dbPTM

CDC37_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDC37_HUMAN
UniProt AC	Q16543
Protein Name	Hsp90 co-chaperone Cdc37
Gene Name	CDC37
Organism	Homo sapiens (Human).
Sequence Length	378
Subcellular Localization	Cytoplasm .
Protein Description	Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. [PubMed: 8666233 Inhibits HSP90AA1 ATPase activity]
Protein Sequence	MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MVDYSVWD -------CCCCCCCC	4.70	19413330
2	Acetylation	------MVDYSVWDH ------CCCCCCCCC	10.73	19413330
4	Phosphorylation	----MVDYSVWDHIE ----CCCCCCCCCCC	8.16	23663014
5	Phosphorylation	---MVDYSVWDHIEV ---CCCCCCCCCCCC	16.56	22115753
13	Phosphorylation	VWDHIEVSDDEDETH CCCCCCCCCCCCCCC	26.93	30266825
19	Phosphorylation	VSDDEDETHPNIDTA CCCCCCCCCCCCCHH	55.76	23663014
25	Phosphorylation	ETHPNIDTASLFRWR CCCCCCCHHHHHHHH	17.85	30266825
27	Phosphorylation	HPNIDTASLFRWRHQ CCCCCHHHHHHHHHH	30.08	28450419
45	Acetylation	ERMEQFQKEKEELDR HHHHHHHHHHHHHHH	72.54	19608861
60	Acetylation	GCRECKRKVAECQRK HHHHHHHHHHHHHHH	31.15	26051181
67	Ubiquitination	KVAECQRKLKELEVA HHHHHHHHHHHHHHH	37.72	-
69	Malonylation	AECQRKLKELEVAEG HHHHHHHHHHHHHHC	64.39	26320211
69	Acetylation	AECQRKLKELEVAEG HHHHHHHHHHHHHHC	64.39	26051181
69	2-Hydroxyisobutyrylation	AECQRKLKELEVAEG HHHHHHHHHHHHHHC	64.39	-
69	Ubiquitination	AECQRKLKELEVAEG HHHHHHHHHHHHHHC	64.39	-
78	Acetylation	LEVAEGGKAELERLQ HHHHHCCHHHHHHHH	49.93	19608861
93	Ubiquitination	AEAQQLRKEERSWEQ HHHHHHHHHHHHHHH	72.95	-
97	Phosphorylation	QLRKEERSWEQKLEE HHHHHHHHHHHHHHH	37.94	26714015
101	Acetylation	EERSWEQKLEEMRKK HHHHHHHHHHHHHHH	46.48	26822725
101	Malonylation	EERSWEQKLEEMRKK HHHHHHHHHHHHHHH	46.48	26320211
101	Ubiquitination	EERSWEQKLEEMRKK HHHHHHHHHHHHHHH	46.48	21890473
110	Acetylation	EEMRKKEKSMPWNVD HHHHHHHHCCCCCHH	62.02	25953088
110	2-Hydroxyisobutyrylation	EEMRKKEKSMPWNVD HHHHHHHHCCCCCHH	62.02	-
110	Ubiquitination	EEMRKKEKSMPWNVD HHHHHHHHCCCCCHH	62.02	21890473
111	Phosphorylation	EMRKKEKSMPWNVDT HHHHHHHCCCCCHHH	31.04	28857561
112	Sulfoxidation	MRKKEKSMPWNVDTL HHHHHHCCCCCHHHC	7.07	30846556
118	Phosphorylation	SMPWNVDTLSKDGFS CCCCCHHHCCCCCCC	28.75	28348404
120	Phosphorylation	PWNVDTLSKDGFSKS CCCHHHCCCCCCCHH	30.69	25159151
121	Acetylation	WNVDTLSKDGFSKSM CCHHHCCCCCCCHHH	66.05	26822725
121	Ubiquitination	WNVDTLSKDGFSKSM CCHHHCCCCCCCHHH	66.05	21890473
125	Phosphorylation	TLSKDGFSKSMVNTK HCCCCCCCHHHCCCC	29.38	23186163
126	Ubiquitination	LSKDGFSKSMVNTKP CCCCCCCHHHCCCCC	40.07	-
126	Acetylation	LSKDGFSKSMVNTKP CCCCCCCHHHCCCCC	40.07	25953088
127	Phosphorylation	SKDGFSKSMVNTKPE CCCCCCHHHCCCCCC	27.11	25849741
128	Sulfoxidation	KDGFSKSMVNTKPEK CCCCCHHHCCCCCCC	2.87	30846556
131	Phosphorylation	FSKSMVNTKPEKTEE CCHHHCCCCCCCCCC	36.24	24043423
132	Sumoylation	SKSMVNTKPEKTEED CHHHCCCCCCCCCCC	46.07	-
132	Sumoylation	SKSMVNTKPEKTEED CHHHCCCCCCCCCCC	46.07	-
132	Acetylation	SKSMVNTKPEKTEED CHHHCCCCCCCCCCC	46.07	25953088
135	Ubiquitination	MVNTKPEKTEEDSEE HCCCCCCCCCCCHHH	70.53	21890473
136	Phosphorylation	VNTKPEKTEEDSEEV CCCCCCCCCCCHHHH	42.83	23312004
140	Phosphorylation	PEKTEEDSEEVREQK CCCCCCCHHHHHHHH	38.65	25849741
149	2-Hydroxyisobutyrylation	EVREQKHKTFVEKYE HHHHHHHHHHHHHHH	51.17	-
154	Malonylation	KHKTFVEKYEKQIKH HHHHHHHHHHHHHHH	54.10	26320211
154	2-Hydroxyisobutyrylation	KHKTFVEKYEKQIKH HHHHHHHHHHHHHHH	54.10	-
154	Acetylation	KHKTFVEKYEKQIKH HHHHHHHHHHHHHHH	54.10	19608861
155	Phosphorylation	HKTFVEKYEKQIKHF HHHHHHHHHHHHHHH	18.17	28152594
157	Acetylation	TFVEKYEKQIKHFGM HHHHHHHHHHHHHCC	54.99	23749302
157	Ubiquitination	TFVEKYEKQIKHFGM HHHHHHHHHHHHHCC	54.99	-
227	Acetylation	LELAKSLKVDPRACF HHHHHHCCCCHHHHH	52.24	25953088
240	Acetylation	CFRQFFTKIKTADRQ HHHHHHHHHHHHCHH	36.73	19608861
246	Methylation	TKIKTADRQYMEGFN HHHHHHCHHHHCCCH	27.37	-
249	Sulfoxidation	KTADRQYMEGFNDEL HHHCHHHHCCCHHHH	2.84	28465586
260	Acetylation	NDELEAFKERVRGRA HHHHHHHHHHHHHHH	52.22	27452117
260	Ubiquitination	NDELEAFKERVRGRA HHHHHHHHHHHHHHH	52.22	21890473
273	Acetylation	RAKLRIEKAMKEYEE HHHHHHHHHHHHHHH	51.95	25953088
278	Phosphorylation	IEKAMKEYEEEERKK HHHHHHHHHHHHHHH	24.11	28796482
298	Phosphorylation	GLDPVEVYESLPEEL CCCHHHHHHHCHHHH	6.06	28796482
300	Phosphorylation	DPVEVYESLPEELQK CHHHHHHHCHHHHHH	31.38	25849741
307	Ubiquitination	SLPEELQKCFDVKDV HCHHHHHHCCCHHHH	49.87	-
308	S-nitrosylation	LPEELQKCFDVKDVQ CHHHHHHCCCHHHHH	1.96	19483679
308	Glutathionylation	LPEELQKCFDVKDVQ CHHHHHHCCCHHHHH	1.96	22555962
308	S-nitrosocysteine	LPEELQKCFDVKDVQ CHHHHHHCCCHHHHH	1.96	-
312	Acetylation	LQKCFDVKDVQMLQD HHHCCCHHHHHHHHH	54.77	26051181
312	Ubiquitination	LQKCFDVKDVQMLQD HHHCCCHHHHHHHHH	54.77	-
316	Sulfoxidation	FDVKDVQMLQDAISK CCHHHHHHHHHHHHC	3.49	21406390
322	Phosphorylation	QMLQDAISKMDPTDA HHHHHHHHCCCHHHH	24.53	23911959
323	Ubiquitination	MLQDAISKMDPTDAK HHHHHHHCCCHHHHH	41.01	21890473
323	2-Hydroxyisobutyrylation	MLQDAISKMDPTDAK HHHHHHHCCCHHHHH	41.01	-
330	Acetylation	KMDPTDAKYHMQRCI CCCHHHHHHHHHHHH	38.20	23749302
330	2-Hydroxyisobutyrylation	KMDPTDAKYHMQRCI CCCHHHHHHHHHHHH	38.20	-
330	Ubiquitination	KMDPTDAKYHMQRCI CCCHHHHHHHHHHHH	38.20	21906983
336	Glutathionylation	AKYHMQRCIDSGLWV HHHHHHHHHHCCCCC	1.97	22555962
336	S-nitrosylation	AKYHMQRCIDSGLWV HHHHHHHHHHCCCCC	1.97	19483679
336	S-nitrosocysteine	AKYHMQRCIDSGLWV HHHHHHHHHHCCCCC	1.97	-
339	Phosphorylation	HMQRCIDSGLWVPNS HHHHHHHCCCCCCCC	18.84	-
346	Phosphorylation	SGLWVPNSKASEAKE CCCCCCCCCHHHCCC	24.43	27251275
347	Ubiquitination	GLWVPNSKASEAKEG CCCCCCCCHHHCCCC	63.67	-
352	Ubiquitination	NSKASEAKEGEEAGP CCCHHHCCCCCCCCC	63.30	21890473
369	Ubiquitination	PLLEAVPKTGDEKDV CHHHCCCCCCCCCCC	59.55	-
370	Phosphorylation	LLEAVPKTGDEKDVS HHHCCCCCCCCCCCC	43.74	23917254
374	Ubiquitination	VPKTGDEKDVSV--- CCCCCCCCCCCC---	69.07	21890473
377	Phosphorylation	TGDEKDVSV------ CCCCCCCCC------	32.04	23401153

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
4	Y	Phosphorylation	Kinase	YES	P07947	PSP
13	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
13	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
13	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
13	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
97	S	Phosphorylation	Kinase	PKACA	P17612	PSP
298	Y	Phosphorylation	Kinase	YES1	P07947	GPS
339	S	Phosphorylation	Kinase	ULK1	O75385	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CDC37_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 CDC37_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	11085988
SRC_HUMAN	SRC	physical	11085988
CDK4_HUMAN	CDK4	physical	8703009
HS90A_HUMAN	HSP90AA1	physical	9685350
CDK4_HUMAN	CDK4	physical	8666233
CDK7_HUMAN	CDK7	physical	8666233
CDK6_HUMAN	CDK6	physical	8666233
HS90A_HUMAN	HSP90AA1	physical	12176997
AKT1_HUMAN	AKT1	physical	12176997
FGFR3_HUMAN	FGFR3	physical	21487019
CS044_HUMAN	C19orf44	physical	21900206
DEAF1_HUMAN	DEAF1	physical	21900206
MIC60_HUMAN	IMMT	physical	21900206
CRYM_HUMAN	CRYM	physical	21900206
ZN667_HUMAN	ZNF667	physical	21900206
MTOR_HUMAN	MTOR	physical	21900206
ANM1_HUMAN	PRMT1	physical	21900206
C2D1A_HUMAN	CC2D1A	physical	21900206
PPHLN_HUMAN	PPHLN1	physical	21900206
PSME1_HUMAN	PSME1	physical	21900206
SPTN4_HUMAN	SPTBN4	physical	21900206
ZN205_HUMAN	ZNF205	physical	21900206
CMGA_HUMAN	CHGA	physical	21900206
ZN266_HUMAN	ZNF266	physical	21900206
RS15A_HUMAN	RPS15A	physical	21900206
SQSTM_HUMAN	SQSTM1	physical	21900206
SAFB1_HUMAN	SAFB	physical	21900206
GCH1_HUMAN	GCH1	physical	21900206
BTBDA_HUMAN	BTBD10	physical	21900206
NCOA5_HUMAN	NCOA5	physical	21900206
MZT2B_HUMAN	MZT2B	physical	21900206
LC7L2_HUMAN	LUC7L2	physical	21900206
SNX5_HUMAN	SNX5	physical	21900206
DCTN1_HUMAN	DCTN1	physical	21900206
ZN235_HUMAN	ZNF235	physical	21900206
E2AK1_HUMAN	EIF2AK1	physical	11036079
CDK4_HUMAN	CDK4	physical	21675959
CDC37_HUMAN	CDC37	physical	21675959
HS90A_HUMAN	HSP90AA1	physical	15647277
IRAK1_HUMAN	IRAK1	physical	15647277
APOE_HUMAN	APOE	physical	21163940
NOS3_HUMAN	NOS3	physical	21163940
A4_HUMAN	APP	physical	21163940
CDK5_HUMAN	CDK5	physical	21163940
DNJB1_HUMAN	DNAJB1	physical	21163940
ECSIT_HUMAN	ECSIT	physical	21163940
ELAV3_HUMAN	ELAVL3	physical	21163940
EXOS1_HUMAN	EXOSC1	physical	21163940
FXL12_HUMAN	FBXL12	physical	21163940
GCDH_HUMAN	GCDH	physical	21163940
IFIT3_HUMAN	IFIT3	physical	21163940
IFIT5_HUMAN	IFIT5	physical	21163940
LONM_HUMAN	LONP1	physical	21163940
LOXL4_HUMAN	LOXL4	physical	21163940
OGA_HUMAN	MGEA5	physical	21163940
PRAM_HUMAN	PRAM1	physical	21163940
PRDX2_HUMAN	PRDX2	physical	21163940
RD23A_HUMAN	RAD23A	physical	21163940
RNF32_HUMAN	RNF32	physical	21163940
FBXW4_HUMAN	FBXW4	physical	21163940
CP2C9_HUMAN	CYP2C9	physical	21163940
STALP_HUMAN	STAMBPL1	physical	21163940
PSN1_HUMAN	PSEN1	physical	21163940
KS6A6_HUMAN	RPS6KA6	physical	22939629
HS90A_HUMAN	HSP90AA1	physical	22939624
HS90A_HUMAN	HSP90AA1	physical	15001580
M3K11_HUMAN	MAP3K11	physical	15001580
HS90B_HUMAN	HSP90AB1	physical	23428871
MK07_HUMAN	MAPK7	physical	23428871
RHBT2_HUMAN	RHOBTB2	physical	24608665
RAF1_HUMAN	RAF1	physical	25036637
IKKA_HUMAN	CHUK	physical	25036637
CDK4_HUMAN	CDK4	physical	25036637
IKKB_HUMAN	IKBKB	physical	25036637
AURKB_HUMAN	AURKB	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	25036637
FKBP5_HUMAN	FKBP5	physical	25036637
FKBP4_HUMAN	FKBP4	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	25036637
UBP19_HUMAN	USP19	physical	25036637
PPP5_HUMAN	PPP5C	physical	25036637
AHSA1_HUMAN	AHSA1	physical	25036637
SMYD3_HUMAN	SMYD3	physical	25036637
SRC8_HUMAN	CTTN	physical	25036637
RENT1_HUMAN	UPF1	physical	25036637
CHIP_HUMAN	STUB1	physical	25036637
SKP1_HUMAN	SKP1	physical	25036637
UN45A_HUMAN	UNC45A	physical	25036637
NEMO_HUMAN	IKBKG	physical	25036637
CHRD1_HUMAN	CHORDC1	physical	25036637
TTC4_HUMAN	TTC4	physical	25036637
TOM34_HUMAN	TOMM34	physical	25036637
RAE1L_HUMAN	RAE1	physical	25036637
SYNE2_HUMAN	SYNE2	physical	25036637
PPID_HUMAN	PPID	physical	25036637
TTC9C_HUMAN	TTC9C	physical	25036637
AIP_HUMAN	AIP	physical	25036637
ARAF_HUMAN	ARAF	physical	25036637
CDK1_HUMAN	CDK1	physical	25036637
CD11A_HUMAN	CDK11A	physical	25036637
NUP98_HUMAN	NUP98	physical	25036637
FKBPL_HUMAN	FKBPL	physical	25036637
DNJB1_HUMAN	DNAJB1	physical	25036637
FER_HUMAN	FER	physical	25036637
GLMN_HUMAN	GLMN	physical	25036637
DDX17_HUMAN	DDX17	physical	25036637
RPAP3_HUMAN	RPAP3	physical	25036637
ABL2_HUMAN	ABL2	physical	25036637
SYTM_HUMAN	TARS2	physical	25036637
DNJC7_HUMAN	DNAJC7	physical	25036637
HNRPM_HUMAN	HNRNPM	physical	25036637
NHRF3_HUMAN	PDZK1	physical	24869908
AKT1_HUMAN	AKT1	physical	24869908
CDC37_HUMAN	CDC37	physical	11916974
SAHH2_HUMAN	AHCYL1	physical	26344197
PATL1_HUMAN	PATL1	physical	26344197
LA_HUMAN	SSB	physical	26344197
HS90A_HUMAN	HSP90AA1	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
IKKB_HUMAN	IKBKB	physical	26496610
NEMO_HUMAN	IKBKG	physical	26496610
WDR6_HUMAN	WDR6	physical	26496610
TRM7_HUMAN	FTSJ1	physical	26496610
PANX1_HUMAN	PANX1	physical	26496610
1433T_HUMAN	YWHAQ	physical	24189400
ADT2_HUMAN	SLC25A5	physical	24189400
ADT3_HUMAN	SLC25A6	physical	24189400
ARAF_HUMAN	ARAF	physical	24189400
CD11A_HUMAN	CDK11A	physical	24189400
CD11B_HUMAN	CDK11B	physical	24189400
CDC37_HUMAN	CDC37	physical	24189400
CDK4_HUMAN	CDK4	physical	24189400
CDK9_HUMAN	CDK9	physical	24189400
CLK3_HUMAN	CLK3	physical	24189400
DDR1_HUMAN	DDR1	physical	24189400
DDX17_HUMAN	DDX17	physical	24189400
DDX5_HUMAN	DDX5	physical	24189400
E2AK2_HUMAN	EIF2AK2	physical	24189400
EF1A1_HUMAN	EEF1A1	physical	24189400
EF1A2_HUMAN	EEF1A2	physical	24189400
EGFR_HUMAN	EGFR	physical	24189400
EIF3B_HUMAN	EIF3B	physical	24189400
ERBB2_HUMAN	ERBB2	physical	24189400
GFAP_HUMAN	GFAP	physical	24189400
GRP78_HUMAN	HSPA5	physical	24189400
HS90A_HUMAN	HSP90AA1	physical	24189400
HS90B_HUMAN	HSP90AB1	physical	24189400
HSP7C_HUMAN	HSPA8	physical	24189400
IKKA_HUMAN	CHUK	physical	24189400
KPYM_HUMAN	PKM	physical	24189400
KS6A1_HUMAN	RPS6KA1	physical	24189400
KS6A3_HUMAN	RPS6KA3	physical	24189400
KS6A4_HUMAN	RPS6KA4	physical	24189400
KS6A6_HUMAN	RPS6KA6	physical	24189400
MASP1_HUMAN	MASP1	physical	24189400
NEMO_HUMAN	IKBKG	physical	24189400
RAF1_HUMAN	RAF1	physical	24189400
RS2_HUMAN	RPS2	physical	24189400
RS27_HUMAN	RPS27	physical	24189400
RS27L_HUMAN	RPS27L	physical	24189400
SQSTM_HUMAN	SQSTM1	physical	24189400
SRC8_HUMAN	CTTN	physical	24189400
TBA1B_HUMAN	TUBA1B	physical	24189400
TBA1C_HUMAN	TUBA1C	physical	24189400
TBB5_HUMAN	TUBB	physical	24189400
HS90A_HUMAN	HSP90AA1	physical	12930845
HS90A_HUMAN	HSP90AA1	physical	11413142
HCK_HUMAN	HCK	physical	11413142
HS90A_HUMAN	HSP90AA1	physical	22504172

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 CDC37_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-45; LYS-78; LYS-154; LYS-240AND LYS-330, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-13, 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-377, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-298, AND MASSSPECTROMETRY.	15592455 [Abstract]