SRSF9_HUMAN - dbPTM
SRSF9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF9_HUMAN
UniProt AC Q13242
Protein Name Serine/arginine-rich splicing factor 9
Gene Name SRSF9
Organism Homo sapiens (Human).
Sequence Length 221
Subcellular Localization Nucleus . Cellular stresses such as heat shock may induce localization to discrete nuclear bodies termed SAM68 nuclear bodies (SNBs), HAP bodies, or stress bodies. Numerous splicing factors including SRSF1/SFRS1/SF2, SRSF7/SFRS7, SAFB and KHDRBS1/SAM
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..
Protein Sequence MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
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------MSGWADERG
------CCCCCCCCC		42.9430108239
8MethylationMSGWADERGGEGDGR
CCCCCCCCCCCCCCC		59.99115916817
17PhosphorylationGEGDGRIYVGNLPTD
CCCCCCEEECCCCCC		10.8428152594
23PhosphorylationIYVGNLPTDVREKDL
EEECCCCCCCCHHHH		50.7428555341
28AcetylationLPTDVREKDLEDLFY
CCCCCCHHHHHHHHH		57.9825953088
28UbiquitinationLPTDVREKDLEDLFY
CCCCCCHHHHHHHHH		57.9823000965
35PhosphorylationKDLEDLFYKYGRIRE
HHHHHHHHHHCCEEE		15.5917360941
36AcetylationDLEDLFYKYGRIREI
HHHHHHHHHCCEEEE		33.6225825284
36NeddylationDLEDLFYKYGRIREI
HHHHHHHHHCCEEEE		33.6232015554
36SumoylationDLEDLFYKYGRIREI
HHHHHHHHHCCEEEE		33.6228112733
36UbiquitinationDLEDLFYKYGRIREI
HHHHHHHHHCCEEEE		33.6223000965
46UbiquitinationRIREIELKNRHGLVP
CEEEEEECCCCCCCC		38.8624816145
63MethylationFVRFEDPRDAEDAIY
EEEECCCCCHHHHHC		69.00115916813
70PhosphorylationRDAEDAIYGRNGYDY
CCHHHHHCCCCCCCC		16.2620090780
75PhosphorylationAIYGRNGYDYGQCRL
HHCCCCCCCCCCEEE		15.0020090780
88MethylationRLRVEFPRTYGGRGG
EEEEECCCCCCCCCC		45.9954559257
89PhosphorylationLRVEFPRTYGGRGGW
EEEECCCCCCCCCCC		27.1030206219
90PhosphorylationRVEFPRTYGGRGGWP
EEECCCCCCCCCCCC		20.8930206219
93MethylationFPRTYGGRGGWPRGG
CCCCCCCCCCCCCCC		35.7724394749
98MethylationGGRGGWPRGGRNGPP
CCCCCCCCCCCCCCC		54.4030761011
101MethylationGGWPRGGRNGPPTRR
CCCCCCCCCCCCCCH		47.9980701701
106PhosphorylationGGRNGPPTRRSDFRV
CCCCCCCCCHHCCEE		41.6828555341
109PhosphorylationNGPPTRRSDFRVLVS
CCCCCCHHCCEEEEE		37.5029214152
123PhosphorylationSGLPPSGSWQDLKDH
ECCCCCCCHHHHHHH		26.3827067055
128UbiquitinationSGSWQDLKDHMREAG
CCCHHHHHHHHHHHC		54.6123000965
132MethylationQDLKDHMREAGDVCY
HHHHHHHHHHCCEEE		27.48115916793
138GlutathionylationMREAGDVCYADVQKD
HHHHCCEEEEEHHHC		2.4922555962
139PhosphorylationREAGDVCYADVQKDG
HHHCCEEEEEHHHCC		12.9928796482
144UbiquitinationVCYADVQKDGVGMVE
EEEEEHHHCCCCHHH		57.1932015554
144AcetylationVCYADVQKDGVGMVE
EEEEEHHHCCCCHHH		57.1926051181
152PhosphorylationDGVGMVEYLRKEDME
CCCCHHHHHCHHHHH		10.61-
154MethylationVGMVEYLRKEDMEYA
CCHHHHHCHHHHHHH		39.14115916797
155UbiquitinationGMVEYLRKEDMEYAL
CHHHHHCHHHHHHHH		56.3121906983
155AcetylationGMVEYLRKEDMEYAL
CHHHHHCHHHHHHHH		56.3126051181
160PhosphorylationLRKEDMEYALRKLDD
HCHHHHHHHHHHCCC		12.3328152594
163MethylationEDMEYALRKLDDTKF
HHHHHHHHHCCCCCC		29.35115916801
164UbiquitinationDMEYALRKLDDTKFR
HHHHHHHHCCCCCCC		58.0633845483
168PhosphorylationALRKLDDTKFRSHEG
HHHHCCCCCCCCCCC		31.5821406692
169UbiquitinationLRKLDDTKFRSHEGE
HHHCCCCCCCCCCCC		45.8627667366
169AcetylationLRKLDDTKFRSHEGE
HHHCCCCCCCCCCCC		45.8625953088
171MethylationKLDDTKFRSHEGETS
HCCCCCCCCCCCCCE		38.36115916805
172PhosphorylationLDDTKFRSHEGETSY
CCCCCCCCCCCCCEE		29.0828555341
177PhosphorylationFRSHEGETSYIRVYP
CCCCCCCCEEEEEEC		37.3728152594
178PhosphorylationRSHEGETSYIRVYPE
CCCCCCCEEEEEECC		17.7928152594
179PhosphorylationSHEGETSYIRVYPER
CCCCCCEEEEEECCC		10.5225884760
181MethylationEGETSYIRVYPERST
CCCCEEEEEECCCCC		17.43115916809
183PhosphorylationETSYIRVYPERSTSY
CCEEEEEECCCCCCC		6.9026074081
187PhosphorylationIRVYPERSTSYGYSR
EEEECCCCCCCCCCC		21.7522167270
188PhosphorylationRVYPERSTSYGYSRS
EEECCCCCCCCCCCC		31.9922167270
189PhosphorylationVYPERSTSYGYSRSR
EECCCCCCCCCCCCC		20.1522167270
190PhosphorylationYPERSTSYGYSRSRS
ECCCCCCCCCCCCCC		21.8522167270
192PhosphorylationERSTSYGYSRSRSGS
CCCCCCCCCCCCCCC		7.8322167270
193PhosphorylationRSTSYGYSRSRSGSR
CCCCCCCCCCCCCCC		21.2923401153
194MethylationSTSYGYSRSRSGSRG
CCCCCCCCCCCCCCC		27.8380701693
195PhosphorylationTSYGYSRSRSGSRGR
CCCCCCCCCCCCCCC		25.5125159151
197PhosphorylationYGYSRSRSGSRGRDS
CCCCCCCCCCCCCCC		42.2223898821
199PhosphorylationYSRSRSGSRGRDSPY
CCCCCCCCCCCCCCC		32.5725367160
204PhosphorylationSGSRGRDSPYQSRGS
CCCCCCCCCCCCCCC		24.9329255136
206PhosphorylationSRGRDSPYQSRGSPH
CCCCCCCCCCCCCCC		24.0723927012
208PhosphorylationGRDSPYQSRGSPHYF
CCCCCCCCCCCCCCC		32.5329255136
209MethylationRDSPYQSRGSPHYFS
CCCCCCCCCCCCCCC		33.8054559265
211PhosphorylationSPYQSRGSPHYFSPF
CCCCCCCCCCCCCCC		13.8525159151
214PhosphorylationQSRGSPHYFSPFRPY
CCCCCCCCCCCCCCC		14.7723927012
216PhosphorylationRGSPHYFSPFRPY--
CCCCCCCCCCCCC--		18.9023927012
221PhosphorylationYFSPFRPY-------
CCCCCCCC-------		27.2521945579
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
216SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF9_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YBOX1_HUMANYBX1physical
12604611
NOL3_HUMANNOL3physical
10196175
SAFB1_RATSafbphysical
9671816
HNRPR_HUMANHNRNPRphysical
17643375
NCBP1_HUMANNCBP1physical
17643375
A4_HUMANAPPphysical
21832049
U2AF2_HUMANU2AF2physical
22939629
T2FA_HUMANGTF2F1physical
22939629
VASP_HUMANVASPphysical
22939629
SIM20_HUMANSMIM20physical
22939629
SLD5_HUMANGINS4physical
22939629
U119B_HUMANUNC119Bphysical
22939629
UBE3A_HUMANUBE3Aphysical
22939629
HABP4_HUMANHABP4physical
19523114
SRSF1_HUMANSRSF1physical
19523114
HNRL1_HUMANHNRNPUL1physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
SRSF1_HUMANSRSF1physical
26344197
SRSF6_HUMANSRSF6physical
26344197
TRA2B_HUMANTRA2Bphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRSF9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-189; TYR-192;SER-195; SER-211 AND SER-216, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-216, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; TYR-214 ANDSER-216, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-216, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-216, ANDMASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-216, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-211, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-214, AND MASSSPECTROMETRY.

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