SRSF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SRSF2_MOUSE
• UniProt AC: Q62093
• Protein Name: Serine/arginine-rich splicing factor 2
• Gene Name: Srsf2
• Organism: Mus musculus (Mouse).
• 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 (By similarity). Can bind to the myelin basic protein (MBP) gene MB3 regulatory region and increase transcription of the mbp promoter in cells derived from the CNS. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity)..
• Protein Sequence: MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYGRPPPD ------CCCCCCCCC	35.97	26824392
2	Acetylation	------MSYGRPPPD ------CCCCCCCCC	35.97	-
3	Phosphorylation	-----MSYGRPPPDV -----CCCCCCCCCC	18.82	24224561
14	Phosphorylation	PPDVEGMTSLKVDNL CCCCCCCCEEEECCE	41.59	22345495
15	Phosphorylation	PDVEGMTSLKVDNLT CCCCCCCEEEECCEE	19.80	22345495
17	Ubiquitination	VEGMTSLKVDNLTYR CCCCCEEEECCEEEE	47.51	-
22	Phosphorylation	SLKVDNLTYRTSPDT EEEECCEEEECCHHH	19.74	24925903
23	Phosphorylation	LKVDNLTYRTSPDTL EEECCEEEECCHHHH	18.30	24925903
25	Phosphorylation	VDNLTYRTSPDTLRR ECCEEEECCHHHHHH	33.91	25521595
26	Phosphorylation	DNLTYRTSPDTLRRV CCEEEECCHHHHHHH	16.27	24925903
29	Phosphorylation	TYRTSPDTLRRVFEK EEECCHHHHHHHHHH	26.08	24925903
36	Malonylation	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	26320211
36	Acetylation	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	23806337
36	Ubiquitination	TLRRVFEKYGRVGDV HHHHHHHHHCCCCCE	41.35	27667366
44	Phosphorylation	YGRVGDVYIPRDRYT HCCCCCEEECCHHCC	15.22	24759943
52	Acetylation	IPRDRYTKESRGFAF ECCHHCCCCCCCEEE	44.77	-
92	Phosphorylation	LRVQMARYGRPPDSH HHHHHHHHCCCCCCC	14.14	25367039
98	Phosphorylation	RYGRPPDSHHSRRGP HHCCCCCCCCCCCCC	28.95	25367039
101	Phosphorylation	RPPDSHHSRRGPPPR CCCCCCCCCCCCCCC	20.46	25266776
109	Methylation	RRGPPPRRYGGGGYG CCCCCCCCCCCCCCC	39.98	54541429
109	Dimethylation	RRGPPPRRYGGGGYG CCCCCCCCCCCCCCC	39.98	-
119	Phosphorylation	GGGYGRRSRSPRRRR CCCCCCCCCCHHHHH	35.43	20450229
121	Phosphorylation	GYGRRSRSPRRRRRS CCCCCCCCHHHHHHH	24.81	20450229
142	Phosphorylation	RSRSRSRSRYSRSKS HHHHHHHHHHHHHHH	36.50	20139300
144	Phosphorylation	RSRSRSRYSRSKSRS HHHHHHHHHHHHHHH	15.07	23737553
145	Phosphorylation	SRSRSRYSRSKSRSR HHHHHHHHHHHHHHH	29.03	23737553
147	Phosphorylation	SRSRYSRSKSRSRTR HHHHHHHHHHHHHHH	29.10	23737553
185	Phosphorylation	RSRSRSRSRSRSRSP HHHHHHHHCCCCCCC	35.54	28066266
187	Phosphorylation	RSRSRSRSRSRSPPP HHHHHHCCCCCCCCC	35.54	25521595
189	Phosphorylation	RSRSRSRSRSPPPVS HHHHCCCCCCCCCCC	38.05	25521595
191	Phosphorylation	RSRSRSRSPPPVSKR HHCCCCCCCCCCCHH	42.90	25521595
196	Phosphorylation	SRSPPPVSKRESKSR CCCCCCCCHHHHCCC	31.59	23684622
200	Phosphorylation	PPVSKRESKSRSRSK CCCCHHHHCCCCCCC	39.71	29514104
202	Phosphorylation	VSKRESKSRSRSKSP CCHHHHCCCCCCCCC	44.78	23375375
204	Phosphorylation	KRESKSRSRSKSPPK HHHHCCCCCCCCCCC	48.25	21183079
206	Phosphorylation	ESKSRSRSKSPPKSP HHCCCCCCCCCCCCH	38.44	25521595
208	Phosphorylation	KSRSRSKSPPKSPEE CCCCCCCCCCCCHHH	47.91	25521595
212	Phosphorylation	RSKSPPKSPEEEGAV CCCCCCCCHHHCCCC	43.23	25521595
220	Phosphorylation	PEEEGAVSS------ HHHCCCCCC------	29.78	25521595
221	Phosphorylation	EEEGAVSS------- HHCCCCCC-------	37.33	25521595

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SRSF2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	K	Acetylation	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.

Oops, there are no SNP-PTM records of SRSF2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SRSF2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-189; SER-191;SER-206 AND SER-208, AND MASS SPECTROMETRY.
PubMed: 19367708

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-208 ANDSER-212, AND MASS SPECTROMETRY.
PubMed: 17242355

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.
PubMed: 17203969