dbPTM

STK4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STK4_HUMAN
UniProt AC	Q13043
Protein Name	Serine/threonine-protein kinase 4
Gene Name	STK4
Organism	Homo sapiens (Human).
Sequence Length	487
Subcellular Localization	Cytoplasm. Nucleus. The caspase-cleaved form cycles between the nucleus and cytoplasm.
Protein Description	Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes..
Protein Sequence	METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------METVQLRN -------CCCCCCCC	9.82	19369195
3	Phosphorylation	-----METVQLRNPP -----CCCCCCCCCC	16.56	27174698
21	Phosphorylation	LKKLDEDSLTKQPEE HHCCCCCCCCCCHHH	35.57	27067055
23	Phosphorylation	KLDEDSLTKQPEEVF CCCCCCCCCCHHHHH	31.42	20873877
24	Ubiquitination	LDEDSLTKQPEEVFD CCCCCCCCCHHHHHH	69.97	29967540
35	Ubiquitination	EVFDVLEKLGEGSYG HHHHHHHHHCCCCCH	58.60	29967540
35	Acetylation	EVFDVLEKLGEGSYG HHHHHHHHHCCCCCH	58.60	7695199
40	Phosphorylation	LEKLGEGSYGSVYKA HHHHCCCCCHHHHHH	23.24	22322096
41	Phosphorylation	EKLGEGSYGSVYKAI HHHCCCCCHHHHHHH	25.03	22322096
43	Phosphorylation	LGEGSYGSVYKAIHK HCCCCCHHHHHHHHC	17.65	28152594
43	Ubiquitination	LGEGSYGSVYKAIHK HCCCCCHHHHHHHHC	17.65	22817900
45	Phosphorylation	EGSYGSVYKAIHKET CCCCHHHHHHHHCCC	9.08	28152594
46	Ubiquitination	GSYGSVYKAIHKETG CCCHHHHHHHHCCCC	38.41	29967540
50	Ubiquitination	SVYKAIHKETGQIVA HHHHHHHCCCCCEEE	51.35	29967540
52	Phosphorylation	YKAIHKETGQIVAIK HHHHHCCCCCEEEEE	38.91	24114839
59	Methylation	TGQIVAIKQVPVESD CCCEEEEEEECCCCC	35.19	126257615
59	Ubiquitination	TGQIVAIKQVPVESD CCCEEEEEEECCCCC	35.19	29967540
72	Ubiquitination	SDLQEIIKEISIMQQ CCHHHHHHHHHHHHH	55.44	29967540
82	Phosphorylation	SIMQQCDSPHVVKYY HHHHHCCCCHHHHCC	25.24	20028971
90	Ubiquitination	PHVVKYYGSYFKNTD CHHHHCCCCCCCCCC	16.87	22817900
104	Ubiquitination	DLWIVMEYCGAGSVS CEEEEEECCCCCCHH	4.32	22053931
106	Ubiquitination	WIVMEYCGAGSVSDI EEEEECCCCCCHHHH	31.88	22817900
119	Ubiquitination	DIIRLRNKTLTEDEI HHHHHHCCCCCHHHH	38.18	21906983
119 (in isoform 1)	Ubiquitination	-	38.18	21906983
119 (in isoform 2)	Ubiquitination	-	38.18	21906983
120	Phosphorylation	IIRLRNKTLTEDEIA HHHHHCCCCCHHHHH	42.32	20873877
122	Phosphorylation	RLRNKTLTEDEIATI HHHCCCCCHHHHHHH	46.77	27067055
128	Phosphorylation	LTEDEIATILQSTLK CCHHHHHHHHHHHHH	28.07	27067055
132	Phosphorylation	EIATILQSTLKGLEY HHHHHHHHHHHHHHH	32.06	20873877
133	Phosphorylation	IATILQSTLKGLEYL HHHHHHHHHHHHHHH	21.38	20873877
135	Ubiquitination	TILQSTLKGLEYLHF HHHHHHHHHHHHHHH	62.63	22817900
139	Phosphorylation	STLKGLEYLHFMRKI HHHHHHHHHHHHHHH	15.54	27067055
151 (in isoform 2)	Ubiquitination	-	55.31	21906983
151	Ubiquitination	RKIHRDIKAGNILLN HHHHCCHHHCCEEEC	55.31	21906983
151 (in isoform 1)	Ubiquitination	-	55.31	21906983
164	Ubiquitination	LNTEGHAKLADFGVA ECCCCCHHHHHCCCC	38.23	-
167	Ubiquitination	EGHAKLADFGVAGQL CCCHHHHHCCCCCHH	51.79	22053931
175	Phosphorylation	FGVAGQLTDTMAKRN CCCCCHHHHHHHHHC	22.87	29255136
177	Phosphorylation	VAGQLTDTMAKRNTV CCCHHHHHHHHHCCC	17.50	29255136
178	Sulfoxidation	AGQLTDTMAKRNTVI CCHHHHHHHHHCCCC	4.63	21406390
180	Ubiquitination	QLTDTMAKRNTVIGT HHHHHHHHHCCCCCC	35.05	22053931
180 (in isoform 1)	Ubiquitination	-	35.05	21906983
180 (in isoform 2)	Ubiquitination	-	35.05	21906983
183	Phosphorylation	DTMAKRNTVIGTPFW HHHHHHCCCCCCCCC	19.96	18328708
187	Phosphorylation	KRNTVIGTPFWMAPE HHCCCCCCCCCCCHH	12.28	12223493
196	Ubiquitination	FWMAPEVIQEIGYNC CCCCHHHHHHHCCCH	2.65	22053931
235	Sulfoxidation	HPMRAIFMIPTNPPP CCCEEEEEEECCCCC	2.68	21406390
238	Phosphorylation	RAIFMIPTNPPPTFR EEEEEEECCCCCCCC	49.81	20068231
243	Phosphorylation	IPTNPPPTFRKPELW EECCCCCCCCCHHHC	41.67	20068231
246	Ubiquitination	NPPPTFRKPELWSDN CCCCCCCCHHHCCCC	38.36	-
264	Ubiquitination	FVKQCLVKSPEQRAT HHHHHHCCCHHHHHH	47.55	29967540
265	Phosphorylation	VKQCLVKSPEQRATA HHHHHCCCHHHHHHH	26.62	17192257
285	Ubiquitination	HPFVRSAKGVSILRD CHHHHCCHHHHHHHH	62.18	29967540
288	Phosphorylation	VRSAKGVSILRDLIN HHCCHHHHHHHHHHH	25.27	24719451
298	Sulfoxidation	RDLINEAMDVKLKRQ HHHHHHHHHHHHHHH	5.06	21406390
301	Ubiquitination	INEAMDVKLKRQESQ HHHHHHHHHHHHHHH	43.99	-
303	Ubiquitination	EAMDVKLKRQESQQR HHHHHHHHHHHHHHC	46.44	-
307	Phosphorylation	VKLKRQESQQREVDQ HHHHHHHHHHCCCCC	24.23	28450419
320	Phosphorylation	DQDDEENSEEDEMDS CCCCHHCCHHHHHCC	45.72	23927012
327	Phosphorylation	SEEDEMDSGTMVRAV CHHHHHCCCCEEEEC	34.55	23927012
329	Phosphorylation	EDEMDSGTMVRAVGD HHHHCCCCEEEECCC	19.22	23927012
338	Sulfoxidation	VRAVGDEMGTVRVAS EEECCCCCCCEEEEE	6.93	21406390
340	Phosphorylation	AVGDEMGTVRVASTM ECCCCCCCEEEEEEE	12.11	23401153
353	Phosphorylation	TMTDGANTMIEHDDT EECCCCCCEEECCCC	20.99	27251275
360	Phosphorylation	TMIEHDDTLPSQLGT CEEECCCCCCHHCCE	46.77	22817900
363	Phosphorylation	EHDDTLPSQLGTMVI ECCCCCCHHCCEEEE	40.94	19369195
367	Phosphorylation	TLPSQLGTMVINAED CCCHHCCEEEEECCC	19.50	22817900
380	Phosphorylation	EDEEEEGTMKRRDET CCCCCCCCCCCCHHH	23.85	30576142
387	Phosphorylation	TMKRRDETMQPAKPS CCCCCHHHCCCCCHH	25.95	28674151
389	Ubiquitination	KRRDETMQPAKPSFL CCCHHHCCCCCHHHH	42.07	24816145
394	Phosphorylation	TMQPAKPSFLEYFEQ HCCCCCHHHHHHHHH	41.58	25159151
398	Phosphorylation	AKPSFLEYFEQKEKE CCHHHHHHHHHHHHH	17.98	28796482
404	Ubiquitination	EYFEQKEKENQINSF HHHHHHHHHHCCCCC	69.84	24816145
410	Phosphorylation	EKENQINSFGKSVPG HHHHCCCCCCCCCCC	36.68	30266825
413	Ubiquitination	NQINSFGKSVPGPLK HCCCCCCCCCCCCCC	46.39	29967540
414	Phosphorylation	QINSFGKSVPGPLKN CCCCCCCCCCCCCCC	33.64	23401153
420	Ubiquitination	KSVPGPLKNSSDWKI CCCCCCCCCCCCCCC	58.90	29967540
422	Phosphorylation	VPGPLKNSSDWKIPQ CCCCCCCCCCCCCCC	28.25	29978859
423	Phosphorylation	PGPLKNSSDWKIPQD CCCCCCCCCCCCCCC	57.81	29978859
426	Ubiquitination	LKNSSDWKIPQDGDY CCCCCCCCCCCCCCC	49.88	29967540
433	Phosphorylation	KIPQDGDYEFLKSWT CCCCCCCCHHHHHCC	17.70	25159151
436	Ubiquitination	QDGDYEFLKSWTVED CCCCCHHHHHCCHHH	2.61	24816145
437	Ubiquitination	DGDYEFLKSWTVEDL CCCCHHHHHCCHHHH	49.63	29967540
438	Phosphorylation	GDYEFLKSWTVEDLQ CCCHHHHHCCHHHHH	30.08	25159151
440	Phosphorylation	YEFLKSWTVEDLQKR CHHHHHCCHHHHHHH	22.55	28796482
446	Ubiquitination	WTVEDLQKRLLALDP CCHHHHHHHHHHHCH	52.92	29967540
451	Ubiquitination	LQKRLLALDPMMEQE HHHHHHHHCHHHHHH	8.40	24816145
452	Ubiquitination	QKRLLALDPMMEQEI HHHHHHHCHHHHHHH	24.36	24816145
465	Ubiquitination	EIEEIRQKYQSKRQP HHHHHHHHHHHCCCH	35.09	24816145
467	Ubiquitination	EEIRQKYQSKRQPIL HHHHHHHHHCCCHHH	49.89	24816145
480	Ubiquitination	ILDAIEAKKRRQQNF HHHHHHHHHHHHHCC	33.74	24816145
481	Ubiquitination	LDAIEAKKRRQQNF- HHHHHHHHHHHHCC-	60.92	24816145
496	Ubiquitination	---------------- ----------------		24816145

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
82	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
120	T	Phosphorylation	Kinase	AKT1	P31749	PSP
183	T	Phosphorylation	Kinase	AKT1	P31749	PSP
183	T	Phosphorylation	Kinase	STK4	Q13043	PhosphoELM
340	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
353	T	Phosphorylation	Kinase	STK4	Q13043	GPS
367	T	Phosphorylation	Kinase	STK4	Q13043	GPS
387	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
433	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
433	Y	Phosphorylation	Kinase	FGFR4	P22455	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:18381433

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
183	T	Phosphorylation	15109305
Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183.
387	T	Phosphorylation	17726016
Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183.

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 STK4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STK4_HUMAN	STK4	physical	8702870
H2B2E_HUMAN	HIST2H2BE	physical	12757711
RASF2_HUMAN	RASSF2	physical	20562859
RASF4_HUMAN	RASSF4	physical	20562859
STK3_HUMAN	STK3	physical	20562859
SAV1_HUMAN	SAV1	physical	20562859
MAP1B_HUMAN	MAP1B	physical	20562859
RASF5_HUMAN	RASSF5	physical	20562859
RASF1_HUMAN	RASSF1	physical	20562859
TAOK1_HUMAN	TAOK1	physical	20562859
SIR1_HUMAN	SIRT1	physical	21212262
ABL1_HUMAN	ABL1	physical	21715626
FOXO3_HUMAN	FOXO3	physical	21715626
H2AX_HUMAN	H2AFX	physical	20921231
AKT1_HUMAN	AKT1	physical	19940129
H2B2E_HUMAN	HIST2H2BE	physical	19940129
STK4_HUMAN	STK4	physical	22863277
SMS1_HUMAN	SGMS1	physical	22863277
AKT1_HUMAN	AKT1	physical	17932490
RASF3_HUMAN	RASSF3	physical	24255178
AURKB_HUMAN	AURKB	physical	24255178
STRP1_HUMAN	STRIP1	physical	24255178
FGOP2_HUMAN	FGFR1OP2	physical	24255178
KIF2A_HUMAN	KIF2A	physical	24255178
KIF2C_HUMAN	KIF2C	physical	24255178
MAP1S_HUMAN	MAP1S	physical	24255178
MOB1A_HUMAN	MOB1A	physical	24255178
PHOCN_HUMAN	MOB4	physical	24255178
P52K_HUMAN	PRKRIR	physical	24255178
RAB8A_HUMAN	RAB8A	physical	24255178
RASF1_HUMAN	RASSF1	physical	24255178
RASF2_HUMAN	RASSF2	physical	24255178
RASF5_HUMAN	RASSF5	physical	24255178
SAV1_HUMAN	SAV1	physical	24255178
SHLB2_HUMAN	SH3GLB2	physical	24255178
SLMAP_HUMAN	SLMAP	physical	24255178
SNX5_HUMAN	SNX5	physical	24255178
STK3_HUMAN	STK3	physical	24255178
STRN_HUMAN	STRN	physical	24255178
STRN3_HUMAN	STRN3	physical	24255178
STRN4_HUMAN	STRN4	physical	24255178
MAP1B_HUMAN	MAP1B	physical	23455922
RASF2_HUMAN	RASSF2	physical	23455922
CDK3_HUMAN	CDK3	physical	23455922
STK3_HUMAN	STK3	physical	23455922
MAP1S_HUMAN	MAP1S	physical	23455922
RASF3_HUMAN	RASSF3	physical	23455922
RB6I2_HUMAN	ERC1	physical	23455922
RASF5_HUMAN	RASSF5	physical	23455922
RASF4_HUMAN	RASSF4	physical	23455922
SAV1_HUMAN	SAV1	physical	23455922
RASF1_HUMAN	RASSF1	physical	23455922
ANXA1_HUMAN	ANXA1	physical	24366813
CDC37_HUMAN	CDC37	physical	24366813
MAP1B_HUMAN	MAP1B	physical	24366813
MAP1S_HUMAN	MAP1S	physical	24366813
STK3_HUMAN	STK3	physical	24366813
RASF1_HUMAN	RASSF1	physical	24366813
RASF2_HUMAN	RASSF2	physical	24366813
RASF3_HUMAN	RASSF3	physical	24366813
RASF4_HUMAN	RASSF4	physical	24366813
RASF5_HUMAN	RASSF5	physical	24366813
RASF6_HUMAN	RASSF6	physical	24366813
SAV1_HUMAN	SAV1	physical	24366813
SLMAP_HUMAN	SLMAP	physical	24366813
STRN_HUMAN	STRN	physical	24366813
VAPA_HUMAN	VAPA	physical	24366813
XPO6_HUMAN	XPO6	physical	24366813
STK3_HUMAN	STK3	physical	26344197
STK4_HUMAN	STK4	physical	21572393
DAXX_HUMAN	DAXX	physical	21572393
H2B2E_HUMAN	HIST2H2BE	physical	21572393
RASF1_HUMAN	RASSF1	physical	26578655
STK4_HUMAN	STK4	physical	26578655
LATS2_HUMAN	LATS2	physical	26898830
DYRK2_HUMAN	DYRK2	physical	27173435
SAV1_HUMAN	SAV1	physical	27173435
KIF3C_HUMAN	KIF3C	physical	27173435
KIF3B_HUMAN	KIF3B	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614868	T-cell immunodeficiency, recurrent infections, and autoimmunity with or without cardiac malformations (TIIAC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STK4_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-320, 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 THR-3; SER-40; TYR-41;THR-175; THR-177; SER-320; SER-327; THR-329; THR-340; THR-353;THR-360; THR-367; THR-380; THR-387; SER-394; SER-410; SER-414; SER-422AND SER-438, AND MASS SPECTROMETRY.	19369195 [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-320, AND MASSSPECTROMETRY.	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-265; SER-320; THR-340;SER-410 AND SER-438, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphoinositide 3-kinase/Akt inhibits MST1-mediated pro-apoptoticsignaling through phosphorylation of threonine 120."; Yuan Z., Kim D., Shu S., Wu J., Guo J., Xiao L., Kaneko S.,Coppola D., Cheng J.Q.; J. Biol. Chem. 285:3815-3824(2010). Cited for: PHOSPHORYLATION AT THR-120.	19940129 [Abstract]
"Akt phosphorylates MstI and prevents its proteolytic activation,blocking FOXO3 phosphorylation and nuclear translocation."; Jang S.W., Yang S.J., Srinivasan S., Ye K.; J. Biol. Chem. 282:30836-30844(2007). Cited for: PHOSPHORYLATION AT THR-387, AND INTERACTION WITH PKB/AKT1.	17726016 [Abstract]
"Regulation of the MST1 kinase by autophosphorylation, by the growthinhibitory proteins, RASSF1 and NORE1, and by Ras."; Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.; Biochem. J. 381:453-462(2004). Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, PHOSPHORYLATION ATTHR-183, MUTAGENESIS OF LYS-59; THR-175; THR-177; THR-183 AND LEU-444,AND INTERACTION WITH RASSF1 AND NORE1.	15109305 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-433, AND MASSSPECTROMETRY.	17192257 [Abstract]

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