dbPTM

CBX5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBX5_HUMAN
UniProt AC	P45973
Protein Name	Chromobox protein homolog 5
Gene Name	CBX5
Organism	Homo sapiens (Human).
Sequence Length	191
Subcellular Localization	Nucleus . Chromosome . Chromosome, centromere . Colocalizes with HNRNPU in the nucleus (PubMed:19617346). Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin
Protein Description	Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins..
Protein Sequence	MGKKTKRTADSSSSEDEEEYVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSESNKRKSNFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKETAKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MGKKTKRTADSS ---CCCCCCCCCCCC	29.28	25072903
8	Phosphorylation	MGKKTKRTADSSSSE CCCCCCCCCCCCCCC	36.05	22167270
11	Phosphorylation	KTKRTADSSSSEDEE CCCCCCCCCCCCCHH	29.65	22167270
12	Phosphorylation	TKRTADSSSSEDEEE CCCCCCCCCCCCHHH	38.13	22167270
13	Phosphorylation	KRTADSSSSEDEEEY CCCCCCCCCCCHHHH	41.52	22167270
14	Phosphorylation	RTADSSSSEDEEEYV CCCCCCCCCCHHHHH	51.52	22167270
20	Phosphorylation	SSEDEEEYVVEKVLD CCCCHHHHHHHHHHH	17.05	22167270
32	Malonylation	VLDRRVVKGQVEYLL HHHHHHHHHHHHHHH	40.54	26320211
32	Methylation	VLDRRVVKGQVEYLL HHHHHHHHHHHHHHH	40.54	-
32	Ubiquitination	VLDRRVVKGQVEYLL HHHHHHHHHHHHHHH	40.54	21890473
32	Sumoylation	VLDRRVVKGQVEYLL HHHHHHHHHHHHHHH	40.54	-
32	Sumoylation	VLDRRVVKGQVEYLL HHHHHHHHHHHHHHH	40.54	28112733
32	2-Hydroxyisobutyrylation	VLDRRVVKGQVEYLL HHHHHHHHHHHHHHH	40.54	-
37	Phosphorylation	VVKGQVEYLLKWKGF HHHHHHHHHHHCCCC	20.62	29759185
40	Acetylation	GQVEYLLKWKGFSEE HHHHHHHHCCCCCCH	44.24	26051181
40	Ubiquitination	GQVEYLLKWKGFSEE HHHHHHHHCCCCCCH	44.24	21890473
40	Methylation	GQVEYLLKWKGFSEE HHHHHHHHCCCCCCH	44.24	-
42	Ubiquitination	VEYLLKWKGFSEEHN HHHHHHCCCCCCHHC	48.79	-
42	Acetylation	VEYLLKWKGFSEEHN HHHHHHCCCCCCHHC	48.79	26051181
45	Phosphorylation	LLKWKGFSEEHNTWE HHHCCCCCCHHCCCC	51.23	25159151
55	Ubiquitination	HNTWEPEKNLDCPEL HCCCCCCCCCCHHHH	73.80	-
55	Acetylation	HNTWEPEKNLDCPEL HCCCCCCCCCCHHHH	73.80	26051181
59	Glutathionylation	EPEKNLDCPELISEF CCCCCCCHHHHHHHH	2.96	22555962
68	Acetylation	ELISEFMKKYKKMKE HHHHHHHHHHHHHHC	59.27	25953088
68	Ubiquitination	ELISEFMKKYKKMKE HHHHHHHHHHHHHHC	59.27	-
69	Ubiquitination	LISEFMKKYKKMKEG HHHHHHHHHHHHHCC	50.98	-
69	Sumoylation	LISEFMKKYKKMKEG HHHHHHHHHHHHHCC	50.98	-
71	Sumoylation	SEFMKKYKKMKEGEN HHHHHHHHHHHCCCC	56.10	-
74	2-Hydroxyisobutyrylation	MKKYKKMKEGENNKP HHHHHHHHCCCCCCC	72.02	-
80	Acetylation	MKEGENNKPREKSES HHCCCCCCCCCHHHH	57.97	26051181
80	Ubiquitination	MKEGENNKPREKSES HHCCCCCCCCCHHHH	57.97	-
84	Sumoylation	ENNKPREKSESNKRK CCCCCCCHHHHHHHH	61.88	-
85	Phosphorylation	NNKPREKSESNKRKS CCCCCCHHHHHHHHH	41.31	29214152
91	Methylation	KSESNKRKSNFSNSA HHHHHHHHHCCCCCH	51.89	-
91	Sumoylation	KSESNKRKSNFSNSA HHHHHHHHHCCCCCH	51.89	28112733
91	Ubiquitination	KSESNKRKSNFSNSA HHHHHHHHHCCCCCH	51.89	21906983
91	Acetylation	KSESNKRKSNFSNSA HHHHHHHHHCCCCCH	51.89	26051181
92	Phosphorylation	SESNKRKSNFSNSAD HHHHHHHHCCCCCHH	47.33	29255136
95	Phosphorylation	NKRKSNFSNSADDIK HHHHHCCCCCHHHHH	33.84	30266825
97	Phosphorylation	RKSNFSNSADDIKSK HHHCCCCCHHHHHHH	31.70	23927012
102	Acetylation	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	25953088
102	Sumoylation	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	28112733
102	2-Hydroxyisobutyrylation	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	-
102	Ubiquitination	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	21906983
102	Sumoylation	SNSADDIKSKKKREQ CCCHHHHHHHHHHHH	64.32	-
103	Phosphorylation	NSADDIKSKKKREQS CCHHHHHHHHHHHHH	50.47	30622161
104	Sumoylation	SADDIKSKKKREQSN CHHHHHHHHHHHHHH	58.26	-
104	Ubiquitination	SADDIKSKKKREQSN CHHHHHHHHHHHHHH	58.26	-
105	Ubiquitination	ADDIKSKKKREQSND HHHHHHHHHHHHHHH	65.24	-
106	Acetylation	DDIKSKKKREQSNDI HHHHHHHHHHHHHHH	65.97	17074863
106	Sumoylation	DDIKSKKKREQSNDI HHHHHHHHHHHHHHH	65.97	28112733
106	Ubiquitination	DDIKSKKKREQSNDI HHHHHHHHHHHHHHH	65.97	-
110	Phosphorylation	SKKKREQSNDIARGF HHHHHHHHHHHHHHH	31.55	25159151
115	Methylation	EQSNDIARGFERGLE HHHHHHHHHHHHCCC	51.14	115479653
119	Methylation	DIARGFERGLEPEKI HHHHHHHHCCCHHHE	53.38	115479645
125	Ubiquitination	ERGLEPEKIIGATDS HHCCCHHHEEEECCC	50.79	-
130	Phosphorylation	PEKIIGATDSCGDLM HHHEEEECCCCCCEE	24.19	30108239
132	Phosphorylation	KIIGATDSCGDLMFL HEEEECCCCCCEEEE	18.69	28102081
133	Glutathionylation	IIGATDSCGDLMFLM EEEECCCCCCEEEEE	5.67	22555962
143	Acetylation	LMFLMKWKDTDEADL EEEEEECCCCCHHHE	45.27	26051181
143	Ubiquitination	LMFLMKWKDTDEADL EEEEEECCCCCHHHE	45.27	21890473
143	Methylation	LMFLMKWKDTDEADL EEEEEECCCCCHHHE	45.27	-
154	Methylation	EADLVLAKEANVKCP HHHEEEEHHHCCCCC	53.88	-
154	Acetylation	EADLVLAKEANVKCP HHHEEEEHHHCCCCC	53.88	25953088
154	Sumoylation	EADLVLAKEANVKCP HHHEEEEHHHCCCCC	53.88	28112733
154	"N6,N6-dimethyllysine"	EADLVLAKEANVKCP HHHEEEEHHHCCCCC	53.88	-
154	Ubiquitination	EADLVLAKEANVKCP HHHEEEEHHHCCCCC	53.88	21890473
159	Ubiquitination	LAKEANVKCPQIVIA EEHHHCCCCCEEEEE	39.75	-
168	Phosphorylation	PQIVIAFYEERLTWH CEEEEEEEHHHHCCC	14.09	28152594
177	Phosphorylation	ERLTWHAYPEDAENK HHHCCCCCHHHHHHH	8.35	-
184	Ubiquitination	YPEDAENKEKETAKS CHHHHHHHHHHHHCC	62.76	2190698
184	Acetylation	YPEDAENKEKETAKS CHHHHHHHHHHHHCC	62.76	26051181
184	Sumoylation	YPEDAENKEKETAKS CHHHHHHHHHHHHCC	62.76	28112733
186	Ubiquitination	EDAENKEKETAKS-- HHHHHHHHHHHCC--	63.07	-
188	Phosphorylation	AENKEKETAKS---- HHHHHHHHHCC----	50.91	24732914
191	Phosphorylation	KEKETAKS------- HHHHHHCC-------	42.88	24732914

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
92	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW10	Q5XX13	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	RNF123	Q5XPI4	PMID:23077635

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CBX5_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 CBX5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	11112778
SUV91_HUMAN	SUV39H1	physical	12711603
LBR_HUMAN	LBR	physical	8663349
PRR14_HUMAN	PRR14	physical	16189514
ELOA2_HUMAN	TCEB3B	physical	16189514
DNM3B_HUMAN	DNMT3B	physical	12867029
CAF1A_HUMAN	CHAF1A	physical	12697822
MBD1_HUMAN	MBD1	physical	12697822
SMCA4_HUMAN	SMARCA4	physical	12411497
TIF1B_HUMAN	TRIM28	physical	12411497
RB_HUMAN	RB1	physical	11484059
TAF4_HUMAN	TAF4	physical	11959914
TBP_HUMAN	TBP	physical	11959914
TIF1B_HUMAN	TRIM28	physical	12154074
TIF1B_HUMAN	TRIM28	physical	11336697
CBX1_HUMAN	CBX1	physical	11336697
CBX3_HUMAN	CBX3	physical	11336697
CBX5_HUMAN	CBX5	physical	11336697
H2A3_HUMAN	HIST3H2A	physical	11336697
H2B3B_HUMAN	HIST3H2BB	physical	11336697
ARL5A_HUMAN	ARL5A	physical	12414990
MECP2_HUMAN	MECP2	physical	17698499
ATRX_HUMAN	ATRX	physical	20110566
PAX3_MOUSE	Pax3	physical	16945326
SETB1_HUMAN	SETDB1	physical	19498464
H31_HUMAN	HIST1H3A	physical	16687578
PARP2_HUMAN	PARP2	physical	18676401
VIGLN_HUMAN	HDLBP	physical	18648073
TIF1B_HUMAN	TRIM28	physical	15882967
SP100_HUMAN	SP100	physical	15882967
LBR_HUMAN	LBR	physical	15882967
CAF1B_HUMAN	CHAF1B	physical	15882967
NIPBL_HUMAN	NIPBL	physical	15882967
CHD4_HUMAN	CHD4	physical	15882967
SMCA4_HUMAN	SMARCA4	physical	15882967
CAF1A_HUMAN	CHAF1A	physical	15882967
RBBP4_HUMAN	RBBP4	physical	15882967
BC11B_HUMAN	BCL11B	physical	15849318
RB_HUMAN	RB1	physical	15485920
ATRX_HUMAN	ATRX	physical	10699177
DNM3B_HUMAN	DNMT3B	physical	15120635
TIF1B_HUMAN	TRIM28	physical	10330177
CBX1_HUMAN	CBX1	physical	17314413
CBX3_HUMAN	CBX3	physical	17314413
CAF1A_HUMAN	CHAF1A	physical	15306854
CAF1B_HUMAN	CHAF1B	physical	15306854
RBBP4_HUMAN	RBBP4	physical	15306854
CBX3_HUMAN	CBX3	physical	15306854
H31T_HUMAN	HIST3H3	physical	15306854
TCP4_HUMAN	SUB1	physical	20080105
H33_BOVIN	H3F3A	physical	20011120
H31_HUMAN	HIST1H3A	physical	20011120
SMCA2_HUMAN	SMARCA2	physical	20011120
SMCA4_HUMAN	SMARCA4	physical	20011120
LRIF1_HUMAN	LRIF1	physical	21900206
GDIR1_HUMAN	ARHGDIA	physical	21900206
MIS12_HUMAN	MIS12	physical	20231385
DSN1_HUMAN	DSN1	physical	20231385
CBX3_HUMAN	CBX3	physical	20231385
AURKB_HUMAN	AURKB	physical	20231385
NSL1_HUMAN	NSL1	physical	20231385
H31_HUMAN	HIST1H3A	physical	19783980
DNMT1_HUMAN	DNMT1	physical	17470536
DNM3A_HUMAN	DNMT3A	physical	17470536
DNM3B_HUMAN	DNMT3B	physical	17470536
H15_HUMAN	HIST1H1B	physical	16762841
TIF1B_HUMAN	TRIM28	physical	21888893
ADNP_HUMAN	ADNP	physical	21888893
ADNP2_HUMAN	ADNP2	physical	21888893
TIF1B_HUMAN	TRIM28	physical	22496453
KLF11_HUMAN	KLF11	physical	22318730
TIF1B_HUMAN	TRIM28	physical	22205726
H2AY_HUMAN	H2AFY	physical	22939629
H2AW_HUMAN	H2AFY2	physical	22939629
TIF1B_HUMAN	TRIM28	physical	20562864
CBX3_HUMAN	CBX3	physical	20562864
NIPBL_HUMAN	NIPBL	physical	20562864
POGZ_HUMAN	POGZ	physical	20562864
SMCA4_HUMAN	SMARCA4	physical	20562864
ZN462_HUMAN	ZNF462	physical	20562864
CAF1A_HUMAN	CHAF1A	physical	20562864
CHAP1_HUMAN	CHAMP1	physical	20562864
CAF1B_HUMAN	CHAF1B	physical	20562864
DSN1_HUMAN	DSN1	physical	20562864
IMA1_HUMAN	KPNA2	physical	20562864
SGO1_HUMAN	SGOL1	physical	20562864
EHMT2_HUMAN	EHMT2	physical	20562864
EHMT1_HUMAN	EHMT1	physical	20562864
IMA4_HUMAN	KPNA3	physical	20562864
LRIF1_HUMAN	LRIF1	physical	20562864
SUV92_HUMAN	SUV39H2	physical	20562864
RBBP4_HUMAN	RBBP4	physical	20562864
ADNP_HUMAN	ADNP	physical	20562864
SMCA2_HUMAN	SMARCA2	physical	20562864
IMA3_HUMAN	KPNA4	physical	20562864
RL26_HUMAN	RPL26	physical	20562864
SENP7_HUMAN	SENP7	physical	20562864
ZN829_HUMAN	ZNF829	physical	20562864
ACL6A_HUMAN	ACTL6A	physical	20562864
WIZ_HUMAN	WIZ	physical	20562864
SUV91_HUMAN	SUV39H1	physical	20562864
ZN483_HUMAN	ZNF483	physical	20562864
CBX1_HUMAN	CBX1	physical	20562864
ZNF8_HUMAN	ZNF8	physical	20562864
ZMYM3_HUMAN	ZMYM3	physical	20562864
NSL1_HUMAN	NSL1	physical	20562864
Z280D_HUMAN	ZNF280D	physical	20562864
AHDC1_HUMAN	AHDC1	physical	20562864
Z324A_HUMAN	ZNF324	physical	20562864
ZN302_HUMAN	ZNF302	physical	20562864
IPO8_HUMAN	IPO8	physical	20562864
ZN747_HUMAN	ZNF747	physical	20562864
ZFP1_HUMAN	ZFP1	physical	20562864
PP2AB_HUMAN	PPP2CB	physical	20562864
AURKB_HUMAN	AURKB	physical	20562864
RBBP7_HUMAN	RBBP7	physical	20562864
BOREA_HUMAN	CDCA8	physical	20562864
MIS12_HUMAN	MIS12	physical	20562864
SCAI_HUMAN	SCAI	physical	20562864
INCE_HUMAN	INCENP	physical	20562864
PRR14_HUMAN	PRR14	physical	20562864
PP2AA_HUMAN	PPP2CA	physical	20562864
ZN568_HUMAN	ZNF568	physical	20562864
ZN764_HUMAN	ZNF764	physical	20562864
ZN460_HUMAN	ZNF460	physical	20562864
ZN625_HUMAN	ZNF625	physical	20562864
SCC4_HUMAN	MAU2	physical	20562864
ZN773_HUMAN	ZNF773	physical	20562864
OSTCN_HUMAN	BGLAP	physical	20562864
NARF_HUMAN	NARF	physical	20562864
MA7D3_HUMAN	MAP7D3	physical	20562864
TIM50_HUMAN	TIMM50	physical	20562864
2A5A_HUMAN	PPP2R5A	physical	20562864
ZN689_HUMAN	ZNF689	physical	20562864
ZN566_HUMAN	ZNF566	physical	20562864
ZN569_HUMAN	ZNF569	physical	20562864
ZN227_HUMAN	ZNF227	physical	20562864
ZN264_HUMAN	ZNF264	physical	20562864
Z324B_HUMAN	ZNF324B	physical	20562864
2A5E_HUMAN	PPP2R5E	physical	20562864
SUZ12_HUMAN	SUZ12	physical	20562864
Z585B_HUMAN	ZNF585B	physical	20562864
Z585A_HUMAN	ZNF585A	physical	20562864
ZN620_HUMAN	ZNF620	physical	20562864
ZN688_HUMAN	ZNF688	physical	20562864
ZFP82_HUMAN	ZFP82	physical	20562864
ZN552_HUMAN	ZNF552	physical	20562864
RL5_HUMAN	RPL5	physical	20562864
ZN274_HUMAN	ZNF274	physical	20562864
ZNF45_HUMAN	ZNF45	physical	20562864
ZN195_HUMAN	ZNF195	physical	20562864
BCL7A_HUMAN	BCL7A	physical	20562864
ZN649_HUMAN	ZNF649	physical	20562864
Z518A_HUMAN	ZNF518A	physical	20562864
H31T_HUMAN	HIST3H3	physical	23281010
CRCM_HUMAN	MCC	physical	21988832
ELOC_HUMAN	TCEB1	physical	21988832
TIF1B_HUMAN	TRIM28	physical	23645696
H31T_HUMAN	HIST3H3	physical	23645696
TIF1B_HUMAN	TRIM28	physical	24018422
SENP7_HUMAN	SENP7	physical	24018422
VPS28_HUMAN	VPS28	physical	25416956
NSD3_HUMAN	WHSC1L1	physical	25416956
SUV92_HUMAN	SUV39H2	physical	25416956
UBE2A_HUMAN	UBE2A	physical	25384975
UBE2B_HUMAN	UBE2B	physical	25384975
POGZ_HUMAN	POGZ	physical	20850016
AHDC1_HUMAN	AHDC1	physical	20850016
CBX3_HUMAN	CBX3	physical	20850016
NUCL_HUMAN	NCL	physical	20850016
CAF1B_HUMAN	CHAF1B	physical	20850016
CHAP1_HUMAN	CHAMP1	physical	20850016
H31T_HUMAN	HIST3H3	physical	18404153
NSD3_HUMAN	WHSC1L1	physical	21516116
SP100_HUMAN	SP100	physical	21516116
RRP1B_HUMAN	RRP1B	physical	25092915
STA5A_HUMAN	STAT5A	physical	23733954

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 CBX5_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-11; SER-12; SER-14;SER-92 AND SER-97, AND MASS SPECTROMETRY.	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-11; SER-12; SER-13;SER-14 AND SER-92, 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-92, 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-92 AND SER-97, AND MASSSPECTROMETRY.	19007248 [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-8; SER-11; SER-13;SER-14; SER-92 AND SER-110, AND MASS SPECTROMETRY.	17287340 [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-92, AND MASSSPECTROMETRY.	17924679 [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-11; SER-12; SER-13 ANDSER-14, AND MASS SPECTROMETRY.	17081983 [Abstract]