dbPTM

SRSF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRSF2_HUMAN
UniProt AC	Q01130
Protein Name	Serine/arginine-rich splicing factor 2
Gene Name	SRSF2
Organism	Homo sapiens (Human).
Sequence Length	221
Subcellular Localization	Nucleus . Nucleus, nucleoplasm . Nucleus speckle . Phosphorylation by SRPK2 provokes its redistribution from the nuclear specke to nucleoplasm.
Protein Description	Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment..
Protein Sequence	MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYGRPPPD ------CCCCCCCCC	35.97	23401153
2	Acetylation	------MSYGRPPPD ------CCCCCCCCC	35.97	20068231
3	Nitration	-----MSYGRPPPDV -----CCCCCCCCCC	18.82	-
3	Phosphorylation	-----MSYGRPPPDV -----CCCCCCCCCC	18.82	29255136
5	Methylation	---MSYGRPPPDVEG ---CCCCCCCCCCCC	32.11	24410243
5	Dimethylation	---MSYGRPPPDVEG ---CCCCCCCCCCCC	32.11	-
14	Phosphorylation	PPDVEGMTSLKVDNL CCCCCCCCEEEECCE	41.59	26552605
15	Phosphorylation	PDVEGMTSLKVDNLT CCCCCCCEEEECCEE	19.80	28464451
22	Phosphorylation	SLKVDNLTYRTSPDT EEEECCEEEECCHHH	19.74	22167270
23	Phosphorylation	LKVDNLTYRTSPDTL EEECCEEEECCHHHH	18.30	22167270
25	Phosphorylation	VDNLTYRTSPDTLRR ECCEEEECCHHHHHH	33.91	29255136
26	Phosphorylation	DNLTYRTSPDTLRRV CCEEEECCHHHHHHH	16.27	29255136
29	Phosphorylation	TYRTSPDTLRRVFEK EEECCHHHHHHHHHH	26.08	22167270
31	Methylation	RTSPDTLRRVFEKYG ECCHHHHHHHHHHHC	34.51	115916709
36	Ubiquitination	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	21890473
36	Ubiquitination	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	21890473
36	Acetylation	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	-
36	Acetylation	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	23749302
36	Ubiquitination	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	21906983
39	Methylation	RVFEKYGRVGDVYIP HHHHHHCCCCCEEEC	26.59	-
44	Phosphorylation	YGRVGDVYIPRDRYT HCCCCCEEECCHHCC	15.22	28152594
52	Acetylation	IPRDRYTKESRGFAF ECCHHCCCCCCCEEE	44.77	21157427
55	Methylation	DRYTKESRGFAFVRF HHCCCCCCCEEEEEE	45.39	80702277
66	Methylation	FVRFHDKRDAEDAMD EEEECCCCCHHHHHH	55.20	115916717
72	Sulfoxidation	KRDAEDAMDAMDGAV CCCHHHHHHHHCCCE	5.37	28465586
75	Sulfoxidation	AEDAMDAMDGAVLDG HHHHHHHHCCCEECH	4.21	28465586
83	Methylation	DGAVLDGRELRVQMA CCCEECHHHHHHHHH	39.17	116265259
92	Phosphorylation	LRVQMARYGRPPDSH HHHHHHHHCCCCCCC	14.14	28152594
94	Methylation	VQMARYGRPPDSHHS HHHHHHCCCCCCCCC	30.55	115916721
98	Phosphorylation	RYGRPPDSHHSRRGP HHCCCCCCCCCCCCC	28.95	28152594
101	Phosphorylation	RPPDSHHSRRGPPPR CCCCCCCCCCCCCCC	20.46	20201521
103	Methylation	PDSHHSRRGPPPRRY CCCCCCCCCCCCCCC	66.05	-
109	Methylation	RRGPPPRRYGGGGYG CCCCCCCCCCCCCCC	39.98	54548809
109 (in isoform 2)	Phosphorylation	-	39.98	24532841
109	Dimethylation	RRGPPPRRYGGGGYG CCCCCCCCCCCCCCC	39.98	-
110	Phosphorylation	RGPPPRRYGGGGYGR CCCCCCCCCCCCCCC	22.77	28152594
115	Phosphorylation	RRYGGGGYGRRSRSP CCCCCCCCCCCCCCH	15.67	28152594
119	Phosphorylation	GGGYGRRSRSPRRRR CCCCCCCCCCHHHHH	35.43	30576142
121	Phosphorylation	GYGRRSRSPRRRRRS CCCCCCCCHHHHHHH	24.81	30576142
128	Phosphorylation	SPRRRRRSRSRSRSR CHHHHHHHHHHHHHH	32.56	-
130	Phosphorylation	RRRRRSRSRSRSRSR HHHHHHHHHHHHHHH	35.54	-
134	Phosphorylation	RSRSRSRSRSRSRSR HHHHHHHHHHHHHHH	35.54	-
136	Phosphorylation	RSRSRSRSRSRSRSR HHHHHHHHHHHHHHH	35.54	-
142	Phosphorylation	RSRSRSRSRYSRSKS HHHHHHHHHHHHHHH	36.50	20068231
144	Phosphorylation	RSRSRSRYSRSKSRS HHHHHHHHHHHHHHH	15.07	20068231
145	Phosphorylation	SRSRSRYSRSKSRSR HHHHHHHHHHHHHHH	29.03	20068231
147	Phosphorylation	SRSRYSRSKSRSRTR HHHHHHHHHHHHHHH	29.10	24144214
149	Phosphorylation	SRYSRSKSRSRTRSR HHHHHHHHHHHHHHH	36.41	24144214
151	Phosphorylation	YSRSKSRSRTRSRSR HHHHHHHHHHHHHCH	45.13	24144214
153	Phosphorylation	RSKSRSRTRSRSRST HHHHHHHHHHHCHHH	33.95	24144214
157	Phosphorylation	RSRTRSRSRSTSKSR HHHHHHHCHHHHHHH	31.65	27251275
161	Phosphorylation	RSRSRSTSKSRSARR HHHCHHHHHHHHHHH	29.85	27251275
163	Phosphorylation	RSRSTSKSRSARRSK HCHHHHHHHHHHHHH	31.10	27251275
165	Phosphorylation	RSTSKSRSARRSKSK HHHHHHHHHHHHHCC	32.97	27251275
169	Phosphorylation	KSRSARRSKSKSSSV HHHHHHHHHCCCCHH	35.41	-
171	Phosphorylation	RSARRSKSKSSSVSR HHHHHHHCCCCHHHH	38.73	-
172	Methylation	SARRSKSKSSSVSRS HHHHHHCCCCHHHHH	59.08	-
173	Phosphorylation	ARRSKSKSSSVSRSR HHHHHCCCCHHHHHH	34.63	-
174	Phosphorylation	RRSKSKSSSVSRSRS HHHHCCCCHHHHHHH	38.20	26546556
175	Phosphorylation	RSKSKSSSVSRSRSR HHHCCCCHHHHHHHH	31.07	-
177	Phosphorylation	KSKSSSVSRSRSRSR HCCCCHHHHHHHHHH	26.87	-
179	Phosphorylation	KSSSVSRSRSRSRSR CCCHHHHHHHHHHHC	27.40	-
183	Phosphorylation	VSRSRSRSRSRSRSR HHHHHHHHHHCCCCC	35.54	27135362
185	Phosphorylation	RSRSRSRSRSRSRSP HHHHHHHHCCCCCCC	35.54	29116813
187	Phosphorylation	RSRSRSRSRSRSPPP HHHHHHCCCCCCCCC	35.54	22167270
189	Phosphorylation	RSRSRSRSRSPPPVS HHHHCCCCCCCCCCC	38.05	29255136
191	Phosphorylation	RSRSRSRSPPPVSKR HHCCCCCCCCCCCHH	42.90	29255136
196	Phosphorylation	SRSPPPVSKRESKSR CCCCCCCCHHHHCCC	31.59	30266825
200	Phosphorylation	PPVSKRESKSRSRSK CCCCHHHHCCCCCCC	39.71	23909892
202	Phosphorylation	VSKRESKSRSRSKSP CCHHHHCCCCCCCCC	44.78	24505115
204	Phosphorylation	KRESKSRSRSKSPPK HHHHCCCCCCCCCCC	48.25	21712546
206	Phosphorylation	ESKSRSRSKSPPKSP HHCCCCCCCCCCCCH	38.44	19664994
208	Phosphorylation	KSRSRSKSPPKSPEE CCCCCCCCCCCCHHH	47.91	19664994
212	Phosphorylation	RSKSPPKSPEEEGAV CCCCCCCCHHHCCCC	43.23	29255136
220	Phosphorylation	PEEEGAVSS------ HHHCCCCCC------	29.78	22167270
221	Phosphorylation	EEEGAVSS------- HHCCCCCC-------	37.33	22167270

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
121	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
121	S	Phosphorylation	Kinase	PKACB	P22694	PSP
128	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
128	S	Phosphorylation	Kinase	PKACB	P22694	PSP
130	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
130	S	Phosphorylation	Kinase	PKACB	P22694	PSP
171	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
171	S	Phosphorylation	Kinase	PKACB	P22694	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	K	Acetylation		21157427
Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal degradation.

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 SRSF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRSF1_HUMAN	SRSF1	physical	8816452
U2AF1_HUMAN	U2AF1	physical	8816452
PRGC1_HUMAN	PPARGC1A	physical	10983978
AIRE_HUMAN	AIRE	physical	20085707
U2AF2_HUMAN	U2AF2	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
T126A_HUMAN	TMEM126A	physical	22939629
TITIN_HUMAN	TTN	physical	22939629
XPO1_HUMAN	XPO1	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
TPM4_HUMAN	TPM4	physical	22939629
TCPE_HUMAN	CCT5	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22365833
SRSF3_HUMAN	SRSF3	physical	22365833
SRSF4_HUMAN	SRSF4	physical	22365833
SRSF2_HUMAN	SRSF2	physical	22365833
TRA2B_HUMAN	TRA2B	physical	22365833
CIR1_HUMAN	CIR1	physical	15652350
ITF2_HUMAN	TCF4	physical	25416956
CEP72_HUMAN	CEP72	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
GCP60_HUMAN	ACBD3	physical	26344197
COPE_HUMAN	COPE	physical	26344197
PSME3_HUMAN	PSME3	physical	26344197
SBNO1_HUMAN	SBNO1	physical	26344197
SRSF1_HUMAN	SRSF1	physical	26344197
SRSF9_HUMAN	SRSF9	physical	26344197
STIP1_HUMAN	STIP1	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 SRSF2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation and phosphorylation of SRSF2 control cell fate decisionin response to cisplatin."; Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C.,Brambilla E., Gazzeri S., Eymin B.; EMBO J. 30:510-523(2011). Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, ANDPHOSPHORYLATION BY SRPK2.	21157427 [Abstract]
"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-36, AND MASS SPECTROMETRY.	19608861 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-212; SER-220AND SER-221, 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-26; SER-204; SER-206;SER-208; SER-212; SER-220 AND SER-221, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23; SER-26 AND SER-206,AND MASS SPECTROMETRY.	18187866 [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-26, AND MASSSPECTROMETRY.	19007248 [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-26, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-208 ANDSER-212, AND MASS SPECTROMETRY.	16964243 [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-187; SER-189; SER-191;SER-206; SER-208 AND SER-212, AND MASS SPECTROMETRY.	17081983 [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-26; SER-189; SER-191 ANDSER-212, AND MASS SPECTROMETRY.	15302935 [Abstract]

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