SRSF9_MOUSE - dbPTM
SRSF9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF9_MOUSE
UniProt AC Q9D0B0
Protein Name Serine/arginine-rich splicing factor 9
Gene Name Srsf9
Organism Mus musculus (Mouse).
Sequence Length 222
Subcellular Localization Nucleus.
Protein Description Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10 (By similarity)..
Protein Sequence MSSGWADERGGEGDGRIYVGNLPSDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGARNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGMGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
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 Orthologous
Protein Cluster
2Phosphorylation------MSSGWADER
------CCCCCCCCC
37.2426824392
3Phosphorylation-----MSSGWADERG
-----CCCCCCCCCC
36.7420469934
37UbiquitinationDLEDLFYKYGRIREI
HHHHHHHHHCCEEEE
33.62-
71PhosphorylationRDAEDAIYGRNGYDY
CCHHHHHCCCCCCCC
16.2622817900
94MethylationFPRTYGGRGGWPRGA
CCCCCCCCCCCCCCC
35.7724394753
99MethylationGGRGGWPRGARNGPP
CCCCCCCCCCCCCCC
44.9130761013
124PhosphorylationSGLPPSGSWQDLKDH
ECCCCCCCHHHHHHH
26.38-
129UbiquitinationSGSWQDLKDHMREAG
CCCHHHHHHHHHHHC
54.6127667366
161PhosphorylationLRKEDMEYALRKLDD
HCHHHHHHHHHHCCC
12.3322817900
180PhosphorylationSHEGETSYIRVYPER
CCCCCCEEEEEECCC
10.5222817900
188PhosphorylationIRVYPERSTSYGYSR
EEEECCCCCCCCCCC
21.7525159016
189PhosphorylationRVYPERSTSYGYSRS
EEECCCCCCCCCCCC
31.9924453211
190PhosphorylationVYPERSTSYGYSRSR
EECCCCCCCCCCCCC
20.1523684622
191PhosphorylationYPERSTSYGYSRSRS
ECCCCCCCCCCCCCC
21.8525159016
193PhosphorylationERSTSYGYSRSRSGS
CCCCCCCCCCCCCCC
7.8320139300
194PhosphorylationRSTSYGYSRSRSGSR
CCCCCCCCCCCCCCC
21.2923684622
196PhosphorylationTSYGYSRSRSGSRGR
CCCCCCCCCCCCCCC
25.5129550500
198PhosphorylationYGYSRSRSGSRGRDS
CCCCCCCCCCCCCCC
42.2221659605
200PhosphorylationYSRSRSGSRGRDSPY
CCCCCCCCCCCCCCC
32.5721659605
205PhosphorylationSGSRGRDSPYQSRGS
CCCCCCCCCCCCCCC
24.9325521595
207PhosphorylationSRGRDSPYQSRGSPH
CCCCCCCCCCCCCCC
24.0725159016
209PhosphorylationGRDSPYQSRGSPHYF
CCCCCCCCCCCCCCC
32.5325159016
212PhosphorylationSPYQSRGSPHYFSPF
CCCCCCCCCCCCCCC
13.8527087446
215PhosphorylationQSRGSPHYFSPFRPY
CCCCCCCCCCCCCCC
14.7727742792
217PhosphorylationRGSPHYFSPFRPY--
CCCCCCCCCCCCC--
18.9027087446
222PhosphorylationYFSPFRPY-------
CCCCCCCC-------
27.2525619855

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

Oops, there are no upstream regulatory protein records of SRSF9_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF9_MOUSE !!

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 SRSF9_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SRSF9_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRSF9_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-205; SER-212 ANDSER-217, AND MASS SPECTROMETRY.
"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-212 AND SER-217, ANDMASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.

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