SRSF6_HUMAN - dbPTM
SRSF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF6_HUMAN
UniProt AC Q13247
Protein Name Serine/arginine-rich splicing factor 6
Gene Name SRSF6
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing..
Protein Sequence MPRVYIGRLSYNVREKDIQRFFSGYGRLLEVDLKNGYGFVEFEDSRDADDAVYELNGKELCGERVIVEHARGPRRDRDGYSYGSRSGGGGYSSRRTSGRDKYGPPVRTEYRLIVENLSSRCSWQDLKDFMRQAGEVTYADAHKERTNEGVIEFRSYSDMKRALDKLDGTEINGRNIRLIEDKPRTSHRRSYSGSRSRSRSRRRSRSRSRRSSRSRSRSISKSRSRSRSRSKGRSRSRSKGRKSRSKSKSKPKSDRGSHSHSRSRSKDEYEKSRSRSRSRSPKENGKGDIKSKSRSRSQSRSNSPLPVPPSKARSVSPPPKRATSRSRSRSRSKSRSRSRSSSRD
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
10PhosphorylationRVYIGRLSYNVREKD
CEEEEEEEECCCHHH		17.1928555341
23PhosphorylationKDIQRFFSGYGRLLE
HHHHHHHCCCCCEEE		28.5228152594
25PhosphorylationIQRFFSGYGRLLEVD
HHHHHCCCCCEEEEE		9.6223186163
37PhosphorylationEVDLKNGYGFVEFED
EEECCCCCEEEEEEC		19.4528152594
45PhosphorylationGFVEFEDSRDADDAV
EEEEEECCCCCCCCE		25.5119664994
53PhosphorylationRDADDAVYELNGKEL
CCCCCCEEEECCEEC		19.2028450419
58UbiquitinationAVYELNGKELCGERV
CEEEECCEECCCCEE		46.5733845483
58AcetylationAVYELNGKELCGERV
CEEEECCEECCCCEE		46.5726051181
71MethylationRVIVEHARGPRRDRD
EEEEEECCCCCCCCC		58.52-
80PhosphorylationPRRDRDGYSYGSRSG
CCCCCCCCCCCCCCC		11.7420068231
81PhosphorylationRRDRDGYSYGSRSGG
CCCCCCCCCCCCCCC		28.6621712546
82PhosphorylationRDRDGYSYGSRSGGG
CCCCCCCCCCCCCCC		15.6130576142
84PhosphorylationRDGYSYGSRSGGGGY
CCCCCCCCCCCCCCC		18.2926055452
85MethylationDGYSYGSRSGGGGYS
CCCCCCCCCCCCCCC		34.6580700761
86PhosphorylationGYSYGSRSGGGGYSS
CCCCCCCCCCCCCCC		43.4125849741
91PhosphorylationSRSGGGGYSSRRTSG
CCCCCCCCCCCCCCC		13.5220068231
92PhosphorylationRSGGGGYSSRRTSGR
CCCCCCCCCCCCCCC		22.2026074081
93PhosphorylationSGGGGYSSRRTSGRD
CCCCCCCCCCCCCCC		19.8026074081
96PhosphorylationGGYSSRRTSGRDKYG
CCCCCCCCCCCCCCC		34.1327174698
97PhosphorylationGYSSRRTSGRDKYGP
CCCCCCCCCCCCCCC		29.9829496963
101UbiquitinationRRTSGRDKYGPPVRT
CCCCCCCCCCCCCCC		51.2323000965
1012-HydroxyisobutyrylationRRTSGRDKYGPPVRT
CCCCCCCCCCCCCCC		51.23-
101AcetylationRRTSGRDKYGPPVRT
CCCCCCCCCCCCCCC		51.2323749302
102PhosphorylationRTSGRDKYGPPVRTE
CCCCCCCCCCCCCCC		38.8728152594
108PhosphorylationKYGPPVRTEYRLIVE
CCCCCCCCCHHHHHH		37.2928152594
110PhosphorylationGPPVRTEYRLIVENL
CCCCCCCHHHHHHCH		15.3128152594
118PhosphorylationRLIVENLSSRCSWQD
HHHHHCHHHCCCHHH		27.5829255136
119PhosphorylationLIVENLSSRCSWQDL
HHHHCHHHCCCHHHH		40.2419664994
122PhosphorylationENLSSRCSWQDLKDF
HCHHHCCCHHHHHHH		27.0225159151
127AcetylationRCSWQDLKDFMRQAG
CCCHHHHHHHHHHCC		58.1526051181
127UbiquitinationRCSWQDLKDFMRQAG
CCCHHHHHHHHHHCC		58.1521906983
127 (in isoform 1)Ubiquitination-58.1521890473
127 (in isoform 3)Ubiquitination-58.1521890473
137PhosphorylationMRQAGEVTYADAHKE
HHHCCCCEEHHHHHH		14.5328152594
138PhosphorylationRQAGEVTYADAHKER
HHCCCCEEHHHHHHH		13.9928152594
143AcetylationVTYADAHKERTNEGV
CEEHHHHHHHCCCCE		51.0826051181
143UbiquitinationVTYADAHKERTNEGV
CEEHHHHHHHCCCCE		51.0833845483
1432-HydroxyisobutyrylationVTYADAHKERTNEGV
CEEHHHHHHHCCCCE		51.08-
146PhosphorylationADAHKERTNEGVIEF
HHHHHHHCCCCEEEE		38.4225849741
155PhosphorylationEGVIEFRSYSDMKRA
CCEEEEECHHHHHHH		34.0228555341
157PhosphorylationVIEFRSYSDMKRALD
EEEEECHHHHHHHHH		32.2621815630
160UbiquitinationFRSYSDMKRALDKLD
EECHHHHHHHHHHCC		39.2422817900
1602-HydroxyisobutyrylationFRSYSDMKRALDKLD
EECHHHHHHHHHHCC		39.24-
165 (in isoform 3)Ubiquitination-49.6921890473
1652-HydroxyisobutyrylationDMKRALDKLDGTEIN
HHHHHHHHCCCCEEC		49.69-
165UbiquitinationDMKRALDKLDGTEIN
HHHHHHHHCCCCEEC		49.6922817900
165 (in isoform 1)Ubiquitination-49.6921890473
165AcetylationDMKRALDKLDGTEIN
HHHHHHHHCCCCEEC		49.6923954790
169PhosphorylationALDKLDGTEINGRNI
HHHHCCCCEECCEEE		33.1024719451
1822-HydroxyisobutyrylationNIRLIEDKPRTSHRR
EEEEECCCCCCCCCC		24.49-
182AcetylationNIRLIEDKPRTSHRR
EEEEECCCCCCCCCC		24.4923749302
182SumoylationNIRLIEDKPRTSHRR
EEEEECCCCCCCCCC		24.4928112733
182UbiquitinationNIRLIEDKPRTSHRR
EEEEECCCCCCCCCC		24.4929967540
185PhosphorylationLIEDKPRTSHRRSYS
EECCCCCCCCCCCCC		37.0924719451
186PhosphorylationIEDKPRTSHRRSYSG
ECCCCCCCCCCCCCC		19.1029449344
190PhosphorylationPRTSHRRSYSGSRSR
CCCCCCCCCCCCHHH		24.4920363803
191PhosphorylationRTSHRRSYSGSRSRS
CCCCCCCCCCCHHHH		18.4220363803
192PhosphorylationTSHRRSYSGSRSRSR
CCCCCCCCCCHHHHH		31.3820363803
194PhosphorylationHRRSYSGSRSRSRSR
CCCCCCCCHHHHHHH		22.5720363803
196PhosphorylationRSYSGSRSRSRSRRR
CCCCCCHHHHHHHHH		35.9820363803
198PhosphorylationYSGSRSRSRSRRRSR
CCCCHHHHHHHHHHH		35.5429449344
204PhosphorylationRSRSRRRSRSRSRRS
HHHHHHHHHHHHHHH		32.5626074081
206PhosphorylationRSRRRSRSRSRRSSR
HHHHHHHHHHHHHHH		35.5426074081
208PhosphorylationRRRSRSRSRRSSRSR
HHHHHHHHHHHHHHH		33.0426074081
216PhosphorylationRRSSRSRSRSISKSR
HHHHHHHHHHHHHHH		31.4624144214
218PhosphorylationSSRSRSRSISKSRSR
HHHHHHHHHHHHHHH		32.2424144214
220PhosphorylationRSRSRSISKSRSRSR
HHHHHHHHHHHHHHH		26.3124719451
222PhosphorylationRSRSISKSRSRSRSR
HHHHHHHHHHHHHHH		28.7924144214
242MethylationRSRSKGRKSRSKSKS
CCHHHCCCCCCCCCC		59.9123748837
253PhosphorylationKSKSKPKSDRGSHSH
CCCCCCCCCCCCCCC		40.8623403867
257PhosphorylationKPKSDRGSHSHSRSR
CCCCCCCCCCCCCCC		23.7827422710
259PhosphorylationKSDRGSHSHSRSRSK
CCCCCCCCCCCCCCH		25.5120068231
261PhosphorylationDRGSHSHSRSRSKDE
CCCCCCCCCCCCHHH		34.6620068231
263PhosphorylationGSHSHSRSRSKDEYE
CCCCCCCCCCHHHHH		43.8726055452
265PhosphorylationHSHSRSRSKDEYEKS
CCCCCCCCHHHHHHH		45.7826055452
269PhosphorylationRSRSKDEYEKSRSRS
CCCCHHHHHHHHHHH		38.5028985074
272PhosphorylationSKDEYEKSRSRSRSR
CHHHHHHHHHHHCCC		24.4525849741
274PhosphorylationDEYEKSRSRSRSRSP
HHHHHHHHHHCCCCC		41.5224719451
278PhosphorylationKSRSRSRSRSPKENG
HHHHHHCCCCCCCCC		38.0524144214
280PhosphorylationRSRSRSRSPKENGKG
HHHHCCCCCCCCCCC		41.3824719451
290AcetylationENGKGDIKSKSRSRS
CCCCCCCCCCCCCCC		57.487297899
291PhosphorylationNGKGDIKSKSRSRSQ
CCCCCCCCCCCCCCC		35.8830576142
293PhosphorylationKGDIKSKSRSRSQSR
CCCCCCCCCCCCCCC		42.4520363803
295PhosphorylationDIKSKSRSRSQSRSN
CCCCCCCCCCCCCCC		43.2925159151
297PhosphorylationKSKSRSRSQSRSNSP
CCCCCCCCCCCCCCC		33.4825159151
299PhosphorylationKSRSRSQSRSNSPLP
CCCCCCCCCCCCCCC		38.6330278072
301PhosphorylationRSRSQSRSNSPLPVP
CCCCCCCCCCCCCCC		47.0829255136
303PhosphorylationRSQSRSNSPLPVPPS
CCCCCCCCCCCCCHH		29.1219664994
303 (in isoform 3)Phosphorylation-29.1229743597
310PhosphorylationSPLPVPPSKARSVSP
CCCCCCHHHHCCCCC		32.6423927012
314PhosphorylationVPPSKARSVSPPPKR
CCHHHHCCCCCCCCC		31.6322167270
316PhosphorylationPSKARSVSPPPKRAT
HHHHCCCCCCCCCCC		32.7022167270
323PhosphorylationSPPPKRATSRSRSRS
CCCCCCCCCHHHHHH		28.8020068231
324PhosphorylationPPPKRATSRSRSRSR
CCCCCCCCHHHHHHH		27.5520068231
326PhosphorylationPKRATSRSRSRSRSK
CCCCCCHHHHHHHHH		34.0820068231
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
303SPhosphorylationKinaseDYRK1AQ13627
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF6_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 SRSF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNPS1_HUMANRNPS1physical
16189514
A4_HUMANAPPphysical
21832049
SF3B4_HUMANSF3B4physical
22365833
RBM10_HUMANRBM10physical
22365833
TRA2B_HUMANTRA2Bphysical
22365833
TOE1_HUMANTOE1physical
22365833
RL24_HUMANRPL24physical
22863883
LC7L2_HUMANLUC7L2physical
25416956
ATLA3_HUMANATL3physical
26344197
RBBP4_HUMANRBBP4physical
26344197
RNPS1_HUMANRNPS1physical
26344197
SRSF1_HUMANSRSF1physical
26344197
TRA2A_HUMANTRA2Aphysical
26344197
TRA2B_HUMANTRA2Bphysical
26344197
SRSF3_HUMANSRSF3physical
27173435
PR38A_HUMANPRPF38Aphysical
27173435
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 SRSF6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-303, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-303; SER-314AND SER-316, AND MASS SPECTROMETRY.
"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-297; SER-299; SER-303;SER-314 AND SER-316, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASSSPECTROMETRY.
"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-303; SER-314 ANDSER-316, AND MASS 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-303, AND MASSSPECTROMETRY.
"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-45; SER-259; SER-297;SER-299; SER-301; SER-303; SER-314 AND SER-316, AND MASS SPECTROMETRY.
"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-301; SER-314 ANDSER-316, AND MASS SPECTROMETRY.

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