dbPTM

DAB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DAB2_HUMAN
UniProt AC	P98082
Protein Name	Disabled homolog 2
Gene Name	DAB2
Organism	Homo sapiens (Human).
Sequence Length	770
Subcellular Localization	Cytoplasm. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane a
Protein Description	Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor..
Protein Sequence	MSNEVETSATNGQPDQQAAPKAPSKKEKKKGPEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEEKKKIEEASKAVENGSEALMILDDQTNKLKSGVDQMDLFGDMSTPPDLNSPTESKDILLVDLNSEIDTNQNSLRENPFLTNGITSCSLPRPTPQASFLPENAFSANLNFFPTPNPDPFRDDPFTQPDQSTPSSFDSLKSPDQKKENSSSSSTPLSNGPLNGDVDYFGQQFDQISNRTGKQEAQAGPWPFSSSQTQPAVRTQNGVSEREQNGFSVKSSPNPFVGSPPKGLSIQNGVKQDLESSVQSSPHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFAPPVSEPSGQASPTGQPTALQPNPLDLFKTSAPAPVGPLVGLGGVTVTLPQAGPWNTASLVFNQSPSMAPGAMMGGQPSGFSQPVIFGTSPAVSGWNQPSPFAASTPPPVPVVWGPSASVAPNAWSTTSPLGNPFQSNIFPAPAVSTQPPSMHSSLLVTPPQPPPRAGPPKDISSDAFTALDPLGDKEIKDVKEMFKDFQLRQPPAVPARKGEQTSSGTLSAFASYFNSKVGIPQENADHDDFDANQLLNKINEPPKPAPRQVSLPVTKSTDNAFENPFFKDSFGSSQASVASSQPVSSEMYRDPFGNPFA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSNEVETSA ------CCCCCCCCC	41.52	19413330
2	Phosphorylation	------MSNEVETSA ------CCCCCCCCC	41.52	22199227
7	Phosphorylation	-MSNEVETSATNGQP -CCCCCCCCCCCCCC	28.92	25159151
8	Phosphorylation	MSNEVETSATNGQPD CCCCCCCCCCCCCCC	21.42	27486199
10	Phosphorylation	NEVETSATNGQPDQQ CCCCCCCCCCCCCCC	39.38	27486199
24	Phosphorylation	QAAPKAPSKKEKKKG CCCCCCCCHHHHCCC	62.31	28842319
34	Ubiquitination	EKKKGPEKTDEYLLA HHCCCCCCCCHHHHH	65.49	-
38	Phosphorylation	GPEKTDEYLLARFKG CCCCCCHHHHHHHCC	15.15	27642862
53	Malonylation	DGVKYKAKLIGIDDV CCCEEEEEEECCCCC	36.16	26320211
53	Ubiquitination	DGVKYKAKLIGIDDV CCCEEEEEEECCCCC	36.16	-
64	Methylation	IDDVPDARGDKMSQD CCCCCCCCCCCCCHH	62.31	-
67	Acetylation	VPDARGDKMSQDSMM CCCCCCCCCCHHHHH	43.19	7672303
67	Ubiquitination	VPDARGDKMSQDSMM CCCCCCCCCCHHHHH	43.19	-
69	Phosphorylation	DARGDKMSQDSMMKL CCCCCCCCHHHHHHH	36.25	20873877
72	Phosphorylation	GDKMSQDSMMKLKGM CCCCCHHHHHHHHHH	17.09	20873877
77	Ubiquitination	QDSMMKLKGMAAAGR HHHHHHHHHHHHCCC	40.91	-
98	Phosphorylation	QRIWVNISLSGIKII CCEEEEEECCCEEEE	15.98	-
100	Phosphorylation	IWVNISLSGIKIIDE EEEEEECCCEEEEEC	31.51	-
108	Ubiquitination	GIKIIDEKTGVIEHE CEEEEECCCCCEECC	47.00	-
120	Ubiquitination	EHEHPVNKISFIARD ECCCCCCEEEEEEEC	39.70	-
151	Phosphorylation	HQFFAIKTGQQAEPL EEEEEEEECCCCCCE	33.82	22817900
163	Methylation	EPLVVDLKDLFQVIY CCEEEEHHHHHHHHH	48.17	-
170	Phosphorylation	KDLFQVIYNVKKKEE HHHHHHHHHCCCHHH	18.29	25159151
173	Methylation	FQVIYNVKKKEEEKK HHHHHHCCCHHHHHH	55.26	-
193	Phosphorylation	SKAVENGSEALMILD HHHHHHCCCEEEEEE	31.14	25159151
197	Sulfoxidation	ENGSEALMILDDQTN HHCCCEEEEEEHHHC	3.54	30846556
203	Phosphorylation	LMILDDQTNKLKSGV EEEEEHHHCCCCCCC	41.12	28555341
208	Phosphorylation	DQTNKLKSGVDQMDL HHHCCCCCCCCHHHH	55.26	23403867
220	Phosphorylation	MDLFGDMSTPPDLNS HHHCCCCCCCCCCCC	42.37	25159151
221	Phosphorylation	DLFGDMSTPPDLNSP HHCCCCCCCCCCCCC	32.00	25159151
227	Phosphorylation	STPPDLNSPTESKDI CCCCCCCCCCCCCCE	40.26	25159151
229	Phosphorylation	PPDLNSPTESKDILL CCCCCCCCCCCCEEE	53.35	25159151
231	Phosphorylation	DLNSPTESKDILLVD CCCCCCCCCCEEEEE	37.80	25159151
241	Phosphorylation	ILLVDLNSEIDTNQN EEEEECCCCCCCCCC	43.13	20873877
245	Phosphorylation	DLNSEIDTNQNSLRE ECCCCCCCCCCCCCC	44.35	28060719
249	Phosphorylation	EIDTNQNSLRENPFL CCCCCCCCCCCCCCC	21.02	27535140
262	Phosphorylation	FLTNGITSCSLPRPT CCCCCCCCCCCCCCC	10.37	25627689
264	Phosphorylation	TNGITSCSLPRPTPQ CCCCCCCCCCCCCCC	40.97	25159151
301	Phosphorylation	PFRDDPFTQPDQSTP CCCCCCCCCCCCCCC	44.58	23663014
306	Phosphorylation	PFTQPDQSTPSSFDS CCCCCCCCCCCCHHH	50.06	23663014
307	Phosphorylation	FTQPDQSTPSSFDSL CCCCCCCCCCCHHHC	22.89	23663014
309	Phosphorylation	QPDQSTPSSFDSLKS CCCCCCCCCHHHCCC	43.66	23663014
310	Phosphorylation	PDQSTPSSFDSLKSP CCCCCCCCHHHCCCC	33.99	23663014
313	Phosphorylation	STPSSFDSLKSPDQK CCCCCHHHCCCCCCC	35.37	23663014
315	Ubiquitination	PSSFDSLKSPDQKKE CCCHHHCCCCCCCCC	64.99	-
316	Phosphorylation	SSFDSLKSPDQKKEN CCHHHCCCCCCCCCC	38.72	23663014
321	Ubiquitination	LKSPDQKKENSSSSS CCCCCCCCCCCCCCC	57.40	-
324	Phosphorylation	PDQKKENSSSSSTPL CCCCCCCCCCCCCCC	32.46	23663014
325	Phosphorylation	DQKKENSSSSSTPLS CCCCCCCCCCCCCCC	45.91	23663014
326	Phosphorylation	QKKENSSSSSTPLSN CCCCCCCCCCCCCCC	28.29	23663014
327	Phosphorylation	KKENSSSSSTPLSNG CCCCCCCCCCCCCCC	39.93	23663014
328	Phosphorylation	KENSSSSSTPLSNGP CCCCCCCCCCCCCCC	35.67	23663014
329	Phosphorylation	ENSSSSSTPLSNGPL CCCCCCCCCCCCCCC	30.14	23663014
332	Phosphorylation	SSSSTPLSNGPLNGD CCCCCCCCCCCCCCC	40.73	23663014
335 (in isoform 3)	Ubiquitination	-	27.23	-
342	Phosphorylation	PLNGDVDYFGQQFDQ CCCCCCCHHHHHHHH	14.95	23663014
356	Ubiquitination	QISNRTGKQEAQAGP HHHCCCCCHHHHCCC	44.33	-
367	Phosphorylation	QAGPWPFSSSQTQPA HCCCCCCCCCCCCCC	25.63	25159151
368	Phosphorylation	AGPWPFSSSQTQPAV CCCCCCCCCCCCCCE	27.18	25627689
369	Phosphorylation	GPWPFSSSQTQPAVR CCCCCCCCCCCCCEE	35.73	25159151
371	Phosphorylation	WPFSSSQTQPAVRTQ CCCCCCCCCCCEECC	38.17	21712546
390	Phosphorylation	EREQNGFSVKSSPNP HHHHCCCCCCCCCCC	29.99	25159151
392	Ubiquitination	EQNGFSVKSSPNPFV HHCCCCCCCCCCCCC	43.98	-
393	Phosphorylation	QNGFSVKSSPNPFVG HCCCCCCCCCCCCCC	49.20	25463755
394	Phosphorylation	NGFSVKSSPNPFVGS CCCCCCCCCCCCCCC	23.99	25463755
401	Phosphorylation	SPNPFVGSPPKGLSI CCCCCCCCCCCCCEE	32.50	19664994
407	O-linked_Glycosylation	GSPPKGLSIQNGVKQ CCCCCCCEECCCCHH	30.69	30059200
407	Phosphorylation	GSPPKGLSIQNGVKQ CCCCCCCEECCCCHH	30.69	27251789
418	Phosphorylation	GVKQDLESSVQSSPH CCHHHHHHHHCCCCC	43.01	23663014
419	Phosphorylation	VKQDLESSVQSSPHD CHHHHHHHHCCCCCC	18.14	23663014
422	Phosphorylation	DLESSVQSSPHDSIA HHHHHHCCCCCCCEE	43.62	22167270
423	Phosphorylation	LESSVQSSPHDSIAI HHHHHCCCCCCCEEE	14.79	22167270
427	Phosphorylation	VQSSPHDSIAIIPPP HCCCCCCCEEEECCC	15.75	22167270
436	Phosphorylation	AIIPPPQSTKPGRGR EEECCCCCCCCCCCC	44.14	25159151
437	Phosphorylation	IIPPPQSTKPGRGRR EECCCCCCCCCCCCC	35.69	22817900
438	Ubiquitination	IPPPQSTKPGRGRRT ECCCCCCCCCCCCCC	51.20	-
448	Phosphorylation	RGRRTAKSSANDLLA CCCCCCCCHHHHHHH	32.02	20068231
449	Phosphorylation	GRRTAKSSANDLLAS CCCCCCCHHHHHHHH	30.31	20873877
456	Phosphorylation	SANDLLASDIFAPPV HHHHHHHHCCCCCCC	31.07	20068231
464	Phosphorylation	DIFAPPVSEPSGQAS CCCCCCCCCCCCCCC	49.95	23663014
467	Phosphorylation	APPVSEPSGQASPTG CCCCCCCCCCCCCCC	39.21	23663014
471	Phosphorylation	SEPSGQASPTGQPTA CCCCCCCCCCCCCCC	18.33	23663014
473	Phosphorylation	PSGQASPTGQPTALQ CCCCCCCCCCCCCCC	46.05	23663014
477	Phosphorylation	ASPTGQPTALQPNPL CCCCCCCCCCCCCCC	31.92	23663014
633	Phosphorylation	AGPPKDISSDAFTAL CCCCCCCCCCCCHHC	32.09	22199227
634	Phosphorylation	GPPKDISSDAFTALD CCCCCCCCCCCHHCC	33.04	29214152
638	Phosphorylation	DISSDAFTALDPLGD CCCCCCCHHCCCCCC	28.21	23186163
646	Ubiquitination	ALDPLGDKEIKDVKE HCCCCCCHHHHHHHH	60.59	-
652	Ubiquitination	DKEIKDVKEMFKDFQ CHHHHHHHHHHHHCC	54.30	-
670	Ubiquitination	PPAVPARKGEQTSSG CCCCCCCCCCCCCCC	69.75	-
674	Phosphorylation	PARKGEQTSSGTLSA CCCCCCCCCCCHHHH	22.13	21945579
675	Phosphorylation	ARKGEQTSSGTLSAF CCCCCCCCCCHHHHH	26.85	21945579
676	Phosphorylation	RKGEQTSSGTLSAFA CCCCCCCCCHHHHHH	38.90	21945579
678	O-linked_Glycosylation	GEQTSSGTLSAFASY CCCCCCCHHHHHHHH	21.35	30059200
678	Phosphorylation	GEQTSSGTLSAFASY CCCCCCCHHHHHHHH	21.35	21945579
680	Phosphorylation	QTSSGTLSAFASYFN CCCCCHHHHHHHHHH	22.60	21945579
684	Phosphorylation	GTLSAFASYFNSKVG CHHHHHHHHHHHCCC	24.65	21945579
685	Phosphorylation	TLSAFASYFNSKVGI HHHHHHHHHHHCCCC	11.89	21945579
688	Phosphorylation	AFASYFNSKVGIPQE HHHHHHHHCCCCCHH	20.86	21945579
723	O-linked_Glycosylation	KPAPRQVSLPVTKST CCCCCCEECCEECCC	20.72	30059200
723	Phosphorylation	KPAPRQVSLPVTKST CCCCCCEECCEECCC	20.72	25463755
727	O-linked_Glycosylation	RQVSLPVTKSTDNAF CCEECCEECCCCCCC	19.82	30059200
727	Phosphorylation	RQVSLPVTKSTDNAF CCEECCEECCCCCCC	19.82	25463755
728	Ubiquitination	QVSLPVTKSTDNAFE CEECCEECCCCCCCC	52.14	-
729	O-linked_Glycosylation	VSLPVTKSTDNAFEN EECCEECCCCCCCCC	31.46	30059200
729	Phosphorylation	VSLPVTKSTDNAFEN EECCEECCCCCCCCC	31.46	30266825
730	O-linked_Glycosylation	SLPVTKSTDNAFENP ECCEECCCCCCCCCC	34.52	30059200
730	Phosphorylation	SLPVTKSTDNAFENP ECCEECCCCCCCCCC	34.52	30266825
742	Phosphorylation	ENPFFKDSFGSSQAS CCCCHHCCCCCCCHH	31.90	28450419
745	Phosphorylation	FFKDSFGSSQASVAS CHHCCCCCCCHHHHC	19.78	28450419
746	Phosphorylation	FKDSFGSSQASVASS HHCCCCCCCHHHHCC	30.09	28450419
749	O-linked_Glycosylation	SFGSSQASVASSQPV CCCCCCHHHHCCCCC	15.58	30059200
749	Phosphorylation	SFGSSQASVASSQPV CCCCCCHHHHCCCCC	15.58	28450419
752	Phosphorylation	SSQASVASSQPVSSE CCCHHHHCCCCCCHH	27.61	28450419
753	Phosphorylation	SQASVASSQPVSSEM CCHHHHCCCCCCHHH	28.85	28450419
757	Phosphorylation	VASSQPVSSEMYRDP HHCCCCCCHHHHCCC	27.54	28450419
758	Phosphorylation	ASSQPVSSEMYRDPF HCCCCCCHHHHCCCC	26.98	28450419
761	Phosphorylation	QPVSSEMYRDPFGNP CCCCHHHHCCCCCCC	14.07	28450419

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
24	S	Phosphorylation	Kinase	PRKCB	P05771-2	GPS
24	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
24	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
24	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
24	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
723	S	Phosphorylation	Kinase	CAMK2G	Q13555	PSP
723	S	Phosphorylation	Kinase	ROCK2	O75116	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DAB2_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 DAB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DVL3_HUMAN	DVL3	physical	12805222
DVL2_HUMAN	DVL2	physical	12805222
DVL1_HUMAN	DVL1	physical	12805222
AXIN1_HUMAN	AXIN1	physical	12805222
TGFR1_HUMAN	TGFBR1	physical	11387212
TGFR2_HUMAN	TGFBR2	physical	11387212
LDLR_HUMAN	LDLR	physical	11247302
A4_HUMAN	APP	physical	11247302
APLP1_HUMAN	APLP1	physical	11247302
APLP2_HUMAN	APLP2	physical	11247302
SHIP1_HUMAN	INPP5D	physical	11247302
LRP1_HUMAN	LRP1	physical	11247302
MYO6_HUMAN	MYO6	physical	11967127
DAB2P_HUMAN	DAB2IP	physical	11812785
MYO6_HUMAN	MYO6	physical	11906161
CSK_HUMAN	CSK	physical	12473651
SRC_HUMAN	SRC	physical	12473651
FGR_HUMAN	FGR	physical	12473651
SH3K1_HUMAN	SH3KBP1	physical	14596919
MYO6_HUMAN	MYO6	physical	19855435
AP2B1_HUMAN	AP2B1	physical	22323290
FCHO2_HUMAN	FCHO2	physical	22323290
AP2A1_HUMAN	AP2A1	physical	22323290
MYO6_HUMAN	MYO6	physical	22323290
ACOT9_HUMAN	ACOT9	physical	22323290
CLH1_HUMAN	CLTC	physical	22323290
AP2A2_HUMAN	AP2A2	physical	22323290
NU155_HUMAN	NUP155	physical	22323290
SC24B_HUMAN	SEC24B	physical	22323290
PRDX1_HUMAN	PRDX1	physical	22323290
AP2M1_HUMAN	AP2M1	physical	22323290
MALT1_HUMAN	MALT1	physical	22323290
SF3B2_HUMAN	SF3B2	physical	22323290
CCNT1_HUMAN	CCNT1	physical	22323290
YLPM1_HUMAN	YLPM1	physical	22323290
SC23B_HUMAN	SEC23B	physical	22323290
P5CR1_HUMAN	PYCR1	physical	22323290
AURKA_HUMAN	AURKA	physical	22323290
CN166_HUMAN	C14orf166	physical	22323290
CPSF6_HUMAN	CPSF6	physical	22323290
HS105_HUMAN	HSPH1	physical	22323290
TRIO_HUMAN	TRIO	physical	22323290
HNRPL_HUMAN	HNRNPL	physical	22323290
SAHH_HUMAN	AHCY	physical	22323290
GRB2_HUMAN	GRB2	physical	22323290
CPSF7_HUMAN	CPSF7	physical	22323290
ACTB_HUMAN	ACTB	physical	22323290
FCHO2_HUMAN	FCHO2	physical	28514442
SPB4_HUMAN	SERPINB4	physical	28514442

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 DAB2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-394 AND SER-401, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; TYR-170 ANDSER-401, AND MASS SPECTROMETRY.	18187866 [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-393; SER-394 ANDSER-401, AND MASS SPECTROMETRY.	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-342; SER-393 ANDSER-394, AND MASS SPECTROMETRY.	17081983 [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 THR-221; SER-227 ANDSER-401, AND MASS SPECTROMETRY.	15302935 [Abstract]