dbPTM

CTND1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CTND1_MOUSE
UniProt AC	P30999
Protein Name	Catenin delta-1
Gene Name	Ctnnd1
Organism	Mus musculus (Mouse).
Sequence Length	938
Subcellular Localization	Cytoplasm . Nucleus . Cell membrane . Interaction with GLIS2 promotes nuclear translocation (PubMed:17344476). Detected at cell-cell contacts (By similarity). NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm (By simil
Protein Description	Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage..
Protein Sequence	MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANSLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHNHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETTDDGTTRRTETTVKKVVKTMTTRTVQPVPMGPDGLPVDASAVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYGRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPPDQYYWAPLAQHERGSLASLDSLRKGMPPPSNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPILVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEALPTVANSTGPHAASCFGAKKGKDEWFSRGKKPTEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIAELLTSEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVVSILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIPMSNMGSNTKSLDNNYSTLNERGDHNRTLDRSGDLGDMEPLKGAPLMQKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDSEVES -------CCHHHHHH	13.42	-
4	Phosphorylation	----MDDSEVESTAS ----CCHHHHHHHHH	39.00	25619855
8	Phosphorylation	MDDSEVESTASILAS CCHHHHHHHHHHHHH	34.15	25619855
9	Phosphorylation	DDSEVESTASILASV CHHHHHHHHHHHHHH	15.77	25619855
11	Phosphorylation	SEVESTASILASVKE HHHHHHHHHHHHHHH	20.44	25619855
15	Phosphorylation	STASILASVKEQEAQ HHHHHHHHHHHHHHH	30.21	25619855
25	Ubiquitination	EQEAQFEKLTRALEE HHHHHHHHHHHHHHH	57.35	22790023
38	Phosphorylation	EEERRHVSAQLERVR HHHHHHHHHHHHEEE	12.27	22324799
47	Phosphorylation	QLERVRVSPQDANSL HHHEEECCHHHHHHH	13.28	25521595
53	Phosphorylation	VSPQDANSLMANGTL CCHHHHHHHHHCCCE	22.65	25619855
59	Phosphorylation	NSLMANGTLTRRHQN HHHHHCCCEEEECCC	25.43	25521595
61	Phosphorylation	LMANGTLTRRHQNGR HHHCCCEEEECCCCC	26.04	25619855
81	Phosphorylation	DLERQKFSDLKLNGP HHCCCCCCCCCCCCC	49.41	29514104
84	Ubiquitination	RQKFSDLKLNGPQDH CCCCCCCCCCCCCCC	44.92	22790023
96	Phosphorylation	QDHNHLLYSTIPRMQ CCCCHHHHEECCCCC	15.32	18515860
97	Phosphorylation	DHNHLLYSTIPRMQE CCCHHHHEECCCCCC	21.60	22499769
98	Phosphorylation	HNHLLYSTIPRMQEP CCHHHHEECCCCCCC	22.80	22499769
112	Phosphorylation	PGQIVETYTEEDPEG CCCEEEEECCCCCCC	9.92	17194753
122	Phosphorylation	EDPEGAMSVVSVETT CCCCCCEEEEEEEEC	20.87	12885254
125	Phosphorylation	EGAMSVVSVETTDDG CCCEEEEEEEECCCC	16.45	27087446
128	Phosphorylation	MSVVSVETTDDGTTR EEEEEEEECCCCCCE	33.11	27087446
140	Phosphorylation	TTRRTETTVKKVVKT CCEEEHHHHHHHHHH	24.89	20139300
150	Phosphorylation	KVVKTMTTRTVQPVP HHHHHCCCCCCCCCC	17.33	20139300
152	Phosphorylation	VKTMTTRTVQPVPMG HHHCCCCCCCCCCCC	22.77	25619855
168	Phosphorylation	DGLPVDASAVSNNYI CCCCCCHHHHCCCHH	25.41	25619855
171	Phosphorylation	PVDASAVSNNYIQTL CCCHHHHCCCHHHHH	21.05	25619855
174	Phosphorylation	ASAVSNNYIQTLGRD HHHHCCCHHHHHCCC	9.92	25619855
177	Phosphorylation	VSNNYIQTLGRDFRK HCCCHHHHHCCCHHH	22.94	25619855
184	Ubiquitination	TLGRDFRKNGNGGPG HHCCCHHHCCCCCCC	70.02	22790023
193	Phosphorylation	GNGGPGPYVGQAGTA CCCCCCCCCCCCCCC	24.11	25619855
199	Phosphorylation	PYVGQAGTATLPRNF CCCCCCCCCCCCCCC	21.34	25619855
201	Phosphorylation	VGQAGTATLPRNFHY CCCCCCCCCCCCCCC	36.81	25521595
208	Phosphorylation	TLPRNFHYPPDGYGR CCCCCCCCCCCCCCC	16.60	29514104
217	Phosphorylation	PDGYGRHYEDGYPGG CCCCCCCCCCCCCCC	17.85	25619855
221	Phosphorylation	GRHYEDGYPGGSDNY CCCCCCCCCCCCCCC	15.83	25619855
225	Phosphorylation	EDGYPGGSDNYGSLS CCCCCCCCCCCCCHH	28.70	27087446
228	Phosphorylation	YPGGSDNYGSLSRVT CCCCCCCCCCHHHHH	17.06	18515860
230	Phosphorylation	GGSDNYGSLSRVTRI CCCCCCCCHHHHHHH	16.89	27087446
232	Phosphorylation	SDNYGSLSRVTRIEE CCCCCCHHHHHHHHH	26.80	25521595
241	Phosphorylation	VTRIEERYRPSMEGY HHHHHHHHCCCCCCC	30.10	27717184
244	Phosphorylation	IEERYRPSMEGYRAP HHHHHCCCCCCCCCC	22.07	28973931
248	Phosphorylation	YRPSMEGYRAPSRQD HCCCCCCCCCCCCCC	7.12	29514104
252	Phosphorylation	MEGYRAPSRQDVYGP CCCCCCCCCCCCCCC	41.40	25521595
257	Phosphorylation	APSRQDVYGPQPQVR CCCCCCCCCCCCEEE	31.23	18515860
268	Phosphorylation	PQVRVGGSSVDLHRF CEEEECCCEEEHHHC	22.66	27087446
269	Phosphorylation	QVRVGGSSVDLHRFH EEEECCCEEEHHHCC	23.95	25521595
280	Phosphorylation	HRFHPEPYGLEDDQR HHCCCCCCCCCCCCC	32.45	18515860
288	Phosphorylation	GLEDDQRSMGYDDLD CCCCCCCCCCCCCCC	15.78	25521595
291	Phosphorylation	DDQRSMGYDDLDYGM CCCCCCCCCCCCCCC	9.53	27087446
296	Phosphorylation	MGYDDLDYGMMSDYG CCCCCCCCCCCCCCC	17.76	18515860
300	Phosphorylation	DLDYGMMSDYGTARR CCCCCCCCCCCCCCC	20.84	26643407
302	Phosphorylation	DYGMMSDYGTARRTG CCCCCCCCCCCCCCC	14.74	26643407
304	Phosphorylation	GMMSDYGTARRTGTP CCCCCCCCCCCCCCC	15.68	26643407
308	Phosphorylation	DYGTARRTGTPSDPR CCCCCCCCCCCCCHH	39.59	21743459
310	Phosphorylation	GTARRTGTPSDPRRR CCCCCCCCCCCHHHH	21.00	27087446
312	Phosphorylation	ARRTGTPSDPRRRLR CCCCCCCCCHHHHHH	61.15	12885254
320	Phosphorylation	DPRRRLRSYEDMIGE CHHHHHHCHHHHHCC	37.15	27087446
321	Phosphorylation	PRRRLRSYEDMIGEE HHHHHHCHHHHHCCC	14.98	18515860
334	Phosphorylation	EEVPPDQYYWAPLAQ CCCCHHHCCCCCHHC	14.35	18515860
335	Phosphorylation	EVPPDQYYWAPLAQH CCCHHHCCCCCHHCC	6.89	18515860
346	Phosphorylation	LAQHERGSLASLDSL HHCCCCCCCCHHHHH	27.30	25521595
349	Phosphorylation	HERGSLASLDSLRKG CCCCCCCHHHHHHCC	37.69	27087446
352	Phosphorylation	GSLASLDSLRKGMPP CCCCHHHHHHCCCCC	35.05	27087446
355	Ubiquitination	ASLDSLRKGMPPPSN CHHHHHHCCCCCCCC	65.93	22790023
383	Ubiquitination	GFRLDAVKSNAAAYL CCCHHHHHHCHHHHH	39.45	22790023
394	S-nitrosocysteine	AAYLQHLCYRNDKVK HHHHHHHHHCCCCHH	2.55	-
394	S-nitrosylation	AAYLQHLCYRNDKVK HHHHHHHHHCCCCHH	2.55	20925432
394	S-palmitoylation	AAYLQHLCYRNDKVK HHHHHHHHHCCCCHH	2.55	28526873
421	Ubiquitination	VGLLDHPKKEVHLGA EECCCCCCCEEEHHH	59.14	22790023
429	S-nitrosocysteine	KEVHLGACGALKNIS CEEEHHHCCCCCCCC	2.88	-
429	S-nitrosylation	KEVHLGACGALKNIS CEEEHHHCCCCCCCC	2.88	20925432
433	Ubiquitination	LGACGALKNISFGRD HHHCCCCCCCCCCCC	52.26	22790023
450	S-nitrosocysteine	NKIAIKNCDGVPALV CCEEEECCCHHHHHH	4.01	-
450	S-nitrosylation	NKIAIKNCDGVPALV CCEEEECCCHHHHHH	4.01	21278135
517	Acetylation	REPNEDCKPRHIEWE CCCCCCCCCCCCCHH	58.36	23201123
517	Ubiquitination	REPNEDCKPRHIEWE CCCCCCCCCCCCCHH	58.36	22790023
533	S-nitrosocysteine	VLTNTAGCLRNVSSE HHHHHHHHHHCCCHH	2.75	-
533	Glutathionylation	VLTNTAGCLRNVSSE HHHHHHHHHHCCCHH	2.75	24333276
533	S-nitrosylation	VLTNTAGCLRNVSSE HHHHHHHHHHCCCHH	2.75	20925432
533	S-palmitoylation	VLTNTAGCLRNVSSE HHHHHHHHHHCCCHH	2.75	28526873
579	S-palmitoylation	DSKLVENCVCLLRNL CCHHHHHHHHHHHHH	1.13	28526873
581	S-palmitoylation	KLVENCVCLLRNLSY HHHHHHHHHHHHHHH	3.01	28526873
587	Phosphorylation	VCLLRNLSYQVHREI HHHHHHHHHHHHHHC	19.64	26370283
600	Phosphorylation	EIPQAERYQEALPTV HCCHHHHHHHHCCCH	11.38	29514104
617	Phosphorylation	STGPHAASCFGAKKG CCCCCHHHHCCCCCC	15.68	19060867
617 (in isoform 2)	Phosphorylation	-	15.68	30352176
618	Glutathionylation	TGPHAASCFGAKKGK CCCCHHHHCCCCCCC	2.90	24333276
618	S-palmitoylation	TGPHAASCFGAKKGK CCCCHHHHCCCCCCC	2.90	28526873
622	Acetylation	AASCFGAKKGKDEWF HHHHCCCCCCCCCCC	63.54	7378465
622	Ubiquitination	AASCFGAKKGKDEWF HHHHCCCCCCCCCCC	63.54	22790023
623	Acetylation	ASCFGAKKGKDEWFS HHHCCCCCCCCCCCC	71.33	30585493
625	Acetylation	CFGAKKGKDEWFSRG HCCCCCCCCCCCCCC	62.44	34783199
633	Ubiquitination	DEWFSRGKKPTEDPA CCCCCCCCCCCCCCC	55.24	22790023
634	Ubiquitination	EWFSRGKKPTEDPAN CCCCCCCCCCCCCCC	61.06	22790023
636	Phosphorylation	FSRGKKPTEDPANDT CCCCCCCCCCCCCCC	63.00	-
643	Phosphorylation	TEDPANDTVDFPKRT CCCCCCCCCCCCCCC	23.06	29550500
650	Phosphorylation	TVDFPKRTSPARGYE CCCCCCCCCCCCCCH	45.23	23984901
651	Phosphorylation	VDFPKRTSPARGYEL CCCCCCCCCCCCCHH	22.16	23984901
656	Phosphorylation	RTSPARGYELLFQPE CCCCCCCCHHHCCHH	9.61	26643407
676	Ubiquitination	ISLLKESKTPAILEA HHHHHCCCCCHHHHH	60.67	22790023
692	Glutathionylation	AGAIQNLCAGRWTYG HHHHHHHHCCHHHHH	5.04	24333276
692	S-palmitoylation	AGAIQNLCAGRWTYG HHHHHHHHCCHHHHH	5.04	28526873
710	Ubiquitination	RSALRQEKALSAIAE HHHHHHHHHHHHHHH	46.41	22790023
713	Phosphorylation	LRQEKALSAIAELLT HHHHHHHHHHHHHHH	23.61	26824392
728	Ubiquitination	SEHERVVKAASGALR HHHHHHHHHHHHHHH	35.06	22790023
749	Ubiquitination	RNKELIGKHAIPNLV CCHHHHHHHHCCCHH	23.91	22790023
810	Ubiquitination	EKLVLINKSGNRSEK CEEEEEECCCCCCHH	53.39	22790023
811	Phosphorylation	KLVLINKSGNRSEKE EEEEEECCCCCCHHH	36.49	-
847	Phosphorylation	EKEGWKKSDFQVNLN HHCCCCHHCEEEECC	39.67	25521595
853	Phosphorylation	KSDFQVNLNNASRSQ HHCEEEECCCCCCCC	5.70	17242355
857	Phosphorylation	QVNLNNASRSQSSHS EEECCCCCCCCCCCC	34.29	26824392
859	Phosphorylation	NLNNASRSQSSHSYD ECCCCCCCCCCCCCC	31.73	27087446
861	Phosphorylation	NNASRSQSSHSYDDS CCCCCCCCCCCCCCC	31.12	27087446
862	Phosphorylation	NASRSQSSHSYDDST CCCCCCCCCCCCCCC	14.60	27087446
862 (in isoform 2)	Phosphorylation	-	14.60	29514104
863 (in isoform 2)	Phosphorylation	-	35.31	26824392
864	Phosphorylation	SRSQSSHSYDDSTLP CCCCCCCCCCCCCCC	32.00	27087446
865	Phosphorylation	RSQSSHSYDDSTLPL CCCCCCCCCCCCCCC	20.53	27742792
868	Phosphorylation	SSHSYDDSTLPLIDR CCCCCCCCCCCCCCC	29.01	27087446
868 (in isoform 3)	Phosphorylation	-	29.01	29514104
869	Phosphorylation	SHSYDDSTLPLIDRN CCCCCCCCCCCCCCC	39.11	27087446
869 (in isoform 3)	Phosphorylation	-	39.11	26824392
873 (in isoform 2)	Phosphorylation	-	4.40	27149854
877 (in isoform 2)	Phosphorylation	-	47.74	22499769
878 (in isoform 2)	Phosphorylation	-	65.26	22499769
878 (in isoform 3)	Ubiquitination	-	65.26	-
879	Phosphorylation	LIDRNQKSDKKPDRE CCCCCCCCCCCCCHH	44.92	12885254
879 (in isoform 2)	Phosphorylation	-	44.92	22499769
879 (in isoform 3)	Phosphorylation	-	44.92	27149854
883 (in isoform 3)	Phosphorylation	-	52.19	22499769
884 (in isoform 3)	Phosphorylation	-	78.49	22499769
885 (in isoform 3)	Phosphorylation	-	52.56	22499769
889 (in isoform 2)	Phosphorylation	-	24.35	26239621
895 (in isoform 3)	Phosphorylation	-	30.47	26239621
898	Ubiquitination	SNMGSNTKSLDNNYS CCCCCCCCCCCCCCC	53.95	22790023
899	Phosphorylation	NMGSNTKSLDNNYST CCCCCCCCCCCCCCC	38.63	25521595
904	Phosphorylation	TKSLDNNYSTLNERG CCCCCCCCCCCHHCC	14.86	26824392
905	Phosphorylation	KSLDNNYSTLNERGD CCCCCCCCCCHHCCC	28.65	18515860
906	Phosphorylation	SLDNNYSTLNERGDH CCCCCCCCCHHCCCC	24.20	25521595
916	Phosphorylation	ERGDHNRTLDRSGDL HCCCCCCCCCCCCCC	38.02	27087446
920	Phosphorylation	HNRTLDRSGDLGDME CCCCCCCCCCCCCCC	36.00	25521595
930	Ubiquitination	LGDMEPLKGAPLMQK CCCCCCCCCCCCCCC	64.84	22790023

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
96	Y	Phosphorylation	Kinase	SRC	P05480	PSP
96	Y	Phosphorylation	Kinase	FYN	P06241	PSP
96	Y	Phosphorylation	Kinase	SRC	P12931	PSP
112	Y	Phosphorylation	Kinase	FYN	P06241	PSP
112	Y	Phosphorylation	Kinase	SRC	P05480	PSP
112	Y	Phosphorylation	Kinase	FYN	P39688	Uniprot
217	Y	Phosphorylation	Kinase	SRC	P12931	PSP
228	Y	Phosphorylation	Kinase	SRC	P12931	PSP
228	Y	Phosphorylation	Kinase	SRC	P05480	PSP
228	Y	Phosphorylation	Kinase	FYN	P06241	PSP
252	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
257	Y	Phosphorylation	Kinase	SRC	P05480	PSP
280	Y	Phosphorylation	Kinase	SRC	P05480	PSP
291	Y	Phosphorylation	Kinase	SRC	P05480	PSP
296	Y	Phosphorylation	Kinase	SRC	P05480	PSP
302	Y	Phosphorylation	Kinase	SRC	P05480	PSP
310	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
879	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
288	S	Phosphorylation		17242355
Phosphorylated at Ser-288 by PAK5.

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 CTND1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTNB1_MOUSE	Ctnnb1	physical	12695331
KIFA3_MOUSE	Kifap3	physical	15834408
KIF3B_MOUSE	Kif3b	physical	15834408
CADH2_MOUSE	Cdh2	physical	15834408
CTNB1_MOUSE	Ctnnb1	physical	15834408
KAISO_MOUSE	Zbtb33	physical	15282317
GSK3A_MOUSE	Gsk3a	physical	19706605
GSK3B_MOUSE	Gsk3b	physical	19706605
RGRF1_MOUSE	Rasgrf1	physical	17993462

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CTND1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; TYR-257; SER-349;SER-352 AND TYR-904, AND MASS SPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-252; SER-269;SER-346; SER-349; SER-352; SER-857; SER-864 AND SER-920, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; TYR-291; SER-320;SER-349; SER-352; SER-859 AND TYR-865, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, AND MASSSPECTROMETRY.	17947660 [Abstract]

show