dbPTM

PELP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PELP1_HUMAN
UniProt AC	Q8IZL8
Protein Name	Proline-, glutamic acid- and leucine-rich protein 1
Gene Name	PELP1
Organism	Homo sapiens (Human).
Sequence Length	1130
Subcellular Localization	Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus. Cytoplasm. Mainly found in the nucleoplasm, with low levels detected in the cytoplasm (By similarity). Also found associated with the plasma membrane. Mainly in cytoplasm in a subset of breast tumo
Protein Description	Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence-specific transcription factors. Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Involved in nuclear receptor signaling via its interaction with AR and NR3C1. May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K. Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit. Regulates pre-60S association of the critical remodeling factor MDN1. [PubMed: 21326211]
Protein Sequence	MAAAVLSGPSAGSAAGVPGGTGGLSAVSSGPRLRLLLLESVSGLLQPRTGSAVAPVHPPNRSAPHLPGLMCLLRLHGSVGGAQNLSALGALVSLSNARLSSIKTRFEGLCLLSLLVGESPTELFQQHCVSWLRSIQQVLQTQDPPATMELAVAVLRDLLRYAAQLPALFRDISMNHLPGLLTSLLGLRPECEQSALEGMKACMTYFPRACGSLKGKLASFFLSRVDALSPQLQQLACECYSRLPSLGAGFSQGLKHTESWEQELHSLLASLHTLLGALYEGAETAPVQNEGPGVEMLLSSEDGDAHVLLQLRQRFSGLARCLGLMLSSEFGAPVSVPVQEILDFICRTLSVSSKNISLHGDGPLRLLLLPSIHLEALDLLSALILACGSRLLRFGILIGRLLPQVLNSWSIGRDSLSPGQERPYSTVRTKVYAILELWVQVCGASAGMLQGGASGEALLTHLLSDISPPADALKLRSPRGSPDGSLQTGKPSAPKKLKLDVGEAMAPPSHRKGDSNANSDVCAAALRGLSRTILMCGPLIKEETHRRLHDLVLPLVMGVQQGEVLGSSPYTSSRCRRELYCLLLALLLAPSPRCPPPLACALQAFSLGQREDSLEVSSFCSEALVTCAALTHPRVPPLQPMGPTCPTPAPVPPPEAPSPFRAPPFHPPGPMPSVGSMPSAGPMPSAGPMPSAGPVPSARPGPPTTANHLGLSVPGLVSVPPRLLPGPENHRAGSNEDPILAPSGTPPPTIPPDETFGGRVPRPAFVHYDKEEASDVEISLESDSDDSVVIVPEGLPPLPPPPPSGATPPPIAPTGPPTASPPVPAKEEPEELPAAPGPLPPPPPPPPPVPGPVTLPPPQLVPEGTPGGGGPPALEEDLTVININSSDEEEEEEEEEEEEEEEEEEEEEDFEEEEEDEEEYFEEEEEEEEEFEEEFEEEEGELEEEEEEEDEEEEEELEEVEDLEFGTAGGEVEEGAPPPPTLPPALPPPESPPKVQPEPEPEPGLLLEVEEPGTEEERGADTAPTLAPEALPSQGEVEREGESPAAGPPPQELVEEEPSAPPTLLEEETEDGSDKVQPPPETPAEEEMETETEAEALQEKEQDDTAAMLADFIDCPPDDEKPPPPTEPDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAVLSGP ------CCCCHHCCC	18.55	22223895
7	Phosphorylation	-MAAAVLSGPSAGSA -CCCCHHCCCCCCCC	41.90	19664995
10	Phosphorylation	AAVLSGPSAGSAAGV CCHHCCCCCCCCCCC	49.11	25850435
13	Phosphorylation	LSGPSAGSAAGVPGG HCCCCCCCCCCCCCC	18.05	25850435
21	Phosphorylation	AAGVPGGTGGLSAVS CCCCCCCCCCHHHHC	33.71	25850435
25	Phosphorylation	PGGTGGLSAVSSGPR CCCCCCHHHHCCCHH	29.87	25850435
28	Phosphorylation	TGGLSAVSSGPRLRL CCCHHHHCCCHHHEE	29.33	25850435
29	Phosphorylation	GGLSAVSSGPRLRLL CCHHHHCCCHHHEEE	46.33	27732954
32	Methylation	SAVSSGPRLRLLLLE HHHCCCHHHEEEHHH	35.65	115387635
34	Methylation	VSSGPRLRLLLLESV HCCCHHHEEEHHHHH	25.27	115387643
40	Phosphorylation	LRLLLLESVSGLLQP HEEEHHHHHHCCCCC	22.88	24670416
42	Phosphorylation	LLLLESVSGLLQPRT EEHHHHHHCCCCCCC	32.76	24670416
49	O-linked_Glycosylation	SGLLQPRTGSAVAPV HCCCCCCCCCCCCCC	42.02	30059200
49	Phosphorylation	SGLLQPRTGSAVAPV HCCCCCCCCCCCCCC	42.02	21955146
51	Phosphorylation	LLQPRTGSAVAPVHP CCCCCCCCCCCCCCC	20.96	29396449
62	Phosphorylation	PVHPPNRSAPHLPGL CCCCCCCCCCCCCHH	53.44	21955146
82	Methylation	LHGSVGGAQNLSALG HCCCCCHHHCHHHHH	6.80	-
84	Methylation	GSVGGAQNLSALGAL CCCCHHHCHHHHHHH	35.11	-
86	Phosphorylation	VGGAQNLSALGALVS CCHHHCHHHHHHHHH	29.06	-
90	Phosphorylation	QNLSALGALVSLSNA HCHHHHHHHHHHHCC	12.97	-
92	Phosphorylation	LSALGALVSLSNARL HHHHHHHHHHHCCCH	5.54	-
100	Phosphorylation	SLSNARLSSIKTRFE HHHCCCHHHCHHHHH	25.19	24719451
101	Phosphorylation	LSNARLSSIKTRFEG HHCCCHHHCHHHHHH	32.47	-
103	Ubiquitination	NARLSSIKTRFEGLC CCCHHHCHHHHHHHH	35.28	-
104	Phosphorylation	ARLSSIKTRFEGLCL CCHHHCHHHHHHHHH	38.63	-
216	Acetylation	ACGSLKGKLASFFLS HHHCCHHHHHHHHHH	39.01	25953088
216	Ubiquitination	ACGSLKGKLASFFLS HHHCCHHHHHHHHHH	39.01	-
216 (in isoform 2)	Ubiquitination	-	39.01	-
251	Phosphorylation	PSLGAGFSQGLKHTE CHHCCCCCCCCCCCH	23.56	-
266	Ubiquitination	SWEQELHSLLASLHT HHHHHHHHHHHHHHH	37.39	-
353	Phosphorylation	CRTLSVSSKNISLHG HHHCCCCCCCEEECC	27.80	28555341
354	Acetylation	RTLSVSSKNISLHGD HHCCCCCCCEEECCC	51.28	26051181
354	Malonylation	RTLSVSSKNISLHGD HHCCCCCCCEEECCC	51.28	26320211
354	Ubiquitination	RTLSVSSKNISLHGD HHCCCCCCCEEECCC	51.28	-
396 (in isoform 2)	Phosphorylation	-	2.02	21406692
404	Ubiquitination	LIGRLLPQVLNSWSI HHHHHHHHHHHHCCC	52.91	-
404 (in isoform 1)	Ubiquitination	-	52.91	21906983
426	O-linked_Glycosylation	GQERPYSTVRTKVYA CCCCCCHHHHHHHHH	14.25	30059200
477	Phosphorylation	ADALKLRSPRGSPDG HHHHCCCCCCCCCCC	29.41	22167270
481	Phosphorylation	KLRSPRGSPDGSLQT CCCCCCCCCCCCCCC	22.54	29255136
485	Phosphorylation	PRGSPDGSLQTGKPS CCCCCCCCCCCCCCC	25.37	20201521
488	Phosphorylation	SPDGSLQTGKPSAPK CCCCCCCCCCCCCCC	53.09	23927012
490	Acetylation	DGSLQTGKPSAPKKL CCCCCCCCCCCCCCE	38.90	26051181
492	Phosphorylation	SLQTGKPSAPKKLKL CCCCCCCCCCCCEEC	61.77	23927012
495	Acetylation	TGKPSAPKKLKLDVG CCCCCCCCCEECCCC	71.15	26051181
505	Sulfoxidation	KLDVGEAMAPPSHRK ECCCCCCCCCCCCCC	5.11	21406390
509	Phosphorylation	GEAMAPPSHRKGDSN CCCCCCCCCCCCCCC	34.56	24505115
512	Ubiquitination	MAPPSHRKGDSNANS CCCCCCCCCCCCCCH	62.74	-
515	Phosphorylation	PSHRKGDSNANSDVC CCCCCCCCCCCHHHH	46.65	24144214
519	Phosphorylation	KGDSNANSDVCAAAL CCCCCCCHHHHHHHH	29.07	24144214
527	Phosphorylation	DVCAAALRGLSRTIL HHHHHHHHHHHHHHH	39.00	20068231
531	Phosphorylation	AALRGLSRTILMCGP HHHHHHHHHHHHHCC	30.72	19664995
535	Phosphorylation	GLSRTILMCGPLIKE HHHHHHHHHCCCCCH	1.88	20068231
538	Phosphorylation	RTILMCGPLIKEETH HHHHHHCCCCCHHHH	26.45	17081983
540	Ubiquitination	ILMCGPLIKEETHRR HHHHCCCCCHHHHHH	6.25	-
541	2-Hydroxyisobutyrylation	LMCGPLIKEETHRRL HHHCCCCCHHHHHHH	58.12	-
542	Phosphorylation	MCGPLIKEETHRRLH HHCCCCCHHHHHHHH	62.22	17081983
545	Ubiquitination	PLIKEETHRRLHDLV CCCCHHHHHHHHHHH	19.02	-
562	Ubiquitination	LVMGVQQGEVLGSSP HHHCCCCCCCCCCCC	15.19	-
591	Ubiquitination	LALLLAPSPRCPPPL HHHHHCCCCCCCHHH	21.26	-
626	Phosphorylation	FCSEALVTCAALTHP HHHHHHHHHHHHCCC	9.40	22798277
641 (in isoform 2)	Ubiquitination	-	6.91	-
644	Phosphorylation	PLQPMGPTCPTPAPV CCCCCCCCCCCCCCC	25.95	29978859
647	Phosphorylation	PMGPTCPTPAPVPPP CCCCCCCCCCCCCCC	33.94	29978859
657 (in isoform 2)	Ubiquitination	-	40.65	-
658	Phosphorylation	VPPPEAPSPFRAPPF CCCCCCCCCCCCCCC	43.66	29255136
686 (in isoform 2)	Ubiquitination	-	21.90	-
697	Phosphorylation	PSAGPVPSARPGPPT CCCCCCCCCCCCCCC	36.82	-
704	O-linked_Glycosylation	SARPGPPTTANHLGL CCCCCCCCCCCCCCC	41.49	30059200
708	Phosphorylation	GPPTTANHLGLSVPG CCCCCCCCCCCCCCC	20.86	-
718	Phosphorylation	LSVPGLVSVPPRLLP CCCCCCCCCCCCCCC	33.67	23312004
734	Phosphorylation	PENHRAGSNEDPILA CCCCCCCCCCCCCCC	35.74	30266825
743	Phosphorylation	EDPILAPSGTPPPTI CCCCCCCCCCCCCCC	50.09	29255136
745	Phosphorylation	PILAPSGTPPPTIPP CCCCCCCCCCCCCCC	36.64	29255136
749	Phosphorylation	PSGTPPPTIPPDETF CCCCCCCCCCCCCCC	52.47	30266825
755	Phosphorylation	PTIPPDETFGGRVPR CCCCCCCCCCCCCCC	34.65	23927012
793	Phosphorylation	DSVVIVPEGLPPLPP CCEEEECCCCCCCCC	63.57	19664995
795	Phosphorylation	VVIVPEGLPPLPPPP EEEECCCCCCCCCCC	3.63	19664995
799	Phosphorylation	PEGLPPLPPPPPSGA CCCCCCCCCCCCCCC	45.16	17081983
804	Phosphorylation	PLPPPPPSGATPPPI CCCCCCCCCCCCCCC	47.00	24275569
807	Phosphorylation	PPPPSGATPPPIAPT CCCCCCCCCCCCCCC	39.59	24275569
814	Phosphorylation	TPPPIAPTGPPTASP CCCCCCCCCCCCCCC	53.98	24275569
826	Sumoylation	ASPPVPAKEEPEELP CCCCCCCCCCCCCCC	57.45	21326211
854	Phosphorylation	PPVPGPVTLPPPQLV CCCCCCCCCCCCCCC	36.36	-
857	Phosphorylation	PGPVTLPPPQLVPEG CCCCCCCCCCCCCCC	32.17	-
920	Phosphorylation	EEEDEEEYFEEEEEE HHHHHHHHHHHHHHH	21.41	17194752
970	Phosphorylation	LEFGTAGGEVEEGAP CCCCCCCCCCCCCCC	33.06	-
981	Phosphorylation	EGAPPPPTLPPALPP CCCCCCCCCCCCCCC	58.64	26074081
991	Phosphorylation	PALPPPESPPKVQPE CCCCCCCCCCCCCCC	52.88	26074081
1014	Phosphorylation	LEVEEPGTEEERGAD EEEECCCCHHHCCCC	51.44	30266825
1022	Phosphorylation	EEERGADTAPTLAPE HHHCCCCCCCCCCCH	33.72	29255136
1025	Phosphorylation	RGADTAPTLAPEALP CCCCCCCCCCCHHCC	32.84	29255136
1033	Phosphorylation	LAPEALPSQGEVERE CCCHHCCCCCCCCCC	52.23	23401153
1041	Phosphorylation	QGEVEREGESPAAGP CCCCCCCCCCCCCCC	47.07	-
1043	Phosphorylation	EVEREGESPAAGPPP CCCCCCCCCCCCCCC	30.60	30266825
1059	Phosphorylation	ELVEEEPSAPPTLLE HHHCCCCCCCCCCCC	57.60	30206219
1063	Phosphorylation	EEPSAPPTLLEEETE CCCCCCCCCCCEECC	42.80	26657352
1064	Phosphorylation	EPSAPPTLLEEETED CCCCCCCCCCEECCC	7.55	-
1069	Phosphorylation	PTLLEEETEDGSDKV CCCCCEECCCCCCCC	42.53	20873877
1073	Phosphorylation	EEETEDGSDKVQPPP CEECCCCCCCCCCCC	46.72	21955146
1082	Phosphorylation	KVQPPPETPAEEEME CCCCCCCCCCHHHCC	33.31	29255136
1083	Phosphorylation	VQPPPETPAEEEMET CCCCCCCCCHHHCCH	35.69	19691289
1090	Phosphorylation	PAEEEMETETEAEAL CCHHHCCHHHHHHHH	47.07	29255136
1092	Phosphorylation	EEEMETETEAEALQE HHHCCHHHHHHHHHH	48.17	29255136
1093	Phosphorylation	EEMETETEAEALQEK HHCCHHHHHHHHHHH	37.98	19664995
1105	Phosphorylation	QEKEQDDTAAMLADF HHHHCCCHHHHHHHH	25.30	19007248
1123	Phosphorylation	PPDDEKPPPPTEPDS CCCCCCCCCCCCCCC	59.58	18452278
1130	Phosphorylation	PPPTEPDS------- CCCCCCCC-------	53.49	28348404
1132	Phosphorylation	PTEPDS--------- CCCCCC---------		-
1140	Phosphorylation	----------------- -----------------		19664995
1155	Phosphorylation	-------------------------------- --------------------------------		19007248

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
350	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
415	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
477	S	Phosphorylation	Kinase	CDK2	P24941	PSP
477	S	Phosphorylation	Kinase	CDK4	P11802	PSP
477	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
613	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
920	Y	Phosphorylation	Kinase	SRC	P12931	PSP
991	S	Phosphorylation	Kinase	CDK2	P24941	PSP
991	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
1033	S	Phosphorylation	Kinase	ATM	Q13315	PSP
1033	S	Phosphorylation	Kinase	ATR	Q13535	PSP
1033	S	Phosphorylation	Kinase	DNAPK	P78527	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PELP1_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 PELP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	11481323
EP300_HUMAN	EP300	physical	11481323
CBP_HUMAN	CREBBP	physical	11481323
BAG6_HUMAN	BAG6	physical	16169070
TM1L1_HUMAN	TOM1L1	physical	16169070
STAT3_HUMAN	STAT3	physical	15994929
SRF_HUMAN	SRF	physical	15456770
H31_HUMAN	HIST1H3A	physical	15456770
H2A2C_HUMAN	HIST2H2AC	physical	15456770
H2B2E_HUMAN	HIST2H2BE	physical	15456770
H11_HUMAN	HIST1H1A	physical	15456770
HDAC2_HUMAN	HDAC2	physical	15456770
KDM1A_HUMAN	KDM1A	physical	20448663
H31_HUMAN	HIST1H3A	physical	20448663
H31_HUMAN	HIST1H3A	physical	20442285
LAS1L_HUMAN	LAS1L	physical	20442285
SENP3_HUMAN	SENP3	physical	20442285
BL1S1_HUMAN	BLOC1S1	physical	12639951
HGS_HUMAN	HGS	physical	16352611
ESR1_HUMAN	ESR1	physical	14963108
SRC_HUMAN	SRC	physical	14963108
IPO5_HUMAN	IPO5	physical	22190735
TEX10_HUMAN	TEX10	physical	22190735
NOL9_HUMAN	NOL9	physical	22190735
SENP3_HUMAN	SENP3	physical	22190735
WDR18_HUMAN	WDR18	physical	22190735
LAS1L_HUMAN	LAS1L	physical	22190735
RL26_HUMAN	RPL26	physical	22190735
RL11_HUMAN	RPL11	physical	22190735
BCAS3_HUMAN	BCAS3	physical	17505058
NOL9_HUMAN	NOL9	physical	26344197
NOLC1_HUMAN	NOLC1	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
SENP3_HUMAN	SENP3	physical	26344197

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 PELP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-477; SER-481; SER-485; SER-743; THR-745 ANDTHR-1090, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-477; SER-481; SER-485; SER-743; THR-745 ANDTHR-1090, AND MASS SPECTROMETRY.	19413330 [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-477; SER-481; THR-745AND SER-1043, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; SER-1043 ANDTHR-1105, AND MASS SPECTROMETRY.	19007248 [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-1033, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1043, AND MASSSPECTROMETRY.	16565220 [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-481, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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 THR-745, AND MASSSPECTROMETRY.	19690332 [Abstract]