dbPTM

BRE1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRE1A_HUMAN
UniProt AC	Q5VTR2
Protein Name	E3 ubiquitin-protein ligase BRE1A
Gene Name	RNF20
Organism	Homo sapiens (Human).
Sequence Length	975
Subcellular Localization	Nucleus .
Protein Description	Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation..
Protein Sequence	MSGIGNKRAAGEPGTSMPPEKKAAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDNLIVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTHQHQVELIERDEVSLHKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTKKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGIGNKRA ------CCCCCCCCC	38.83	20068231
7	Acetylation	-MSGIGNKRAAGEPG -CCCCCCCCCCCCCC	37.90	25953088
15	Phosphorylation	RAAGEPGTSMPPEKK CCCCCCCCCCCHHHH	32.35	20068231
16	Phosphorylation	AAGEPGTSMPPEKKA CCCCCCCCCCHHHHH	34.90	20068231
21	Acetylation	GTSMPPEKKAAVEDS CCCCCHHHHHHHCCC	54.19	25953088
28	Phosphorylation	KKAAVEDSGTTVETI HHHHHCCCCCEEEEE	25.24	20068231
30	Phosphorylation	AAVEDSGTTVETIKL HHHCCCCCEEEEEEE	31.46	20068231
31	Phosphorylation	AVEDSGTTVETIKLG HHCCCCCEEEEEEEC	21.62	20068231
34	Phosphorylation	DSGTTVETIKLGGVS CCCCEEEEEEECCCC	21.05	20068231
41	Phosphorylation	TIKLGGVSSTEELDI EEEECCCCCCCCCCH	34.51	23917254
42	Phosphorylation	IKLGGVSSTEELDIR EEECCCCCCCCCCHH	37.11	23917254
43	Phosphorylation	KLGGVSSTEELDIRT EECCCCCCCCCCHHH	26.44	26471730
53	Phosphorylation	LDIRTLQTKNRKLAE CCHHHHHHHCHHHHH	33.14	29970186
57	Ubiquitination	TLQTKNRKLAEMLDQ HHHHHCHHHHHHHHH	62.53	29967540
61	Sulfoxidation	KNRKLAEMLDQRQAI HCHHHHHHHHHHHHH	4.09	21406390
85	Phosphorylation	KLERRQATDDASLLI HHHHHCCCCCCCHHH	26.52	27732954
89	Phosphorylation	RQATDDASLLIVNRY HCCCCCCCHHHHHHH	30.61	27732954
111	Phosphorylation	IRIILKRYDLEQGLG HHHHHHHCCHHHCHH	24.24	20068231
122	Phosphorylation	QGLGDLLTERKALVV HCHHHHHHCCCEEEC	40.83	20068231
125	Ubiquitination	GDLLTERKALVVPEP HHHHHCCCEEECCCC	39.58	33845483
136	Phosphorylation	VPEPEPDSDSNQERK CCCCCCCCCCCCCCH	54.37	29255136
138	Phosphorylation	EPEPDSDSNQERKDD CCCCCCCCCCCCHHH	44.35	19664994
157	Phosphorylation	EGQEPAFSFLATLAS CCCCCHHHHHHHHHC	22.81	26074081
172	Phosphorylation	SSSEEMESQLQERVE CCHHHHHHHHHHHHH	34.58	21362549
194	Ubiquitination	QIVTVYDKLQEKVEL HHHHHHHHHHHHHHH	34.09	21890473
196	Ubiquitination	VTVYDKLQEKVELLS HHHHHHHHHHHHHHH	54.96	21890473
198	Ubiquitination	VYDKLQEKVELLSRK HHHHHHHHHHHHHHH	28.22	22817900
203	Phosphorylation	QEKVELLSRKLNSGD HHHHHHHHHHCCCCC	39.74	24719451
208	Phosphorylation	LLSRKLNSGDNLIVE HHHHHCCCCCCCHHH	58.94	26074081
242	Acetylation	LTDLLQEKHRTMSQE HHHHHHHHHHHHHHH	25.98	21466224
242	Ubiquitination	LTDLLQEKHRTMSQE HHHHHHHHHHHHHHH	25.98	23000965
244	Ubiquitination	DLLQEKHRTMSQEFS HHHHHHHHHHHHHHH	43.10	21890473
252	Ubiquitination	TMSQEFSKLQSKVET HHHHHHHHHHHHHHH	56.73	24816145
256	Acetylation	EFSKLQSKVETAESR HHHHHHHHHHHHHHH	31.00	26051181
256	Ubiquitination	EFSKLQSKVETAESR HHHHHHHHHHHHHHH	31.00	33845483
262	Phosphorylation	SKVETAESRVSVLES HHHHHHHHHHHHHHH	35.20	-
265	Phosphorylation	ETAESRVSVLESMID HHHHHHHHHHHHHHH	21.63	-
269	Phosphorylation	SRVSVLESMIDDLQW HHHHHHHHHHHHHHH	19.51	-
304	Phosphorylation	ERVNSKGYKVYGAGS HHHHCCCCEEEECCC	10.87	20068231
307	Phosphorylation	NSKGYKVYGAGSSLY HCCCCEEEECCCCCC	9.34	25072903
311	Phosphorylation	YKVYGAGSSLYGGTI CEEEECCCCCCCCEE	19.35	25072903
312	Phosphorylation	KVYGAGSSLYGGTIT EEEECCCCCCCCEEE	25.37	25072903
314	Phosphorylation	YGAGSSLYGGTITIN EECCCCCCCCEEEEE	18.56	20068231
317	Phosphorylation	GSSLYGGTITINARK CCCCCCCEEEEEHHH	15.58	20068231
319	Phosphorylation	SLYGGTITINARKFE CCCCCEEEEEHHHHH	14.17	25072903
324	Sumoylation	TITINARKFEEMNAE EEEEEHHHHHHHHHH	55.51	-
324	Acetylation	TITINARKFEEMNAE EEEEEHHHHHHHHHH	55.51	26051181
324	Sumoylation	TITINARKFEEMNAE EEEEEHHHHHHHHHH	55.51	-
336	Ubiquitination	NAELEENKELAQNRL HHHHHHHHHHHHHHH	58.34	24816145
348	Acetylation	NRLCELEKLRQDFEE HHHHHHHHHHHHHHH	62.69	19608861
348	Ubiquitination	NRLCELEKLRQDFEE HHHHHHHHHHHHHHH	62.69	33845483
362	Ubiquitination	EVTTQNEKLKVELRS HHCCCCHHHHHHHHH	62.24	33845483
376	Ubiquitination	SAVEQVVKETPEYRC HHHHHHHHHCHHCCH	57.95	21906983
378	Ubiquitination	VEQVVKETPEYRCMQ HHHHHHHCHHCCHHH	18.72	21890473
444	Phosphorylation	EVIQLEDTLAQVRKE HHHHHHHHHHHHHHH	18.02	-
450	Ubiquitination	DTLAQVRKEYEMLRI HHHHHHHHHHHHHHH	66.83	-
506	Phosphorylation	RKLREAQSDLNKTRL HHHHHHHHHHCHHHH	51.63	26074081
510	Acetylation	EAQSDLNKTRLRSGS HHHHHHCHHHHHHHH	42.17	25953088
511	Phosphorylation	AQSDLNKTRLRSGSA HHHHHCHHHHHHHHH	33.59	26074081
515	Phosphorylation	LNKTRLRSGSALLQS HCHHHHHHHHHHHHC	41.51	23927012
517	Phosphorylation	KTRLRSGSALLQSQS HHHHHHHHHHHHCCC	19.59	25159151
522	Phosphorylation	SGSALLQSQSSTEDP HHHHHHHCCCCCCCC	31.81	23927012
524	Phosphorylation	SALLQSQSSTEDPKD HHHHHCCCCCCCCCC	44.46	23927012
525	Phosphorylation	ALLQSQSSTEDPKDE HHHHCCCCCCCCCCC	28.33	25159151
526	Phosphorylation	LLQSQSSTEDPKDEP HHHCCCCCCCCCCCC	50.05	23927012
540	Phosphorylation	PAELKPDSEDLSSQS CCCCCCCCHHCCCCH	41.35	23401153
544	Phosphorylation	KPDSEDLSSQSSASK CCCCHHCCCCHHHHH	38.36	29978859
545	Phosphorylation	PDSEDLSSQSSASKA CCCHHCCCCHHHHHH	41.18	17525332
547	Phosphorylation	SEDLSSQSSASKASQ CHHCCCCHHHHHHCH	29.80	29978859
548	Phosphorylation	EDLSSQSSASKASQE HHCCCCHHHHHHCHH	28.99	20044836
550	Phosphorylation	LSSQSSASKASQEDA CCCCHHHHHHCHHHH	30.60	20044836
553	Phosphorylation	QSSASKASQEDANEI CHHHHHHCHHHHHHH	37.53	17525332
562	Phosphorylation	EDANEIKSKRDEEER HHHHHHHHHHHHHHH	38.29	29449344
596	Ubiquitination	EREREKQKLKESEKE HHHHHHHHHHHHHHH	73.01	24816145
608	Ubiquitination	EKERDSAKDKEKGKH HHHHHHHHHHHCCCC	73.59	24816145
610	Methylation	ERDSAKDKEKGKHDD HHHHHHHHHCCCCCC	61.70	-
614	Methylation	AKDKEKGKHDDGRKK HHHHHCCCCCCCHHH	55.73	-
627	Acetylation	KKEAEIIKQLKIELK HHHHHHHHHHHHHHH	56.06	25953088
650	Phosphorylation	MKLLLDMYRSAPKEQ HHHHHHHHHHCCHHH	10.90	-
660	Acetylation	APKEQRDKVQLMAAE CCHHHHHHHHHHHHH	33.79	25953088
668	Acetylation	VQLMAAEKKSKAELE HHHHHHHHHCHHHHH	58.58	25953088
671	Ubiquitination	MAAEKKSKAELEDLR HHHHHHCHHHHHHHH	55.55	33845483
690	Ubiquitination	DLEDKEKKENKKMAD HHHHHHHHHHHHCCC	68.55	24816145
713	Phosphorylation	AVEEQIEYLQKKLAM HHHHHHHHHHHHHHH	18.96	28152594
716	Acetylation	EQIEYLQKKLAMAKQ HHHHHHHHHHHHHHH	47.35	26051181
716	Ubiquitination	EQIEYLQKKLAMAKQ HHHHHHHHHHHHHHH	47.35	32015554
730	Phosphorylation	QEEEALLSEMDVTGQ HHHHHHHHHCCCCCH	31.55	22210691
756	Ubiquitination	LMQQLREKDDANFKL HHHHHHHCCCCCHHH	55.25	23000965
762	Ubiquitination	EKDDANFKLMSERIK HCCCCCHHHHHHHHH	42.99	23000965
764	Ubiquitination	DDANFKLMSERIKSN CCCCHHHHHHHHHHH	3.94	21890473
769	Methylation	KLMSERIKSNQIHKL HHHHHHHHHHHHHHH	49.96	-
770	Phosphorylation	LMSERIKSNQIHKLL HHHHHHHHHHHHHHH	31.43	24532841
775	Ubiquitination	IKSNQIHKLLKEEKE HHHHHHHHHHHHHHH	58.08	33845483
778	Sumoylation	NQIHKLLKEEKEELA HHHHHHHHHHHHHHH	74.41	-
778	Acetylation	NQIHKLLKEEKEELA HHHHHHHHHHHHHHH	74.41	26051181
778	Sumoylation	NQIHKLLKEEKEELA HHHHHHHHHHHHHHH	74.41	-
781	Acetylation	HKLLKEEKEELADQV HHHHHHHHHHHHHHH	58.54	26051181
781	Ubiquitination	HKLLKEEKEELADQV HHHHHHHHHHHHHHH	58.54	33845483
804	Acetylation	AQLQVVRKLEEKEHL HHHHHHHHHHHHHHH	48.95	25953088
804	Ubiquitination	AQLQVVRKLEEKEHL HHHHHHHHHHHHHHH	48.95	29967540
808	Acetylation	VVRKLEEKEHLLQSN HHHHHHHHHHHHHCC	40.85	25953088
808	Ubiquitination	VVRKLEEKEHLLQSN HHHHHHHHHHHHHCC	40.85	29967540
821	Acetylation	SNIGTGEKELGLRTQ CCCCCCHHHHHHHHH	60.63	26051181
821	Ubiquitination	SNIGTGEKELGLRTQ CCCCCCHHHHHHHHH	60.63	22817900
823	Ubiquitination	IGTGEKELGLRTQAL CCCCHHHHHHHHHHH	13.34	21890473
834	Acetylation	TQALEMNKRKAMEAA HHHHHHHHHHHHHHH	54.70	25953088
834	Ubiquitination	TQALEMNKRKAMEAA HHHHHHHHHHHHHHH	54.70	24816145
838	Sulfoxidation	EMNKRKAMEAAQLAD HHHHHHHHHHHHHHH	3.95	21406390
856	Ubiquitination	AQLELAQKKLHDFQD HHHHHHHHHHHHCHH	52.26	33845483
857	Ubiquitination	QLELAQKKLHDFQDE HHHHHHHHHHHCHHH	38.69	29967540
872	Ubiquitination	IVENSVTKEKDMFNF HHHCCCCCHHHCCCH	61.69	32015554
874	Acetylation	ENSVTKEKDMFNFKR HCCCCCHHHCCCHHH	56.92	7705987
874	Ubiquitination	ENSVTKEKDMFNFKR HCCCCCHHHCCCHHH	56.92	33845483
880	Acetylation	EKDMFNFKRAQEDIS HHHCCCHHHHHHHHH	48.18	7705999
880	Methylation	EKDMFNFKRAQEDIS HHHCCCHHHHHHHHH	48.18	7705999
916	Phosphorylation	LMEEIKDYKARLTCP HHHHHHHHHHHHCCC	11.10	29116813
929	Ubiquitination	CPCCNMRKKDAVLTK CCCCCCCCHHHHHHH	44.21	-
930	Ubiquitination	PCCNMRKKDAVLTKC CCCCCCCHHHHHHHH	40.32	-
948	Phosphorylation	FCFECVKTRYDTRQR HHHHHHHHCHHHCCC	17.67	28152594
950	Phosphorylation	FECVKTRYDTRQRKC HHHHHHCHHHCCCCC	27.22	28152594
952	Phosphorylation	CVKTRYDTRQRKCPK HHHHCHHHCCCCCCC	21.55	28152594

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
172	S	Phosphorylation	Kinase	ATM	Q13315	PSP
522	S	Phosphorylation	Kinase	ATM	Q13315	PSP
545	S	Phosphorylation	Kinase	ATM	Q13315	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:22231558

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BRE1A_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 BRE1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	16337599
BRE1B_HUMAN	RNF40	physical	21329877
WAC_HUMAN	WAC	physical	21329877
BRE1B_HUMAN	RNF40	physical	22155569
ANDR_HUMAN	AR	physical	22155569
BRE1A_HUMAN	RNF20	physical	21443952
H2B2E_HUMAN	HIST2H2BE	physical	21443952
H2A2A_HUMAN	HIST2H2AA3	physical	21443952
H2A2C_HUMAN	HIST2H2AC	physical	21443952
H32_HUMAN	HIST2H3C	physical	21443952
SMUF2_HUMAN	SMURF2	physical	22231558
CDC73_HUMAN	CDC73	physical	22021426
BRE1B_HUMAN	RNF40	physical	21362549
BRE1B_HUMAN	RNF40	physical	16307923
H2B2E_HUMAN	HIST2H2BE	physical	16307923
UB2E1_HUMAN	UBE2E1	physical	16307923
UBE2B_HUMAN	UBE2B	physical	21443952
MYO1E_HUMAN	MYO1E	physical	22939629
CDN2B_HUMAN	CDKN2B	physical	23718855
KINH_HUMAN	KIF5B	physical	22863883
SP16H_HUMAN	SUPT16H	physical	24357716
H2B2E_HUMAN	HIST2H2BE	physical	24837678
UBE2A_HUMAN	UBE2A	physical	24837678
MSL1_HUMAN	MSL1	physical	24837678
MSL2_HUMAN	MSL2	physical	24837678
PAF1_HUMAN	PAF1	physical	24837678
CDK9_HUMAN	CDK9	physical	24837678
PA2G4_HUMAN	PA2G4	physical	19037095
BRE1B_HUMAN	RNF40	physical	19410543
UBE2A_HUMAN	UBE2A	physical	19410543
UBE2B_HUMAN	UBE2B	physical	19410543
BRE1A_HUMAN	RNF20	physical	19410543
H2B1B_HUMAN	HIST1H2BB	physical	19410543
USBP1_HUMAN	USHBP1	physical	25416956
UB2L3_HUMAN	UBE2L3	physical	19037095
XPP1_HUMAN	XPNPEP1	physical	26344197
SPT6H_HUMAN	SUPT6H	physical	24441044
BRE1B_HUMAN	RNF40	physical	24441044
CHK2_HUMAN	CHEK2	physical	25640309
TPM3_HUMAN	TPM3	physical	27557628
RS3_HUMAN	RPS3	physical	27557628
BRE1B_HUMAN	RNF40	physical	27557628
KIF11_HUMAN	KIF11	physical	27557628
WAC_HUMAN	WAC	physical	27557628
HNRPF_HUMAN	HNRNPF	physical	27557628
TRAIP_HUMAN	TRAIP	physical	26781088
BRE1A_HUMAN	RNF20	physical	27569044
UBE2B_HUMAN	UBE2B	physical	27569044
BRE1B_HUMAN	RNF40	physical	27569044
FXL19_HUMAN	FBXL19	physical	28453857

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 BRE1A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-348, AND MASS SPECTROMETRY.	19608861 [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-138, AND MASSSPECTROMETRY.	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-136 AND SER-138, ANDMASS 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-136 AND SER-138, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-545 ANDSER-553, AND MASS SPECTROMETRY.	17525332 [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-138, AND MASSSPECTROMETRY.	15302935 [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-314, AND MASSSPECTROMETRY.	18083107 [Abstract]