dbPTM

RNPS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RNPS1_HUMAN
UniProt AC	Q15287
Protein Name	RNA-binding protein with serine-rich domain 1
Gene Name	RNPS1
Organism	Homo sapiens (Human).
Sequence Length	305
Subcellular Localization	Nucleus. Nucleus speckle. Cytoplasm. Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
Protein Description	Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions..
Protein Sequence	MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKERKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPHLSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRFSPPRRMLPPPPMWRRSPPRMRRRSRSPRRRSPVRRRSRSPGRRRHRSRSSSNSSR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MDLSGVKKKSL ----CCCCCCCCHHH	36.96	22199227
4 (in isoform 2)	Phosphorylation	-	36.96	25849741
4 (in isoform 3)	Phosphorylation	-	36.96	25849741
6 (in isoform 2)	Phosphorylation	-	8.05	29514088
6 (in isoform 3)	Phosphorylation	-	8.05	29514088
7	2-Hydroxyisobutyrylation	-MDLSGVKKKSLLGV -CCCCCCCCHHHCCC	58.99	-
7	Acetylation	-MDLSGVKKKSLLGV -CCCCCCCCHHHCCC	58.99	25953088
7	Sumoylation	-MDLSGVKKKSLLGV -CCCCCCCCHHHCCC	58.99	28112733
10	Phosphorylation	LSGVKKKSLLGVKEN CCCCCCHHHCCCCCC	37.39	26074081
15	Sumoylation	KKSLLGVKENNKKSS CHHHCCCCCCCCCCC	53.58	28112733
21	Phosphorylation	VKENNKKSSTRAPSP CCCCCCCCCCCCCCC	38.25	23403867
22	Phosphorylation	KENNKKSSTRAPSPT CCCCCCCCCCCCCCC	30.69	23403867
23	Phosphorylation	ENNKKSSTRAPSPTK CCCCCCCCCCCCCCC	37.63	30183078
27	Phosphorylation	KSSTRAPSPTKRKDR CCCCCCCCCCCCCCC	44.19	30266825
29	Phosphorylation	STRAPSPTKRKDRSD CCCCCCCCCCCCCCC	48.06	30266825
35	Phosphorylation	PTKRKDRSDEKSKDR CCCCCCCCCHHHCHH	61.32	20068231
39	Phosphorylation	KDRSDEKSKDRSKDK CCCCCHHHCHHHHCC	37.43	-
40	Methylation	DRSDEKSKDRSKDKG CCCCHHHCHHHHCCC	69.13	116252731
43	Phosphorylation	DEKSKDRSKDKGATK CHHHCHHHHCCCCCH	56.17	30576142
49	Phosphorylation	RSKDKGATKESSEKD HHHCCCCCHHHHHHH	43.97	24144214
52	Phosphorylation	DKGATKESSEKDRGR CCCCCHHHHHHHHCC	45.40	26657352
53	Phosphorylation	KGATKESSEKDRGRD CCCCHHHHHHHHCCC	50.16	20068231
67	Phosphorylation	DKTRKRRSASSGSSS CCHHHHHHCCCCCCC	36.21	-
69	Phosphorylation	TRKRRSASSGSSSTR HHHHHHCCCCCCCCC	36.16	29052541
70	Phosphorylation	RKRRSASSGSSSTRS HHHHHCCCCCCCCCC	42.27	29052541
72	Phosphorylation	RRSASSGSSSTRSRS HHHCCCCCCCCCCCC	24.06	29052541
73	Phosphorylation	RSASSGSSSTRSRSS HHCCCCCCCCCCCCC	38.97	29052541
74	Phosphorylation	SASSGSSSTRSRSSS HCCCCCCCCCCCCCC	29.54	29052541
77	Phosphorylation	SGSSSTRSRSSSTSS CCCCCCCCCCCCCCC	36.28	-
78	Methylation	GSSSTRSRSSSTSSS CCCCCCCCCCCCCCC	36.95	115386567
80	Phosphorylation	SSTRSRSSSTSSSGS CCCCCCCCCCCCCCC	36.20	-
81	Phosphorylation	STRSRSSSTSSSGSS CCCCCCCCCCCCCCC	33.29	-
82	Phosphorylation	TRSRSSSTSSSGSST CCCCCCCCCCCCCCC	34.28	-
83	Phosphorylation	RSRSSSTSSSGSSTS CCCCCCCCCCCCCCC	25.18	-
84	Phosphorylation	SRSSSTSSSGSSTST CCCCCCCCCCCCCCC	38.51	30576142
85	Phosphorylation	RSSSTSSSGSSTSTG CCCCCCCCCCCCCCC	42.32	-
87	Phosphorylation	SSTSSSGSSTSTGSS CCCCCCCCCCCCCCC	32.18	-
88	Phosphorylation	STSSSGSSTSTGSSS CCCCCCCCCCCCCCC	29.87	-
89	Phosphorylation	TSSSGSSTSTGSSSG CCCCCCCCCCCCCCC	31.82	-
90	Phosphorylation	SSSGSSTSTGSSSGS CCCCCCCCCCCCCCC	32.49	30576142
91	Phosphorylation	SSGSSTSTGSSSGSS CCCCCCCCCCCCCCC	40.97	-
93	Phosphorylation	GSSTSTGSSSGSSSS CCCCCCCCCCCCCCC	22.78	-
94	Phosphorylation	SSTSTGSSSGSSSSS CCCCCCCCCCCCCCC	39.81	-
95	Phosphorylation	STSTGSSSGSSSSSA CCCCCCCCCCCCCCC	44.37	-
97	Phosphorylation	STGSSSGSSSSSASS CCCCCCCCCCCCCCC	29.06	-
98	Phosphorylation	TGSSSGSSSSSASSR CCCCCCCCCCCCCCC	37.45	-
100	Phosphorylation	SSSGSSSSSASSRSG CCCCCCCCCCCCCCC	31.69	-
101	Phosphorylation	SSGSSSSSASSRSGS CCCCCCCCCCCCCCC	33.83	-
103	Phosphorylation	GSSSSSASSRSGSSS CCCCCCCCCCCCCCC	28.38	-
104	Phosphorylation	SSSSSASSRSGSSST CCCCCCCCCCCCCCC	30.13	-
106	Phosphorylation	SSSASSRSGSSSTSR CCCCCCCCCCCCCCC	45.00	30576142
108	Phosphorylation	SASSRSGSSSTSRSS CCCCCCCCCCCCCCC	23.51	-
109	Phosphorylation	ASSRSGSSSTSRSSS CCCCCCCCCCCCCCC	40.95	30576142
112	Phosphorylation	RSGSSSTSRSSSSSS CCCCCCCCCCCCCCC	31.92	30576142
114	Phosphorylation	GSSSTSRSSSSSSSS CCCCCCCCCCCCCCC	34.05	29262532
115	Phosphorylation	SSSTSRSSSSSSSSG CCCCCCCCCCCCCCC	32.88	29262532
116	Phosphorylation	SSTSRSSSSSSSSGS CCCCCCCCCCCCCCC	35.17	29262532
117	Phosphorylation	STSRSSSSSSSSGSP CCCCCCCCCCCCCCC	35.87	29262532
118	Phosphorylation	TSRSSSSSSSSGSPS CCCCCCCCCCCCCCC	35.87	29262532
119	Phosphorylation	SRSSSSSSSSGSPSP CCCCCCCCCCCCCCC	30.39	29262532
120	Phosphorylation	RSSSSSSSSGSPSPS CCCCCCCCCCCCCCC	40.44	27174698
121	Phosphorylation	SSSSSSSSGSPSPSR CCCCCCCCCCCCCCH	45.28	27174698
123	Phosphorylation	SSSSSSGSPSPSRRR CCCCCCCCCCCCHHH	24.93	25849741
125	Phosphorylation	SSSSGSPSPSRRRHD CCCCCCCCCCHHHHH	36.89	21082442
127	Phosphorylation	SSGSPSPSRRRHDNR CCCCCCCCHHHHHCC	42.64	30576142
139	Phosphorylation	DNRRRSRSKSKPPKR HCCHHHHCCCCCCCC	42.39	26657352
141	Phosphorylation	RRRSRSKSKPPKRDE CHHHHCCCCCCCCCH	52.20	26657352
155	Phosphorylation	EKERKRRSPSPKPTK HHHHHHCCCCCCCCE	33.49	22167270
157	Phosphorylation	ERKRRSPSPKPTKVH HHHHCCCCCCCCEEE	46.96	22167270
161	Phosphorylation	RSPSPKPTKVHIGRL CCCCCCCCEEEHHHH	52.40	30266825
166 (in isoform 3)	Ubiquitination	-	12.03	21890473
173	Phosphorylation	GRLTRNVTKDHIMEI HHHCCCCCHHHHHHH	34.01	20860994
174	2-Hydroxyisobutyrylation	RLTRNVTKDHIMEIF HHCCCCCHHHHHHHH	42.92	-
174	Acetylation	RLTRNVTKDHIMEIF HHCCCCCHHHHHHHH	42.92	26051181
180 (in isoform 2)	Ubiquitination	-	1.50	21890473
182	Phosphorylation	DHIMEIFSTYGKIKM HHHHHHHHHCCCEEE	26.78	20068231
183	Phosphorylation	HIMEIFSTYGKIKMI HHHHHHHHCCCEEEE	26.08	21406692
184	Phosphorylation	IMEIFSTYGKIKMID HHHHHHHCCCEEEEE	18.41	21406692
186	Acetylation	EIFSTYGKIKMIDMP HHHHHCCCEEEEECC	28.83	25953088
186	Ubiquitination	EIFSTYGKIKMIDMP HHHHHCCCEEEEECC	28.83	-
188	2-Hydroxyisobutyrylation	FSTYGKIKMIDMPVE HHHCCCEEEEECCHH	33.03	-
188	Ubiquitination	FSTYGKIKMIDMPVE HHHCCCEEEEECCHH	33.03	-
195	Acetylation	KMIDMPVERMHPHLS EEEECCHHHCCCCCC	38.11	19608861
196	Methylation	MIDMPVERMHPHLSK EEECCHHHCCCCCCC	29.01	116279419
202	Phosphorylation	ERMHPHLSKGYAYVE HHCCCCCCCCEEEEE	22.47	28851738
203	Acetylation	RMHPHLSKGYAYVEF HCCCCCCCCEEEEEE	63.40	26051181
203	Ubiquitination	RMHPHLSKGYAYVEF HCCCCCCCCEEEEEE	63.40	21890473
203 (in isoform 1)	Ubiquitination	-	63.40	21890473
205	Phosphorylation	HPHLSKGYAYVEFEN CCCCCCCEEEEEECC	9.86	21082442
207	Phosphorylation	HLSKGYAYVEFENPD CCCCCEEEEEECCHH	7.63	28152594
218	Acetylation	ENPDEAEKALKHMDG CCHHHHHHHHHHCCC	67.10	19608861
218	Malonylation	ENPDEAEKALKHMDG CCHHHHHHHHHHCCC	67.10	32601280
218	Ubiquitination	ENPDEAEKALKHMDG CCHHHHHHHHHHCCC	67.10	19608861
234	Phosphorylation	QIDGQEITATAVLAP CCCCEEEEEEEEECC	19.73	-
236	Phosphorylation	DGQEITATAVLAPWP CCEEEEEEEEECCCC	14.51	-
251	Phosphorylation	RPPPRRFSPPRRMLP CCCCCCCCCCHHCCC	31.98	22167270
266	Phosphorylation	PPPMWRRSPPRMRRR CCCHHHCCCHHHHHC	30.59	22617229
274	Phosphorylation	PPRMRRRSRSPRRRS CHHHHHCCCCCCCCC	34.99	26657352
276	Phosphorylation	RMRRRSRSPRRRSPV HHHHCCCCCCCCCCC	24.81	30576142
281	Phosphorylation	SRSPRRRSPVRRRSR CCCCCCCCCCHHHCC	26.40	20068231
287	Phosphorylation	RSPVRRRSRSPGRRR CCCCHHHCCCCCCCC	34.99	30576142
289	Phosphorylation	PVRRRSRSPGRRRHR CCHHHCCCCCCCCCC	32.71	30576142

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
53	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
53	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
43	S	Phosphorylation	15684395
Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).
49	T	Phosphorylation	15684395
Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).
52	S	Phosphorylation	15684395
Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).
53	S	Phosphorylation	15684395
Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).
53	S	Phosphorylation	15684395
Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro.

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 RNPS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U520_HUMAN	SNRNP200	physical	17353931
CD11B_HUMAN	CDK11B	physical	17353931
GEMI4_HUMAN	GEMIN4	physical	17353931
MKLN1_HUMAN	MKLN1	physical	17353931
SK2L2_HUMAN	SKIV2L2	physical	17353931
PRP8_HUMAN	PRPF8	physical	17353931
U5S1_HUMAN	EFTUD2	physical	17353931
LC7L2_HUMAN	LUC7L2	physical	17353931
PRP4B_HUMAN	PRPF4B	physical	17353931
PR40A_HUMAN	PRPF40A	physical	17353931
NRDE2_HUMAN	NRDE2	physical	17353931
DDX20_HUMAN	DDX20	physical	17353931
RBM25_HUMAN	RBM25	physical	17353931
CSK22_HUMAN	CSNK2A2	physical	17353931
LUC7L_HUMAN	LUC7L	physical	17353931
SRPK1_HUMAN	SRPK1	physical	17353931
CSK2B_HUMAN	CSNK2B	physical	17353931
PININ_HUMAN	PNN	physical	17353931
U2AF2_HUMAN	U2AF2	physical	17353931
SRSF1_HUMAN	SRSF1	physical	17353931
LC7L3_HUMAN	LUC7L3	physical	17353931
WDR33_HUMAN	WDR33	physical	17353931
SRRT_HUMAN	SRRT	physical	17353931
DDX23_HUMAN	DDX23	physical	17353931
PRP6_HUMAN	PRPF6	physical	17353931
SRRM2_HUMAN	SRRM2	physical	17353931
CPSF5_HUMAN	NUDT21	physical	17353931
CPSF6_HUMAN	CPSF6	physical	17353931
SFSWA_HUMAN	SFSWAP	physical	17353931
TR150_HUMAN	THRAP3	physical	17353931
RANB9_HUMAN	RANBP9	physical	17353931
SRRM1_HUMAN	SRRM1	physical	17353931
CPSF2_HUMAN	CPSF2	physical	17353931
PRPF3_HUMAN	PRPF3	physical	17353931
AP2B1_HUMAN	AP2B1	physical	17353931
KHK_HUMAN	KHK	physical	17353931
SREK1_HUMAN	SREK1	physical	17353931
PUF60_HUMAN	PUF60	physical	17353931
TRA2B_HUMAN	TRA2B	physical	17353931
RU17_HUMAN	SNRNP70	physical	17353931
SRSF2_HUMAN	SRSF2	physical	17353931
CATIN_HUMAN	CACTIN	physical	17353931
SF3B3_HUMAN	SF3B3	physical	17353931
DDX41_HUMAN	DDX41	physical	17353931
SRPK2_HUMAN	SRPK2	physical	17353931
UBP7_HUMAN	USP7	physical	17353931
SYRC_HUMAN	RARS	physical	17353931
PRP16_HUMAN	DHX38	physical	17353931
PSME3_HUMAN	PSME3	physical	17353931
SRSF7_HUMAN	SRSF7	physical	17353931
SNRPA_HUMAN	SNRPA	physical	17353931
GID8_HUMAN	GID8	physical	17353931
CSK21_HUMAN	CSNK2A1	physical	17353931
SF3B1_HUMAN	SF3B1	physical	17353931
GEMI2_HUMAN	GEMIN2	physical	17353931
STRAP_HUMAN	STRAP	physical	17353931
SART3_HUMAN	SART3	physical	11477570
CD11A_HUMAN	CDK11A	physical	9580558
ZN490_HUMAN	ZNF490	physical	20211142
ACINU_HUMAN	ACIN1	physical	22388736
SAP18_HUMAN	SAP18	physical	22388736
REN3A_HUMAN	UPF3A	physical	11546874
REN3B_HUMAN	UPF3B	physical	11546874
RENT2_HUMAN	UPF2	physical	11546874
RENT1_HUMAN	UPF1	physical	11546874
NXF1_HUMAN	NXF1	physical	11546874
SMU1_HUMAN	SMU1	physical	22939629
PYM1_HUMAN	WIBG	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22365833
CHERP_HUMAN	CHERP	physical	22365833
SRSF1_HUMAN	SRSF1	physical	22365833
PR38A_HUMAN	PRPF38A	physical	22365833
ACINU_HUMAN	ACIN1	physical	22365833
SRSF4_HUMAN	SRSF4	physical	22365833
SRPK2_HUMAN	SRPK2	physical	22365833
PININ_HUMAN	PNN	physical	14729963
TAF2_HUMAN	TAF2	physical	14729963
TRA2B_HUMAN	TRA2B	physical	14729963
LC7L3_HUMAN	LUC7L3	physical	14729963
ZN473_HUMAN	ZNF473	physical	25416956
SDCB2_HUMAN	SDCBP2	physical	25416956
TRI41_HUMAN	TRIM41	physical	25416956
HEXI2_HUMAN	HEXIM2	physical	25416956
PININ_HUMAN	PNN	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
GPTC8_HUMAN	GPATCH8	physical	14729963
SRS11_HUMAN	SRSF11	physical	14729963
XIAP_HUMAN	XIAP	physical	26496610
CSK21_HUMAN	CSNK2A1	physical	26496610
CSTF3_HUMAN	CSTF3	physical	26496610
ANM1_HUMAN	PRMT1	physical	26496610
RU17_HUMAN	SNRNP70	physical	26496610
SNRPA_HUMAN	SNRPA	physical	26496610
ZN207_HUMAN	ZNF207	physical	26496610
KAT6A_HUMAN	KAT6A	physical	26496610
STX7_HUMAN	STX7	physical	26496610
CCNK_HUMAN	CCNK	physical	26496610
BUB3_HUMAN	BUB3	physical	26496610
KIF23_HUMAN	KIF23	physical	26496610
CAPON_HUMAN	NOS1AP	physical	26496610
CRTAP_HUMAN	CRTAP	physical	26496610
DDX17_HUMAN	DDX17	physical	26496610
SF3A3_HUMAN	SF3A3	physical	26496610
CPSF5_HUMAN	NUDT21	physical	26496610
GPTC8_HUMAN	GPATCH8	physical	26496610
PRP6_HUMAN	PRPF6	physical	26496610
PRP31_HUMAN	PRPF31	physical	26496610
TIM13_HUMAN	TIMM13	physical	26496610
CDK12_HUMAN	CDK12	physical	26496610
CPSF2_HUMAN	CPSF2	physical	26496610
P3H2_HUMAN	P3H2	physical	26496610
CCNL1_HUMAN	CCNL1	physical	26496610
WDR35_HUMAN	WDR35	physical	26496610
P3H1_HUMAN	P3H1	physical	26496610
CPSF7_HUMAN	CPSF7	physical	26496610
TDRD3_HUMAN	TDRD3	physical	26496610
RIOX2_HUMAN	MINA	physical	26496610
FOXK1_HUMAN	FOXK1	physical	26496610
CCD84_HUMAN	CCDC84	physical	26496610
UBP4_HUMAN	USP4	physical	27990632

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 RNPS1_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-218, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-251, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, ANDMASS SPECTROMETRY.	17287340 [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-27; SER-251; SER-266;SER-287 AND SER-289, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2phosphorylation."; Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,Suzuki H., Endo H., Kidd V.J., Mayeda A.; Mol. Cell. Biol. 25:1446-1457(2005). Cited for: FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVESPLICEOSOME, PHOSPHORYLATION, PHOSPHORYLATION AT SER-53, MASSSPECTROMETRY, INTERACTION WITH CSNK2A1, MUTAGENESIS OF SER-53, ANDSUBCELLULAR LOCATION.	15684395 [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-125; SER-155 ANDSER-157, AND MASS SPECTROMETRY.	15302935 [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-205, AND MASSSPECTROMETRY.	15592455 [Abstract]

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