dbPTM

HMGA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGA1_HUMAN
UniProt AC	P17096
Protein Name	High mobility group protein HMG-I/HMG-Y
Gene Name	HMGA1
Organism	Homo sapiens (Human).
Sequence Length	107
Subcellular Localization	Nucleus. Chromosome.
Protein Description	HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions..
Protein Sequence	MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSESSSKSS ------CCCCCCCCC	46.30	23401153
2	Acetylation	------MSESSSKSS ------CCCCCCCCC	46.30	-
4	Phosphorylation	----MSESSSKSSQP ----CCCCCCCCCCC	32.38	23401153
5	Phosphorylation	---MSESSSKSSQPL ---CCCCCCCCCCCC	37.42	23401153
6	Phosphorylation	--MSESSSKSSQPLA --CCCCCCCCCCCCC	45.92	23401153
7	Methylation	-MSESSSKSSQPLAS -CCCCCCCCCCCCCC	56.95	19608861
7	Acetylation	-MSESSSKSSQPLAS -CCCCCCCCCCCCCC	56.95	23749302
7	Ubiquitination	-MSESSSKSSQPLAS -CCCCCCCCCCCCCC	56.95	19608861
8	Phosphorylation	MSESSSKSSQPLASK CCCCCCCCCCCCCCH	35.83	23401153
8	ADP-ribosylation	MSESSSKSSQPLASK CCCCCCCCCCCCCCH	35.83	28190768
9	ADP-ribosylation	SESSSKSSQPLASKQ CCCCCCCCCCCCCHH	39.28	28190768
9	Phosphorylation	SESSSKSSQPLASKQ CCCCCCCCCCCCCHH	39.28	22167270
14	Phosphorylation	KSSQPLASKQEKDGT CCCCCCCCHHCCCCC	42.42	22167270
15	Acetylation	SSQPLASKQEKDGTE CCCCCCCHHCCCCCC	57.79	19608861
15	Sumoylation	SSQPLASKQEKDGTE CCCCCCCHHCCCCCC	57.79	28112733
15 (in isoform 1)	Ubiquitination	-	57.79	21906983
15 (in isoform 2)	Ubiquitination	-	57.79	21906983
15 (in isoform 3)	Ubiquitination	-	57.79	21906983
15	Methylation	SSQPLASKQEKDGTE CCCCCCCHHCCCCCC	57.79	19608861
15 (in isoform 2)	Acetylation	-	57.79	-
15	Ubiquitination	SSQPLASKQEKDGTE CCCCCCCHHCCCCCC	57.79	19608861
18	Acetylation	PLASKQEKDGTEKRG CCCCHHCCCCCCCCC	59.99	25953088
21	Phosphorylation	SKQEKDGTEKRGRGR CHHCCCCCCCCCCCC	48.76	26074081
23	Acetylation	QEKDGTEKRGRGRPR HCCCCCCCCCCCCCC	61.05	11793957
23	Methylation	QEKDGTEKRGRGRPR HCCCCCCCCCCCCCC	61.05	-
24	Methylation	EKDGTEKRGRGRPRK CCCCCCCCCCCCCCC	33.53	14987631
26	Methylation	DGTEKRGRGRPRKQP CCCCCCCCCCCCCCC	41.82	12653562
26	Asymmetric dimethylarginine	DGTEKRGRGRPRKQP CCCCCCCCCCCCCCC	41.82	-
31	Acetylation	RGRGRPRKQPPVSPG CCCCCCCCCCCCCCC	70.60	21466224
31	Malonylation	RGRGRPRKQPPVSPG CCCCCCCCCCCCCCC	70.60	26320211
31 (in isoform 1)	Ubiquitination	-	70.60	21906983
31 (in isoform 3)	Ubiquitination	-	70.60	21906983
31	Ubiquitination	RGRGRPRKQPPVSPG CCCCCCCCCCCCCCC	70.60	-
31	Methylation	RGRGRPRKQPPVSPG CCCCCCCCCCCCCCC	70.60	18513496
36	Phosphorylation	PRKQPPVSPGTALVG CCCCCCCCCCCCCCC	24.32	29255136
38 (in isoform 2)	Phosphorylation	-	19.00	23927012
39	Phosphorylation	QPPVSPGTALVGSQK CCCCCCCCCCCCCCC	21.87	22167270
42 (in isoform 2)	Phosphorylation	-	6.86	22167270
44	Phosphorylation	PGTALVGSQKEPSEV CCCCCCCCCCCCCCC	30.51	29255136
46 (in isoform 1)	Ubiquitination	-	73.60	21906983
46 (in isoform 3)	Ubiquitination	-	73.60	21906983
46	"N6,N6-dimethyllysine"	TALVGSQKEPSEVPT CCCCCCCCCCCCCCC	73.60	-
46	Acetylation	TALVGSQKEPSEVPT CCCCCCCCCCCCCCC	73.60	25953088
46	Methylation	TALVGSQKEPSEVPT CCCCCCCCCCCCCCC	73.60	15591590
46	Ubiquitination	TALVGSQKEPSEVPT CCCCCCCCCCCCCCC	73.60	2190698
47	Methylation	ALVGSQKEPSEVPTP CCCCCCCCCCCCCCC	46.55	16293633
49	Phosphorylation	VGSQKEPSEVPTPKR CCCCCCCCCCCCCCC	52.93	22167270
49	Methylation	VGSQKEPSEVPTPKR CCCCCCCCCCCCCCC	52.93	16293633
53	Phosphorylation	KEPSEVPTPKRPRGR CCCCCCCCCCCCCCC	46.77	29255136
53 (in isoform 3)	Phosphorylation	-	46.77	29743597
54	Methylation	EPSEVPTPKRPRGRP CCCCCCCCCCCCCCC	25.29	11498590
54	Acetylation	EPSEVPTPKRPRGRP CCCCCCCCCCCCCCC	25.29	11498590
54 (in isoform 2)	Acetylation	-	25.29	-
55	Acetylation	PSEVPTPKRPRGRPK CCCCCCCCCCCCCCC	77.00	14987645
55	Ubiquitination	PSEVPTPKRPRGRPK CCCCCCCCCCCCCCC	77.00	-
55	Methylation	PSEVPTPKRPRGRPK CCCCCCCCCCCCCCC	77.00	18513496
56 (in isoform 2)	Acetylation	-	27.61	-
58	Asymmetric dimethylarginine	VPTPKRPRGRPKGSK CCCCCCCCCCCCCCC	58.76	-
58	Methylation	VPTPKRPRGRPKGSK CCCCCCCCCCCCCCC	58.76	16159886
60	Asymmetric dimethylarginine	TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC	30.91	-
60 (in isoform 2)	Acetylation	-	30.91	-
60	Methylation	TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC	30.91	16159886
60	Acetylation	TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC	30.91	11498590
62	Methylation	KRPRGRPKGSKNKGA CCCCCCCCCCCCCCC	74.57	-
62	Acetylation	KRPRGRPKGSKNKGA CCCCCCCCCCCCCCC	74.57	14987711
63 (in isoform 2)	Acetylation	-	46.68	-
64	Phosphorylation	PRGRPKGSKNKGAAK CCCCCCCCCCCCCCC	38.90	19317492
65	Sumoylation	RGRPKGSKNKGAAKT CCCCCCCCCCCCCCC	71.93	11498590
65	Acetylation	RGRPKGSKNKGAAKT CCCCCCCCCCCCCCC	71.93	17627840
65	Methylation	RGRPKGSKNKGAAKT CCCCCCCCCCCCCCC	71.93	11498590
67	"N6,N6-dimethyllysine"	RPKGSKNKGAAKTRK CCCCCCCCCCCCCCC	54.38	-
67	Acetylation	RPKGSKNKGAAKTRK CCCCCCCCCCCCCCC	54.38	17627840
67	Methylation	RPKGSKNKGAAKTRK CCCCCCCCCCCCCCC	54.38	15591590
67 (in isoform 2)	Phosphorylation	-	54.38	17960875
71	Methylation	SKNKGAAKTRKTTTT CCCCCCCCCCCCCCC	48.61	11498590
71	Acetylation	SKNKGAAKTRKTTTT CCCCCCCCCCCCCCC	48.61	17627840
72	Phosphorylation	KNKGAAKTRKTTTTP CCCCCCCCCCCCCCC	32.44	19317492
73	Methylation	NKGAAKTRKTTTTPG CCCCCCCCCCCCCCC	33.35	14992439
74	Methylation	KGAAKTRKTTTTPGR CCCCCCCCCCCCCCC	56.29	15591590
74	Acetylation	KGAAKTRKTTTTPGR CCCCCCCCCCCCCCC	56.29	17627840
75	Phosphorylation	GAAKTRKTTTTPGRK CCCCCCCCCCCCCCC	26.53	26657352
76	Phosphorylation	AAKTRKTTTTPGRKP CCCCCCCCCCCCCCC	31.54	26657352
77	Phosphorylation	AKTRKTTTTPGRKPR CCCCCCCCCCCCCCC	35.90	26657352
78	Phosphorylation	KTRKTTTTPGRKPRG CCCCCCCCCCCCCCC	22.96	27273156
81	Dimethylation	KTTTTPGRKPRGRPK CCCCCCCCCCCCCCC	47.19	-
81	Methylation	KTTTTPGRKPRGRPK CCCCCCCCCCCCCCC	47.19	14987731
82	Acetylation	TTTTPGRKPRGRPKK CCCCCCCCCCCCCCC	45.01	14987723
84	Dimethylation	TTPGRKPRGRPKKLE CCCCCCCCCCCCCCH	57.71	-
84	Methylation	TTPGRKPRGRPKKLE CCCCCCCCCCCCCCH	57.71	14987729
86	Dimethylation	PGRKPRGRPKKLEKE CCCCCCCCCCCCHHH	40.94	-
86	Methylation	PGRKPRGRPKKLEKE CCCCCCCCCCCCHHH	40.94	14987745
88	Acetylation	RKPRGRPKKLEKEEE CCCCCCCCCCHHHHH	69.50	14987741
92	Methylation	GRPKKLEKEEEEGIS CCCCCCHHHHHCCCC	79.46	15591590
99	Phosphorylation	KEEEEGISQESSEEE HHHHCCCCCCCHHHC	38.46	29255136
102	Phosphorylation	EEGISQESSEEEQ-- HCCCCCCCHHHCC--	35.10	29255136
103	Phosphorylation	EGISQESSEEEQ--- CCCCCCCHHHCC---	48.55	29255136

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
36	S	Phosphorylation	Kinase	CDK1	P06493	PSP
36	S	Phosphorylation	Kinase	CDK2	P24941	PSP
36	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
42	T	Phosphorylation	Kinase	CDK1	P06493	PSP
42	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
53	T	Phosphorylation	Kinase	CDK1	P06493	PSP
53	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
67	T	Phosphorylation	Kinase	CDK1	P06493	GPS
67	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
78	T	Phosphorylation	Kinase	HIPK2	Q9H2X6	Uniprot
78	T	Phosphorylation	Kinase	CDK1	P06493	PSP
99	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
99	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
102	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
102	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
102	S	Phosphorylation	Kinase	CK	-	Uniprot
102	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
103	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
103	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
103	S	Phosphorylation	Kinase	CK	-	Uniprot
103	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
36	S	Phosphorylation	17081983
Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.
42	T	Phosphorylation	17924679
Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.
53	T	Phosphorylation	17924679
Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.
58	R	Methylation	16159886
Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.
60	R	Methylation	16159886
Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.
67	T	Phosphorylation	17960875
Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.
78	T	Phosphorylation	17960875
Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.

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 HMGA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SP1_HUMAN	SP1	physical	12665574
CEBPB_HUMAN	CEBPB	physical	12665574
ELF1_HUMAN	ELF1	physical	7862168
ATF2_HUMAN	ATF2	physical	10357819
JUN_HUMAN	JUN	physical	10357819
IRF1_HUMAN	IRF1	physical	10357819
CHD1_HUMAN	CHD1	physical	18817785
ANM6_HUMAN	PRMT6	physical	16293633
NPM_HUMAN	NPM1	physical	16293633
PARP1_HUMAN	PARP1	physical	16204234
PO2F1_HUMAN	POU2F1	physical	9823775
PO2F2_HUMAN	POU2F2	physical	9823775
NFKB1_HUMAN	NFKB1	physical	9809067
P53_HUMAN	TP53	physical	20335021
SP1_HUMAN	SP1	physical	20335021
ORC6_HUMAN	ORC6	physical	18234858
ORC2_HUMAN	ORC2	physical	18234858
ORF73_HHV8P	HHV8GK18_gp81	physical	22379092
CBX7_HUMAN	CBX7	physical	22214847
HDAC2_HUMAN	HDAC2	physical	22214847
TERF2_HUMAN	TERF2	physical	22939629
PTBP1_HUMAN	PTBP1	physical	18850631
APEX1_HUMAN	APEX1	physical	18850631
HNRPQ_HUMAN	SYNCRIP	physical	18850631
XRCC6_HUMAN	XRCC6	physical	18850631
PSIP1_HUMAN	PSIP1	physical	18850631
PA2G4_HUMAN	PA2G4	physical	18850631
PCBP2_HUMAN	PCBP2	physical	18850631
HD_HUMAN	HTT	physical	23275563
PPARG_HUMAN	PPARG	physical	22207709

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 HMGA1_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-15, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Dynamics of human protein arginine methyltransferase 1(PRMT1) invivo."; Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O.; J. Biol. Chem. 280:38005-38010(2005). Cited for: METHYLATION AT ARG-58 AND ARG-60 BY PRMT6, AND MUTAGENESIS OF ARG-26;ARG-58 AND ARG-60.	16159886 [Abstract]
"Tandem mass spectrometry for the examination of the posttranslationalmodifications of high-mobility group A1 proteins: symmetric andasymmetric dimethylation of Arg25 in HMGA1a protein."; Zou Y., Wang Y.; Biochemistry 44:6293-6301(2005). Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26,AND MASS SPECTROMETRY.	15835918 [Abstract]
"During apoptosis of tumor cells HMGA1a protein undergoes methylation:identification of the modification site by mass spectrometry."; Sgarra R., Diana F., Bellarosa C., Dekleva V., Rustighi A., Toller M.,Manfioletti G., Giancotti V.; Biochemistry 42:3575-3585(2003). Cited for: PHOSPHORYLATION, METHYLATION AT ARG-26, AND MASS SPECTROMETRY.	12653562 [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-99; SER-102 AND SER-103,AND MASS SPECTROMETRY.	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 SER-102 AND SER-103, ANDMASS SPECTROMETRY.	19369195 [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-36; THR-39 AND THR-53,AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, ANDMASS SPECTROMETRY.	18318008 [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-36; THR-39; SER-44;SER-49; THR-53; SER-99; SER-102 AND SER-103, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, ANDMASS SPECTROMETRY.	19367720 [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-44; SER-99; SER-102 ANDSER-103, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylatesHMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA bindingaffinity."; Zhang Q., Wang Y.; J. Proteome Res. 6:4711-4719(2007). Cited for: PHOSPHORYLATION AT SER-36; THR-53 AND THR-78 BY HIPK2 AND CDK1/CDC2.	17960875 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-53, AND MASSSPECTROMETRY.	17924679 [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 SER-36; SER-99; SER-102 ANDSER-103, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103,AND MASS SPECTROMETRY.	16083285 [Abstract]
"Tandem mass spectrometry for the examination of the posttranslationalmodifications of high-mobility group A1 proteins: symmetric andasymmetric dimethylation of Arg25 in HMGA1a protein."; Zou Y., Wang Y.; Biochemistry 44:6293-6301(2005). Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26,AND MASS SPECTROMETRY.	15835918 [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-99; SER-102 AND SER-103,AND MASS SPECTROMETRY.	15302935 [Abstract]

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