SRS10_MOUSE - dbPTM
SRS10_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRS10_MOUSE
UniProt AC Q9R0U0
Protein Name Serine/arginine-rich splicing factor 10
Gene Name Srsf10
Organism Mus musculus (Mouse).
Sequence Length 262
Subcellular Localization Nucleus speckle .
Protein Description Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (By similarity). May be involved in regulation of alternative splicing in neurons. [PubMed: 10583508]
Protein Sequence MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRFKHRNRSFSRSKSNSRSRSKSQPKKEMKAKSRSRSASHTKTRGTSKTDSKTHYKSGSRYEKESRKKEPPRSKSQSRSQSRSRSKSRSRSWTSPKSSGH
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
21PhosphorylationVRNVADDTRSEDLRR
EEECCCCCCCHHHHH		36.3228833060
23PhosphorylationNVADDTRSEDLRREF
ECCCCCCCHHHHHHH		37.2428833060
92PhosphorylationFAQGDRKTPNQMKAK
ECCCCCCCCCCCCCC		28.5023684622
105PhosphorylationAKEGRNVYSSSRYDD
CCCCCCCCCCCCCCC		13.3426643407
106PhosphorylationKEGRNVYSSSRYDDY
CCCCCCCCCCCCCCH		19.9723684622
107PhosphorylationEGRNVYSSSRYDDYD
CCCCCCCCCCCCCHH		10.9329895711
108PhosphorylationGRNVYSSSRYDDYDR
CCCCCCCCCCCCHHH		28.9926643407
110PhosphorylationNVYSSSRYDDYDRYR
CCCCCCCCCCHHHHH		18.3423984901
113PhosphorylationSSSRYDDYDRYRRSR
CCCCCCCHHHHHHHH		10.2223984901
119PhosphorylationDYDRYRRSRSRSYER
CHHHHHHHHCHHHHH		26.1322817900
121PhosphorylationDRYRRSRSRSYERRR
HHHHHHHCHHHHHHH		27.1623684622
123PhosphorylationYRRSRSRSYERRRSR
HHHHHCHHHHHHHHH		32.3723737553
124PhosphorylationRRSRSRSYERRRSRS
HHHHCHHHHHHHHHC		16.6122817900
129PhosphorylationRSYERRRSRSRSFDY
HHHHHHHHHCCCCCC		32.5618388127
131PhosphorylationYERRRSRSRSFDYNY
HHHHHHHCCCCCCCC		33.2618388127
133 (in isoform 2)Phosphorylation-24.5827566939
133PhosphorylationRRRSRSRSFDYNYRR
HHHHHCCCCCCCCCC		24.5818388127
136PhosphorylationSRSRSFDYNYRRSYS
HHCCCCCCCCCCCCC		16.4527742792
136 (in isoform 2)Phosphorylation-16.4529514104
138PhosphorylationSRSFDYNYRRSYSPR
CCCCCCCCCCCCCCC		10.9425619855
141PhosphorylationFDYNYRRSYSPRNSR
CCCCCCCCCCCCCCC		22.4423737553
141 (in isoform 2)Phosphorylation-22.4429514104
142PhosphorylationDYNYRRSYSPRNSRP
CCCCCCCCCCCCCCC		22.3823737553
143 (in isoform 2)Phosphorylation-20.7329514104
143PhosphorylationYNYRRSYSPRNSRPT
CCCCCCCCCCCCCCC		20.7323737553
155 (in isoform 2)Phosphorylation-38.8229514104
156PhosphorylationPTGRPRRSRSHSDND
CCCCCCCCCCCCCCH		39.1426824392
156 (in isoform 3)Phosphorylation-39.1426643407
157 (in isoform 2)Phosphorylation-36.2629514104
158 (in isoform 3)Phosphorylation-28.7023684622
158PhosphorylationGRPRRSRSHSDNDRF
CCCCCCCCCCCCHHH		28.7026824392
159 (in isoform 2)Phosphorylation-37.7529514104
160PhosphorylationPRRSRSHSDNDRFKH
CCCCCCCCCCHHHHH		39.0826824392
160 (in isoform 3)Phosphorylation-39.0825159016
168 (in isoform 3)Phosphorylation-40.6323984901
171PhosphorylationRFKHRNRSFSRSKSN
HHHHHHHHHHHCCCC		30.9923737553
171 (in isoform 3)Phosphorylation-30.9925159016
173 (in isoform 3)Phosphorylation-36.5723984901
173PhosphorylationKHRNRSFSRSKSNSR
HHHHHHHHHCCCCCC		36.5723737553
174 (in isoform 3)Phosphorylation-46.2025293948
175PhosphorylationRNRSFSRSKSNSRSR
HHHHHHHCCCCCCCC		38.9622817900
175 (in isoform 3)Phosphorylation-38.9625293948
195PhosphorylationKKEMKAKSRSRSASH
HHHHHHHHHHCCCCC		40.1123375375
197PhosphorylationEMKAKSRSRSASHTK
HHHHHHHHCCCCCCC		37.3623375375
199PhosphorylationKAKSRSRSASHTKTR
HHHHHHCCCCCCCCC		35.0623375375
201PhosphorylationKSRSRSASHTKTRGT
HHHHCCCCCCCCCCC		32.7029472430
205PhosphorylationRSASHTKTRGTSKTD
CCCCCCCCCCCCCCC		35.1723684622
208PhosphorylationSHTKTRGTSKTDSKT
CCCCCCCCCCCCCCC		24.6123684622
209PhosphorylationHTKTRGTSKTDSKTH
CCCCCCCCCCCCCCC		36.0625266776
211PhosphorylationKTRGTSKTDSKTHYK
CCCCCCCCCCCCCCC		45.3227681418
213PhosphorylationRGTSKTDSKTHYKSG
CCCCCCCCCCCCCCC		44.6927681418
214AcetylationGTSKTDSKTHYKSGS
CCCCCCCCCCCCCCC		41.9723806337
215PhosphorylationTSKTDSKTHYKSGSR
CCCCCCCCCCCCCCC		34.1027681418
235PhosphorylationRKKEPPRSKSQSRSQ
CCCCCCCCHHHHHHH		42.2922817900
249PhosphorylationQSRSRSKSRSRSWTS
HHHHCHHHHCCCCCC		36.4122817900
251PhosphorylationRSRSKSRSRSWTSPK
HHCHHHHCCCCCCCC		37.4427087446
253PhosphorylationRSKSRSRSWTSPKSS
CHHHHCCCCCCCCCC		35.6323684622
255PhosphorylationKSRSRSWTSPKSSGH
HHHCCCCCCCCCCCC		36.0827087446
256PhosphorylationSRSRSWTSPKSSGH-
HHCCCCCCCCCCCC-		24.8727087446
259PhosphorylationRSWTSPKSSGH----
CCCCCCCCCCC----		44.9621183079
260PhosphorylationSWTSPKSSGH-----
CCCCCCCCCC-----		47.1928066266
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 SRS10_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRS10_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 SRS10_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SRS10_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRS10_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-119; SER-121; SER-131;SER-133; SER-158 AND SER-160, 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-158, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-168 (ISOFORM 3), AND MASS SPECTROMETRY.

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