SRSF1_MOUSE - dbPTM
SRSF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF1_MOUSE
UniProt AC Q6PDM2
Protein Name Serine/arginine-rich splicing factor 1
Gene Name Srsf1
Organism Mus musculus (Mouse).
Sequence Length 248
Subcellular Localization Cytoplasm . Nucleus speckle . In nuclear speckles. Shuttles between the nucleus and the cytoplasm.
Protein Description Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. 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. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing (By similarity). Specifically regulates alternative splicing of cardiac isoforms of CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling at the juvenile to adult transition. The inappropriate accumulation of a neonatal and neuronal isoform of CAMKD2 in the adult heart results in aberrant calcium handling and defective excitation-contraction coupling in cardiomyocytes. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway..
Protein Sequence MSGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT
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------MSGGGVIRG
------CCCCCCEEC		46.2626824392
2Acetylation------MSGGGVIRG
------CCCCCCEEC		46.26-
30UbiquitinationLPPDIRTKDIEDVFY
CCCCCCCCCHHHHHH		47.0322790023
30AcetylationLPPDIRTKDIEDVFY
CCCCCCCCCHHHHHH		47.0322826441
38AcetylationDIEDVFYKYGAIRDI
CHHHHHHHHCCEEEC		26.2422826441
38UbiquitinationDIEDVFYKYGAIRDI
CHHHHHHHHCCEEEC		26.2422790023
48UbiquitinationAIRDIDLKNRRGGPP
CEEECCCCCCCCCCC		44.6627667366
51MethylationDIDLKNRRGGPPFAF
ECCCCCCCCCCCEEE		64.9154559173
93Asymmetric dimethylarginineVEFPRSGRGTGRGGG
EECCCCCCCCCCCCC		40.52-
93MethylationVEFPRSGRGTGRGGG
EECCCCCCCCCCCCC		40.5224129315
95PhosphorylationFPRSGRGTGRGGGGG
CCCCCCCCCCCCCCC		23.5027149854
97Asymmetric dimethylarginineRSGRGTGRGGGGGGG
CCCCCCCCCCCCCCC		40.18-
97MethylationRSGRGTGRGGGGGGG
CCCCCCCCCCCCCCC		40.1824129315
109MethylationGGGGGAPRGRYGPPS
CCCCCCCCCCCCCCC		41.5124129315
109Asymmetric dimethylarginineGGGGGAPRGRYGPPS
CCCCCCCCCCCCCCC		41.51-
111MethylationGGGAPRGRYGPPSRR
CCCCCCCCCCCCCCC		34.2230989311
116PhosphorylationRGRYGPPSRRSENRV
CCCCCCCCCCCCCEE		43.3825338131
119PhosphorylationYGPPSRRSENRVVVS
CCCCCCCCCCEEEEE		37.8125293948
126PhosphorylationSENRVVVSGLPPSGS
CCCEEEEECCCCCCC		24.0118779572
133PhosphorylationSGLPPSGSWQDLKDH
ECCCCCCCHHHHHHH		26.3818779572
138UbiquitinationSGSWQDLKDHMREAG
CCCHHHHHHHHHHHC		54.6127667366
148GlutathionylationMREAGDVCYADVYRD
HHHHCCEEEEEEEEC		2.4924333276
148S-palmitoylationMREAGDVCYADVYRD
HHHHCCEEEEEEEEC		2.4928526873
169PhosphorylationFVRKEDMTYAVRKLD
EEEHHHCCEEEEECC		22.2025367039
170PhosphorylationVRKEDMTYAVRKLDN
EEHHHCCEEEEECCC		9.1018563927
174UbiquitinationDMTYAVRKLDNTKFR
HCCEEEEECCCCCCC		54.30-
179AcetylationVRKLDNTKFRSHEGE
EEECCCCCCCCCCCC		45.06-
179UbiquitinationVRKLDNTKFRSHEGE
EEECCCCCCCCCCCC		45.0627667366
187PhosphorylationFRSHEGETAYIRVKV
CCCCCCCEEEEEEEE		35.3020415495
189PhosphorylationSHEGETAYIRVKVDG
CCCCCEEEEEEEECC		9.1825367039
199PhosphorylationVKVDGPRSPSYGRSR
EEECCCCCCCCCCCC		22.7218388127
201PhosphorylationVDGPRSPSYGRSRSR
ECCCCCCCCCCCCCC		41.2718388127
202PhosphorylationDGPRSPSYGRSRSRS
CCCCCCCCCCCCCCC		21.6825521595
205PhosphorylationRSPSYGRSRSRSRSR
CCCCCCCCCCCCHHH		30.1925521595
207PhosphorylationPSYGRSRSRSRSRSR
CCCCCCCCCCHHHHH		35.54-
209PhosphorylationYGRSRSRSRSRSRSR
CCCCCCCCHHHHHCC		35.54-
219PhosphorylationRSRSRSRSNSRSRSY
HHHCCCCCCCCCCCC		40.1618779572
221PhosphorylationRSRSRSNSRSRSYSP
HCCCCCCCCCCCCCC		32.6422324799
223PhosphorylationRSRSNSRSRSYSPRR
CCCCCCCCCCCCCCC		25.9623684622
225PhosphorylationRSNSRSRSYSPRRSR
CCCCCCCCCCCCCCC		31.0723684622
226PhosphorylationSNSRSRSYSPRRSRG
CCCCCCCCCCCCCCC		22.9122802335
227PhosphorylationNSRSRSYSPRRSRGS
CCCCCCCCCCCCCCC		17.1223684622
231PhosphorylationRSYSPRRSRGSPRYS
CCCCCCCCCCCCCCC		42.1225521595
234PhosphorylationSPRRSRGSPRYSPRH
CCCCCCCCCCCCCCC		12.7025521595
237PhosphorylationRSRGSPRYSPRHSRS
CCCCCCCCCCCCCCC		26.8125521595
238PhosphorylationSRGSPRYSPRHSRSR
CCCCCCCCCCCCCCC		19.4125521595
242PhosphorylationPRYSPRHSRSRSRT-
CCCCCCCCCCCCCC-		32.9825521595
244PhosphorylationYSPRHSRSRSRT---
CCCCCCCCCCCC---		37.3123684622
246PhosphorylationPRHSRSRSRT-----
CCCCCCCCCC-----		41.3329899451
248PhosphorylationHSRSRSRT-------
CCCCCCCC-------		44.1829899451
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 SRSF1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF1_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 SRSF1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAR6A_MOUSEPard6aphysical
19379695
DSRAD_HUMANADARphysical
26496610
CLK3_HUMANCLK3physical
26496610
DDX3X_HUMANDDX3Xphysical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
HNRH3_HUMANHNRNPH3physical
26496610
ANM1_HUMANPRMT1physical
26496610
RBM3_HUMANRBM3physical
26496610
SAFB1_HUMANSAFBphysical
26496610
SRSF5_HUMANSRSF5physical
26496610
RU17_HUMANSNRNP70physical
26496610
SMD3_HUMANSNRPD3physical
26496610
DX39B_HUMANDDX39Bphysical
26496610
KAT6A_HUMANKAT6Aphysical
26496610
PABP2_HUMANPABPN1physical
26496610
RBP56_HUMANTAF15physical
26496610
DHX16_HUMANDHX16physical
26496610
THOC5_HUMANTHOC5physical
26496610
SRSF9_HUMANSRSF9physical
26496610
TNK1_HUMANTNK1physical
26496610
PPIG_HUMANPPIGphysical
26496610
ABC3B_HUMANAPOBEC3Bphysical
26496610
FL2D_HUMANWTAPphysical
26496610
SAFB2_HUMANSAFB2physical
26496610
BCLF1_HUMANBCLAF1physical
26496610
BRE1B_HUMANRNF40physical
26496610
ZC11A_HUMANZC3H11Aphysical
26496610
THOC1_HUMANTHOC1physical
26496610
RBM6_HUMANRBM6physical
26496610
SRRM1_HUMANSRRM1physical
26496610
CRTAP_HUMANCRTAPphysical
26496610
DDX17_HUMANDDX17physical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
SRSF8_HUMANSRSF8physical
26496610
CPSF5_HUMANNUDT21physical
26496610
PLPHP_HUMANPROSCphysical
26496610
MINT_HUMANSPENphysical
26496610
U520_HUMANSNRNP200physical
26496610
PPIL2_HUMANPPIL2physical
26496610
VIR_HUMANKIAA1429physical
26496610
RBMX_HUMANRBMXphysical
26496610
ZN638_HUMANZNF638physical
26496610
WAC_HUMANWACphysical
26496610
PPHLN_HUMANPPHLN1physical
26496610
KLF13_HUMANKLF13physical
26496610
RBM27_HUMANRBM27physical
26496610
MPP8_HUMANMPHOSPH8physical
26496610
F208B_HUMANFAM208Bphysical
26496610
P3H2_HUMANP3H2physical
26496610
YLPM1_HUMANYLPM1physical
26496610
THOC2_HUMANTHOC2physical
26496610
NCOA5_HUMANNCOA5physical
26496610
RBM26_HUMANRBM26physical
26496610
P3H1_HUMANP3H1physical
26496610
CSN7B_HUMANCOPS7Bphysical
26496610
RBM15_HUMANRBM15physical
26496610
THOC6_HUMANTHOC6physical
26496610
SLTM_HUMANSLTMphysical
26496610
ZC3HE_HUMANZC3H14physical
26496610
THOC7_HUMANTHOC7physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
THOC3_HUMANTHOC3physical
26496610
K1671_HUMANKIAA1671physical
26496610
TTC14_HUMANTTC14physical
26496610
TXLNA_HUMANTXLNAphysical
26496610
ROA3_HUMANHNRNPA3physical
26496610
ZN326_HUMANZNF326physical
26496610
RB12B_HUMANRBM12Bphysical
26496610
RMXL1_HUMANRBMXL1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRSF1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-201, 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-231 AND SER-238, ANDMASS SPECTROMETRY.

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