dbPTM

SHIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHIP1_HUMAN
UniProt AC	Q92835
Protein Name	Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
Gene Name	INPP5D
Organism	Homo sapiens (Human).
Sequence Length	1189
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein . Membrane raft . Cytoplasm, cytoskeleton . Membrane Peripheral membrane protein . Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms dep
Protein Description	Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6..
Protein Sequence	MVPCWNHGNITRSKAEELLSRTGKDGSFLVRASESISRAYALCVLYRNCVYTYRILPNEDDKFTVQASEGVSMRFFTKLDQLIEFYKKENMGLVTHLQYPVPLEEEDTGDDPEEDTVESVVSPPELPPRNIPLTASSCEAKEVPFSNENPRATETSRPSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLAQDSEFVKTGSSSLPHLKKLTTLLCKELYGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEANPINMVSKLSQLTSLLSSIEDKVKALLHEGPESPHRPSLIPPVTFEVKAESLGIPQKMQLKVDVESGKLIIKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAPPCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGESPPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENPLYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPAPRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPRPPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	CWNHGNITRSKAEEL CCCCCCCCHHHHHHH	32.65	28851738
14	Ubiquitination	HGNITRSKAEELLSR CCCCCHHHHHHHHHH	57.43	29967540
20	Phosphorylation	SKAEELLSRTGKDGS HHHHHHHHHHCCCCC	40.18	24719451
24	Ubiquitination	ELLSRTGKDGSFLVR HHHHHHCCCCCEEEE	59.30	-
27	Phosphorylation	SRTGKDGSFLVRASE HHHCCCCCEEEECCH	26.07	28857561
33	Phosphorylation	GSFLVRASESISRAY CCEEEECCHHHHHHH	22.70	26699800
35	Phosphorylation	FLVRASESISRAYAL EEEECCHHHHHHHHH	24.30	26699800
40	Phosphorylation	SESISRAYALCVLYR CHHHHHHHHHHHHHC	10.05	22817900
46	Phosphorylation	AYALCVLYRNCVYTY HHHHHHHHCCCEEEE	4.56	20090780
78	Ubiquitination	VSMRFFTKLDQLIEF CCHHHHHHHHHHHHH	44.93	-
134	Phosphorylation	PPRNIPLTASSCEAK CCCCCCCCCCCCEEE	21.09	29978859
136	Phosphorylation	RNIPLTASSCEAKEV CCCCCCCCCCEEEEC	30.22	28348404
137	Phosphorylation	NIPLTASSCEAKEVP CCCCCCCCCEEEECC	17.32	29970186
141	Ubiquitination	TASSCEAKEVPFSNE CCCCCEEEECCCCCC	36.63	-
170	Phosphorylation	TLFQRLQSMDTSGLP HHHHHHHCCCCCCCC	24.18	28450419
173	Phosphorylation	QRLQSMDTSGLPEEH HHHHCCCCCCCCHHH	18.95	28450419
174	Phosphorylation	RLQSMDTSGLPEEHL HHHCCCCCCCCHHHH	33.78	28450419
182	Ubiquitination	GLPEEHLKAIQDYLS CCCHHHHHHHHHHHH	45.40	-
200	Ubiquitination	AQDSEFVKTGSSSLP HCCCHHHHCCCCCCH	53.11	-
203	Phosphorylation	SEFVKTGSSSLPHLK CHHHHCCCCCCHHHH	23.22	28270605
204	Phosphorylation	EFVKTGSSSLPHLKK HHHHCCCCCCHHHHH	36.92	28270605
205	Phosphorylation	FVKTGSSSLPHLKKL HHHCCCCCCHHHHHH	47.84	28270605
213	Phosphorylation	LPHLKKLTTLLCKEL CHHHHHHHHHHHHHH	25.03	-
221	Phosphorylation	TLLCKELYGEVIRTL HHHHHHHHHHHHHHC	16.60	28064214
227	Phosphorylation	LYGEVIRTLPSLESL HHHHHHHHCCCHHHH	31.71	30622161
230	Phosphorylation	EVIRTLPSLESLQRL HHHHHCCCHHHHHHH	48.13	30622161
233	Phosphorylation	RTLPSLESLQRLFDQ HHCCCHHHHHHHHHC	34.79	30622161
243	Phosphorylation	RLFDQQLSPGLRPRP HHHHCCCCCCCCCCC	16.75	23401153
243	O-linked_Glycosylation	RLFDQQLSPGLRPRP HHHHCCCCCCCCCCC	16.75	30059200
263	Phosphorylation	ANPINMVSKLSQLTS CCCHHHHHHHHHHHH	19.67	23312004
274	Phosphorylation	QLTSLLSSIEDKVKA HHHHHHHHHHHHHHH	29.93	-
289	Phosphorylation	LLHEGPESPHRPSLI HHCCCCCCCCCCCCC	29.19	22115753
294	Phosphorylation	PESPHRPSLIPPVTF CCCCCCCCCCCCEEE	38.60	26307563
300	Phosphorylation	PSLIPPVTFEVKAES CCCCCCEEEEEEHHH	21.61	28857561
307	Phosphorylation	TFEVKAESLGIPQKM EEEEEHHHCCCCCCE	36.43	28060719
312	Ubiquitination	AESLGIPQKMQLKVD HHHCCCCCCEEEEEE	52.51	21890473
313	Ubiquitination	ESLGIPQKMQLKVDV HHCCCCCCEEEEEEE	24.22	21890473
339	Phosphorylation	DGSEDKFYSHKKILQ CCCCCCCCCHHHHHH	18.66	-
364	Ubiquitination	LVILVETEKEKILRK EEEEEECHHHHHHHC	45.79	20972266
364 (in isoform 2)	Ubiquitination	-	45.79	21906983
365	Ubiquitination	VILVETEKEKILRKE EEEEECHHHHHHHCH	72.26	20972266
365	Acetylation	VILVETEKEKILRKE EEEEECHHHHHHHCH	72.26	21466224
371	Acetylation	EKEKILRKEYVFADS HHHHHHHCHHEECCC	50.37	19608861
373	Phosphorylation	EKILRKEYVFADSKK HHHHHCHHEECCCHH	12.14	-
423	Phosphorylation	APPPKKITSWFLSKG CCCCHHHEEEHHHCC	28.87	-
424	Phosphorylation	PPPKKITSWFLSKGQ CCCHHHEEEHHHCCC	21.21	28555341
428	Phosphorylation	KITSWFLSKGQGKTR HHEEEHHHCCCCCCC	25.85	28555341
517	Phosphorylation	VKTGIANTLGNKGAV CCCCHHHCCCCCCCE	27.33	30108239
556	Phosphorylation	KLRRNQNYMNILRFL HHHHCCCHHHHHHHH	5.04	-
566 (in isoform 3)	Ubiquitination	-	38.80	21906983
607	Ubiquitination	ETIIQKIKQQQYADL HHHHHHHHHHHHHHH	49.44	-
611	Phosphorylation	QKIKQQQYADLLSHD HHHHHHHHHHHHCHH	9.57	-
644	Phosphorylation	EITFAPTYRFERLTR HEEECCCCCCEECCC	16.55	-
656	Phosphorylation	LTRDKYAYTKQKATG CCCCCCCCCCCCCCC	16.04	28509920
657	Phosphorylation	TRDKYAYTKQKATGM CCCCCCCCCCCCCCC	20.87	28509920
699	Phosphorylation	STSDIMTSDHSPVFA CHHHCCCCCCCCCEE	18.88	-
737	Phosphorylation	QIEFLRCYATLKTKS HEEEEEEEEEEECCC	9.00	22964224
739	O-linked_Glycosylation	EFLRCYATLKTKSQT EEEEEEEEEECCCCC	11.43	30059200
739	Phosphorylation	EFLRCYATLKTKSQT EEEEEEEEEECCCCC	11.43	22964224
744	Phosphorylation	YATLKTKSQTKFYLE EEEEECCCCCEEEEE	48.60	18077418
744	O-linked_Glycosylation	YATLKTKSQTKFYLE EEEEECCCCCEEEEE	48.60	30059200
754	Phosphorylation	KFYLEFHSSCLESFV EEEEEEHHHHHHHHH	28.24	18077418
755	Phosphorylation	FYLEFHSSCLESFVK EEEEEHHHHHHHHHH	17.72	18077418
763	Phosphorylation	CLESFVKSQEGENEE HHHHHHHCCCCCCCC	28.32	24719451
772	Phosphorylation	EGENEEGSEGELVVK CCCCCCCCCCEEEEE	45.79	23911959
778	Ubiquitination	GSEGELVVKFGETLP CCCCEEEEEECCCCC	7.13	30230243
778 (in isoform 2)	Ubiquitination	-	7.13	21906983
779	Ubiquitination	SEGELVVKFGETLPK CCCEEEEEECCCCCC	39.92	2190698
779 (in isoform 1)	Ubiquitination	-	39.92	21906983
786	Ubiquitination	KFGETLPKLKPIISD EECCCCCCCCCCCCC	72.72	-
796	Phosphorylation	PIISDPEYLLDQHIL CCCCCHHHHHCCEEE	20.25	27259358
834	Phosphorylation	TETQLPIYTPLTHHG ECCCCCEEECCCCCC	10.60	-
835	Phosphorylation	ETQLPIYTPLTHHGE CCCCCEEECCCCCCE	16.73	-
859	Ubiquitination	KLQTSQGKTREKLYD EEECCCCCCHHHHHH	36.45	-
863	Ubiquitination	SQGKTREKLYDFVKT CCCCCHHHHHHHHHH	49.40	-
865	Phosphorylation	GKTREKLYDFVKTER CCCHHHHHHHHHHHC	20.57	28674151
869	Ubiquitination	EKLYDFVKTERDESS HHHHHHHHHHCCCCC	44.66	-
879	Ubiquitination	RDESSGPKTLKSLTS CCCCCCCCCHHHHCC	70.75	-
880	Phosphorylation	DESSGPKTLKSLTSH CCCCCCCCHHHHCCC	42.42	29978859
882	Ubiquitination	SSGPKTLKSLTSHDP CCCCCCHHHHCCCCH	48.96	-
883	Phosphorylation	SGPKTLKSLTSHDPM CCCCCHHHHCCCCHH	39.74	28857561
885	Phosphorylation	PKTLKSLTSHDPMKQ CCCHHHHCCCCHHHC	30.98	23401153
886	Phosphorylation	KTLKSLTSHDPMKQW CCHHHHCCCCHHHCE	31.05	28450419
891	Ubiquitination	LTSHDPMKQWEVTSR HCCCCHHHCEEEEEC	58.61	-
908	Phosphorylation	PCSGSSITEIINPNY CCCCCCHHEECCCCC	24.07	27251275
915	Phosphorylation	TEIINPNYMGVGPFG HEECCCCCCCCCCCC	9.12	28674151
932	Phosphorylation	MPLHVKQTLSPDQQP CCCEEEECCCCCCCC	24.40	28450419
934	Phosphorylation	LHVKQTLSPDQQPTA CEEEECCCCCCCCCC	29.80	23401153
940	Phosphorylation	LSPDQQPTAWSYDQP CCCCCCCCCCCCCCC	36.10	28060719
943	Phosphorylation	DQQPTAWSYDQPPKD CCCCCCCCCCCCCCC	19.17	28060719
944	Phosphorylation	QQPTAWSYDQPPKDS CCCCCCCCCCCCCCC	14.11	28060719
951	Phosphorylation	YDQPPKDSPLGPCRG CCCCCCCCCCCCCCC	28.31	28450419
960	Phosphorylation	LGPCRGESPPTPPGQ CCCCCCCCCCCCCCC	38.72	23401153
963	Phosphorylation	CRGESPPTPPGQPPI CCCCCCCCCCCCCCC	45.56	23401153
971	Phosphorylation	PPGQPPISPKKFLPS CCCCCCCCHHHCCCC	36.12	23401153
974	Ubiquitination	QPPISPKKFLPSTAN CCCCCHHHCCCCCCC	56.36	-
978	Phosphorylation	SPKKFLPSTANRGLP CHHHCCCCCCCCCCC	42.15	-
979	Phosphorylation	PKKFLPSTANRGLPP HHHCCCCCCCCCCCC	26.47	-
988	O-linked_Glycosylation	NRGLPPRTQESRPSD CCCCCCCCCCCCHHH	42.32	30059200
991	O-linked_Glycosylation	LPPRTQESRPSDLGK CCCCCCCCCHHHCCC	39.41	30059200
994	O-linked_Glycosylation	RTQESRPSDLGKNAG CCCCCCHHHCCCCCC	44.34	30059200
1003	Phosphorylation	LGKNAGDTLPQEDLP CCCCCCCCCCHHHCC	39.15	-
1012	Phosphorylation	PQEDLPLTKPEMFEN CHHHCCCCCHHHHCC	42.48	29978859
1022	Phosphorylation	EMFENPLYGSLSSFP HHHCCCCCCCHHCCC	13.11	28674151
1024	Phosphorylation	FENPLYGSLSSFPKP HCCCCCCCHHCCCCC	16.12	27259358
1026	Phosphorylation	NPLYGSLSSFPKPAP CCCCCCHHCCCCCCC	31.46	29978859
1027	Phosphorylation	PLYGSLSSFPKPAPR CCCCCHHCCCCCCCC	51.35	29978859
1039	Phosphorylation	APRKDQESPKMPRKE CCCCCCCCCCCCCCC	24.96	23401153
1045	Ubiquitination	ESPKMPRKEPPPCPE CCCCCCCCCCCCCCC	69.56	-
1057	Phosphorylation	CPEPGILSPSIVLTK CCCCCCCCCEEEEEE	18.06	23401153
1059	Phosphorylation	EPGILSPSIVLTKAQ CCCCCCCEEEEEEHH	23.19	28450419
1063	Phosphorylation	LSPSIVLTKAQEADR CCCEEEEEEHHHCCC	17.28	29978859
1076	Ubiquitination	DRGEGPGKQVPAPRL CCCCCCCCCCCCCCC	51.78	-
1085	Phosphorylation	VPAPRLRSFTCSSSA CCCCCCCEEEECCCC	29.51	23401153
1087	Phosphorylation	APRLRSFTCSSSAEG CCCCCEEEECCCCCC	16.84	28857561
1089	Phosphorylation	RLRSFTCSSSAEGRA CCCEEEECCCCCCCC	25.03	24719451
1090	Phosphorylation	LRSFTCSSSAEGRAA CCEEEECCCCCCCCC	35.40	28348404
1091	Phosphorylation	RSFTCSSSAEGRAAG CEEEECCCCCCCCCC	17.66	28348404
1102	Phosphorylation	RAAGGDKSQGKPKTP CCCCCCCCCCCCCCC	49.24	23312004
1107	Ubiquitination	DKSQGKPKTPVSSQA CCCCCCCCCCCCCCC	69.79	-
1108	Phosphorylation	KSQGKPKTPVSSQAP CCCCCCCCCCCCCCC	37.13	23401153
1111	Phosphorylation	GKPKTPVSSQAPVPA CCCCCCCCCCCCCCC	20.24	23312004
1112	Phosphorylation	KPKTPVSSQAPVPAK CCCCCCCCCCCCCCC	30.51	23312004
1119	Ubiquitination	SQAPVPAKRPIKPSR CCCCCCCCCCCCCCH	53.27	-
1123	Ubiquitination	VPAKRPIKPSRSEIN CCCCCCCCCCHHHHH	39.36	-
1127	Phosphorylation	RPIKPSRSEINQQTP CCCCCCHHHHHCCCC	47.36	29052541
1133	Phosphorylation	RSEINQQTPPTPTPR HHHHHCCCCCCCCCC	22.82	28450419
1136	Phosphorylation	INQQTPPTPTPRPPL HHCCCCCCCCCCCCC	40.78	28450419
1138	Phosphorylation	QQTPPTPTPRPPLPV CCCCCCCCCCCCCCC	34.11	29052541
1140	Methylation	TPPTPTPRPPLPVKS CCCCCCCCCCCCCCC	48.20	115387943
1147	Phosphorylation	RPPLPVKSPAVLHLQ CCCCCCCCCCEEEEE	20.51	23403867
1156	Phosphorylation	AVLHLQHSKGRDYRD CEEEEECCCCCCCCC	24.68	23403867
1157	Ubiquitination	VLHLQHSKGRDYRDN EEEEECCCCCCCCCC	56.70	-
1161	Phosphorylation	QHSKGRDYRDNTELP ECCCCCCCCCCCCCC	20.64	29978859
1165	Phosphorylation	GRDYRDNTELPHHGK CCCCCCCCCCCCCCC	43.09	29978859
1172	Ubiquitination	TELPHHGKHRPEEGP CCCCCCCCCCCCCCC	31.89	-

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
Oops, there are no upstream regulatory protein records of SHIP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SHIP1_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 SHIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DOK1_HUMAN	DOK1	physical	10822173
DOK2_HUMAN	DOK2	physical	10822173
SHC1_HUMAN	SHC1	physical	10822173
LYN_HUMAN	LYN	physical	12882960
CD22_HUMAN	CD22	physical	10748054
KPCD_HUMAN	PRKCD	physical	12024011
PTN11_HUMAN	PTPN11	physical	9110989
SHC1_HUMAN	SHC1	physical	8643691
BCR_HUMAN	BCR	physical	20304029
CLYBL_HUMAN	CLYBL	physical	20304029
CD2AP_HUMAN	CD2AP	physical	22706086
CBL_HUMAN	CBL	physical	22706086
UBS3B_HUMAN	UBASH3B	physical	22267732
NCK1_HUMAN	NCK1	physical	22267732
KSYK_HUMAN	SYK	physical	22267732
PTN11_HUMAN	PTPN11	physical	11157475
SH3K1_HUMAN	SH3KBP1	physical	22815893
DAB1_HUMAN	DAB1	physical	22815893
XIAP_HUMAN	XIAP	physical	22815893
K1H1_HUMAN	KRT31	physical	25416956
KHDR3_HUMAN	KHDRBS3	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956

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 SHIP1_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-371, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-865 AND TYR-1022, ANDMASS SPECTROMETRY.	18083107 [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-915, AND MASSSPECTROMETRY.	15592455 [Abstract]