQLLL CCCCCCCCHHHHHHH	27.05	24114839
1261	Acetylation	GCDHLRDKLGDHQSP CCHHHHHHHCCCCCC	48.19	26051181
1267	Phosphorylation	DKLGDHQSPATPAFK HHHCCCCCCCCHHHH	17.06	25159151
1270	Phosphorylation	GDHQSPATPAFKSLE CCCCCCCCHHHHHHH	20.66	25159151
1309	Phosphorylation	WVRAGHRTLSVEPSQ EEEECCCEEEECHHH	20.08	23663014
1311	Phosphorylation	RAGHRTLSVEPSQQL EECCCEEEECHHHHC	24.66	23663014
1315	Phosphorylation	RTLSVEPSQQLDTAS CEEEECHHHHCCCCC	19.63	23663014
1320	Phosphorylation	EPSQQLDTASTEETD CHHHHCCCCCCCCCC	30.97	23663014
1322	Phosphorylation	SQQLDTASTEETDPE HHHCCCCCCCCCCCC	38.14	23663014
1323	Phosphorylation	QQLDTASTEETDPET HHCCCCCCCCCCCCC	35.06	23663014
1326	Phosphorylation	DTASTEETDPETSQP CCCCCCCCCCCCCCC	51.09	28348404
1330	Phosphorylation	TEETDPETSQPEPNR CCCCCCCCCCCCCCC	37.74	18691976
1331	Phosphorylation	EETDPETSQPEPNRP CCCCCCCCCCCCCCC	41.92	29978859
1339	Phosphorylation	QPEPNRPSELDLRLT CCCCCCCCHHCEEEC	47.78	27251275
1354	Phosphorylation	EEGERMLSTFKELFS HHHHHHHHHHHHHHH	23.58	24719451
1355	Phosphorylation	EGERMLSTFKELFSE HHHHHHHHHHHHHHH	34.46	24719451
1361	Phosphorylation	STFKELFSEKHASLQ HHHHHHHHHHHHHHH	59.36	24719451
1363	Acetylation	FKELFSEKHASLQNS HHHHHHHHHHHHHHH	43.18	23236377
1363	Malonylation	FKELFSEKHASLQNS HHHHHHHHHHHHHHH	43.18	26320211
1363	Ubiquitination	FKELFSEKHASLQNS HHHHHHHHHHHHHHH	43.18	19608861
1366	Phosphorylation	LFSEKHASLQNSQRT HHHHHHHHHHHHHHH	30.15	30622161
1380	Phosphorylation	TVAEVQETLAEMIRQ HHHHHHHHHHHHHHH	17.74	24425749
1390	Ubiquitination	EMIRQHQKSQLCKST HHHHHHHHHHHHHHC	37.74	-
1391	Phosphorylation	MIRQHQKSQLCKSTA HHHHHHHHHHHHHCC	23.09	18077418
1403	Acetylation	STANGPDKNEPEVEA HCCCCCCCCCCCCCC	67.36	26051181
1416	Phosphorylation	EAEQPLCSSQSQCKE CCCCCCCCCHHHHHH	38.81	25159151
1417	Phosphorylation	AEQPLCSSQSQCKEE CCCCCCCCHHHHHHH	32.62	21815630
1419	Phosphorylation	QPLCSSQSQCKEEKN CCCCCCHHHHHHHCC	39.22	28555341
1422	Acetylation	CSSQSQCKEEKNEPL CCCHHHHHHHCCCCC	62.36	26051181
1425	Acetylation	QSQCKEEKNEPLSLP HHHHHHHCCCCCCHH	68.64	26051181
1425	Ubiquitination	QSQCKEEKNEPLSLP HHHHHHHCCCCCCHH	68.64	-
1430	Phosphorylation	EEKNEPLSLPELTKR HHCCCCCCHHHHHHH	53.22	20873877
1435	Phosphorylation	PLSLPELTKRLTEAN CCCHHHHHHHHHHHH	16.68	29083192
1436	Ubiquitination	LSLPELTKRLTEANQ CCHHHHHHHHHHHHH	59.02	-

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 GEMI5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GEMI5_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 GEMI5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DDX20_HUMAN	DDX20	physical	11714716
GEMI4_HUMAN	GEMIN4	physical	11714716
GEMI2_HUMAN	GEMIN2	physical	11714716
SMN_HUMAN	SMN1	physical	11714716
SMD1_HUMAN	SNRPD1	physical	11714716
SMD2_HUMAN	SNRPD2	physical	11714716
SMD3_HUMAN	SNRPD3	physical	11714716
RUXE_HUMAN	SNRPE	physical	11714716
RUXF_HUMAN	SNRPF	physical	11714716
RUXG_HUMAN	SNRPG	physical	11714716
GEMI2_HUMAN	GEMIN2	physical	23221635
SMN_HUMAN	SMN1	physical	23221635
GEMI6_HUMAN	GEMIN6	physical	23221635
GEMI4_HUMAN	GEMIN4	physical	23221635
DDX20_HUMAN	DDX20	physical	23221635
IF4E_HUMAN	EIF4E	physical	16739988
M3K5_HUMAN	MAP3K5	physical	17541429
MK08_HUMAN	MAPK8	physical	17541429
MP2K4_HUMAN	MAP2K4	physical	17541429
PLOD1_HUMAN	PLOD1	physical	22863883
DDX20_HUMAN	DDX20	physical	24923560
NSD2_HUMAN	WHSC1	physical	24923560
TISD_HUMAN	ZFP36L2	physical	26496610
DDX3X_HUMAN	DDX3X	physical	26496610
DECR_HUMAN	DECR1	physical	26496610
ERF1_HUMAN	ETF1	physical	26496610
GOGA4_HUMAN	GOLGA4	physical	26496610
PFD1_HUMAN	PFDN1	physical	26496610
SMN_HUMAN	SMN1	physical	26496610
RU17_HUMAN	SNRNP70	physical	26496610
SMD1_HUMAN	SNRPD1	physical	26496610
SMD2_HUMAN	SNRPD2	physical	26496610
SMD3_HUMAN	SNRPD3	physical	26496610
THIO_HUMAN	TXN	physical	26496610
H2A2A_HUMAN	HIST2H2AA3	physical	26496610
GEMI2_HUMAN	GEMIN2	physical	26496610
STRAP_HUMAN	STRAP	physical	26496610
DDX20_HUMAN	DDX20	physical	26496610
LPIN1_HUMAN	LPIN1	physical	26496610
GEMI4_HUMAN	GEMIN4	physical	26496610
UBR5_HUMAN	UBR5	physical	26496610
GEMI8_HUMAN	GEMIN8	physical	26496610
GEMI7_HUMAN	GEMIN7	physical	26496610
GEMI6_HUMAN	GEMIN6	physical	26496610
SYNCI_HUMAN	SYNC	physical	26496610
LSM11_HUMAN	LSM11	physical	26496610

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 GEMI5_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-1363, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-751; SER-770;SER-778; THR-807 AND SER-847, AND MASS SPECTROMETRY.	18691976 [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-778, AND MASSSPECTROMETRY.	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-778, AND MASSSPECTROMETRY.	15302935 [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 THR-807, AND MASSSPECTROMETRY.	16964243 [Abstract]