dbPTM

CNDD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CNDD3_HUMAN
UniProt AC	P42695
Protein Name	Condensin-2 complex subunit D3
Gene Name	NCAPD3
Organism	Homo sapiens (Human).
Sequence Length	1498
Subcellular Localization	Nucleus .
Protein Description	Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis..
Protein Sequence	MVALRGLGSGLQPWCPLDLRLEWVDTVWELDFTETEPLDPSIEAEIIETGLAAFTKLYESLLPFATGEHGSMESIWTFFIENNVSHSTLVALFYHFVQIVHKKNVSVQYREYGLHAAGLYFLLLEVPGSVANQVFHPVMFDKCIQTLKKSWPQESNLNRKRKKEQPKSSQANPGRHRKRGKPPRREDIEMDEIIEEQEDENICFSARDLSQIRNAIFHLLKNFLRLLPKFSLKEKPQCVQNCIEVFVSLTNFEPVLHECHVTQARALNQAKYIPELAYYGLYLLCSPIHGEGDKVISCVFHQMLSVILMLEVGEGSHRAPLAVTSQVINCRNQAVQFISALVDELKESIFPVVRILLQHICAKVVDKSEYRTFAAQSLVQLLSKLPCGEYAMFIAWLYKYSRSSKIPHRVFTLDVVLALLELPEREVDNTLSLEHQKFLKHKFLVQEIMFDRCLDKAPTVRSKALSSFAHCLELTVTSASESILELLINSPTFSVIESHPGTLLRNSSAFSYQRQTSNRSEPSGEINIDSSGETVGSGERCVMAMLRRRIRDEKTNVRKSALQVLVSILKHCDVSGMKEDLWILQDQCRDPAVSVRKQALQSLTELLMAQPRCVQIQKAWLRGVVPVVMDCESTVQEKALEFLDQLLLQNIRHHSHFHSGDDSQVLAWALLTLLTTESQELSRYLNKAFHIWSKKEKFSPTFINNVISHTGTEHSAPAWMLLSKIAGSSPRLDYSRIIQSWEKISSQQNPNSNTLGHILCVIGHIAKHLPKSTRDKVTDAVKCKLNGFQWSLEVISSAVDALQRLCRASAETPAEEQELLTQVCGDVLSTCEHRLSNIVLKENGTGNMDEDLLVKYIFTLGDIAQLCPARVEKRIFLLIQSVLASSADADHSPSSQGSSEAPASQPPPQVRGSVMPSVIRAHAIITLGKLCLQHEDLAKKSIPALVRELEVCEDVAVRNNVIIVMCDLCIRYTIMVDKYIPNISMCLKDSDPFIRKQTLILLTNLLQEEFVKWKGSLFFRFVSTLIDSHPDIASFGEFCLAHLLLKRNPVMFFQHFIECIFHFNNYEKHEKYNKFPQSEREKRLFSLKGKSNKERRMKIYKFLLEHFTDEQRFNITSKICLSILACFADGILPLDLDASELLSDTFEVLSSKEIKLLAMRSKPDKDLLMEEDDMALANVVMQEAQKKLISQVQKRNFIENIIPIIISLKTVLEKNKIPALRELMHYLREVMQDYRDELKDFFAVDKQLASELEYDMKKYQEQLVQEQELAKHADVAGTAGGAEVAPVAQVALCLETVPVPAGQENPAMSPAVSQPCTPRASAGHVAVSSPTPETGPLQRLLPKARPMSLSTIAILNSVKKAVESKSRHRSRSLGVLPFTLNSGSPEKTCSQVSSYSLEQESNGEIEHVTKRAISTPEKSISDVTFGAGVSYIGTPRTPSSAKEKIEGRSQGNDILCLSLPDKPPPQPQQWNVRSPARNKDTPACSRRSLRKTPLKTAN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	VALRGLGSGLQPWCP CCCCCCCCCCCCCCC	41.18	28122231
11	Ubiquitination	LRGLGSGLQPWCPLD CCCCCCCCCCCCCCC	6.23	22505724
106	Phosphorylation	IVHKKNVSVQYREYG HHHHCCCCHHHHHHC	16.94	20860994
109	Phosphorylation	KKNVSVQYREYGLHA HCCCCHHHHHHCCHH	11.85	20860994
148	Ubiquitination	DKCIQTLKKSWPQES HHHHHHHHHHCCCHH	48.42	-
149	Ubiquitination	KCIQTLKKSWPQESN HHHHHHHHHCCCHHH	61.95	22505724
167	Ubiquitination	KRKKEQPKSSQANPG HHHHCCCCCCCCCCC	63.53	29967540
229	Ubiquitination	NFLRLLPKFSLKEKP HHHHHHHHCCCCCCH	47.78	29967540
324	Phosphorylation	HRAPLAVTSQVINCR CCCCCEEHHHHHCCH	14.08	28555341
325	Phosphorylation	RAPLAVTSQVINCRN CCCCEEHHHHHCCHH	18.82	20860994
372	Phosphorylation	VDKSEYRTFAAQSLV CCHHHHHHHHHHHHH	19.41	24114839
377	Phosphorylation	YRTFAAQSLVQLLSK HHHHHHHHHHHHHHC	26.27	24114839
383	Phosphorylation	QSLVQLLSKLPCGEY HHHHHHHHCCCCHHH	40.51	24719451
400	Phosphorylation	FIAWLYKYSRSSKIP HHHHHHHHHCCCCCC	8.85	29116813
412	Phosphorylation	KIPHRVFTLDVVLAL CCCCCCHHHHHHHHH	21.13	-
430	Phosphorylation	PEREVDNTLSLEHQK CHHHCCCCCCHHHHH	17.17	19691289
432	Phosphorylation	REVDNTLSLEHQKFL HHCCCCCCHHHHHHH	29.67	19691289
442	Ubiquitination	HQKFLKHKFLVQEIM HHHHHHHHHHHHHHH	38.51	29967540
456	Acetylation	MFDRCLDKAPTVRSK HHHHHHHCCCCHHHH	43.23	26051181
456	Ubiquitination	MFDRCLDKAPTVRSK HHHHHHHCCCCHHHH	43.23	29967540
480	Ubiquitination	ELTVTSASESILELL HCCCCCCCHHHHHHH	31.48	22505724
490	Phosphorylation	ILELLINSPTFSVIE HHHHHHCCCCEEEHH	20.51	26074081
492	Phosphorylation	ELLINSPTFSVIESH HHHHCCCCEEEHHCC	28.50	26074081
507	Phosphorylation	PGTLLRNSSAFSYQR CCCEECCCCCCCCCC	19.33	19691289
508	Phosphorylation	GTLLRNSSAFSYQRQ CCEECCCCCCCCCCC	36.56	25159151
511	Phosphorylation	LRNSSAFSYQRQTSN ECCCCCCCCCCCCCC	21.77	26055452
512	Phosphorylation	RNSSAFSYQRQTSNR CCCCCCCCCCCCCCC	10.97	18083107
516	Phosphorylation	AFSYQRQTSNRSEPS CCCCCCCCCCCCCCC	30.11	28102081
517	Phosphorylation	FSYQRQTSNRSEPSG CCCCCCCCCCCCCCC	23.16	25159151
520	Phosphorylation	QRQTSNRSEPSGEIN CCCCCCCCCCCCEEE	59.10	25159151
523	Phosphorylation	TSNRSEPSGEINIDS CCCCCCCCCEEEECC	45.03	25159151
530	Phosphorylation	SGEINIDSSGETVGS CCEEEECCCCCCCCC	36.12	23401153
531	Phosphorylation	GEINIDSSGETVGSG CEEEECCCCCCCCCH	36.58	30175587
534	Phosphorylation	NIDSSGETVGSGERC EECCCCCCCCCHHHH	33.42	30175587
537	Phosphorylation	SSGETVGSGERCVMA CCCCCCCCHHHHHHH	32.90	29978859
554	Ubiquitination	RRRIRDEKTNVRKSA HHHHHHCCCHHHHHH	50.08	29967540
559	Ubiquitination	DEKTNVRKSALQVLV HCCCHHHHHHHHHHH	35.48	-
560	Phosphorylation	EKTNVRKSALQVLVS CCCHHHHHHHHHHHH	24.52	22199227
567	Phosphorylation	SALQVLVSILKHCDV HHHHHHHHHHHCCCC	20.31	20068231
578	Acetylation	HCDVSGMKEDLWILQ CCCCCCCHHCEEHHH	52.15	25953088
578	Ubiquitination	HCDVSGMKEDLWILQ CCCCCCCHHCEEHHH	52.15	29967540
597	Ubiquitination	DPAVSVRKQALQSLT CCHHHHHHHHHHHHH	37.45	29967540
604	Phosphorylation	KQALQSLTELLMAQP HHHHHHHHHHHHCCC	29.81	24043423
618	Ubiquitination	PRCVQIQKAWLRGVV CCHHHHHHHHHCCCC	43.06	22505724
687	Ubiquitination	ELSRYLNKAFHIWSK HHHHHHHHHHHHHCC	50.24	-
697	Ubiquitination	HIWSKKEKFSPTFIN HHHCCCCCCCHHHHH	61.08	29967540
699	Phosphorylation	WSKKEKFSPTFINNV HCCCCCCCHHHHHCC	33.81	27174698
701	Phosphorylation	KKEKFSPTFINNVIS CCCCCCHHHHHCCCC	35.63	27174698
708	Phosphorylation	TFINNVISHTGTEHS HHHHCCCCCCCCCCC	15.66	27174698
710	Phosphorylation	INNVISHTGTEHSAP HHCCCCCCCCCCCCC	38.72	27174698
712	Phosphorylation	NVISHTGTEHSAPAW CCCCCCCCCCCCCHH	31.51	27174698
715	Phosphorylation	SHTGTEHSAPAWMLL CCCCCCCCCCHHHHH	29.70	27174698
724	Ubiquitination	PAWMLLSKIAGSSPR CHHHHHHHHHCCCCC	36.22	-
728	Phosphorylation	LLSKIAGSSPRLDYS HHHHHHCCCCCCCHH	28.31	26699800
729	Phosphorylation	LSKIAGSSPRLDYSR HHHHHCCCCCCCHHH	17.08	26699800
743	Ubiquitination	RIIQSWEKISSQQNP HHHHHHHHHHCCCCC	41.45	-
771	Ubiquitination	HIAKHLPKSTRDKVT HHHHHCCCCCCCHHH	71.47	29967540
776	Ubiquitination	LPKSTRDKVTDAVKC CCCCCCCHHHHHHHH	43.68	29967540
782	Ubiquitination	DKVTDAVKCKLNGFQ CHHHHHHHHHCCCCH	27.63	29967540
841	Ubiquitination	RLSNIVLKENGTGNM HHHCCEEEECCCCCC	37.93	-
881	Phosphorylation	RIFLLIQSVLASSAD HHHHHHHHHHHHCCC	16.47	28122231
885	Phosphorylation	LIQSVLASSADADHS HHHHHHHHCCCCCCC	23.15	28348404
886	Phosphorylation	IQSVLASSADADHSP HHHHHHHCCCCCCCC	25.26	28348404
892	Phosphorylation	SSADADHSPSSQGSS HCCCCCCCCCCCCCC	27.33	28348404
894	Phosphorylation	ADADHSPSSQGSSEA CCCCCCCCCCCCCCC	38.00	22817901
895	Phosphorylation	DADHSPSSQGSSEAP CCCCCCCCCCCCCCC	41.78	18077418
898	Phosphorylation	HSPSSQGSSEAPASQ CCCCCCCCCCCCCCC	19.85	28348404
899	Phosphorylation	SPSSQGSSEAPASQP CCCCCCCCCCCCCCC	44.60	28348404
929	Ubiquitination	HAIITLGKLCLQHED HHHHHHHHHHHCCHH	38.86	-
939	Acetylation	LQHEDLAKKSIPALV HCCHHHHHCCHHHHH	55.11	26051181
939	Ubiquitination	LQHEDLAKKSIPALV HCCHHHHHCCHHHHH	55.11	29967540
940	Ubiquitination	QHEDLAKKSIPALVR CCHHHHHCCHHHHHH	48.27	-
972	Phosphorylation	MCDLCIRYTIMVDKY ECCHHHHHHHHHCCC	4.82	17924679
973	Phosphorylation	CDLCIRYTIMVDKYI CCHHHHHHHHHCCCC	7.86	22210691
988	Ubiquitination	PNISMCLKDSDPFIR CCHHHHCCCCCHHHH	50.70	29967540
1074	Ubiquitination	EKHEKYNKFPQSERE HHHHHHCCCCHHHHH	56.16	29967540
1086	Phosphorylation	EREKRLFSLKGKSNK HHHHHHHHCCCCCCH	33.49	24719451
1088	Ubiquitination	EKRLFSLKGKSNKER HHHHHHCCCCCCHHH	64.19	-
1101	Acetylation	ERRMKIYKFLLEHFT HHHHHHHHHHHHHCC	32.77	26051181
1108	Ubiquitination	KFLLEHFTDEQRFNI HHHHHHCCHHHHCCC	40.30	22817900
1119	Ubiquitination	RFNITSKICLSILAC HCCCCHHHHHHHHHH	2.60	22817900
1120	Ubiquitination	FNITSKICLSILACF CCCCHHHHHHHHHHH	2.54	21890473
1155	Ubiquitination	VLSSKEIKLLAMRSK HHCHHHHHHHHHCCC	38.24	29967540
1162	Ubiquitination	KLLAMRSKPDKDLLM HHHHHCCCCCHHHCC	47.04	-
1165	Ubiquitination	AMRSKPDKDLLMEED HHCCCCCHHHCCCHH	59.82	-
1175	Phosphorylation	LMEEDDMALANVVMQ CCCHHHHHHHHHHHH	15.54	32645325
1187	Ubiquitination	VMQEAQKKLISQVQK HHHHHHHHHHHHHHH	38.68	29967540
1193	Phosphorylation	KKLISQVQKRNFIEN HHHHHHHHHHCHHHH	31.21	32142685
1194	Ubiquitination	KLISQVQKRNFIENI HHHHHHHHHCHHHHH	50.91	29967540
1207	Phosphorylation	NIIPIIISLKTVLEK HHHHHHHHHHHHHHH	17.26	24719451
1216	Acetylation	KTVLEKNKIPALREL HHHHHHCCCHHHHHH	62.22	7825993
1246	Phosphorylation	KDFFAVDKQLASELE HHHHHHCHHHHHHHH	40.38	32142685
1246	Ubiquitination	KDFFAVDKQLASELE HHHHHHCHHHHHHHH	40.38	21906983
1250	Phosphorylation	AVDKQLASELEYDMK HHCHHHHHHHHHHHH	51.84	19691289
1257	Ubiquitination	SELEYDMKKYQEQLV HHHHHHHHHHHHHHH	45.49	22817900
1258	Ubiquitination	ELEYDMKKYQEQLVQ HHHHHHHHHHHHHHH	45.59	22817900
1278	Phosphorylation	KHADVAGTAGGAEVA HHCCCCCCCCCCCCC	16.64	24043423
1296	Phosphorylation	QVALCLETVPVPAGQ HEEEHHCCCCCCCCC	19.70	26074081
1304	Ubiquitination	VPVPAGQENPAMSPA CCCCCCCCCCCCCCC	65.35	24816145
1309	Phosphorylation	GQENPAMSPAVSQPC CCCCCCCCCCCCCCC	16.29	26074081
1313	Phosphorylation	PAMSPAVSQPCTPRA CCCCCCCCCCCCCCC	30.43	26074081
1317	Phosphorylation	PAVSQPCTPRASAGH CCCCCCCCCCCCCCC	23.61	26074081
1321	Phosphorylation	QPCTPRASAGHVAVS CCCCCCCCCCCEEEE	35.74	25159151
1328	Phosphorylation	SAGHVAVSSPTPETG CCCCEEEECCCCCCC	22.36	25159151
1329	Phosphorylation	AGHVAVSSPTPETGP CCCEEEECCCCCCCH	26.62	25159151
1331	Phosphorylation	HVAVSSPTPETGPLQ CEEEECCCCCCCHHH	35.39	25159151
1334	Phosphorylation	VSSPTPETGPLQRLL EECCCCCCCHHHHHC	45.35	25159151
1348	Phosphorylation	LPKARPMSLSTIAIL CCCCCCCCHHHHHHH	23.11	22167270
1350	Phosphorylation	KARPMSLSTIAILNS CCCCCCHHHHHHHHH	15.51	22167270
1351	Phosphorylation	ARPMSLSTIAILNSV CCCCCHHHHHHHHHH	21.52	22167270
1353	Ubiquitination	PMSLSTIAILNSVKK CCCHHHHHHHHHHHH	10.58	24816145
1357	Phosphorylation	STIAILNSVKKAVES HHHHHHHHHHHHHHC	31.69	22167270
1360	Ubiquitination	AILNSVKKAVESKSR HHHHHHHHHHHCCCC	56.35	-
1366	Phosphorylation	KKAVESKSRHRSRSL HHHHHCCCCHHCCCC	42.47	-
1370	Phosphorylation	ESKSRHRSRSLGVLP HCCCCHHCCCCCEEE	21.79	22617229
1372	Phosphorylation	KSRHRSRSLGVLPFT CCCHHCCCCCEEEEE	30.62	28355574
1379	Phosphorylation	SLGVLPFTLNSGSPE CCCEEEEECCCCCCC	24.08	30266825
1382	Phosphorylation	VLPFTLNSGSPEKTC EEEEECCCCCCCCCH	43.70	29255136
1384	Phosphorylation	PFTLNSGSPEKTCSQ EEECCCCCCCCCHHH	29.70	29255136
1388	Phosphorylation	NSGSPEKTCSQVSSY CCCCCCCCHHHHCCC	18.74	22210691
1390	Phosphorylation	GSPEKTCSQVSSYSL CCCCCCHHHHCCCEE	38.56	22210691
1393	Phosphorylation	EKTCSQVSSYSLEQE CCCHHHHCCCEEECC	18.87	16565220
1410	Ubiquitination	GEIEHVTKRAISTPE CCEEEHHHHCCCCCC	38.45	29967540
1414	Phosphorylation	HVTKRAISTPEKSIS EHHHHCCCCCCCCHH	36.60	30576142
1415	Phosphorylation	VTKRAISTPEKSISD HHHHCCCCCCCCHHH	29.38	25159151
1418	Acetylation	RAISTPEKSISDVTF HCCCCCCCCHHHCEE	55.05	26051181
1419	Phosphorylation	AISTPEKSISDVTFG CCCCCCCCHHHCEEC	26.18	30624053
1421	Phosphorylation	STPEKSISDVTFGAG CCCCCCHHHCEECCC	32.87	30624053
1424	Phosphorylation	EKSISDVTFGAGVSY CCCHHHCEECCCCEE	22.72	-
1434	Phosphorylation	AGVSYIGTPRTPSSA CCCEECCCCCCCCCH	10.47	21712546
1437	Phosphorylation	SYIGTPRTPSSAKEK EECCCCCCCCCHHHH	28.82	21712546
1439	Phosphorylation	IGTPRTPSSAKEKIE CCCCCCCCCHHHHHC	42.17	20860994
1442	Ubiquitination	PRTPSSAKEKIEGRS CCCCCCHHHHHCCCC	62.58	24816145
1449	Phosphorylation	KEKIEGRSQGNDILC HHHHCCCCCCCCEEE	53.98	25159151
1458	Phosphorylation	GNDILCLSLPDKPPP CCCEEEEECCCCCCC	36.54	25159151
1462	Ubiquitination	LCLSLPDKPPPQPQQ EEEECCCCCCCCCCC	58.44	29967540
1474	Phosphorylation	PQQWNVRSPARNKDT CCCCCCCCCCCCCCC	20.73	30576142
1481	Phosphorylation	SPARNKDTPACSRRS CCCCCCCCCCCCCCH	17.88	26074081
1485	Phosphorylation	NKDTPACSRRSLRKT CCCCCCCCCCHHCCC	32.60	26074081
1488	Phosphorylation	TPACSRRSLRKTPLK CCCCCCCHHCCCCCC	31.26	29496963
1491	Ubiquitination	CSRRSLRKTPLKTAN CCCCHHCCCCCCCCC	60.84	24816145
1492	Phosphorylation	SRRSLRKTPLKTAN- CCCHHCCCCCCCCC-	27.67	29496963
1496	Phosphorylation	LRKTPLKTAN----- HCCCCCCCCC-----	38.83	21712546

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
1415	T	Phosphorylation	Kinase	CDK1	P06493	PSP
1419	S	Phosphorylation	Kinase	PLK1	P53350	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CNDD3_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 CNDD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CNDG2_HUMAN	NCAPG2	physical	17268547
CNDG2_HUMAN	NCAPG2	physical	14532007
SMC4_HUMAN	SMC4	physical	14532007
SMC2_HUMAN	SMC2	physical	14532007
CNDH2_HUMAN	NCAPH2	physical	14532007
TEKT1_HUMAN	TEKT1	physical	25416956
CLCB_HUMAN	CLTB	physical	26344197
PI42C_HUMAN	PIP4K2C	physical	26344197
2ABA_HUMAN	PPP2R2A	physical	26344197
PSMD4_HUMAN	PSMD4	physical	26344197
SPTN1_HUMAN	SPTAN1	physical	26344197
SPTN2_HUMAN	SPTBN2	physical	26344197
SNUT2_HUMAN	USP39	physical	26344197
1433B_HUMAN	YWHAB	physical	26344197
1433Z_HUMAN	YWHAZ	physical	26344197
LG3BP_HUMAN	LGALS3BP	physical	26496610
SMC4_HUMAN	SMC4	physical	26496610
SMC2_HUMAN	SMC2	physical	26496610
CNDH2_HUMAN	NCAPH2	physical	26496610
CNDG2_HUMAN	NCAPG2	physical	26496610
NEUL_HUMAN	NLN	physical	26496610
ESCO2_HUMAN	ESCO2	physical	26496610
CISD3_HUMAN	CISD3	physical	26496610
2ABD_HUMAN	PPP2R2D	physical	28514442
PP2AA_HUMAN	PPP2CA	physical	28514442
BIN1_HUMAN	BIN1	physical	28514442
H12_HUMAN	HIST1H1C	physical	28514442
G3PT_HUMAN	GAPDHS	physical	28514442
2AAB_HUMAN	PPP2R1B	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
2AAA_HUMAN	PPP2R1A	physical	28514442

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 CNDD3_HUMAN

Related Literatures of Post-Translational Modification

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-1384, AND MASSSPECTROMETRY.	19690332 [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-1329; THR-1331;SER-1348; SER-1357 AND SER-1384, 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-1328; SER-1329; THR-1331AND SER-1384, AND MASS 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-1329 AND THR-1331, ANDMASS SPECTROMETRY.	18220336 [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-1357, AND MASSSPECTROMETRY.	18187866 [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-507 AND SER-508, ANDMASS 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 SER-1393, AND MASSSPECTROMETRY.	16565220 [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-531 AND SER-1384, ANDMASS SPECTROMETRY.	15302935 [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 TYR-972, AND MASSSPECTROMETRY.	17924679 [Abstract]