SRS10_HUMAN - dbPTM
SRS10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRS10_HUMAN
UniProt AC O75494
Protein Name Serine/arginine-rich splicing factor 10
Gene Name SRSF10
Organism Homo sapiens (Human).
Sequence Length 262
Subcellular Localization Nucleus speckle . Cytoplasm .
Protein Description Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. [PubMed: 11684676]
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
2Phosphorylation------MSRYLRPPN
------CCCCCCCCC
29.6324719451
4Phosphorylation----MSRYLRPPNTS
----CCCCCCCCCCC
10.3528152594
6Methylation--MSRYLRPPNTSLF
--CCCCCCCCCCCEE
35.3881453731
10PhosphorylationRYLRPPNTSLFVRNV
CCCCCCCCCEEEEEC
32.3624719451
11PhosphorylationYLRPPNTSLFVRNVA
CCCCCCCCEEEEECC
26.8428152594
15MethylationPNTSLFVRNVADDTR
CCCCEEEEECCCCCC
25.27115917845
21PhosphorylationVRNVADDTRSEDLRR
EEECCCCCCCHHHHH
36.3223401153
22MethylationRNVADDTRSEDLRRE
EECCCCCCCHHHHHH
45.07115917849
23PhosphorylationNVADDTRSEDLRREF
ECCCCCCCHHHHHHH
37.2429255136
40PhosphorylationYGPIVDVYVPLDFYT
CCCEEEEEEEEHHHC
7.59-
55PhosphorylationRRPRGFAYVQFEDVR
CCCCCEEEEEEECCC
7.7927642862
62MethylationYVQFEDVRDAEDALH
EEEEECCCCHHHHHH
50.14115917853
92PhosphorylationFAQGDRKTPNQMKAK
ECCCCCCCCCCCCCC
28.5023401153
99AcetylationTPNQMKAKEGRNVYS
CCCCCCCCCCCCCCC
56.0011922409
105PhosphorylationAKEGRNVYSSSRYDD
CCCCCCCCCCCCCCC
13.3423927012
106PhosphorylationKEGRNVYSSSRYDDY
CCCCCCCCCCCCCCH
19.9725159151
107PhosphorylationEGRNVYSSSRYDDYD
CCCCCCCCCCCCCHH
10.9330266825
108PhosphorylationGRNVYSSSRYDDYDR
CCCCCCCCCCCCHHH
28.9923927012
110PhosphorylationNVYSSSRYDDYDRYR
CCCCCCCCCCHHHHH
18.3423927012
113PhosphorylationSSSRYDDYDRYRRSR
CCCCCCCHHHHHHHH
10.2223403867
116PhosphorylationRYDDYDRYRRSRSRS
CCCCHHHHHHHHCHH
13.8923186163
119PhosphorylationDYDRYRRSRSRSYER
CHHHHHHHHCHHHHH
26.1323898821
121PhosphorylationDRYRRSRSRSYERRR
HHHHHHHCHHHHHHH
27.1626055452
123PhosphorylationYRRSRSRSYERRRSR
HHHHHCHHHHHHHHH
32.3726055452
124PhosphorylationRRSRSRSYERRRSRS
HHHHCHHHHHHHHHC
16.6130576142
129PhosphorylationRSYERRRSRSRSFDY
HHHHHHHHHCCCCCC
32.5626846344
131PhosphorylationYERRRSRSRSFDYNY
HHHHHHHCCCCCCCC
33.2622167270
133PhosphorylationRRRSRSRSFDYNYRR
HHHHHCCCCCCCCCC
24.5819664994
133 (in isoform 2)Phosphorylation-24.5825849741
133 (in isoform 6)Phosphorylation-24.5825849741
136PhosphorylationSRSRSFDYNYRRSYS
HHCCCCCCCCCCCCC
16.4526846344
136 (in isoform 2)Phosphorylation-16.4529116813
136 (in isoform 6)Phosphorylation-16.4529116813
138PhosphorylationSRSFDYNYRRSYSPR
CCCCCCCCCCCCCCC
10.9423927012
141PhosphorylationFDYNYRRSYSPRNSR
CCCCCCCCCCCCCCC
22.4421955146
141 (in isoform 2)Phosphorylation-22.4425849741
141 (in isoform 5)Phosphorylation-22.4424719451
141 (in isoform 6)Phosphorylation-22.4425849741
142PhosphorylationDYNYRRSYSPRNSRP
CCCCCCCCCCCCCCC
22.3823403867
142 (in isoform 5)Phosphorylation-22.3828450419
143PhosphorylationYNYRRSYSPRNSRPT
CCCCCCCCCCCCCCC
20.7321955146
143 (in isoform 2)Phosphorylation-20.7325849741
143 (in isoform 5)Phosphorylation-20.7328450419
143 (in isoform 6)Phosphorylation-20.7325849741
147PhosphorylationRSYSPRNSRPTGRPR
CCCCCCCCCCCCCCC
40.7023186163
150PhosphorylationSPRNSRPTGRPRRSR
CCCCCCCCCCCCCCC
44.7224719451
150 (in isoform 5)Phosphorylation-44.7228450419
153 (in isoform 5)Phosphorylation-37.0627251275
155 (in isoform 2)Phosphorylation-38.8229116813
155 (in isoform 6)Phosphorylation-38.8222617229
156PhosphorylationPTGRPRRSRSHSDND
CCCCCCCCCCCCCCH
39.1426846344
156 (in isoform 3)Phosphorylation-39.1422617229
156 (in isoform 4)Phosphorylation-39.1423663014
157 (in isoform 2)Phosphorylation-36.2625849741
157 (in isoform 6)Phosphorylation-36.2622167270
158PhosphorylationGRPRRSRSHSDNDRF
CCCCCCCCCCCCHHH
28.7030266825
158 (in isoform 3)Phosphorylation-28.7022167270
158 (in isoform 4)Phosphorylation-28.7025849741
159 (in isoform 2)Phosphorylation-37.7525849741
159 (in isoform 6)Phosphorylation-37.7522167270
160PhosphorylationPRRSRSHSDNDRFKH
CCCCCCCCCCHHHHH
39.0830266825
160 (in isoform 3)Phosphorylation-39.0822167270
160 (in isoform 4)Phosphorylation-39.0823663014
164 (in isoform 4)Phosphorylation-49.0923663014
167 (in isoform 4)Phosphorylation-29.5420068231
167 (in isoform 6)Phosphorylation-29.5422167270
168 (in isoform 3)Phosphorylation-40.6322167270
170 (in isoform 6)Phosphorylation-38.7522167270
171PhosphorylationRFKHRNRSFSRSKSN
HHHHHHHHHHHCCCC
30.9920363803
171 (in isoform 3)Phosphorylation-30.9922167270
172 (in isoform 6)Phosphorylation-6.7622167270
173PhosphorylationKHRNRSFSRSKSNSR
HHHHHHHHHCCCCCC
36.5720363803
173 (in isoform 3)Phosphorylation-36.5722167270
173 (in isoform 6)Phosphorylation-36.5722167270
174 (in isoform 3)Phosphorylation-46.2022167270
174 (in isoform 6)Phosphorylation-46.2028450419
175PhosphorylationRNRSFSRSKSNSRSR
HHHHHHHCCCCCCCC
38.9620363803
175 (in isoform 3)Phosphorylation-38.9628450419
176 (in isoform 6)Phosphorylation-53.1728450419
177 (in isoform 3)Phosphorylation-41.0828450419
177 (in isoform 6)Phosphorylation-41.0820068231
178 (in isoform 3)Phosphorylation-45.2220068231
178 (in isoform 6)Phosphorylation-45.2220068231
179 (in isoform 3)Phosphorylation-38.4320068231
179 (in isoform 6)Phosphorylation-38.4320068231
180 (in isoform 3)Phosphorylation-40.1020068231
185PhosphorylationNSRSRSKSQPKKEMK
CCCCCCCCCCHHHHH
53.6226657352
195PhosphorylationKKEMKAKSRSRSASH
HHHHHHHHHHCCCCC
40.1130576142
197PhosphorylationEMKAKSRSRSASHTK
HHHHHHHHCCCCCCC
37.3630576142
199PhosphorylationKAKSRSRSASHTKTR
HHHHHHCCCCCCCCC
35.0630576142
201PhosphorylationKSRSRSASHTKTRGT
HHHHCCCCCCCCCCC
32.7028176443
203PhosphorylationRSRSASHTKTRGTSK
HHCCCCCCCCCCCCC
31.4528176443
205PhosphorylationRSASHTKTRGTSKTD
CCCCCCCCCCCCCCC
35.1723312004
208PhosphorylationSHTKTRGTSKTDSKT
CCCCCCCCCCCCCCC
24.6124719451
209PhosphorylationHTKTRGTSKTDSKTH
CCCCCCCCCCCCCCC
36.0630576142
211PhosphorylationKTRGTSKTDSKTHYK
CCCCCCCCCCCCCCC
45.3226074081
213PhosphorylationRGTSKTDSKTHYKSG
CCCCCCCCCCCCCCC
44.6926657352
215PhosphorylationTSKTDSKTHYKSGSR
CCCCCCCCCCCCCCC
34.1026074081
217PhosphorylationKTDSKTHYKSGSRYE
CCCCCCCCCCCCCCC
16.4526074081
219PhosphorylationDSKTHYKSGSRYEKE
CCCCCCCCCCCCCHH
34.5326074081
221PhosphorylationKTHYKSGSRYEKESR
CCCCCCCCCCCHHHC
38.4924719451
223PhosphorylationHYKSGSRYEKESRKK
CCCCCCCCCHHHCCC
32.8126074081
235PhosphorylationRKKEPPRSKSQSRSQ
CCCCCCCCHHHHHHH
42.2926657352
237O-linked_GlycosylationKEPPRSKSQSRSQSR
CCCCCCHHHHHHHHH
34.3330379171
239O-linked_GlycosylationPPRSKSQSRSQSRSR
CCCCHHHHHHHHHHC
40.7830379171
249PhosphorylationQSRSRSKSRSRSWTS
HHHHCHHHHCCCCCC
36.4120164059
251PhosphorylationRSRSKSRSRSWTSPK
HHCHHHHCCCCCCCC
37.4422167270
253PhosphorylationRSKSRSRSWTSPKSS
CHHHHCCCCCCCCCC
35.6322167270
255PhosphorylationKSRSRSWTSPKSSGH
HHHCCCCCCCCCCCC
36.0822167270
256PhosphorylationSRSRSWTSPKSSGH-
HHCCCCCCCCCCCC-
24.8728355574
259PhosphorylationRSWTSPKSSGH----
CCCCCCCCCCC----
44.9623663014
260PhosphorylationSWTSPKSSGH-----
CCCCCCCCCC-----
47.1920363803

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRS10_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 SRS10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRA2A_HUMANTRA2Aphysical
22939629
VTNC_HUMANVTNphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
TRI55_HUMANTRIM55physical
22939629
SYEP_HUMANEPRSphysical
22939629
TCRG1_HUMANTCERG1physical
22939629
SPF27_HUMANBCAS2physical
22939629
VASN_HUMANVASNphysical
22939629
THOC6_HUMANTHOC6physical
22939629
ZN687_HUMANZNF687physical
22939629
SNUT2_HUMANUSP39physical
22939629
TR112_HUMANTRMT112physical
22939629
TCOF_HUMANTCOF1physical
22939629
SMU1_HUMANSMU1physical
22939629
SRSF6_HUMANSRSF6physical
22939629
SRSF1_HUMANSRSF1physical
22365833
SRSF4_HUMANSRSF4physical
22365833
TRA2B_HUMANTRA2Bphysical
22365833

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 SRS10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, 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-133, AND MASSSPECTROMETRY.
"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-129; SER-131 ANDSER-133, 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-131 AND SER-133, ANDMASS 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-129; SER-131 ANDSER-133, AND MASS 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 TYR-110; SER-129; SER-131;SER-133; SER-156; SER-158; SER-160; SER-235; SER-251; SER-253; THR-255AND SER-256, 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-133, AND MASSSPECTROMETRY.

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