dbPTM

ACTB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTB_HUMAN
UniProt AC	P60709
Protein Name	Actin, cytoplasmic 1
Gene Name	ACTB
Organism	Homo sapiens (Human).
Sequence Length	375
Subcellular Localization	Cytoplasm, cytoskeleton . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells..
Protein Sequence	MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDDIAAL -------CCCCCEEE	13.23	22814378
2	Acetylation	------MDDDIAALV ------CCCCCEEEE	63.39	29581253
14	Phosphorylation	ALVVDNGSGMCKAGF EEEEECCCCCEECCC	29.61	20164059
16	Sulfoxidation	VVDNGSGMCKAGFAG EEECCCCCEECCCCC	1.96	21406390
17	S-palmitoylation	VDNGSGMCKAGFAGD EECCCCCEECCCCCC	2.89	29575903
18	Methylation	DNGSGMCKAGFAGDD ECCCCCEECCCCCCC	42.52	-
18	Ubiquitination	DNGSGMCKAGFAGDD ECCCCCEECCCCCCC	42.52	-
33	Phosphorylation	APRAVFPSIVGRPRH CCCCCCHHHCCCCCC	20.59	30266825
44	Oxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	-
44	Sulfoxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	21406390
47	Oxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	-
47	Sulfoxidation	HQGVMVGMGQKDSYV CCCEEEECCCCCCCC	3.32	28183972
50	Acetylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	23954790
50	Methylation	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	23644510
50	Ubiquitination	VMVGMGQKDSYVGDE EEEECCCCCCCCCCH	42.80	21906983
52	Phosphorylation	VGMGQKDSYVGDEAQ EECCCCCCCCCCHHH	28.84	23401153
53	Phosphorylation	GMGQKDSYVGDEAQS ECCCCCCCCCCHHHC	20.70	23927012
60	Phosphorylation	YVGDEAQSKRGILTL CCCCHHHCCCCEEEE	31.22	23401153
61	Sumoylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
61	Acetylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	16916647
61	Malonylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	21908771
61	Sumoylation	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	-
61	Ubiquitination	VGDEAQSKRGILTLK CCCHHHCCCCEEEEE	42.43	21890473
66	Phosphorylation	QSKRGILTLKYPIEH HCCCCEEEEECEECC	21.20	28102081
68	Sumoylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	-
68	Acetylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	21466224
68	Methylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	23644510
68	Sumoylation	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	-
68	Ubiquitination	KRGILTLKYPIEHGI CCCEEEEECEECCCC	43.69	21890473
69	Phosphorylation	RGILTLKYPIEHGIV CCEEEEECEECCCCC	16.74	22817900
73	Methylation	TLKYPIEHGIVTNWD EEECEECCCCCCCHH	31.81	30785395
77	Phosphorylation	PIEHGIVTNWDDMEK EECCCCCCCHHHHHH	28.77	110747731
82	Oxidation	IVTNWDDMEKIWHHT CCCCHHHHHHHHHHH	5.39	16446289
84	Methylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	23673617
84	Sumoylation	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	23673617
84	Ubiquitination	TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH	44.45	21890473
89	Phosphorylation	MEKIWHHTFYNELRV HHHHHHHHHHCCCCC	18.22	27273156
91	Phosphorylation	KIWHHTFYNELRVAP HHHHHHHHCCCCCCC	14.64	27273156
106	Phosphorylation	EEHPVLLTEAPLNPK CCCCEEEEECCCCCC	26.41	57405023
113	Sumoylation	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	-
113	Acetylation	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	66729135
113	Sumoylation	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	-
113	Ubiquitination	TEAPLNPKANREKMT EECCCCCCCCHHHHH	58.16	21890473
119	Sulfoxidation	PKANREKMTQIMFET CCCCHHHHHHHHHHH	2.60	28183972
120	Phosphorylation	KANREKMTQIMFETF CCCHHHHHHHHHHHC	26.47	-
123	Sulfoxidation	REKMTQIMFETFNTP HHHHHHHHHHHCCCH	1.46	28183972
132	Sulfoxidation	ETFNTPAMYVAIQAV HHCCCHHHHHHHHHH	2.66	28183972
143	Phosphorylation	IQAVLSLYASGRTTG HHHHHHHHHCCCCEE	8.71	30803939
148	Phosphorylation	SLYASGRTTGIVMDS HHHHCCCCEEEEEEC	32.66	30140170
149	Phosphorylation	LYASGRTTGIVMDSG HHHCCCCEEEEEECC	24.45	30140170
153	Sulfoxidation	GRTTGIVMDSGDGVT CCCEEEEEECCCCCE	2.99	28183972
155	Phosphorylation	TTGIVMDSGDGVTHT CEEEEEECCCCCEEE	22.23	30140170
160	O-linked_Glycosylation	MDSGDGVTHTVPIYE EECCCCCEEEEEEEC	19.84	23301498
160	Phosphorylation	MDSGDGVTHTVPIYE EECCCCCEEEEEEEC	19.84	28152594
162	Phosphorylation	SGDGVTHTVPIYEGY CCCCCEEEEEEECCC	20.72	30140170
166	Phosphorylation	VTHTVPIYEGYALPH CEEEEEEECCCCCCH	9.38	27273156
169	Phosphorylation	TVPIYEGYALPHAIL EEEEECCCCCCHHHH	7.94	21082442
177	ADP-ribosylation	ALPHAILRLDLAGRD CCCHHHHHHHHCCCC	21.75	-
186	Phosphorylation	DLAGRDLTDYLMKIL HHCCCCHHHHHHHHH	27.21	28152594
188	Phosphorylation	AGRDLTDYLMKILTE CCCCHHHHHHHHHHH	11.94	26846344
190	Sulfoxidation	RDLTDYLMKILTERG CCHHHHHHHHHHHCC	1.75	21406390
191	Acetylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	19608861
191	Methylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	-
191	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	20639865
194	Phosphorylation	DYLMKILTERGYSFT HHHHHHHHHCCCCCC	27.40	19060867
198	Phosphorylation	KILTERGYSFTTTAE HHHHHCCCCCCCCHH	13.56	27273156
199	Phosphorylation	ILTERGYSFTTTAER HHHHCCCCCCCCHHH	20.95	30266825
201	Phosphorylation	TERGYSFTTTAEREI HHCCCCCCCCHHHHH	19.80	30266825
202	Phosphorylation	ERGYSFTTTAEREIV HCCCCCCCCHHHHHH	23.23	30266825
203	Phosphorylation	RGYSFTTTAEREIVR CCCCCCCCHHHHHHH	24.38	30266825
213	Acetylation	REIVRDIKEKLCYVA HHHHHHHHHHHHEEE	53.75	8275705
213	Ubiquitination	REIVRDIKEKLCYVA HHHHHHHHHHHHEEE	53.75	21906983
215	Ubiquitination	IVRDIKEKLCYVALD HHHHHHHHHHEEECC	38.56	21906983
217	S-nitrosocysteine	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	-
217	Glutathionylation	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	22555962
217	S-nitrosylation	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	25040305
217	S-palmitoylation	RDIKEKLCYVALDFE HHHHHHHHEEECCHH	3.68	29575903
218	Phosphorylation	DIKEKLCYVALDFEQ HHHHHHHEEECCHHH	10.13	27461979
227	Sulfoxidation	ALDFEQEMATAASSS ECCHHHHHHHHHCCC	3.92	28183972
229	Phosphorylation	DFEQEMATAASSSSL CHHHHHHHHHCCCCC	22.80	27461979
232	Phosphorylation	QEMATAASSSSLEKS HHHHHHHCCCCCCCC	28.43	30278072
233	Phosphorylation	EMATAASSSSLEKSY HHHHHHCCCCCCCCE	21.15	30278072
234	Phosphorylation	MATAASSSSLEKSYE HHHHHCCCCCCCCEE	36.13	30278072
235	Phosphorylation	ATAASSSSLEKSYEL HHHHCCCCCCCCEEC	42.36	30278072
238	Ubiquitination	ASSSSLEKSYELPDG HCCCCCCCCEECCCC	64.73	-
239	Phosphorylation	SSSSLEKSYELPDGQ CCCCCCCCEECCCCC	17.92	29255136
240	Phosphorylation	SSSLEKSYELPDGQV CCCCCCCEECCCCCE	32.33	29255136
249	Phosphorylation	LPDGQVITIGNERFR CCCCCEEEECCCEEC	24.79	26846344
265	O-linked_Glycosylation	PEALFQPSFLGMESC CHHHHCCHHHCCCCC	23.48	23301498
265	Phosphorylation	PEALFQPSFLGMESC CHHHHCCHHHCCCCC	23.48	26074081
271	O-linked_Glycosylation	PSFLGMESCGIHETT CHHHCCCCCCCCCCC	14.57	23301498
271	Phosphorylation	PSFLGMESCGIHETT CHHHCCCCCCCCCCC	14.57	26074081
272	Glutathionylation	SFLGMESCGIHETTF HHHCCCCCCCCCCCH	3.65	22555962
272	S-nitrosylation	SFLGMESCGIHETTF HHHCCCCCCCCCCCH	3.65	25040305
277	O-linked_Glycosylation	ESCGIHETTFNSIMK CCCCCCCCCHHHHHC	23.64	23301498
277	Phosphorylation	ESCGIHETTFNSIMK CCCCCCCCCHHHHHC	23.64	30140170
278	O-linked_Glycosylation	SCGIHETTFNSIMKC CCCCCCCCHHHHHCC	20.17	23301498
278	Phosphorylation	SCGIHETTFNSIMKC CCCCCCCCHHHHHCC	20.17	30140170
281	O-linked_Glycosylation	IHETTFNSIMKCDVD CCCCCHHHHHCCCCC	21.62	23301498
284	Sumoylation	TTFNSIMKCDVDIRK CCHHHHHCCCCCCCC	26.13	-
284	Sumoylation	TTFNSIMKCDVDIRK CCHHHHHCCCCCCCC	26.13	-
284	Ubiquitination	TTFNSIMKCDVDIRK CCHHHHHCCCCCCCC	26.13	-
285	S-nitrosocysteine	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	-
285	Glutathionylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	22555962
285	S-nitrosylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	19483679
285	S-palmitoylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	29575903
291	Acetylation	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	21466224
291	Sumoylation	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	-
291	Ubiquitination	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	20639865
294	Phosphorylation	VDIRKDLYANTVLSG CCCCCHHHCCCEECC	14.13	27273156
297	Phosphorylation	RKDLYANTVLSGGTT CCHHHCCCEECCCCC	18.04	27155012
300	Phosphorylation	LYANTVLSGGTTMYP HHCCCEECCCCCCCC	30.73	21712546
303	Phosphorylation	NTVLSGGTTMYPGIA CCEECCCCCCCCCHH	16.35	21712546
304	Phosphorylation	TVLSGGTTMYPGIAD CEECCCCCCCCCHHH	20.27	21712546
305	Sulfoxidation	VLSGGTTMYPGIADR EECCCCCCCCCHHHH	3.69	28183972
306	Nitration	LSGGTTMYPGIADRM ECCCCCCCCCHHHHH	9.01	-
306	Phosphorylation	LSGGTTMYPGIADRM ECCCCCCCCCHHHHH	9.01	21712546
315	Sumoylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
315	Acetylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	21466224
315	Sumoylation	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	-
315	Ubiquitination	GIADRMQKEITALAP CHHHHHHHHHHHHCC	41.56	21890473
318	Phosphorylation	DRMQKEITALAPSTM HHHHHHHHHHCCCCE	19.40	30266825
323	Phosphorylation	EITALAPSTMKIKII HHHHHCCCCEEEEEE	35.21	29255136
324	Phosphorylation	ITALAPSTMKIKIIA HHHHCCCCEEEEEEC	22.79	46158473
325	Sulfoxidation	TALAPSTMKIKIIAP HHHCCCCEEEEEECC	5.05	21406390
326	Sumoylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
326	Acetylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	23954790
326	Methylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
326	Sumoylation	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	-
326	Ubiquitination	ALAPSTMKIKIIAPP HHCCCCEEEEEECCC	40.72	21906983
328	Sumoylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	-
328	Acetylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	23954790
328	Sumoylation	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	-
328	Ubiquitination	APSTMKIKIIAPPER CCCCEEEEEECCCCC	23.65	21906983
336	Sumoylation	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	-
348	Phosphorylation	IGGSILASLSTFQQM ECHHHHHHHHHHHHH	21.29	-
355	Sulfoxidation	SLSTFQQMWISKQEY HHHHHHHHHHHCCCC	2.09	28183972
359	Ubiquitination	FQQMWISKQEYDESG HHHHHHHCCCCCCCC	37.71	-
362	Phosphorylation	MWISKQEYDESGPSI HHHHCCCCCCCCCCC	23.63	23401153
365	Phosphorylation	SKQEYDESGPSIVHR HCCCCCCCCCCCCCC	53.78	23401153
368	Phosphorylation	EYDESGPSIVHRKCF CCCCCCCCCCCCCCC	40.54	30266825
373	Ubiquitination	GPSIVHRKCF----- CCCCCCCCCC-----	25.72	-
374	Glutathionylation	PSIVHRKCF------ CCCCCCCCC------	5.02	16251471

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
Oops, there are no upstream regulatory protein records of ACTB_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	M	Oxidation	-
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
47	M	Oxidation	-
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
73	H	Methylation	30526847
Methylated at His-73 by SETD3.
73	H	Methylation	30526847
Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).
84	K	Methylation	23673617
Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes.

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 ACTB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COF1_HUMAN	CFL1	physical	16189514
COF2_HUMAN	CFL2	physical	16189514
ACTB_HUMAN	ACTB	physical	16189514
DEST_HUMAN	DSTN	physical	16189514
ACTG_HUMAN	ACTG1	physical	16189514
NCALD_HUMAN	NCALD	physical	16189514
ACTB_HUMAN	ACTB	physical	9209005
TCPE_MOUSE	Cct5	physical	10748209
TCPQ_MOUSE	Cct8	physical	10748209
HS71B_MOUSE	Hspa1b	physical	10748209
NCF1_HUMAN	NCF1	physical	11027608
RAC1_HUMAN	RAC1	physical	11027608
RAC2_HUMAN	RAC2	physical	11027608
PCY1B_HUMAN	PCYT1B	physical	11580269
TCPE_HUMAN	CCT5	physical	11580269
TCPB_HUMAN	CCT2	physical	11580269
SSH1_HUMAN	SSH1	physical	11832213
SSH2_HUMAN	SSH2	physical	11832213
ESR1_HUMAN	ESR1	physical	20308691
ARP3_HUMAN	ACTR3	physical	20308691
ARP2_HUMAN	ACTR2	physical	20308691
HMMR_HUMAN	HMMR	physical	10547355
CTGF_HUMAN	CTGF	physical	12470643
RPB1_HUMAN	POLR2A	physical	15502823
TAF11_HUMAN	TAF11	physical	15502823
HNRPU_HUMAN	HNRNPU	physical	15711563
DHX9_HUMAN	DHX9	physical	19309309
SYUA_HUMAN	SNCA	physical	18331289
SC6A2_HUMAN	SLC6A2	physical	18331289
FAN_HUMAN	NSMAF	physical	17599063
RUVB1_HUMAN	RUVBL1	physical	22939629
RUVB2_HUMAN	RUVBL2	physical	22939629
MYH11_HUMAN	MYH11	physical	22939629
COR1C_HUMAN	CORO1C	physical	22939629
PP1A_HUMAN	PPP1CA	physical	22939629
FHOD1_HUMAN	FHOD1	physical	12665555
MIPT3_HUMAN	TRAF3IP1	physical	20391533
ERBB2_HUMAN	ERBB2	physical	21555369
RPA2_HUMAN	POLR1B	physical	21555369
OTUB1_HUMAN	OTUB1	physical	16364312
NOS3_HUMAN	NOS3	physical	17502619
ICAM1_HUMAN	ICAM1	physical	23463506
CD81_HUMAN	CD81	physical	23463506
VCAM1_HUMAN	VCAM1	physical	23463506
ICAM3_HUMAN	ICAM3	physical	23463506
PROF1_HUMAN	PFN1	physical	19338310
CAV1_HUMAN	CAV1	physical	17502619
EP300_HUMAN	EP300	physical	21988832
CSK2B_HUMAN	CSNK2B	physical	21988832
KHDR1_HUMAN	KHDRBS1	physical	21988832
PRSR2_HUMAN	PROSER2	physical	21988832
RL10A_HUMAN	RPL10A	physical	21988832
COTL1_HUMAN	COTL1	physical	11583571
AMOT_HUMAN	AMOT	physical	24225952
ACTB_HUMAN	ACTB	physical	25416956
ACTG_HUMAN	ACTG1	physical	25416956
COF1_HUMAN	CFL1	physical	25416956
COF2_HUMAN	CFL2	physical	25416956
ECHP_HUMAN	EHHADH	physical	25416956
TBA8_HUMAN	EHHADH	physical	25416956
CAP2_HUMAN	CAP2	physical	25416956
DEST_HUMAN	DSTN	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
RPB1_HUMAN	POLR2A	physical	18710935
KAT2B_HUMAN	KAT2B	physical	18710935
HNRPU_HUMAN	HNRNPU	physical	18710935
PYR1_HUMAN	CAD	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
EF1A2_HUMAN	EEF1A2	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
SYYC_HUMAN	YARS	physical	26344197
TCPA_MOUSE	Tcp1	physical	10748209
TCPB_MOUSE	Cct2	physical	10748209
ACTB_HUMAN	ACTB	physical	21516116
ACTG_HUMAN	ACTG1	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607371	Dystonia, juvenile-onset (DYTJ)
243310	Baraitser-Winter syndrome 1 (BRWS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACTB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, AND MASSSPECTROMETRY.	18088087 [Abstract]
"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 TYR-169; TYR-198; TYR-218AND TYR-294, AND MASS SPECTROMETRY.	19690332 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-169 ANDTYR-198, AND MASS SPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-198 ANDTYR-294, AND MASS SPECTROMETRY.	18083107 [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-166; TYR-218 ANDTYR-294, AND MASS SPECTROMETRY.	15592455 [Abstract]

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