dbPTM

ZEB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZEB1_HUMAN
UniProt AC	P37275
Protein Name	Zinc finger E-box-binding homeobox 1
Gene Name	ZEB1
Organism	Homo sapiens (Human).
Sequence Length	1124
Subcellular Localization	Nucleus .
Protein Description	Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs..
Protein Sequence	MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPVDYEFKPIVVASGINCSTPLQNGVFTGGGPLQATSSPQGMVQAVVLPTVGLVSPISINLSDIQNVLKVAVDGNVIRQVLENNQANLASKEQETINASPIQQGGHSVISAISLPLVDQDGTTKIIINYSLEQPSQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNDSTCLLCDDCPGDINALPELKHYDLKQPTQPPPLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANPINIAIPTVTAQLPTIVAIADQNSVPCLRALAANKQTILIPQVAYTYSTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEEDKEMEELQEEKECEKPQGDEEEEEEEEEVEEEEVEEAENEGEEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Phosphorylation	NYNTVVETNSDSDDE CCCEEEECCCCCCCC	28.54	30576142
31	Phosphorylation	NTVVETNSDSDDEDK CEEEECCCCCCCCCC	46.00	25159151
31 (in isoform 2)	Phosphorylation	-	46.00	27251275
33	Phosphorylation	VVETNSDSDDEDKLH EEECCCCCCCCCCEE	46.94	25159151
33 (in isoform 2)	Phosphorylation	-	46.94	27251275
46	Phosphorylation	LHIVEEESVTDAADC EEEEEEEECCCHHHC	33.33	30576142
48	Phosphorylation	IVEEESVTDAADCEG EEEEEECCCHHHCCC	29.24	30576142
48 (in isoform 2)	Phosphorylation	-	29.24	27251275
114	Phosphorylation	VKDDECESDAENEQN ECCCCCCCCCCCCCC	54.50	26471730
135	Phosphorylation	EFLQQQDTAVIFPEA HHHHHCCCEEECCCC	20.63	26074081
151	Phosphorylation	EEDQRQGTPEASGHD HHHHCCCCCCCCCCC	15.04	26074081
155	Phosphorylation	RQGTPEASGHDENGT CCCCCCCCCCCCCCC	34.69	28122231
162	Phosphorylation	SGHDENGTPDAFSQL CCCCCCCCCCHHHHH	29.58	28122231
167	Phosphorylation	NGTPDAFSQLLTCPY CCCCCHHHHHHCCCC	22.95	27080861
171	Phosphorylation	DAFSQLLTCPYCDRG CHHHHHHCCCCCCCC	21.74	27080861
174	Phosphorylation	SQLLTCPYCDRGYKR HHHHCCCCCCCCCHH	14.77	27080861
184	Phosphorylation	RGYKRFTSLKEHIKY CCCHHHHHHHHHHHH	34.43	-
186	Sumoylation	YKRFTSLKEHIKYRH CHHHHHHHHHHHHHH	47.19	28112733
186	Ubiquitination	YKRFTSLKEHIKYRH CHHHHHHHHHHHHHH	47.19	-
195	Sumoylation	HIKYRHEKNEDNFSC HHHHHHHHCCCCCEE	60.56	28112733
243	Phosphorylation	CNRKFKCTECGKAFK CCCEEEECCCCHHHH	34.60	-
263	Phosphorylation	KEHLRIHSGEKPYEC HHHHEECCCCCCCCC	46.40	28450419
278	Phosphorylation	PNCKKRFSHSGSYSS CCCCCCCCCCCCCCC	22.30	28555341
280	Phosphorylation	CKKRFSHSGSYSSHI CCCCCCCCCCCCCCC	28.39	28555341
282	Phosphorylation	KRFSHSGSYSSHISS CCCCCCCCCCCCCCC	25.51	28555341
283	Phosphorylation	RFSHSGSYSSHISSK CCCCCCCCCCCCCCC	20.09	30576142
284	Phosphorylation	FSHSGSYSSHISSKK CCCCCCCCCCCCCCC	19.69	30576142
285	Phosphorylation	SHSGSYSSHISSKKC CCCCCCCCCCCCCCE	19.33	30576142
288	Phosphorylation	GSYSSHISSKKCISL CCCCCCCCCCCEEEE	30.59	-
289	Phosphorylation	SYSSHISSKKCISLI CCCCCCCCCCEEEEE	35.22	-
304	Phosphorylation	PVNGRPRTGLKTSQC ECCCEECCCCCCCCC	49.93	23312004
307	Sumoylation	GRPRTGLKTSQCSSP CEECCCCCCCCCCCC	47.69	28112733
308	Phosphorylation	RPRTGLKTSQCSSPS EECCCCCCCCCCCCC	29.13	21712546
309	Phosphorylation	PRTGLKTSQCSSPSL ECCCCCCCCCCCCCC	27.83	21712546
312	Phosphorylation	GLKTSQCSSPSLSAS CCCCCCCCCCCCCCC	37.33	21712546
313	Phosphorylation	LKTSQCSSPSLSASP CCCCCCCCCCCCCCC	26.57	23401153
313 (in isoform 2)	Phosphorylation	-	26.57	24719451
314 (in isoform 2)	Phosphorylation	-	24.01	27251275
315	Phosphorylation	TSQCSSPSLSASPGS CCCCCCCCCCCCCCC	36.58	21712546
317	Phosphorylation	QCSSPSLSASPGSPT CCCCCCCCCCCCCCC	30.91	21712546
319	Phosphorylation	SSPSLSASPGSPTRP CCCCCCCCCCCCCCH	26.81	25159151
322	Phosphorylation	SLSASPGSPTRPQIR CCCCCCCCCCCHHHH	26.87	25159151
323 (in isoform 2)	Phosphorylation	-	38.04	24719451
324	Phosphorylation	SASPGSPTRPQIRQK CCCCCCCCCHHHHHH	57.59	22617229
331	Sumoylation	TRPQIRQKIENKPLQ CCHHHHHHHHCCCHH	41.98	28112733
335	Sumoylation	IRQKIENKPLQEQLS HHHHHHCCCHHHCCC	34.02	28112733
335	Ubiquitination	IRQKIENKPLQEQLS HHHHHHCCCHHHCCC	34.02	-
342	Phosphorylation	KPLQEQLSVNQIKTE CCHHHCCCCCCCCCC	20.79	25159151
343 (in isoform 2)	Phosphorylation	-	9.21	27251275
347	Sumoylation	QLSVNQIKTEPVDYE CCCCCCCCCCCCCCC	36.75	-
347	Sumoylation	QLSVNQIKTEPVDYE CCCCCCCCCCCCCCC	36.75	28112733
439	Sumoylation	NQANLASKEQETINA CCHHCCCCCHHCCCC	58.78	28112733
443	Phosphorylation	LASKEQETINASPIQ CCCCCHHCCCCCCCC	21.16	30108239
447	Phosphorylation	EQETINASPIQQGGH CHHCCCCCCCCCCCE	20.32	30108239
455	Phosphorylation	PIQQGGHSVISAISL CCCCCCEEEEEEEEC	25.15	30108239
458	Phosphorylation	QGGHSVISAISLPLV CCCEEEEEEEECEEE	19.86	30108239
461	Phosphorylation	HSVISAISLPLVDQD EEEEEEEECEEECCC	24.53	30108239
470	Phosphorylation	PLVDQDGTTKIIINY EEECCCCCEEEEEEE	32.95	27080861
471	Phosphorylation	LVDQDGTTKIIINYS EECCCCCEEEEEEEE	26.27	27080861
493	Sumoylation	QVVPQNLKKENPVAT EECCCCCCCCCCCCC	66.64	-
493	Sumoylation	QVVPQNLKKENPVAT EECCCCCCCCCCCCC	66.64	28112733
504	Sumoylation	PVATNSCKSEKLPED CCCCCCCCCCCCCCC	62.56	-
504	Sumoylation	PVATNSCKSEKLPED CCCCCCCCCCCCCCC	62.56	28112733
504	Ubiquitination	PVATNSCKSEKLPED CCCCCCCCCCCCCCC	62.56	-
507	Ubiquitination	TNSCKSEKLPEDLTV CCCCCCCCCCCCCCC	76.16	-
515	Sumoylation	LPEDLTVKSEKDKSF CCCCCCCCCCCCCCC	47.89	-
515	Sumoylation	LPEDLTVKSEKDKSF CCCCCCCCCCCCCCC	47.89	28112733
515	Ubiquitination	LPEDLTVKSEKDKSF CCCCCCCCCCCCCCC	47.89	-
516	Phosphorylation	PEDLTVKSEKDKSFE CCCCCCCCCCCCCCC	45.61	21712546
521	Phosphorylation	VKSEKDKSFEGGVND CCCCCCCCCCCCCCC	38.37	30576142
529	Phosphorylation	FEGGVNDSTCLLCDD CCCCCCCCCEEEECC	18.80	30576142
530	Phosphorylation	EGGVNDSTCLLCDDC CCCCCCCCEEEECCC	15.27	27732954
548	Sumoylation	INALPELKHYDLKQP CCCCCCCCCCCCCCC	38.16	28112733
553	Sumoylation	ELKHYDLKQPTQPPP CCCCCCCCCCCCCCC	51.86	28112733
571	Phosphorylation	AEAEKPESSVSSATG HHCCCCCCCCCCCCC	44.56	23663014
572	Phosphorylation	EAEKPESSVSSATGD HCCCCCCCCCCCCCC	25.10	23663014
574	Phosphorylation	EKPESSVSSATGDGN CCCCCCCCCCCCCCC	19.06	23663014
575	Phosphorylation	KPESSVSSATGDGNL CCCCCCCCCCCCCCC	27.91	23663014
576 (in isoform 2)	Phosphorylation	-	14.22	27251275
577	Phosphorylation	ESSVSSATGDGNLSP CCCCCCCCCCCCCCC	37.44	23663014
583	Phosphorylation	ATGDGNLSPSQPPLK CCCCCCCCCCCCCHH	26.89	25159151
585	Phosphorylation	GDGNLSPSQPPLKNL CCCCCCCCCCCHHHH	52.52	23663014
594	Phosphorylation	PPLKNLLSLLKAYYA CCHHHHHHHHHHHHH	34.52	24719451
613	Ubiquitination	PSAEELSKIADSVNL CCHHHHHHHHHHCCC	55.31	-
638	Phosphorylation	KMQAGQISVQSSEPS HHHCCCCEEECCCCC	13.25	22115753
641	Phosphorylation	AGQISVQSSEPSSPE CCCCEEECCCCCCCC	34.22	25159151
642	Phosphorylation	GQISVQSSEPSSPEP CCCEEECCCCCCCCC	36.11	25159151
642 (in isoform 2)	Phosphorylation	-	36.11	27251275
645	Phosphorylation	SVQSSEPSSPEPGKV EEECCCCCCCCCCCC	55.24	25159151
646	Phosphorylation	VQSSEPSSPEPGKVN EECCCCCCCCCCCCC	43.95	25159151
646 (in isoform 2)	Phosphorylation	-	43.95	27251275
664	Phosphorylation	KNNDQPQSANANEPQ CCCCCCCCCCCCCCC	30.12	23403867
673	Phosphorylation	NANEPQDSTVNLQSP CCCCCCCCCCCCCCC	29.07	30266825
674	Phosphorylation	ANEPQDSTVNLQSPL CCCCCCCCCCCCCCC	23.00	30266825
679	Phosphorylation	DSTVNLQSPLKMTNS CCCCCCCCCCCCCCC	35.05	25159151
680 (in isoform 2)	Phosphorylation	-	24.04	27251275
684	Phosphorylation	LQSPLKMTNSPVLPV CCCCCCCCCCCEECC	30.84	30108239
686	Phosphorylation	SPLKMTNSPVLPVGS CCCCCCCCCEECCCC	13.76	25159151
693	Phosphorylation	SPVLPVGSTTNGSRS CCEECCCCCCCCCCC	32.09	30576142
694	Phosphorylation	PVLPVGSTTNGSRSS CEECCCCCCCCCCCC	20.53	19690332
695	Phosphorylation	VLPVGSTTNGSRSST EECCCCCCCCCCCCC	39.00	19690332
698	Phosphorylation	VGSTTNGSRSSTPSP CCCCCCCCCCCCCCC	30.93	30576142
699 (in isoform 2)	Phosphorylation	-	35.70	27251275
700	Phosphorylation	STTNGSRSSTPSPSP CCCCCCCCCCCCCCC	40.02	25159151
701	Phosphorylation	TTNGSRSSTPSPSPL CCCCCCCCCCCCCCC	43.13	25159151
702	Phosphorylation	TNGSRSSTPSPSPLN CCCCCCCCCCCCCCC	29.09	25159151
704	Phosphorylation	GSRSSTPSPSPLNLS CCCCCCCCCCCCCCC	37.79	25159151
706	Phosphorylation	RSSTPSPSPLNLSSS CCCCCCCCCCCCCCC	46.48	22617229
711	Phosphorylation	SPSPLNLSSSRNTQG CCCCCCCCCCCCCCC	25.79	30576142
712	Phosphorylation	PSPLNLSSSRNTQGY CCCCCCCCCCCCCCE	36.16	30576142
713	Phosphorylation	SPLNLSSSRNTQGYL CCCCCCCCCCCCCEE	26.61	26074081
716	Phosphorylation	NLSSSRNTQGYLYTA CCCCCCCCCCEEEEC	23.43	-
774	Sumoylation	PLNLSCAKKEPQKDS CCCCCCCCCCCCCCC	63.09	-
774	Sumoylation	PLNLSCAKKEPQKDS CCCCCCCCCCCCCCC	63.09	28112733
848	Phosphorylation	VAYTYSTTVSPAVQE EEEEEECCCCHHHCC	17.04	27690223
850	Phosphorylation	YTYSTTVSPAVQEPP EEEECCCCHHHCCCC	12.68	27690223
873	Phosphorylation	NQDERQDTSSEGVSN CCCCCCCCCCCCCCC	26.30	30576142
874	Phosphorylation	QDERQDTSSEGVSNV CCCCCCCCCCCCCCC	34.38	30177828
875	Phosphorylation	DERQDTSSEGVSNVE CCCCCCCCCCCCCCC	40.23	30177828
879	Phosphorylation	DTSSEGVSNVEDQND CCCCCCCCCCCCCCC	46.12	30177828
887	Phosphorylation	NVEDQNDSDSTPPKK CCCCCCCCCCCCCCH	40.80	26657352
889	Phosphorylation	EDQNDSDSTPPKKKM CCCCCCCCCCCCHHH	46.92	20873877
890	Phosphorylation	DQNDSDSTPPKKKMR CCCCCCCCCCCHHHC	48.91	28985074
890 (in isoform 2)	Phosphorylation	-	48.91	27251275
917	Phosphorylation	DKIFQKSSSLLRHKY HHHHHHCHHHHHHHC	31.85	24719451
918	Phosphorylation	KIFQKSSSLLRHKYE HHHHHCHHHHHHHCC	38.21	24719451
918 (in isoform 2)	Phosphorylation	-	38.21	24719451
927	Phosphorylation	LRHKYEHTGKRPHEC HHHHCCCCCCCCHHC	32.24	-
955	Phosphorylation	IEHMRLHSGEKPYQC HHHHHCCCCCCCCCC	53.92	26055452
960	Phosphorylation	LHSGEKPYQCDKCGK CCCCCCCCCCCCCCC	32.61	27732954
970	Phosphorylation	DKCGKRFSHSGSYSQ CCCCCCCCCCCCCHH	22.30	25262027
972	Phosphorylation	CGKRFSHSGSYSQHM CCCCCCCCCCCHHHH	28.39	25262027
974	Phosphorylation	KRFSHSGSYSQHMNH CCCCCCCCCHHHHCH	25.32	25262027
975	Phosphorylation	RFSHSGSYSQHMNHR CCCCCCCCHHHHCHH	18.84	25262027
976	Phosphorylation	FSHSGSYSQHMNHRY CCCCCCCHHHHCHHH	18.46	25262027
995	Phosphorylation	REAEERDSTEQEEAG HHHHHCCCHHHHHHC	39.81	30266825
996	Phosphorylation	EAEERDSTEQEEAGP HHHHCCCHHHHHHCH	46.08	30266825
1007	Phosphorylation	EAGPEILSNEHVGAR HHCHHHHCCCCCCCC	45.92	26074081
1016	Phosphorylation	EHVGARASPSQGDSD CCCCCCCCCCCCCCH	21.38	23663014
1018	Phosphorylation	VGARASPSQGDSDER CCCCCCCCCCCCHHH	44.28	20873877
1022	Phosphorylation	ASPSQGDSDERESLT CCCCCCCCHHHHHCC	48.47	23663014
1027	Phosphorylation	GDSDERESLTREEDE CCCHHHHHCCCCCCC	41.06	23663014
1029	Phosphorylation	SDERESLTREEDEDS CHHHHHCCCCCCCCH	45.36	27732954
1036	Phosphorylation	TREEDEDSEKEEEEE CCCCCCCHHHHHHHH	48.82	28985074
1100	Phosphorylation	MKDDRAESQASSLGQ CCCHHHHHHHHHHHH	30.02	25159151
1103	Phosphorylation	DRAESQASSLGQKVG HHHHHHHHHHHHHHC	20.61	29978859
1104	Phosphorylation	RAESQASSLGQKVGE HHHHHHHHHHHHHCC	39.26	28387310
1108	Acetylation	QASSLGQKVGESSEQ HHHHHHHHHCCCHHH	50.86	26051181
1108	Ubiquitination	QASSLGQKVGESSEQ HHHHHHHHHCCCHHH	50.86	-
1112	Phosphorylation	LGQKVGESSEQVSEE HHHHHCCCHHHHCHH	32.99	29978859
1113	Phosphorylation	GQKVGESSEQVSEEK HHHHCCCHHHHCHHH	27.96	29978859
1117	Phosphorylation	GESSEQVSEEKTNEA CCCHHHHCHHHHCCC	39.47	29978859

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
585	S	Phosphorylation	Kinase	ATM	Q13315	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO45	P0C2W1	PMID:25460509
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:25528765
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:25528765

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZEB1_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 ZEB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NC2A_HUMAN	DRAP1	physical	9418848
KAT5_HUMAN	KAT5	physical	11275565
SMAD2_HUMAN	SMAD2	physical	12743038
SMAD3_HUMAN	SMAD3	physical	12743038
SMAD1_HUMAN	SMAD1	physical	12743038
SMCA4_HUMAN	SMARCA4	physical	20418909
SMAD6_HUMAN	SMAD6	physical	20514018
SMAD7_HUMAN	SMAD7	physical	20514018
CTBP1_HUMAN	CTBP1	physical	10567582
CTBP2_HUMAN	CTBP2	physical	10567582
EP300_HUMAN	EP300	physical	12743039
CTBP2_HUMAN	CTBP2	physical	25086746
CTBP1_HUMAN	CTBP1	physical	25086746
SIR1_HUMAN	SIRT1	physical	25086746
UBP7_HUMAN	USP7	physical	25086746
CHK1_HUMAN	CHEK1	physical	25086746
ATM_HUMAN	ATM	physical	25086746
MPP8_HUMAN	MPHOSPH8	physical	25870236
SIR1_HUMAN	SIRT1	physical	25870236
UBP7_HUMAN	USP7	physical	29119051
UBP10_HUMAN	USP10	physical	29119051
UBP13_HUMAN	USP13	physical	29119051
UBP26_HUMAN	USP26	physical	29119051
UBP29_HUMAN	USP29	physical	29119051
UBP51_HUMAN	USP51	physical	29119051
PAN2_HUMAN	PAN2	physical	29119051
UBP53_HUMAN	USP53	physical	29119051
UCHL3_HUMAN	UCHL3	physical	29119051
VCIP1_HUMAN	VCPIP1	physical	29119051

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609141	Corneal dystrophy, posterior polymorphous, 3 (PPCD3)
613270	Corneal dystrophy, Fuchs endothelial, 6 (FECD6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ZEB1_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-642; SER-679 ANDTHR-702, AND MASS SPECTROMETRY.	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-583; SER-646; THR-702AND SER-704, 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-322 AND SER-646, ANDMASS SPECTROMETRY.	18669648 [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-31 AND SER-33, 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-679, AND MASSSPECTROMETRY.	15302935 [Abstract]
Sumoylation
Reference	PubMed
"Pc2-mediated sumoylation of Smad-interacting protein 1 attenuatestranscriptional repression of E-cadherin."; Long J., Zuo D., Park M.; J. Biol. Chem. 280:35477-35489(2005). Cited for: SUMOYLATION AT LYS-347 AND LYS-774.	16061479 [Abstract]