SRSF7_MOUSE - dbPTM
SRSF7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF7_MOUSE
UniProt AC Q8BL97
Protein Name Serine/arginine-rich splicing factor 7
Gene Name Srsf7
Organism Mus musculus (Mouse).
Sequence Length 267
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Required for pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific (By similarity)..
Protein Sequence MRSSARGRPLQAATAFFLSLFFFLRRFERGFWLWGGDSETKVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVELSTGMPRRSRFDRPPARRPFDPNDRCYECGEKGHYAYDCHRYSRRRRSRSRSRSHSRSRGRRYSRSRSRSRGRRSRSASPRRSRSVSLRRSRSASLRRSRSGSIIGSRYFQSRSRSRSRSRSISRPRSSRSKSRSPSPKRSRSPSGSPHRSASPERMD
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
2 (in isoform 2)Phosphorylation-39.0423375375
2 (in isoform 3)Phosphorylation-39.0423375375
2 (in isoform 4)Phosphorylation-39.0423375375
53MalonylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9926320211
53SuccinylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.99-
53UbiquitinationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.99-
53AcetylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9923806337
61PhosphorylationGELERAFSYYGPLRT
HHHHHHHHCCCCCEE		19.23-
62PhosphorylationELERAFSYYGPLRTV
HHHHHHHCCCCCEEE		13.14-
99MalonylationAVRGLDGKVICGSRV
HHCCCCCEEECCCEE		28.2626320211
99UbiquitinationAVRGLDGKVICGSRV
HHCCCCCEEECCCEE		28.26-
118PhosphorylationSTGMPRRSRFDRPPA
CCCCCCCCCCCCCCC		38.2829176673
152PhosphorylationAYDCHRYSRRRRSRS
HHHHHHHHHHHHHHH		21.1925266776
165 (in isoform 2)Phosphorylation-32.9524719451
167 (in isoform 2)Phosphorylation-41.9424719451
172PhosphorylationSRSRGRRYSRSRSRS
HHHHHHHHHHHHHHH		13.6923737553
173PhosphorylationRSRGRRYSRSRSRSR
HHHHHHHHHHHHHHH		23.2023737553
175PhosphorylationRGRRYSRSRSRSRGR
HHHHHHHHHHHHHCC		28.7723737553
181 (in isoform 2)Phosphorylation-30.5124719451
184PhosphorylationSRSRGRRSRSASPRR
HHHHCCCCCCCCCCH		29.2623737553
186PhosphorylationSRGRRSRSASPRRSR
HHCCCCCCCCCCHHH		34.0523737553
188PhosphorylationGRRSRSASPRRSRSV
CCCCCCCCCCHHHHH		21.8623737553
192PhosphorylationRSASPRRSRSVSLRR
CCCCCCHHHHHHHHH		30.1327818261
192 (in isoform 2)Phosphorylation-30.1324719451
194PhosphorylationASPRRSRSVSLRRSR
CCCCHHHHHHHHHHH		19.8022942356
196PhosphorylationPRRSRSVSLRRSRSA
CCHHHHHHHHHHHCH		19.8722802335
200PhosphorylationRSVSLRRSRSASLRR
HHHHHHHHHCHHHHH		24.9325338131
202PhosphorylationVSLRRSRSASLRRSR
HHHHHHHCHHHHHHC		24.3722802335
204PhosphorylationLRRSRSASLRRSRSG
HHHHHCHHHHHHCCC		24.5322802335
208 (in isoform 4)Phosphorylation-25.1029895711
208PhosphorylationRSASLRRSRSGSIIG
HCHHHHHHCCCCCCC		25.1025521595
209 (in isoform 4)Phosphorylation-43.1329895711
210PhosphorylationASLRRSRSGSIIGSR
HHHHHHCCCCCCCHH		37.8327087446
211 (in isoform 4)Phosphorylation-23.0429895711
212PhosphorylationLRRSRSGSIIGSRYF
HHHHCCCCCCCHHHH		16.5727087446
216PhosphorylationRSGSIIGSRYFQSRS
CCCCCCCHHHHHCCC		17.2526824392
218PhosphorylationGSIIGSRYFQSRSRS
CCCCCHHHHHCCCCC		13.9923737553
221 (in isoform 4)Phosphorylation-23.4829895711
221PhosphorylationIGSRYFQSRSRSRSR
CCHHHHHCCCCCCCC		23.4821659605
223PhosphorylationSRYFQSRSRSRSRSR
HHHHHCCCCCCCCCC		39.5925263469
225PhosphorylationYFQSRSRSRSRSRSI
HHHCCCCCCCCCCCC		35.5419854140
227PhosphorylationQSRSRSRSRSRSISR
HCCCCCCCCCCCCCC		35.5419854140
229PhosphorylationRSRSRSRSRSISRPR
CCCCCCCCCCCCCCC		31.4619854140
231PhosphorylationRSRSRSRSISRPRSS
CCCCCCCCCCCCCCC		26.6023737553
233PhosphorylationRSRSRSISRPRSSRS
CCCCCCCCCCCCCCC		37.1625159016
237PhosphorylationRSISRPRSSRSKSRS
CCCCCCCCCCCCCCC		32.5525159016
238PhosphorylationSISRPRSSRSKSRSP
CCCCCCCCCCCCCCC		41.6825159016
242PhosphorylationPRSSRSKSRSPSPKR
CCCCCCCCCCCCCCC		38.9618779572
244PhosphorylationSSRSKSRSPSPKRSR
CCCCCCCCCCCCCCC		36.5023737553
246PhosphorylationRSKSRSPSPKRSRSP
CCCCCCCCCCCCCCC		44.2823737553
250PhosphorylationRSPSPKRSRSPSGSP
CCCCCCCCCCCCCCC		43.1423684622
252PhosphorylationPSPKRSRSPSGSPHR
CCCCCCCCCCCCCCC		25.3523684622
254PhosphorylationPKRSRSPSGSPHRSA
CCCCCCCCCCCCCCC		53.8223684622
256PhosphorylationRSRSPSGSPHRSASP
CCCCCCCCCCCCCCC		23.1323684622
260PhosphorylationPSGSPHRSASPERMD
CCCCCCCCCCCCCCC		30.0225521595
262PhosphorylationGSPHRSASPERMD--
CCCCCCCCCCCCC--		28.6525521595
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 SRSF7_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF7_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 SRSF7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SRSF7_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRSF7_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-192; SER-194; SER-196;SER-208; SER-210; SER-212; SER-216; SER-252; SER-254 AND SER-256, ANDMASS 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-254, AND MASSSPECTROMETRY.

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