dbPTM

CND2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CND2_HUMAN
UniProt AC	Q15003
Protein Name	Condensin complex subunit 2
Gene Name	NCAPH
Organism	Homo sapiens (Human).
Sequence Length	741
Subcellular Localization	Nucleus . Cytoplasm . Chromosome . In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chro
Protein Description	Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases..
Protein Sequence	MGPPGPALPATMNNSSSETRGHPHSASSPSERVFPMPLPRKAPLNIPGTPVLEDFPQNDDEKERLQRRRSRVFDLQFSTDSPRLLASPSSRSIDISATIPKFTNTQITEHYSTCIKLSTENKITTKNAFGLHLIDFMSEILKQKDTEPTNFKVAAGTLDASTKIYAVRVDAVHADVYRVLGGLGKDAPSLEEVEGHVADGSATEMGTTKKAVKPKKKHLHRTIEQNINNLNVSEADRKCEIDPMFQKTAASFDECSTAGVFLSTLHCQDYRSELLFPSDVQTLSTGEPLELPELGCVEMTDLKAPLQQCAEDRQICPSLAGFQFTQWDSETHNESVSALVDKFKKNDQVFDINAEVDESDCGDFPDGSLGDDFDANDEPDHTAVGDHEEFRSWKEPCQVQSCQEEMISLGDGDIRTMCPLLSMKPGEYSYFSPRTMSMWAGPDHWRFRPRRKQDAPSQSENKKKSTKKDFEIDFEDDIDFDVYFRKTKAATILTKSTLENQNWRATTLPTDFNYNVDTLVQLHLKPGTRLLKMAQGHRVETEHYEEIEDYDYNNPNDTSNFCPGLQAADSDDEDLDDLFVGPVGNSDLSPYPCHPPKTAQQNGDTPEAQGLDITTYGESNLVAEPQKVNKIEIHYAKTAKKMDMKKLKQSMWSLLTALSGKEADAEANHREAGKEAALAEVADEKMLSGLTKDLQRSLPPVMAQNLSIPLAFACLLHLANEKNLKLEGTEDLSDVLVRQGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MGPPGPALPATMNNS CCCCCCCCCCCCCCC	3.14	-
11	Phosphorylation	PGPALPATMNNSSSE CCCCCCCCCCCCCCC	20.63	23663014
12	Sulfoxidation	GPALPATMNNSSSET CCCCCCCCCCCCCCC	4.92	21406390
15	Phosphorylation	LPATMNNSSSETRGH CCCCCCCCCCCCCCC	30.18	25159151
16	Ubiquitination	PATMNNSSSETRGHP CCCCCCCCCCCCCCC	34.03	-
16	Phosphorylation	PATMNNSSSETRGHP CCCCCCCCCCCCCCC	34.03	25159151
17	Phosphorylation	ATMNNSSSETRGHPH CCCCCCCCCCCCCCC	42.69	25159151
19	Phosphorylation	MNNSSSETRGHPHSA CCCCCCCCCCCCCCC	43.85	23663014
20	Methylation	NNSSSETRGHPHSAS CCCCCCCCCCCCCCC	37.05	115484557
25	Phosphorylation	ETRGHPHSASSPSER CCCCCCCCCCCCCCC	34.01	26055452
27	Ubiquitination	RGHPHSASSPSERVF CCCCCCCCCCCCCCC	45.88	-
27	Phosphorylation	RGHPHSASSPSERVF CCCCCCCCCCCCCCC	45.88	25159151
28	Phosphorylation	GHPHSASSPSERVFP CCCCCCCCCCCCCCC	31.96	30278072
30	Phosphorylation	PHSASSPSERVFPMP CCCCCCCCCCCCCCC	39.73	26329039
32	Methylation	SASSPSERVFPMPLP CCCCCCCCCCCCCCC	39.45	115484551
41	Ubiquitination	FPMPLPRKAPLNIPG CCCCCCCCCCCCCCC	53.03	21890473
49	Ubiquitination	APLNIPGTPVLEDFP CCCCCCCCCCCCCCC	12.60	-
49	Phosphorylation	APLNIPGTPVLEDFP CCCCCCCCCCCCCCC	12.60	29255136
62	Ubiquitination	FPQNDDEKERLQRRR CCCCHHHHHHHHHHH	55.94	-
70	Phosphorylation	ERLQRRRSRVFDLQF HHHHHHHHHHHEEEC	30.86	30266825
74	Ubiquitination	RRRSRVFDLQFSTDS HHHHHHHEEECCCCC	36.38	-
78	Phosphorylation	RVFDLQFSTDSPRLL HHHEEECCCCCCCEE	20.53	30266825
79	Phosphorylation	VFDLQFSTDSPRLLA HHEEECCCCCCCEEC	41.61	30266825
81	Phosphorylation	DLQFSTDSPRLLASP EEECCCCCCCEECCC	16.41	25159151
87	Phosphorylation	DSPRLLASPSSRSID CCCCEECCCCCCCCE	25.86	22167270
89	Phosphorylation	PRLLASPSSRSIDIS CCEECCCCCCCCEEE	35.57	30266825
90	Phosphorylation	RLLASPSSRSIDISA CEECCCCCCCCEEEE	33.17	30266825
92	Phosphorylation	LASPSSRSIDISATI ECCCCCCCCEEEEEC	26.93	30266825
96	Phosphorylation	SSRSIDISATIPKFT CCCCCEEEEECCCCC	18.66	30266825
98	Phosphorylation	RSIDISATIPKFTNT CCCEEEEECCCCCCC	30.90	30266825
102	Ubiquitination	ISATIPKFTNTQITE EEEECCCCCCCCCCC	5.52	-
103	Phosphorylation	SATIPKFTNTQITEH EEECCCCCCCCCCCC	43.41	28555341
111	Phosphorylation	NTQITEHYSTCIKLS CCCCCCCHHHEEECC	10.23	-
122	Ubiquitination	IKLSTENKITTKNAF EECCCCCCCCCCCHH	34.89	-
126	Ubiquitination	TENKITTKNAFGLHL CCCCCCCCCHHHHHH	37.31	21906983
138	Phosphorylation	LHLIDFMSEILKQKD HHHHHHHHHHHHCCC	22.83	27174698
142	Ubiquitination	DFMSEILKQKDTEPT HHHHHHHHCCCCCCC	62.05	21906983
144	Acetylation	MSEILKQKDTEPTNF HHHHHHCCCCCCCCC	66.10	25953088
144	Ubiquitination	MSEILKQKDTEPTNF HHHHHHCCCCCCCCC	66.10	-
146	Phosphorylation	EILKQKDTEPTNFKV HHHHCCCCCCCCCEE	51.40	24719451
149	Phosphorylation	KQKDTEPTNFKVAAG HCCCCCCCCCEEEEE	47.24	27174698
152	Acetylation	DTEPTNFKVAAGTLD CCCCCCCEEEEEECC	32.79	25953088
152	Methylation	DTEPTNFKVAAGTLD CCCCCCCEEEEEECC	32.79	24791763
152	Ubiquitination	DTEPTNFKVAAGTLD CCCCCCCEEEEEECC	32.79	-
157	Phosphorylation	NFKVAAGTLDASTKI CCEEEEEECCCCCCE	19.42	27174698
161	Phosphorylation	AAGTLDASTKIYAVR EEEECCCCCCEEEEE	29.87	25159151
162	Phosphorylation	AGTLDASTKIYAVRV EEECCCCCCEEEEEE	24.15	25159151
163	Ubiquitination	GTLDASTKIYAVRVD EECCCCCCEEEEEEC	31.09	-
165	Phosphorylation	LDASTKIYAVRVDAV CCCCCCEEEEEECCC	10.70	-
177	Phosphorylation	DAVHADVYRVLGGLG CCCCHHHHHHHCCCC	8.78	28674419
185	Acetylation	RVLGGLGKDAPSLEE HHHCCCCCCCCCHHH	56.62	26051181
185	Ubiquitination	RVLGGLGKDAPSLEE HHHCCCCCCCCCHHH	56.62	-
189	Phosphorylation	GLGKDAPSLEEVEGH CCCCCCCCHHHCCCC	50.57	21712546
201	Phosphorylation	EGHVADGSATEMGTT CCCCCCCCCCCCCCC	32.34	22167270
203	Phosphorylation	HVADGSATEMGTTKK CCCCCCCCCCCCCCC	28.35	30266825
207	Phosphorylation	GSATEMGTTKKAVKP CCCCCCCCCCCCCCC	33.85	30266825
208	Phosphorylation	SATEMGTTKKAVKPK CCCCCCCCCCCCCCC	25.48	30266825
209	Acetylation	ATEMGTTKKAVKPKK CCCCCCCCCCCCCCH	38.28	26051181
210	Ubiquitination	TEMGTTKKAVKPKKK CCCCCCCCCCCCCHH	57.21	-
222	Phosphorylation	KKKHLHRTIEQNINN CHHHHHHHHHHHHHH	20.37	23186163
233	Phosphorylation	NINNLNVSEADRKCE HHHHCCHHHHHHHCC	26.45	25159151
238	Ubiquitination	NVSEADRKCEIDPMF CHHHHHHHCCCCHHH	36.45	-
258	Ubiquitination	SFDECSTAGVFLSTL CHHHHHCHHHHHHHC	8.89	-
288	Ubiquitination	QTLSTGEPLELPELG EECCCCCCCCCCCCC	32.26	-
325	Phosphorylation	SLAGFQFTQWDSETH HHCCCEEEECCCCCC	20.26	28122231
329	Phosphorylation	FQFTQWDSETHNESV CEEEECCCCCCCHHH	41.24	20068231
331	Phosphorylation	FTQWDSETHNESVSA EEECCCCCCCHHHHH	33.67	28122231
335	Phosphorylation	DSETHNESVSALVDK CCCCCCHHHHHHHHH	27.04	20068231
337	Phosphorylation	ETHNESVSALVDKFK CCCCHHHHHHHHHHH	25.76	20068231
352	Ubiquitination	KNDQVFDINAEVDES HCCEEEEECCEECHH	3.41	-
359	Ubiquitination	INAEVDESDCGDFPD ECCEECHHHCCCCCC	33.46	21890473
359	Phosphorylation	INAEVDESDCGDFPD ECCEECHHHCCCCCC	33.46	30576142
368	Phosphorylation	CGDFPDGSLGDDFDA CCCCCCCCCCCCCCC	36.24	22468782
394	Ubiquitination	HEEFRSWKEPCQVQS HHHHHHCCCCCCCCC	53.69	-
396	Ubiquitination	EFRSWKEPCQVQSCQ HHHHCCCCCCCCCCC	15.32	-
401	Phosphorylation	KEPCQVQSCQEEMIS CCCCCCCCCCHHHHH	20.93	30576142
408	Phosphorylation	SCQEEMISLGDGDIR CCCHHHHHCCCCCHH	25.62	25159151
422	Phosphorylation	RTMCPLLSMKPGEYS HHHHHHHCCCCCCCC	32.23	21945579
424	Ubiquitination	MCPLLSMKPGEYSYF HHHHHCCCCCCCCEE	46.63	-
428	Phosphorylation	LSMKPGEYSYFSPRT HCCCCCCCCEECCCC	18.00	21945579
429	Phosphorylation	SMKPGEYSYFSPRTM CCCCCCCCEECCCCC	18.52	21945579
430	Phosphorylation	MKPGEYSYFSPRTMS CCCCCCCEECCCCCC	13.74	21945579
432	Phosphorylation	PGEYSYFSPRTMSMW CCCCCEECCCCCCCC	12.77	19664994
435	Phosphorylation	YSYFSPRTMSMWAGP CCEECCCCCCCCCCC	19.58	26074081
457	Phosphorylation	RRKQDAPSQSENKKK CCCCCCCCCCCCCCC	48.32	20068231
459	Phosphorylation	KQDAPSQSENKKKST CCCCCCCCCCCCCCC	47.69	20068231
465	Phosphorylation	QSENKKKSTKKDFEI CCCCCCCCCCCCCEE	55.10	26670566
466	Phosphorylation	SENKKKSTKKDFEID CCCCCCCCCCCCEEC	51.50	26670566
488	Sumoylation	DVYFRKTKAATILTK EEEEECCCEEEEEEH	38.77	28112733
488	Ubiquitination	DVYFRKTKAATILTK EEEEECCCEEEEEEH	38.77	-
491	Phosphorylation	FRKTKAATILTKSTL EECCCEEEEEEHHHH	22.75	23186163
494	Acetylation	TKAATILTKSTLENQ CCEEEEEEHHHHCCC	21.06	-
494	Phosphorylation	TKAATILTKSTLENQ CCEEEEEEHHHHCCC	21.06	23186163
495	Ubiquitination	KAATILTKSTLENQN CEEEEEEHHHHCCCC	37.69	21890473
496	Phosphorylation	AATILTKSTLENQNW EEEEEEHHHHCCCCC	32.75	25159151
497	Phosphorylation	ATILTKSTLENQNWR EEEEEHHHHCCCCCE	39.38	20068231
501	Acetylation	TKSTLENQNWRATTL EHHHHCCCCCEEEEC	41.30	-
501	Ubiquitination	TKSTLENQNWRATTL EHHHHCCCCCEEEEC	41.30	-
501	Acetylation	TKSTLENQNWRATTL EHHHHCCCCCEEEEC	41.30	19608861
504	Ubiquitination	TLENQNWRATTLPTD HHCCCCCEEEECCCC	29.61	-
506	Phosphorylation	ENQNWRATTLPTDFN CCCCCEEEECCCCCC	21.94	26074081
507	Phosphorylation	NQNWRATTLPTDFNY CCCCEEEECCCCCCC	29.74	26074081
510	Phosphorylation	WRATTLPTDFNYNVD CEEEECCCCCCCCHH	57.23	26074081
512	Ubiquitination	ATTLPTDFNYNVDTL EEECCCCCCCCHHHE	13.22	-
514	Phosphorylation	TLPTDFNYNVDTLVQ ECCCCCCCCHHHEEE	19.29	-
532	Ubiquitination	KPGTRLLKMAQGHRV CCCCHHHHHHCCCCC	36.46	-
538	Acetylation	LKMAQGHRVETEHYE HHHHCCCCCCCCCCH	34.49	-
538	Ubiquitination	LKMAQGHRVETEHYE HHHHCCCCCCCCCCH	34.49	-
549	Ubiquitination	EHYEEIEDYDYNNPN CCCHHHHCCCCCCCC	47.46	-
556	Acetylation	DYDYNNPNDTSNFCP CCCCCCCCCCCCCCC	68.28	-
570	Phosphorylation	PGLQAADSDDEDLDD CCCCCCCCCCCCHHH	42.08	29496963
586	Phosphorylation	FVGPVGNSDLSPYPC CCCCCCCCCCCCCCC	33.72	26074081
589	Ubiquitination	PVGNSDLSPYPCHPP CCCCCCCCCCCCCCC	27.64	-
589	Phosphorylation	PVGNSDLSPYPCHPP CCCCCCCCCCCCCCC	27.64	26074081
591	Phosphorylation	GNSDLSPYPCHPPKT CCCCCCCCCCCCCCC	18.34	26074081
598	Phosphorylation	YPCHPPKTAQQNGDT CCCCCCCCHHHCCCC	35.16	30266825
605	Phosphorylation	TAQQNGDTPEAQGLD CHHHCCCCCCCCCCE	25.15	30266825
614	Phosphorylation	EAQGLDITTYGESNL CCCCCEEEEECCCCC	17.40	30266825
615	Phosphorylation	AQGLDITTYGESNLV CCCCEEEEECCCCCE	29.84	30266825
616	Phosphorylation	QGLDITTYGESNLVA CCCEEEEECCCCCEE	15.39	30266825
619	Phosphorylation	DITTYGESNLVAEPQ EEEEECCCCCEECCC	30.97	30266825
626	Acetylation	SNLVAEPQKVNKIEI CCCEECCCEECEEEE	54.56	19608861
630	Acetylation	AEPQKVNKIEIHYAK ECCCEECEEEEEEHH	44.71	23236377
630	Ubiquitination	AEPQKVNKIEIHYAK ECCCEECEEEEEEHH	44.71	-
635	Phosphorylation	VNKIEIHYAKTAKKM ECEEEEEEHHHCCCC	18.56	23917254
637	Acetylation	KIEIHYAKTAKKMDM EEEEEEHHHCCCCCH	41.68	19608861
637	Ubiquitination	KIEIHYAKTAKKMDM EEEEEEHHHCCCCCH	41.68	19608861
640	Ubiquitination	IHYAKTAKKMDMKKL EEEHHHCCCCCHHHH	54.59	-
648	Ubiquitination	KMDMKKLKQSMWSLL CCCHHHHHHHHHHHH	49.56	-
650	Phosphorylation	DMKKLKQSMWSLLTA CHHHHHHHHHHHHHH	22.19	20068231
653	Phosphorylation	KLKQSMWSLLTALSG HHHHHHHHHHHHHHC	12.59	20068231
656	Phosphorylation	QSMWSLLTALSGKEA HHHHHHHHHHHCCHH	30.74	20068231
659	Phosphorylation	WSLLTALSGKEADAE HHHHHHHHCCHHHHH	45.41	20068231
661	Ubiquitination	LLTALSGKEADAEAN HHHHHHCCHHHHHHH	46.48	-
674	Acetylation	ANHREAGKEAALAEV HHHHHHHHHHHHHHH	51.75	23236377
674	Ubiquitination	ANHREAGKEAALAEV HHHHHHHHHHHHHHH	51.75	-
685	Ubiquitination	LAEVADEKMLSGLTK HHHHCCHHHHHCCCH	45.76	-
692	Acetylation	KMLSGLTKDLQRSLP HHHHCCCHHHHHHCC	62.58	22424773
692	Ubiquitination	KMLSGLTKDLQRSLP HHHHCCCHHHHHHCC	62.58	-
725	Sumoylation	LANEKNLKLEGTEDL HHCCCCCCCCCCCCH	54.61	-
725	Sumoylation	LANEKNLKLEGTEDL HHCCCCCCCCCCCCH	54.61	-
725	Ubiquitination	LANEKNLKLEGTEDL HHCCCCCCCCCCCCH	54.61	-
729	Phosphorylation	KNLKLEGTEDLSDVL CCCCCCCCCCHHHHH	19.56	21406692
733	Phosphorylation	LEGTEDLSDVLVRQG CCCCCCHHHHHHHCC	37.69	21406692

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
49	T	Phosphorylation	Kinase	CDK2	P24941	PSP
570	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CND2_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 CND2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC2_HUMAN	SMC2	physical	21633354
CND1_HUMAN	NCAPD2	physical	17268547
CND3_HUMAN	NCAPG	physical	17268547
SMC4_HUMAN	SMC4	physical	17268547
SMC2_HUMAN	SMC2	physical	17268547
CND3_HUMAN	NCAPG	physical	22939629
SMC2_HUMAN	SMC2	physical	22939629
SMC4_HUMAN	SMC4	physical	22939629
HECD3_HUMAN	HECTD3	physical	22863883
LMNB1_HUMAN	LMNB1	physical	22863883
ZZEF1_HUMAN	ZZEF1	physical	22863883
SMC2_HUMAN	SMC2	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26496610
TERA_HUMAN	VCP	physical	26496610
CND1_HUMAN	NCAPD2	physical	26496610
SMC4_HUMAN	SMC4	physical	26496610
SCAM2_HUMAN	SCAMP2	physical	26496610
SMC2_HUMAN	SMC2	physical	26496610
HEXI1_HUMAN	HEXIM1	physical	26496610
RB15B_HUMAN	RBM15B	physical	26496610
HEAT3_HUMAN	HEATR3	physical	26496610
MCAF1_HUMAN	ATF7IP	physical	26496610
CND3_HUMAN	NCAPG	physical	26496610
CEP85_HUMAN	CEP85	physical	26496610
KLC2_HUMAN	KLC2	physical	26496610
S38AA_HUMAN	SLC38A10	physical	26496610
SMC2_HUMAN	SMC2	physical	26166704
SMC4_HUMAN	SMC4	physical	26166704
CND1_HUMAN	NCAPD2	physical	26166704
CND3_HUMAN	NCAPG	physical	26166704
HECD1_HUMAN	HECTD1	physical	26166704
TBP_HUMAN	TBP	physical	26257282

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 CND2_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-637, AND MASS SPECTROMETRY.	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-81, 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-15 AND THR-605, AND MASSSPECTROMETRY.	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 THR-49; SER-70; SER-78;SER-81; SER-87; SER-92; SER-201; SER-432; THR-605 AND THR-614, ANDMASS 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-201, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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-87; SER-201 AND SER-408,AND MASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-78; SER-81;SER-92; SER-96; SER-201; SER-335 AND THR-605, AND MASS SPECTROMETRY.	16565220 [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-81, AND MASSSPECTROMETRY.	16964243 [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 THR-49, AND MASSSPECTROMETRY.	17924679 [Abstract]