dbPTM

CND1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CND1_HUMAN
UniProt AC	Q15021
Protein Name	Condensin complex subunit 1
Gene Name	NCAPD2
Organism	Homo sapiens (Human).
Sequence Length	1401
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. May target the condensin complex to DNA via its C-terminal domain..
Protein Sequence	MAPQMYEFHLPLSPEELLKSGGVNQYVVQEVLSIKHLPPQLRAFQAAFRAQGPLAMLQHFDTIYSILHHFRSIDPGLKEDTLQFLIKVVSRHSQELPAILDDTTLSGSDRNAHLNALKMNCYALIRLLESFETMASQTNLVDLDLGGKGKKARTKAAHGFDWEEERQPILQLLTQLLQLDIRHLWNHSIIEEEFVSLVTGCCYRLLENPTINHQKNRPTREAITHLLGVALTRYNHMLSATVKIIQMLQHFEHLAPVLVAAVSLWATDYGMKSIVGEIVREIGQKCPQELSRDPSGTKGFAAFLTELAERVPAILMSSMCILLDHLDGENYMMRNAVLAAMAEMVLQVLSGDQLEAAARDTRDQFLDTLQAHGHDVNSFVRSRVLQLFTRIVQQKALPLTRFQAVVALAVGRLADKSVLVCKNAIQLLASFLANNPFSCKLSDADLAGPLQKETQKLQEMRAQRRTAAASAVLDPEEEWEAMLPELKSTLQQLLQLPQGEEEIPEQIANTETTEDVKGRIYQLLAKASYKKAIILTREATGHFQESEPFSHIDPEESEETRLLNILGLIFKGPAASTQEKNPRESTGNMVTGQTVCKNKPNMSDPEESRGNDELVKQEMLVQYLQDAYSFSRKITEAIGIISKMMYENTTTVVQEVIEFFVMVFQFGVPQALFGVRRMLPLIWSKEPGVREAVLNAYRQLYLNPKGDSARAKAQALIQNLSLLLVDASVGTIQCLEEILCEFVQKDELKPAVTQLLWERATEKVACCPLERCSSVMLLGMMARGKPEIVGSNLDTLVSIGLDEKFPQDYRLAQQVCHAIANISDRRKPSLGKRHPPFRLPQEHRLFERLRETVTKGFVHPDPLWIPFKEVAVTLIYQLAEGPEVICAQILQGCAKQALEKLEEKRTSQEDPKESPAMLPTFLLMNLLSLAGDVALQQLVHLEQAVSGELCRRRVLREEQEHKTKDPKEKNTSSETTMEEELGLVGATADDTEAELIRGICEMELLDGKQTLAAFVPLLLKVCNNPGLYSNPDLSAAASLALGKFCMISATFCDSQLRLLFTMLEKSPLPIVRSNLMVATGDLAIRFPNLVDPWTPHLYARLRDPAQQVRKTAGLVMTHLILKDMVKVKGQVSEMAVLLIDPEPQIAALAKNFFNELSHKGNAIYNLLPDIISRLSDPELGVEEEPFHTIMKQLLSYITKDKQTESLVEKLCQRFRTSRTERQQRDLAYCVSQLPLTERGLRKMLDNFDCFGDKLSDESIFSAFLSVVGKLRRGAKPEGKAIIDEFEQKLRACHTRGLDGIKELEIGQAGSQRAPSAKKPSTGSRYQPLASTASDNDFVTPEPRRTTRRHPNTQQRASKKKPKVVFSSDESSEEDLSAEMTEDETPKKTTPILRASARRHRS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAPQMYEFHLPLS --CCCCCEEECCCCC	15.36	27642862
13	Phosphorylation	YEFHLPLSPEELLKS EEECCCCCHHHHHHC	28.46	24732914
20	Phosphorylation	SPEELLKSGGVNQYV CHHHHHHCCCCCHHH	40.52	22199227
33	Phosphorylation	YVVQEVLSIKHLPPQ HHHHHHHHCCCCCHH	34.46	27251275
35	Ubiquitination	VQEVLSIKHLPPQLR HHHHHHCCCCCHHHH	35.40	21906983
78	Ubiquitination	RSIDPGLKEDTLQFL HCCCCCCCHHHHHHH	60.50	21906983
87	Ubiquitination	DTLQFLIKVVSRHSQ HHHHHHHHHHHHCCC	38.44	-
103	Phosphorylation	LPAILDDTTLSGSDR CCCCCCCCCCCCCCC	29.33	22817900
106	Phosphorylation	ILDDTTLSGSDRNAH CCCCCCCCCCCCHHH	33.87	-
118	Ubiquitination	NAHLNALKMNCYALI HHHHHHHHHHHHHHH	26.17	-
122	Phosphorylation	NALKMNCYALIRLLE HHHHHHHHHHHHHHH	10.23	-
148	Acetylation	VDLDLGGKGKKARTK CCCCCCCCCHHHHHH	66.80	26051181
148	Ubiquitination	VDLDLGGKGKKARTK CCCCCCCCCHHHHHH	66.80	21906983
151	Ubiquitination	DLGGKGKKARTKAAH CCCCCCHHHHHHHHC	52.34	-
154	Phosphorylation	GKGKKARTKAAHGFD CCCHHHHHHHHCCCC	29.87	-
155	Ubiquitination	KGKKARTKAAHGFDW CCHHHHHHHHCCCCH	37.71	-
215	Ubiquitination	NPTINHQKNRPTREA CCCCCCCCCCCHHHH	47.58	-
234	Phosphorylation	LGVALTRYNHMLSAT HHHHHHHHHHHHHHH	12.27	20860994
239	Phosphorylation	TRYNHMLSATVKIIQ HHHHHHHHHHHHHHH	17.83	20860994
241	Phosphorylation	YNHMLSATVKIIQML HHHHHHHHHHHHHHH	20.96	20860994
285	Ubiquitination	IVREIGQKCPQELSR HHHHHHHHCCHHHCC	42.54	-
286	S-nitrosylation	VREIGQKCPQELSRD HHHHHHHCCHHHCCC	3.02	22178444
291	Phosphorylation	QKCPQELSRDPSGTK HHCCHHHCCCCCCCH	33.61	-
298	Ubiquitination	SRDPSGTKGFAAFLT CCCCCCCHHHHHHHH	56.40	21906983
368	Phosphorylation	TRDQFLDTLQAHGHD HHHHHHHHHHHCCCC	23.94	20068231
378	Phosphorylation	AHGHDVNSFVRSRVL HCCCCHHHHHHHHHH	25.60	20068231
382	Phosphorylation	DVNSFVRSRVLQLFT CHHHHHHHHHHHHHH	22.80	20068231
395	2-Hydroxyisobutyrylation	FTRIVQQKALPLTRF HHHHHHHCCCCCHHH	34.50	-
395	Ubiquitination	FTRIVQQKALPLTRF HHHHHHHCCCCCHHH	34.50	21906983
416	2-Hydroxyisobutyrylation	AVGRLADKSVLVCKN HHHHHCCCHHHHHHH	36.54	-
416	Ubiquitination	AVGRLADKSVLVCKN HHHHHCCCHHHHHHH	36.54	-
452	Ubiquitination	DLAGPLQKETQKLQE HHCCHHHHHHHHHHH	71.11	21906983
454	Phosphorylation	AGPLQKETQKLQEMR CCHHHHHHHHHHHHH	37.73	-
456	Ubiquitination	PLQKETQKLQEMRAQ HHHHHHHHHHHHHHH	60.60	-
517	Ubiquitination	TETTEDVKGRIYQLL CCCCHHHHHHHHHHH	55.59	21906983
526	Ubiquitination	RIYQLLAKASYKKAI HHHHHHHHHCCCEEE	37.52	-
531	Malonylation	LAKASYKKAIILTRE HHHHCCCEEEEEEEC	36.26	26320211
571	Ubiquitination	NILGLIFKGPAASTQ HHHHHHHCCCCCCCC	57.92	-
576	Phosphorylation	IFKGPAASTQEKNPR HHCCCCCCCCCCCCC	32.50	24732914
577	Phosphorylation	FKGPAASTQEKNPRE HCCCCCCCCCCCCCC	35.70	17525332
580	Ubiquitination	PAASTQEKNPRESTG CCCCCCCCCCCCCCC	63.53	21906983
585	Phosphorylation	QEKNPRESTGNMVTG CCCCCCCCCCCCCCC	42.78	23401153
586	Phosphorylation	EKNPRESTGNMVTGQ CCCCCCCCCCCCCCC	28.02	30266825
589	Sulfoxidation	PRESTGNMVTGQTVC CCCCCCCCCCCCCCC	2.78	21406390
591	Phosphorylation	ESTGNMVTGQTVCKN CCCCCCCCCCCCCCC	16.89	24732914
594	Phosphorylation	GNMVTGQTVCKNKPN CCCCCCCCCCCCCCC	29.26	24732914
603	Phosphorylation	CKNKPNMSDPEESRG CCCCCCCCCHHHHCC	57.57	30576142
608	Phosphorylation	NMSDPEESRGNDELV CCCCHHHHCCCHHHH	43.77	25159151
609	Methylation	MSDPEESRGNDELVK CCCHHHHCCCHHHHH	51.73	-
616	Ubiquitination	RGNDELVKQEMLVQY CCCHHHHHHHHHHHH	53.84	21906983
629	Phosphorylation	QYLQDAYSFSRKITE HHHHHHHHHHHHHHH	20.61	17081983
633	Ubiquitination	DAYSFSRKITEAIGI HHHHHHHHHHHHHHH	53.43	-
635	Phosphorylation	YSFSRKITEAIGIIS HHHHHHHHHHHHHHH	23.54	25367160
642	Phosphorylation	TEAIGIISKMMYENT HHHHHHHHHHHCCCH	16.75	24719451
684	Phosphorylation	RMLPLIWSKEPGVRE HHHHHHHCCCCCHHH	21.83	22985185
685	Ubiquitination	MLPLIWSKEPGVREA HHHHHHCCCCCHHHH	53.59	21906983
697	Phosphorylation	REAVLNAYRQLYLNP HHHHHHHHHHHHCCC	9.60	25022875
705	Ubiquitination	RQLYLNPKGDSARAK HHHHCCCCCHHHHHH	74.42	21906983
749	Ubiquitination	FVQKDELKPAVTQLL HHCCCCHHHHHHHHH	28.96	21906983
763	Acetylation	LWERATEKVACCPLE HHHHHHCCCCCCCHH	30.67	25953088
763	Ubiquitination	LWERATEKVACCPLE HHHHHHCCCCCCCHH	30.67	-
785	Ubiquitination	LGMMARGKPEIVGSN HHHHHCCCCEECCCC	33.64	21906983
804	Ubiquitination	VSIGLDEKFPQDYRL HHCCCCCCCCCHHHH	63.11	21906983
855	Ubiquitination	RLRETVTKGFVHPDP HHHHHHHCCCCCCCC	46.12	21906983
900	Ubiquitination	CAKQALEKLEEKRTS HHHHHHHHHHHHCCC	63.15	-
906	Phosphorylation	EKLEEKRTSQEDPKE HHHHHHCCCCCCCCC	45.92	24532841
907	Phosphorylation	KLEEKRTSQEDPKES HHHHHCCCCCCCCCC	35.29	24532841
962	Ubiquitination	LREEQEHKTKDPKEK HHHHHHHCCCCCCCC	57.42	21906983
969	Ubiquitination	KTKDPKEKNTSSETT CCCCCCCCCCCCCCH	72.20	21906983
971	Phosphorylation	KDPKEKNTSSETTME CCCCCCCCCCCCHHH	44.70	24732914
972	Phosphorylation	DPKEKNTSSETTMEE CCCCCCCCCCCHHHH	35.25	24732914
973	Phosphorylation	PKEKNTSSETTMEEE CCCCCCCCCCHHHHH	36.60	24732914
975	Phosphorylation	EKNTSSETTMEEELG CCCCCCCCHHHHHHC	33.13	24732914
976	Phosphorylation	KNTSSETTMEEELGL CCCCCCCHHHHHHCC	20.66	24732914
1002	Sulfoxidation	LIRGICEMELLDGKQ HHHHHHHHHCCCCHH	3.69	21406390
1008	Ubiquitination	EMELLDGKQTLAAFV HHHCCCCHHHHHHHH	39.51	-
1048	Phosphorylation	LGKFCMISATFCDSQ HHCHHHHHHEECHHH	8.38	28258704
1050	Phosphorylation	KFCMISATFCDSQLR CHHHHHHEECHHHHH	20.29	28258704
1061	Phosphorylation	SQLRLLFTMLEKSPL HHHHHHHHHHHCCCC	22.33	20068231
1065	Ubiquitination	LLFTMLEKSPLPIVR HHHHHHHCCCCCCCC	54.11	21906983
1066	Phosphorylation	LFTMLEKSPLPIVRS HHHHHHCCCCCCCCC	23.46	28555341
1073	Phosphorylation	SPLPIVRSNLMVATG CCCCCCCCCCEEEEC	24.34	20068231
1079	Phosphorylation	RSNLMVATGDLAIRF CCCCEEEECCEEEEC	21.59	20068231
1094	Phosphorylation	PNLVDPWTPHLYARL CCCCCCCCHHHHHHH	13.25	-
1098	Phosphorylation	DPWTPHLYARLRDPA CCCCHHHHHHHCCHH	6.14	27642862
1110	Ubiquitination	DPAQQVRKTAGLVMT CHHHHHHHHHHHHHH	43.82	-
1111	Phosphorylation	PAQQVRKTAGLVMTH HHHHHHHHHHHHHHH	18.52	21406692
1117	Phosphorylation	KTAGLVMTHLILKDM HHHHHHHHHHHHHHH	13.17	21406692
1172	Phosphorylation	NLLPDIISRLSDPEL HHHHHHHHHHCCCCC	27.74	21712546
1195	Phosphorylation	TIMKQLLSYITKDKQ HHHHHHHHHHCCCCH	24.07	26074081
1196	Phosphorylation	IMKQLLSYITKDKQT HHHHHHHHHCCCCHH	16.75	26074081
1198	Phosphorylation	KQLLSYITKDKQTES HHHHHHHCCCCHHHH	25.59	26074081
1199	Ubiquitination	QLLSYITKDKQTESL HHHHHHCCCCHHHHH	54.06	-
1201	Ubiquitination	LSYITKDKQTESLVE HHHHCCCCHHHHHHH	61.75	21906983
1209	Ubiquitination	QTESLVEKLCQRFRT HHHHHHHHHHHHHCC	47.27	-
1228	Phosphorylation	RQQRDLAYCVSQLPL HHHHHHHHHHHHCCC	10.73	-
1229	Glutathionylation	QQRDLAYCVSQLPLT HHHHHHHHHHHCCCC	1.65	22555962
1279	Ubiquitination	RGAKPEGKAIIDEFE CCCCCCCCHHHHHHH	34.45	-
1288	Acetylation	IIDEFEQKLRACHTR HHHHHHHHHHHHHHC	32.51	25953088
1288	Ubiquitination	IIDEFEQKLRACHTR HHHHHHHHHHHHHHC	32.51	21906983
1301	Ubiquitination	TRGLDGIKELEIGQA HCCCCCCCEEECCCC	62.87	21906983
1310	Phosphorylation	LEIGQAGSQRAPSAK EECCCCCCCCCCCCC	21.36	23401153
1315	Phosphorylation	AGSQRAPSAKKPSTG CCCCCCCCCCCCCCC	52.30	25159151
1317	Acetylation	SQRAPSAKKPSTGSR CCCCCCCCCCCCCCC	70.34	25953088
1320	Phosphorylation	APSAKKPSTGSRYQP CCCCCCCCCCCCCCC	55.04	26074081
1321	Phosphorylation	PSAKKPSTGSRYQPL CCCCCCCCCCCCCCC	47.94	26074081
1323	Phosphorylation	AKKPSTGSRYQPLAS CCCCCCCCCCCCCCC	28.09	26074081
1325	Phosphorylation	KPSTGSRYQPLASTA CCCCCCCCCCCCCCC	19.04	23927012
1330	Phosphorylation	SRYQPLASTASDNDF CCCCCCCCCCCCCCC	31.99	29255136
1331	Phosphorylation	RYQPLASTASDNDFV CCCCCCCCCCCCCCC	25.27	29255136
1333	Phosphorylation	QPLASTASDNDFVTP CCCCCCCCCCCCCCC	36.71	29255136
1339	Phosphorylation	ASDNDFVTPEPRRTT CCCCCCCCCCCCCCC	23.17	29255136
1345	Phosphorylation	VTPEPRRTTRRHPNT CCCCCCCCCCCCCCH	26.40	-
1352	Phosphorylation	TTRRHPNTQQRASKK CCCCCCCHHHHHCCC	30.45	30576142
1366	Phosphorylation	KKPKVVFSSDESSEE CCCCEEECCCCCCHH	25.85	21955146
1367	Phosphorylation	KPKVVFSSDESSEED CCCEEECCCCCCHHH	33.65	21955146
1370	Phosphorylation	VVFSSDESSEEDLSA EEECCCCCCHHHHHH	48.30	21955146
1371	Phosphorylation	VFSSDESSEEDLSAE EECCCCCCHHHHHHH	42.85	21955146
1376	Phosphorylation	ESSEEDLSAEMTEDE CCCHHHHHHHCCCCC	34.21	25022875
1380	Phosphorylation	EDLSAEMTEDETPKK HHHHHHCCCCCCCCC	31.61	25137130
1384	Phosphorylation	AEMTEDETPKKTTPI HHCCCCCCCCCCCHH	53.37	29514088
1388	Phosphorylation	EDETPKKTTPILRAS CCCCCCCCCHHHHHH	43.88	30266825
1389	Phosphorylation	DETPKKTTPILRASA CCCCCCCCHHHHHHH	19.74	30266825
1395	Phosphorylation	TTPILRASARRHRS- CCHHHHHHHHHHCC-	18.84	12138188

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
1384	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
1389	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CND1_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 CND1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC4_HUMAN	SMC4	physical	10958694
SMC2_HUMAN	SMC2	physical	10958694
PARP1_HUMAN	PARP1	physical	16543152
CND3_HUMAN	NCAPG	physical	17268547
CND2_HUMAN	NCAPH	physical	17268547
SMC2_HUMAN	SMC2	physical	22939629
SMC4_HUMAN	SMC4	physical	22939629
CND3_HUMAN	NCAPG	physical	22939629
MEA1_HUMAN	MEA1	physical	22939629
NU153_HUMAN	NUP153	physical	22939629
PNPT1_HUMAN	PNPT1	physical	22939629
FLNC_HUMAN	FLNC	physical	22863883
CND2_HUMAN	NCAPH	physical	22863883
PABP4_HUMAN	PABPC4	physical	22863883
RABE1_HUMAN	RABEP1	physical	22863883
SMC4_HUMAN	SMC4	physical	22863883
CND3_HUMAN	NCAPG	physical	26344197
CND2_HUMAN	NCAPH	physical	26344197
SMC2_HUMAN	SMC2	physical	26344197
SMC4_HUMAN	SMC4	physical	26344197
HECD1_HUMAN	HECTD1	physical	26166704

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 CND1_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-1333 AND THR-1339, ANDMASS 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-1330, AND MASSSPECTROMETRY.	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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-586; SER-1333 ANDTHR-1339, 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-585; SER-1330; THR-1331;SER-1333; THR-1339; SER-1366; SER-1367; SER-1370 AND SER-1371, ANDMASS SPECTROMETRY.	18669648 [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-585; THR-586 ANDTHR-1339, AND MASS SPECTROMETRY.	18220336 [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-585 AND SER-1310, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"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 THR-577; SER-585 ANDSER-1310, AND MASS SPECTROMETRY.	17525332 [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-103; SER-585; SER-1330;SER-1333 AND THR-1388, AND MASS SPECTROMETRY.	16565220 [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-1330; THR-1331;SER-1366; SER-1367; SER-1370; SER-1371 AND SER-1376, AND MASSSPECTROMETRY.	17081983 [Abstract]