dbPTM

PAXI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAXI_HUMAN
UniProt AC	P49023
Protein Name	Paxillin
Gene Name	PXN
Organism	Homo sapiens (Human).
Sequence Length	591
Subcellular Localization	Cytoplasm, cytoskeleton . Cell junction, focal adhesion . Cytoplasm, cell cortex . Colocalizes with integrins at the cell periphery. Colocalize with PXN to membrane ruffles and the leading edge of migrating cells (PubMed:23128389).
Protein Description	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion)..
Protein Sequence	MDDLDALLADLESTTSHISKRPVFLSEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTILDPLDQWQPSSSRFIHQQPQSSSPVYGSSAKTSSVSNPQDSVGSPCSRVGEEEHVYSFPNKQKSAEPSPTVMSTSLGSNLSELDRLLLELNAVQHNPPGFPADEANSSPPLPGALSPLYGVPETNSPLGGKAGPLTKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSTQQQTRISASSATRELDELMASLSDFKIQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGGFMAQGKTGSSSPPGGPPKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDLDALL -------CCHHHHHH	9.03	19413330
2 (in isoform 4)	Acetylation	-	66.24	22814378
2 (in isoform 4)	Phosphorylation	-	66.24	25159151
3 (in isoform 4)	Phosphorylation	-	45.19	25159151
4 (in isoform 4)	Phosphorylation	-	3.46	29507054
19	Phosphorylation	ESTTSHISKRPVFLS HHHCCCHHCCCEECC	19.72	-
26	Phosphorylation	SKRPVFLSEETPYSY HCCCEECCCCCCCCC	23.17	26356563
29	Phosphorylation	PVFLSEETPYSYPTG CEECCCCCCCCCCCC	24.39	26356563
31	Phosphorylation	FLSEETPYSYPTGNH ECCCCCCCCCCCCCC	28.40	15572663
32	Phosphorylation	LSEETPYSYPTGNHT CCCCCCCCCCCCCCE	26.32	26356563
33	Phosphorylation	SEETPYSYPTGNHTY CCCCCCCCCCCCCEE	10.04	26356563
35	Phosphorylation	ETPYSYPTGNHTYQE CCCCCCCCCCCEEEE	42.24	26356563
39	Phosphorylation	SYPTGNHTYQEIAVP CCCCCCCEEEEEECC	30.79	26356563
40	Phosphorylation	YPTGNHTYQEIAVPP CCCCCCEEEEEECCC	9.15	26356563
74	O-linked_Glycosylation	DQWQPSSSRFIHQQP HHCCCCCCCCCCCCC	35.23	30059200
83	O-linked_Glycosylation	FIHQQPQSSSPVYGS CCCCCCCCCCCCCCC	39.19	30059200
83	Phosphorylation	FIHQQPQSSSPVYGS CCCCCCCCCCCCCCC	39.19	22167270
84	Phosphorylation	IHQQPQSSSPVYGSS CCCCCCCCCCCCCCC	33.15	22167270
85	O-linked_Glycosylation	HQQPQSSSPVYGSSA CCCCCCCCCCCCCCC	24.51	30059200
85	Phosphorylation	HQQPQSSSPVYGSSA CCCCCCCCCCCCCCC	24.51	22167270
87	Phosphorylation	QPQSSSPVYGSSAKT CCCCCCCCCCCCCCC	10.25	17016520
88	Phosphorylation	PQSSSPVYGSSAKTS CCCCCCCCCCCCCCC	18.06	25159151
90	O-linked_Glycosylation	SSSPVYGSSAKTSSV CCCCCCCCCCCCCCC	14.94	30059200
90	Phosphorylation	SSSPVYGSSAKTSSV CCCCCCCCCCCCCCC	14.94	21945579
91	Phosphorylation	SSPVYGSSAKTSSVS CCCCCCCCCCCCCCC	29.44	21945579
94	Phosphorylation	VYGSSAKTSSVSNPQ CCCCCCCCCCCCCCC	26.42	23927012
95	Phosphorylation	YGSSAKTSSVSNPQD CCCCCCCCCCCCCCC	28.21	23927012
96	Phosphorylation	GSSAKTSSVSNPQDS CCCCCCCCCCCCCCC	34.49	23927012
98	Phosphorylation	SAKTSSVSNPQDSVG CCCCCCCCCCCCCCC	44.75	30266825
103	Phosphorylation	SVSNPQDSVGSPCSR CCCCCCCCCCCCCCC	24.11	30266825
106	Phosphorylation	NPQDSVGSPCSRVGE CCCCCCCCCCCCCCC	22.15	19664994
108	S-nitrosylation	QDSVGSPCSRVGEEE CCCCCCCCCCCCCCC	4.31	22126794
109	Phosphorylation	DSVGSPCSRVGEEEH CCCCCCCCCCCCCCC	33.13	30266825
117	Phosphorylation	RVGEEEHVYSFPNKQ CCCCCCCEEECCCCC	4.91	17016520
118	Phosphorylation	VGEEEHVYSFPNKQK CCCCCCEEECCCCCC	13.40	29255136
119	Phosphorylation	GEEEHVYSFPNKQKS CCCCCEEECCCCCCC	32.89	29255136
123	Ubiquitination	HVYSFPNKQKSAEPS CEEECCCCCCCCCCC	60.38	-
125	Ubiquitination	YSFPNKQKSAEPSPT EECCCCCCCCCCCCC	53.92	-
125 (in isoform 4)	Phosphorylation	-	53.92	25311616
126	Phosphorylation	SFPNKQKSAEPSPTV ECCCCCCCCCCCCCE	35.06	29255136
128 (in isoform 4)	Phosphorylation	-	54.09	24719451
130	Phosphorylation	KQKSAEPSPTVMSTS CCCCCCCCCCEEECC	25.38	29255136
132	Phosphorylation	KSAEPSPTVMSTSLG CCCCCCCCEEECCCC	32.93	30266825
134	Sulfoxidation	AEPSPTVMSTSLGSN CCCCCCEEECCCCCC	3.88	30846556
135	Phosphorylation	EPSPTVMSTSLGSNL CCCCCEEECCCCCCH	15.54	30266825
136	Phosphorylation	PSPTVMSTSLGSNLS CCCCEEECCCCCCHH	15.18	29255136
137	Phosphorylation	SPTVMSTSLGSNLSE CCCEEECCCCCCHHH	24.35	19664994
139 (in isoform 4)	Phosphorylation	-	17.79	29507054
140	Phosphorylation	VMSTSLGSNLSELDR EEECCCCCCHHHHHH	39.63	30278072
141 (in isoform 4)	Phosphorylation	-	45.87	24275569
143	Phosphorylation	TSLGSNLSELDRLLL CCCCCCHHHHHHHHH	40.12	23927012
151 (in isoform 4)	Phosphorylation	-	39.69	18691976
154 (in isoform 4)	Phosphorylation	-	18.25	25159151
155 (in isoform 4)	Phosphorylation	-	6.06	29743597
169	Phosphorylation	FPADEANSSPPLPGA CCCCCCCCCCCCCCC	51.80	26356563
170	Phosphorylation	PADEANSSPPLPGAL CCCCCCCCCCCCCCC	30.28	30278072
178	Phosphorylation	PPLPGALSPLYGVPE CCCCCCCCCCCCCCC	16.60	30278072
181	Phosphorylation	PGALSPLYGVPETNS CCCCCCCCCCCCCCC	21.33	27259358
186	Phosphorylation	PLYGVPETNSPLGGK CCCCCCCCCCCCCCC	34.62	26356563
188	Phosphorylation	YGVPETNSPLGGKAG CCCCCCCCCCCCCCC	28.99	26356563
216	Phosphorylation	GLEDVRPSVESLLDE CHHHHCHHHHHHHHH	28.14	29496963
219	Phosphorylation	DVRPSVESLLDELES HHCHHHHHHHHHHHH	31.88	22199227
226	Phosphorylation	SLLDELESSVPSPVP HHHHHHHHCCCCCCC	49.62	29523821
227	Phosphorylation	LLDELESSVPSPVPA HHHHHHHCCCCCCCE	28.77	29523821
230	Phosphorylation	ELESSVPSPVPAITV HHHHCCCCCCCEEEE	36.05	28192239
236	Phosphorylation	PSPVPAITVNQGEMS CCCCCEEEECCCCCC	18.60	23663014
243	Phosphorylation	TVNQGEMSSPQRVTS EECCCCCCCCCCCCC	34.27	25159151
244	Phosphorylation	VNQGEMSSPQRVTST ECCCCCCCCCCCCCH	24.60	25159151
249	Phosphorylation	MSSPQRVTSTQQQTR CCCCCCCCCHHHHHH	28.39	23403867
250	Phosphorylation	SSPQRVTSTQQQTRI CCCCCCCCHHHHHHH	22.74	27273156
251	Phosphorylation	SPQRVTSTQQQTRIS CCCCCCCHHHHHHHC	22.49	23403867
255	Phosphorylation	VTSTQQQTRISASSA CCCHHHHHHHCCHHH	26.15	23403867
258	Phosphorylation	TQQQTRISASSATRE HHHHHHHCCHHHHHH	20.86	30266825
258 (in isoform 2)	Phosphorylation	-	20.86	25311616
260	Phosphorylation	QQTRISASSATRELD HHHHHCCHHHHHHHH	17.45	30266825
261	Phosphorylation	QTRISASSATRELDE HHHHCCHHHHHHHHH	33.12	27273156
261 (in isoform 2)	Phosphorylation	-	33.12	24719451
263	Phosphorylation	RISASSATRELDELM HHCCHHHHHHHHHHH	26.99	22167270
270	Sulfoxidation	TRELDELMASLSDFK HHHHHHHHHHHCCCE	1.93	30846556
272	Phosphorylation	ELDELMASLSDFKIQ HHHHHHHHHCCCEEC	17.91	23911959
272 (in isoform 2)	Phosphorylation	-	17.91	29507054
274	Phosphorylation	DELMASLSDFKIQGL HHHHHHHCCCEECCC	38.21	23403867
274 (in isoform 2)	Phosphorylation	-	38.21	24275569
277	Ubiquitination	MASLSDFKIQGLEQR HHHHCCCEECCCHHH	38.83	21906983
284 (in isoform 2)	Phosphorylation	-	25.85	18691976
287 (in isoform 2)	Phosphorylation	-	24.22	25159151
288 (in isoform 2)	Phosphorylation	-	45.25	29743597
302	Phosphorylation	WPRDGGRSSPGGQDE CCCCCCCCCCCCCCC	44.13	22167270
303	Phosphorylation	PRDGGRSSPGGQDEG CCCCCCCCCCCCCCC	26.63	22167270
311 (in isoform 3)	Phosphorylation	-	13.70	24114839
313 (in isoform 3)	Phosphorylation	-	2.85	24114839
316 (in isoform 3)	Phosphorylation	-	21.69	21815630
318	Phosphorylation	GFMAQGKTGSSSPPG CCCCCCCCCCCCCCC	49.47	22167270
320	Phosphorylation	MAQGKTGSSSPPGGP CCCCCCCCCCCCCCC	32.64	22167270
321	Phosphorylation	AQGKTGSSSPPGGPP CCCCCCCCCCCCCCC	48.48	22167270
322	Phosphorylation	QGKTGSSSPPGGPPK CCCCCCCCCCCCCCC	36.49	22167270
332	Phosphorylation	GGPPKPGSQLDSMLG CCCCCCCHHHHHHHH	35.78	23927012
332 (in isoform 3)	Phosphorylation	-	35.78	25849741
334 (in isoform 3)	Phosphorylation	-	5.88	27762562
335 (in isoform 3)	Phosphorylation	-	25.10	25849741
336	Phosphorylation	KPGSQLDSMLGSLQS CCCHHHHHHHHHHHH	25.21	30266825
336 (in isoform 3)	Phosphorylation	-	25.21	25849741
340	Phosphorylation	QLDSMLGSLQSDLNK HHHHHHHHHHHHHHH	21.19	30266825
343	Phosphorylation	SMLGSLQSDLNKLGV HHHHHHHHHHHHHCH	49.73	23927012
352	Phosphorylation	LNKLGVATVAKGVCG HHHHCHHHHHCCCCC	20.70	28857561
355	Acetylation	LGVATVAKGVCGACK HCHHHHHCCCCCCCC	47.76	25953088
355	Ubiquitination	LGVATVAKGVCGACK HCHHHHHCCCCCCCC	47.76	-
371	Phosphorylation	PIAGQVVTAMGKTWH CCCCCEEECCCCCCC	16.45	21406692
404	Phosphorylation	FERDGQPYCEKDYHN CCCCCCCCCCCCCHH	12.83	28152594
409	Phosphorylation	QPYCEKDYHNLFSPR CCCCCCCCHHCCCCC	12.04	28152594
414	Phosphorylation	KDYHNLFSPRCYYCN CCCHHCCCCCEEEEC	18.01	25159151
468	Phosphorylation	KAYCRKDYFDMFAPK CEEECHHHHHHCCCC	12.43	20562096
471	Sulfoxidation	CRKDYFDMFAPKCGG ECHHHHHHCCCCCCH	1.90	30846556
533	Phosphorylation	HYHERRGSLCSGCQK EEECCCCCCCCCCCC	25.13	23927012
536	Phosphorylation	ERRGSLCSGCQKPIT CCCCCCCCCCCCCCC	48.15	23927012
540	Acetylation	SLCSGCQKPITGRCI CCCCCCCCCCCHHHH	42.33	26210075
540	Ubiquitination	SLCSGCQKPITGRCI CCCCCCCCCCCHHHH	42.33	-
543	Phosphorylation	SGCQKPITGRCITAM CCCCCCCCHHHHHHH	27.40	-
553	Acetylation	CITAMAKKFHPEHFV HHHHHHHHHCHHHHH	39.09	26051181
554 (in isoform 3)	Ubiquitination	-	13.16	-
570	Malonylation	FCLKQLNKGTFKEQN HHHHHHCCCCCCCCC	68.84	26320211
574	Acetylation	QLNKGTFKEQNDKPY HHCCCCCCCCCCCCC	59.22	26051181

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
31	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
31	Y	Phosphorylation	Kinase	EPHB1	P54762	GPS
31	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
31	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
31	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot
40	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
40	Y	Phosphorylation	Kinase	SRC	P12931	GPS
83	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
83	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
85	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
85	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
88	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
88	Y	Phosphorylation	Kinase	SRC	P12931	PSP
118	Y	Phosphorylation	Kinase	FYN	P06241	PSP
118	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
118	Y	Phosphorylation	Kinase	EPHB1	P54762	GPS
118	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
118	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
118	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot
126	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
126	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
126	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
130	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
130	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
178	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
244	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
244	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
250	S	Phosphorylation	Kinase	SLK	Q9H2G2	Uniprot
258	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
272	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
272	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
272	S	Phosphorylation	Kinase	PAK4	O96013	PSP
274	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF5	Q99942	PMID:12861019

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
244	S	Phosphorylation	18042622
Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation.
250	S	Phosphorylation	23128389
Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility.

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 PAXI_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FAK1_HUMAN	PTK2	physical	11514617
FAK2_HUMAN	PTK2B	physical	9099734
FAK2_HUMAN	PTK2B	physical	9422762
PTN12_HUMAN	PTPN12	physical	10400685
ITA4_HUMAN	ITGA4	physical	11533025
LCK_HUMAN	LCK	physical	9488700
VINC_HUMAN	VCL	physical	10330411
FAK1_HUMAN	PTK2	physical	10330411
NCK1_HUMAN	NCK1	physical	10330411
PABP1_HUMAN	PABPC1	physical	11704675
ITA4_HUMAN	ITGA4	physical	11919182
VINC_HUMAN	VCL	physical	9054445
FAK1_HUMAN	PTK2	physical	9054445
TLN1_HUMAN	TLN1	physical	9054445
VINC_HUMAN	VCL	physical	8922390
FAK1_HUMAN	PTK2	physical	8922390
ILK_HUMAN	ILK	physical	11304546
ITB3_HUMAN	ITGB3	physical	11683411
FAK1_HUMAN	PTK2	physical	9756887
CASL_HUMAN	NEDD9	physical	10455189
FAK1_HUMAN	PTK2	physical	10455189
TLN1_HUMAN	TLN1	physical	7534286
BCR_HUMAN	BCR	physical	7534286
TBG1_HUMAN	TUBG1	physical	11950600
FYN_HUMAN	FYN	physical	10804218
ITB1_HUMAN	ITGB1	physical	10804218
ASAP1_HUMAN	ASAP1	physical	12149250
REPS2_MOUSE	Reps2	physical	12149250
TLN1_HUMAN	TLN1	physical	8641358
RNF5_CAEEL	rnf-5	physical	12861019
RNF5_HUMAN	RNF5	physical	12861019
NAA10_HUMAN	NAA10	physical	22863883
SC24D_HUMAN	SEC24D	physical	22863883
ADA17_HUMAN	ADAM17	physical	23317503
ADA10_HUMAN	ADAM10	physical	23317503
HDAC6_HUMAN	HDAC6	physical	25070956
TRI15_HUMAN	TRIM15	physical	25015296
CAP1_HUMAN	CAP1	physical	26344197
SRC8_HUMAN	CTTN	physical	25241761
P85A_HUMAN	PIK3R1	physical	25241761
MK01_HUMAN	MAPK1	physical	25241761

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 PAXI_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-106, AND MASS SPECTROMETRY.	19413330 [Abstract]
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-85 AND SER-126, AND MASSSPECTROMETRY.	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-83; SER-85 AND THR-318,AND MASS SPECTROMETRY.	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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-106, 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-85; SER-106; SER-126;SER-130 AND SER-137, 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-85, AND MASSSPECTROMETRY.	18691976 [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-106, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; TYR-88 AND TYR-118,AND MASS SPECTROMETRY.	17389395 [Abstract]
"Cdk5 regulates differentiation of oligodendrocyte precursor cellsthrough the direct phosphorylation of paxillin."; Miyamoto Y., Yamauchi J., Chan J.R., Okada A., Tomooka Y.,Hisanaga S., Tanoue A.; J. Cell Sci. 120:4355-4366(2007). Cited for: PHOSPHORYLATION AT SER-244.	18042622 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.	16964243 [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 TYR-118 AND SER-303, ANDMASS SPECTROMETRY.	17081983 [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-31; TYR-88 AND TYR-118,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-88 AND TYR-118, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASSSPECTROMETRY.	16094384 [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-118, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASSSPECTROMETRY.	15951569 [Abstract]
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC)."; Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.; J. Proteome Res. 4:1661-1671(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASSSPECTROMETRY.	16212419 [Abstract]
"Brk activates rac1 and promotes cell migration and invasion byphosphorylating paxillin."; Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.; Mol. Cell. Biol. 24:10558-10572(2004). Cited for: PHOSPHORYLATION AT TYR-31 AND TYR-118, AND INTERACTION WITH PTK6.	15572663 [Abstract]
"Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin inMM1 cancer cell migration."; Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H.,Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E.,Akedo H.; Int. J. Cancer 97:330-335(2002). Cited for: PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.	11774284 [Abstract]

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