dbPTM

CCDC6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCDC6_HUMAN
UniProt AC	Q16204
Protein Name	Coiled-coil domain-containing protein 6
Gene Name	CCDC6
Organism	Homo sapiens (Human).
Sequence Length	474
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton . May be a cytoskeletal protein.
Protein Description
Protein Sequence	MADSASESDTDGAGGNSSSSAAMQSSCSSTSGGGGGGGGGGGGGKSGGIVISPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQGLRPRTVSSPIPYTPSPSSSRPISPGLSYASHTVGFTPPTSLTRAGMSYYNSPGLHVQHMGTSHGITRPSPRRSNSPDKFKRPTPPPSPNTQTPVQPPPPPPPPPMQPTVPSAATSQPTPSQHSAHPSSQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSASESD ------CCCCCCCCC	21.33	19413330
4	Phosphorylation	----MADSASESDTD ----CCCCCCCCCCC	24.93	24043423
6	Phosphorylation	--MADSASESDTDGA --CCCCCCCCCCCCC	41.40	24043423
8	Phosphorylation	MADSASESDTDGAGG CCCCCCCCCCCCCCC	43.23	25841592
10	Phosphorylation	DSASESDTDGAGGNS CCCCCCCCCCCCCCC	45.68	24043423
17	Phosphorylation	TDGAGGNSSSSAAMQ CCCCCCCCCCHHHHH	34.57	25841592
18	Phosphorylation	DGAGGNSSSSAAMQS CCCCCCCCCHHHHHH	32.10	25841592
19	Phosphorylation	GAGGNSSSSAAMQSS CCCCCCCCHHHHHHH	24.66	24043423
20	Phosphorylation	AGGNSSSSAAMQSSC CCCCCCCHHHHHHHC	23.22	25841592
25	Phosphorylation	SSSAAMQSSCSSTSG CCHHHHHHHCCCCCC	21.89	24043423
26	Phosphorylation	SSAAMQSSCSSTSGG CHHHHHHHCCCCCCC	10.92	24043423
28	Phosphorylation	AAMQSSCSSTSGGGG HHHHHHCCCCCCCCC	38.30	24043423
29	Phosphorylation	AMQSSCSSTSGGGGG HHHHHCCCCCCCCCC	30.80	24043423
30	Phosphorylation	MQSSCSSTSGGGGGG HHHHCCCCCCCCCCC	18.33	24043423
31	Phosphorylation	QSSCSSTSGGGGGGG HHHCCCCCCCCCCCC	37.07	24043423
46	Phosphorylation	GGGGGGKSGGIVISP CCCCCCCCCCEEECC	45.59	23927012
52	Phosphorylation	KSGGIVISPFRLEEL CCCCEEECCCCHHHH	13.69	19664994
60	Phosphorylation	PFRLEELTNRLASLQ CCCHHHHHHHHHHHH	22.90	23927012
65	Phosphorylation	ELTNRLASLQQENKV HHHHHHHHHHHHCCE	31.16	20068231
71	2-Hydroxyisobutyrylation	ASLQQENKVLKIELE HHHHHHCCEEEEEHH	48.46	-
71	Malonylation	ASLQQENKVLKIELE HHHHHHCCEEEEEHH	48.46	26320211
71	Ubiquitination	ASLQQENKVLKIELE HHHHHHCCEEEEEHH	48.46	-
74	Sumoylation	QQENKVLKIELETYK HHHCCEEEEEHHHHH	36.80	-
74	Sumoylation	QQENKVLKIELETYK HHHCCEEEEEHHHHH	36.80	-
79	Phosphorylation	VLKIELETYKLKCKA EEEEEHHHHHHHHHH	38.28	20068231
80	Phosphorylation	LKIELETYKLKCKAL EEEEHHHHHHHHHHH	12.63	21406692
81	Acetylation	KIELETYKLKCKALQ EEEHHHHHHHHHHHH	49.22	25953088
81	Ubiquitination	KIELETYKLKCKALQ EEEHHHHHHHHHHHH	49.22	-
96	Ubiquitination	EENRDLRKASVTIQA HHCCHHHHHHHEHHH	52.92	-
98	Phosphorylation	NRDLRKASVTIQARA CCHHHHHHHEHHHHH	23.87	28857561
100	Phosphorylation	DLRKASVTIQARAEQ HHHHHHHEHHHHHHH	12.60	23312004
113	Phosphorylation	EQEEEFISNTLFKKI HHHHHHHHHHHHHHH	29.14	19060867
115	Phosphorylation	EEEFISNTLFKKIQA HHHHHHHHHHHHHHH	27.12	17287340
118	Ubiquitination	FISNTLFKKIQALQK HHHHHHHHHHHHHHH	52.67	21890473
119	2-Hydroxyisobutyrylation	ISNTLFKKIQALQKE HHHHHHHHHHHHHHH	32.49	-
119	Ubiquitination	ISNTLFKKIQALQKE HHHHHHHHHHHHHHH	32.49	-
125	Ubiquitination	KKIQALQKEKETLAV HHHHHHHHHHHHHCC	72.16	-
127	2-Hydroxyisobutyrylation	IQALQKEKETLAVNY HHHHHHHHHHHCCCH	64.13	-
127	Ubiquitination	IQALQKEKETLAVNY HHHHHHHHHHHCCCH	64.13	-
134	Phosphorylation	KETLAVNYEKEEEFL HHHHCCCHHHHHHHH	23.06	28796482
136	Ubiquitination	TLAVNYEKEEEFLTN HHCCCHHHHHHHHHH	61.13	-
148	Ubiquitination	LTNELSRKLMQLQHE HHHHHHHHHHHHHHH	44.96	-
173	Acetylation	EQEFQVNKLMKKIKK HHHHHHHHHHHHHHH	51.61	25953088
173	Ubiquitination	EQEFQVNKLMKKIKK HHHHHHHHHHHHHHH	51.61	-
185	Phosphorylation	IKKLENDTISKQLTL HHHHCCCHHHHHHCH	38.44	20068231
187	Phosphorylation	KLENDTISKQLTLEQ HHCCCHHHHHHCHHH	19.22	20068231
188	2-Hydroxyisobutyrylation	LENDTISKQLTLEQL HCCCHHHHHHCHHHH	45.54	-
188	Ubiquitination	LENDTISKQLTLEQL HCCCHHHHHHCHHHH	45.54	21890473
188	Ubiquitination	LENDTISKQLTLEQL HCCCHHHHHHCHHHH	45.54	21890473
199	Ubiquitination	LEQLRREKIDLENTL HHHHHHHCCCCCHHH	39.44	-
205	Phosphorylation	EKIDLENTLEQEQEA HCCCCCHHHHHHHHH	23.46	28555341
234	Ubiquitination	EKRILQEKLDQPVSA HHHHHHHHCCCCCCC	44.39	-
240	Phosphorylation	EKLDQPVSAPPSPRD HHCCCCCCCCCCCCC	41.56	29255136
244	Phosphorylation	QPVSAPPSPRDISME CCCCCCCCCCCCCCC	31.35	19664994
249	Phosphorylation	PPSPRDISMEIDSPE CCCCCCCCCCCCCHH	18.04	25159151
254	Phosphorylation	DISMEIDSPENMMRH CCCCCCCCHHHHHHH	39.51	25159151
266	Sumoylation	MRHIRFLKNEVERLK HHHHHHHHHHHHHHH	48.64	-
266	Malonylation	MRHIRFLKNEVERLK HHHHHHHHHHHHHHH	48.64	26320211
266	Sumoylation	MRHIRFLKNEVERLK HHHHHHHHHHHHHHH	48.64	-
266	Ubiquitination	MRHIRFLKNEVERLK HHHHHHHHHHHHHHH	48.64	-
284	Phosphorylation	RAAQLQHSEKMAQYL HHHHHHHHHHHHHHH	26.42	20068231
286	2-Hydroxyisobutyrylation	AQLQHSEKMAQYLEE HHHHHHHHHHHHHHH	42.42	-
286	Acetylation	AQLQHSEKMAQYLEE HHHHHHHHHHHHHHH	42.42	25953088
286	Ubiquitination	AQLQHSEKMAQYLEE HHHHHHHHHHHHHHH	42.42	-
290	Phosphorylation	HSEKMAQYLEEERHM HHHHHHHHHHHHHHH	13.42	-
323	Phosphorylation	EALCRQLSESESSLE HHHHHHHHHCCCCCC	30.64	25159151
325	Phosphorylation	LCRQLSESESSLEMD HHHHHHHCCCCCCCC	39.13	30278072
327	Phosphorylation	RQLSESESSLEMDDE HHHHHCCCCCCCCCH	49.88	30278072
328	Phosphorylation	QLSESESSLEMDDER HHHHCCCCCCCCCHH	25.05	30278072
336	Phosphorylation	LEMDDERYFNEMSAQ CCCCCHHHHHHHHHC	14.54	28674151
341	Phosphorylation	ERYFNEMSAQGLRPR HHHHHHHHHCCCCCC	15.97	25849741
349	O-linked_Glycosylation	AQGLRPRTVSSPIPY HCCCCCCCCCCCCCC	27.67	30059200
349	Phosphorylation	AQGLRPRTVSSPIPY HCCCCCCCCCCCCCC	27.67	20044836
351	Phosphorylation	GLRPRTVSSPIPYTP CCCCCCCCCCCCCCC	29.77	23927012
352	Phosphorylation	LRPRTVSSPIPYTPS CCCCCCCCCCCCCCC	23.63	23927012
356	Phosphorylation	TVSSPIPYTPSPSSS CCCCCCCCCCCCCCC	31.81	23401153
357	Phosphorylation	VSSPIPYTPSPSSSR CCCCCCCCCCCCCCC	16.37	23927012
359	Phosphorylation	SPIPYTPSPSSSRPI CCCCCCCCCCCCCCC	29.61	23927012
361	Phosphorylation	IPYTPSPSSSRPISP CCCCCCCCCCCCCCC	45.33	25159151
362	Phosphorylation	PYTPSPSSSRPISPG CCCCCCCCCCCCCCC	33.48	25159151
363	Phosphorylation	YTPSPSSSRPISPGL CCCCCCCCCCCCCCC	46.55	23927012
367	Phosphorylation	PSSSRPISPGLSYAS CCCCCCCCCCCCCCC	18.65	29255136
371	Phosphorylation	RPISPGLSYASHTVG CCCCCCCCCCCCCCC	25.27	30266825
372	Phosphorylation	PISPGLSYASHTVGF CCCCCCCCCCCCCCC	19.71	30266825
374	Phosphorylation	SPGLSYASHTVGFTP CCCCCCCCCCCCCCC	16.09	30266825
376	Phosphorylation	GLSYASHTVGFTPPT CCCCCCCCCCCCCCC	21.59	23927012
380	Phosphorylation	ASHTVGFTPPTSLTR CCCCCCCCCCCCCCC	23.56	23401153
383	Phosphorylation	TVGFTPPTSLTRAGM CCCCCCCCCCCCCCC	37.26	23927012
384	O-linked_Glycosylation	VGFTPPTSLTRAGMS CCCCCCCCCCCCCCC	33.25	30059200
384	Phosphorylation	VGFTPPTSLTRAGMS CCCCCCCCCCCCCCC	33.25	23927012
386	O-linked_Glycosylation	FTPPTSLTRAGMSYY CCCCCCCCCCCCCCC	20.45	30059200
386	Phosphorylation	FTPPTSLTRAGMSYY CCCCCCCCCCCCCCC	20.45	23927012
387	Methylation	TPPTSLTRAGMSYYN CCCCCCCCCCCCCCC	34.14	-
391	Phosphorylation	SLTRAGMSYYNSPGL CCCCCCCCCCCCCCE	24.44	28796482
392	Phosphorylation	LTRAGMSYYNSPGLH CCCCCCCCCCCCCEE	9.58	28796482
393	Phosphorylation	TRAGMSYYNSPGLHV CCCCCCCCCCCCEEE	11.23	28796482
395	Phosphorylation	AGMSYYNSPGLHVQH CCCCCCCCCCEEEEE	12.29	25159151
405	Phosphorylation	LHVQHMGTSHGITRP EEEEECCCCCCCCCC	15.24	29496963
406	Phosphorylation	HVQHMGTSHGITRPS EEEECCCCCCCCCCC	17.62	20873877
410	Phosphorylation	MGTSHGITRPSPRRS CCCCCCCCCCCCCCC	40.91	25159151
411	Methylation	GTSHGITRPSPRRSN CCCCCCCCCCCCCCC	27.98	-
413	Phosphorylation	SHGITRPSPRRSNSP CCCCCCCCCCCCCCC	27.96	25159151
415	Methylation	GITRPSPRRSNSPDK CCCCCCCCCCCCCCC	60.02	-
417	Phosphorylation	TRPSPRRSNSPDKFK CCCCCCCCCCCCCCC	42.83	30266825
419	Phosphorylation	PSPRRSNSPDKFKRP CCCCCCCCCCCCCCC	35.40	22167270
424	Sumoylation	SNSPDKFKRPTPPPS CCCCCCCCCCCCCCC	64.31	-
424	Sumoylation	SNSPDKFKRPTPPPS CCCCCCCCCCCCCCC	64.31	-
427	Phosphorylation	PDKFKRPTPPPSPNT CCCCCCCCCCCCCCC	53.08	20873877
431	Phosphorylation	KRPTPPPSPNTQTPV CCCCCCCCCCCCCCC	36.23	20068231
434	Phosphorylation	TPPPSPNTQTPVQPP CCCCCCCCCCCCCCC	36.88	20873877
436	Phosphorylation	PPSPNTQTPVQPPPP CCCCCCCCCCCCCCC	24.32	20068231
452	Phosphorylation	PPPPMQPTVPSAATS CCCCCCCCCCCCCCC	28.32	20068231
455	Phosphorylation	PMQPTVPSAATSQPT CCCCCCCCCCCCCCC	26.63	20068231
458	Phosphorylation	PTVPSAATSQPTPSQ CCCCCCCCCCCCCCC	27.84	20068231
459	Phosphorylation	TVPSAATSQPTPSQH CCCCCCCCCCCCCCC	29.45	20068231
462	Phosphorylation	SAATSQPTPSQHSAH CCCCCCCCCCCCCCC	28.12	20068231
464	Phosphorylation	ATSQPTPSQHSAHPS CCCCCCCCCCCCCCC	42.90	20068231
467	Phosphorylation	QPTPSQHSAHPSSQP CCCCCCCCCCCCCCC	22.19	20068231
471	Phosphorylation	SQHSAHPSSQP---- CCCCCCCCCCC----	31.57	20068231
472	Phosphorylation	QHSAHPSSQP----- CCCCCCCCCC-----	51.42	20068231

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
240	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
244	S	Phosphorylation	Kinase	CDK2	P24941	PSP
244	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
434	T	Phosphorylation	Kinase	ATM	Q13315	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:25885523

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCDC6_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 CCDC6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CREB1_HUMAN	CREB1	physical	20498639
ATF2_HUMAN	ATF2	physical	20498639
PP1A_HUMAN	PPP1CA	physical	20498639
HDAC1_HUMAN	HDAC1	physical	20498639
CUL1_HUMAN	CUL1	physical	23108047
SKP1_HUMAN	SKP1	physical	23108047
FBXW7_HUMAN	FBXW7	physical	23108047
BRCC3_HUMAN	BRCC3	physical	22863883
CD2AP_HUMAN	CD2AP	physical	22863883
GAPD1_HUMAN	GAPVD1	physical	22863883
HDAC1_HUMAN	HDAC1	physical	22863883
HNRPR_HUMAN	HNRNPR	physical	22863883
GCR_HUMAN	NR3C1	physical	22863883
PAAF1_HUMAN	PAAF1	physical	22863883
PP4R2_HUMAN	PPP4R2	physical	22863883
TIF1B_HUMAN	TRIM28	physical	22863883
SEPT2_HUMAN	SEPT2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26496610
2AAA_HUMAN	PPP2R1A	physical	26496610
PP4R1_HUMAN	PPP4R1	physical	26496610
GSK3B_HUMAN	GSK3B	physical	25885523
CCNB1_HUMAN	CCNB1	physical	25885523
CDK1_HUMAN	CDK1	physical	25885523
FBXW7_HUMAN	FBXW7	physical	25885523
UBP7_HUMAN	USP7	physical	25885523
PP4R1_HUMAN	PPP4R1	physical	28514442
CEP55_HUMAN	CEP55	physical	28514442
LZTS3_HUMAN	LZTS3	physical	28514442
MYOME_HUMAN	PDE4DIP	physical	28514442
PP4C_HUMAN	PPP4C	physical	28514442
C102A_HUMAN	CCDC102A	physical	28514442
P4R3B_HUMAN	SMEK2	physical	28514442
P4R3A_HUMAN	SMEK1	physical	28514442
PCBP3_HUMAN	PCBP3	physical	28514442
APC_HUMAN	APC	physical	28514442
ZN445_HUMAN	ZNF445	physical	28514442
RPTOR_HUMAN	RPTOR	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
188550	Thyroid papillary carcinoma (TPC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CCDC6_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-240 AND SER-244, AND MASS SPECTROMETRY.	19413330 [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-52; SER-113; SER-240;SER-244; SER-254; SER-323 AND SER-367, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-244, ANDMASS SPECTROMETRY.	19369195 [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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-240 AND SER-244, 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-52; SER-240; SER-244;SER-249; SER-254; THR-349; SER-351; SER-352; TYR-356; SER-363;SER-367; SER-371; TYR-372 AND THR-376, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-240 AND SER-244, ANDMASS SPECTROMETRY.	18691976 [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-52; SER-240 AND SER-244,AND MASS SPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-351 ANDSER-419, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.	18187866 [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 THR-115; SER-240 ANDSER-244, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.	17693683 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-244, ANDMASS SPECTROMETRY.	17487921 [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-52; SER-240 AND SER-244,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-52; SER-240; SER-244;SER-323; SER-325 AND SER-328, 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-240 AND SER-244, ANDMASS SPECTROMETRY.	15302935 [Abstract]