SRSF1_HUMAN - dbPTM
SRSF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF1_HUMAN
UniProt AC Q07955
Protein Name Serine/arginine-rich splicing factor 1
Gene Name SRSF1
Organism Homo sapiens (Human).
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. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. 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
2 (in isoform 3)Phosphorylation-46.26-
2 (in isoform 3)Acetylation-46.26-
2Phosphorylation------MSGGGVIRG
------CCCCCCEEC		46.2623401153
2Acetylation------MSGGGVIRG
------CCCCCCEEC		46.2620068231
19PhosphorylationGNNDCRIYVGNLPPD
CCCCCEEEECCCCCC		5.2820090780
29PhosphorylationNLPPDIRTKDIEDVF
CCCCCCCCCCHHHHH		33.1423312004
30UbiquitinationLPPDIRTKDIEDVFY
CCCCCCCCCHHHHHH		47.0321890473
30 (in isoform 2)Ubiquitination-47.0321890473
30SumoylationLPPDIRTKDIEDVFY
CCCCCCCCCHHHHHH		47.0328112733
30 (in isoform 1)Ubiquitination-47.0321890473
30AcetylationLPPDIRTKDIEDVFY
CCCCCCCCCHHHHHH		47.0323749302
30 (in isoform 3)Ubiquitination-47.0321890473
37PhosphorylationKDIEDVFYKYGAIRD
CCHHHHHHHHCCEEE		11.8020090780
37NitrationKDIEDVFYKYGAIRD
CCHHHHHHHHCCEEE		11.80-
38 (in isoform 1)Ubiquitination-26.2421890473
38 (in isoform 2)Ubiquitination-26.2421890473
38SumoylationDIEDVFYKYGAIRDI
CHHHHHHHHCCEEEC		26.2428112733
38 (in isoform 3)Acetylation-26.24-
38UbiquitinationDIEDVFYKYGAIRDI
CHHHHHHHHCCEEEC		26.2421890473
38 (in isoform 3)Ubiquitination-26.2421890473
38AcetylationDIEDVFYKYGAIRDI
CHHHHHHHHCCEEEC		26.2419608861
39PhosphorylationIEDVFYKYGAIRDID
HHHHHHHHCCEEECC		10.6228152594
48AcetylationAIRDIDLKNRRGGPP
CEEECCCCCCCCCCC		44.6625953088
48UbiquitinationAIRDIDLKNRRGGPP
CEEECCCCCCCCCCC		44.66-
51MethylationDIDLKNRRGGPPFAF
ECCCCCCCCCCCEEE		64.9154559169
65MethylationFVEFEDPRDAEDAVY
EEEECCCCCHHHCCC		69.00115916557
72PhosphorylationRDAEDAVYGRDGYDY
CCHHHCCCCCCCCCC		14.2521406692
77PhosphorylationAVYGRDGYDYDGYRL
CCCCCCCCCCCCEEE		18.6725884760
79PhosphorylationYGRDGYDYDGYRLRV
CCCCCCCCCCEEEEE		11.64-
82PhosphorylationDGYDYDGYRLRVEFP
CCCCCCCEEEEEECC		11.99-
90MethylationRLRVEFPRSGRGTGR
EEEEECCCCCCCCCC		58.00-
91PhosphorylationLRVEFPRSGRGTGRG
EEEECCCCCCCCCCC		32.8328555341
93MethylationVEFPRSGRGTGRGGG
EECCCCCCCCCCCCC		40.5224129315
93Asymmetric dimethylarginineVEFPRSGRGTGRGGG
EECCCCCCCCCCCCC		40.52-
97Asymmetric dimethylarginineRSGRGTGRGGGGGGG
CCCCCCCCCCCCCCC		40.18-
97MethylationRSGRGTGRGGGGGGG
CCCCCCCCCCCCCCC		40.1824129315
109Asymmetric dimethylarginineGGGGGAPRGRYGPPS
CCCCCCCCCCCCCCC		41.51-
109MethylationGGGGGAPRGRYGPPS
CCCCCCCCCCCCCCC		41.5124129315
111MethylationGGGAPRGRYGPPSRR
CCCCCCCCCCCCCCC		34.2224129315
112PhosphorylationGGAPRGRYGPPSRRS
CCCCCCCCCCCCCCC		36.49-
116PhosphorylationRGRYGPPSRRSENRV
CCCCCCCCCCCCCEE		43.3830576142
119PhosphorylationYGPPSRRSENRVVVS
CCCCCCCCCCEEEEE		37.8123186163
131PhosphorylationVVSGLPPSGSWQDLK
EEECCCCCCCHHHHH		43.4423186163
133PhosphorylationSGLPPSGSWQDLKDH
ECCCCCCCHHHHHHH		26.3823186163
138 (in isoform 1)Ubiquitination-54.6121890473
138AcetylationSGSWQDLKDHMREAG
CCCHHHHHHHHHHHC		54.6169059
138 (in isoform 3)Ubiquitination-54.6121890473
138 (in isoform 2)Ubiquitination-54.6121890473
138UbiquitinationSGSWQDLKDHMREAG
CCCHHHHHHHHHHHC		54.6121890473
148GlutathionylationMREAGDVCYADVYRD
HHHHCCEEEEEEEEC		2.4922555962
148S-palmitoylationMREAGDVCYADVYRD
HHHHCCEEEEEEEEC		2.4926865113
149PhosphorylationREAGDVCYADVYRDG
HHHCCEEEEEEEECC		12.9928796482
153PhosphorylationDVCYADVYRDGTGVV
CEEEEEEEECCCCEE		11.97-
157PhosphorylationADVYRDGTGVVEFVR
EEEEECCCCEEEEEE		30.9621712546
165AcetylationGVVEFVRKEDMTYAV
CEEEEEEHHHCCEEE		53.4126051181
165UbiquitinationGVVEFVRKEDMTYAV
CEEEEEEHHHCCEEE		53.41-
169PhosphorylationFVRKEDMTYAVRKLD
EEEHHHCCEEEEECC		22.2028102081
170NitrationVRKEDMTYAVRKLDN
EEHHHCCEEEEECCC		9.10-
170PhosphorylationVRKEDMTYAVRKLDN
EEHHHCCEEEEECCC		9.1017360941
174UbiquitinationDMTYAVRKLDNTKFR
HCCEEEEECCCCCCC		54.3021890473
174 (in isoform 3)Ubiquitination-54.3021890473
174 (in isoform 2)Ubiquitination-54.3021890473
174 (in isoform 1)Ubiquitination-54.3021890473
179AcetylationVRKLDNTKFRSHEGE
EEECCCCCCCCCCCC		45.0619608861
179 (in isoform 3)Acetylation-45.06-
179 (in isoform 2)Ubiquitination-45.0621890473
179 (in isoform 1)Ubiquitination-45.0621890473
179UbiquitinationVRKLDNTKFRSHEGE
EEECCCCCCCCCCCC		45.0619608861
182PhosphorylationLDNTKFRSHEGETAY
CCCCCCCCCCCCEEE		29.0830624053
187PhosphorylationFRSHEGETAYIRVKV
CCCCCCCEEEEEEEE		35.3028152594
189PhosphorylationSHEGETAYIRVKVDG
CCCCCEEEEEEEECC		9.1827273156
189NitrationSHEGETAYIRVKVDG
CCCCCEEEEEEEECC		9.18-
191MethylationEGETAYIRVKVDGPR
CCCEEEEEEEECCCC		14.99115916553
196 (in isoform 2)Phosphorylation-23.6217693683
199PhosphorylationVKVDGPRSPSYGRSR
EEECCCCCCCCCCCC		22.7229255136
201PhosphorylationVDGPRSPSYGRSRSR
ECCCCCCCCCCCCCC		41.2729255136
202PhosphorylationDGPRSPSYGRSRSRS
CCCCCCCCCCCCCCC		21.6822167270
205PhosphorylationRSPSYGRSRSRSRSR
CCCCCCCCCCCCHHH		30.1926846344
207PhosphorylationPSYGRSRSRSRSRSR
CCCCCCCCCCHHHHH		35.5418155240
209PhosphorylationYGRSRSRSRSRSRSR
CCCCCCCCHHHHHCC		35.5418155240
211PhosphorylationRSRSRSRSRSRSRSR
CCCCCCHHHHHCCCC		35.5418155240
213PhosphorylationRSRSRSRSRSRSRSN
CCCCHHHHHCCCCCC		35.5418155240
215PhosphorylationRSRSRSRSRSRSNSR
CCHHHHHCCCCCCCC		35.5418155240
217PhosphorylationRSRSRSRSRSNSRSR
HHHHHCCCCCCCCCC		41.1118155240
219PhosphorylationRSRSRSRSNSRSRSY
HHHCCCCCCCCCCCC		40.1618155240
221PhosphorylationRSRSRSNSRSRSYSP
HCCCCCCCCCCCCCC		32.6426846344
223PhosphorylationRSRSNSRSRSYSPRR
CCCCCCCCCCCCCCC		25.9626846344
225PhosphorylationRSNSRSRSYSPRRSR
CCCCCCCCCCCCCCC		31.0726846344
226PhosphorylationSNSRSRSYSPRRSRG
CCCCCCCCCCCCCCC		22.9126846344
227PhosphorylationNSRSRSYSPRRSRGS
CCCCCCCCCCCCCCC		17.1228355574
231PhosphorylationRSYSPRRSRGSPRYS
CCCCCCCCCCCCCCC		42.1226846344
234PhosphorylationSPRRSRGSPRYSPRH
CCCCCCCCCCCCCCC		12.7022167270
237PhosphorylationRSRGSPRYSPRHSRS
CCCCCCCCCCCCCCC		26.8122167270
238PhosphorylationSRGSPRYSPRHSRSR
CCCCCCCCCCCCCCC		19.4122167270
242PhosphorylationPRYSPRHSRSRSRT-
CCCCCCCCCCCCCC-		32.9822617229
244PhosphorylationYSPRHSRSRSRT---
CCCCCCCCCCCC---		37.3120068231
246PhosphorylationPRHSRSRSRT-----
CCCCCCCCCC-----		41.33-
248PhosphorylationHSRSRSRT-------
CCCCCCCC-------		44.18-
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
119SPhosphorylationKinasePRKACAP17612
GPS
133SPhosphorylationKinaseAMPKB1Q9Y478
PSP
133SPhosphorylationKinaseAMPKG2Q9UGJ0
PSP
133SPhosphorylationKinaseAMPKA1Q13131
PSP
205SPhosphorylationKinaseSRPK1Q96SB4
PSP
207SPhosphorylationKinaseSRPK1Q96SB4
PSP
209SPhosphorylationKinaseSRPK1Q96SB4
PSP
211SPhosphorylationKinaseSRPK1Q96SB4
PSP
213SPhosphorylationKinaseSRPK1Q96SB4
PSP
215SPhosphorylationKinaseSRPK1Q96SB4
PSP
217SPhosphorylationKinaseSRPK1Q96SB4
PSP
219SPhosphorylationKinaseSRPK1Q96SB4
PSP
221SPhosphorylationKinaseSRPK1Q96SB4
PSP
223SPhosphorylationKinaseSRPK1Q96SB4
PSP
225SPhosphorylationKinaseSRPK1Q96SB4
PSP
227SPhosphorylationKinaseSRPK1Q96SB4
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF1_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 SRSF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LNX1_HUMANLNX1physical
16189514
U2AF2_HUMANU2AF2physical
16189514
DIDO1_HUMANDIDO1physical
16189514
SRPK1_HUMANSRPK1physical
17517895
SKY1_YEASTSKY1physical
17517895
U2AF1_HUMANU2AF1physical
9799243
SRSF1_HUMANSRSF1physical
9799243
SRSF5_HUMANSRSF5physical
9799243
RU17_HUMANSNRNP70physical
9799243
SRSF2_HUMANSRSF2physical
8816452
SRSF1_HUMANSRSF1physical
8816452
U2AF1_HUMANU2AF1physical
8816452
SRPK1_HUMANSRPK1physical
10196197
PSIP1_HUMANPSIP1physical
9885563
SAFB1_RATSafbphysical
9671816
XBP1_HUMANXBP1physical
20211142
P53_HUMANTP53physical
20805487
TOP1_HUMANTOP1physical
20805487
PIAS1_HUMANPIAS1physical
20805487
NXF1_HUMANNXF1physical
15184380
NPM_HUMANNPM1physical
16376875
A4_HUMANAPPphysical
21832049
U2AF2_HUMANU2AF2physical
22939629
U2AF1_HUMANU2AF1physical
22939629
U5S1_HUMANEFTUD2physical
22939629
U520_HUMANSNRNP200physical
22939629
TRA2B_HUMANTRA2Bphysical
22939629
SMU1_HUMANSMU1physical
22939629
SNUT1_HUMANSART1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
VTNC_HUMANVTNphysical
22939629
ZNT5_HUMANSLC30A5physical
22939629
SURF4_HUMANSURF4physical
22939629
ZN326_HUMANZNF326physical
22939629
SNP23_HUMANSNAP23physical
22939629
VASN_HUMANVASNphysical
22939629
TRI55_HUMANTRIM55physical
22939629
TR112_HUMANTRMT112physical
22939629
ZNT1_HUMANSLC30A1physical
22939629
TMM43_HUMANTMEM43physical
22939629
SSRA_HUMANSSR1physical
22939629
TOM20_HUMANTOMM20physical
22939629
WDR18_HUMANWDR18physical
22939629
ROA0_HUMANHNRNPA0physical
22365833
RNPS1_HUMANRNPS1physical
22365833
SRSF4_HUMANSRSF4physical
22365833
SRS10_HUMANSRSF10physical
22365833
CIR1_HUMANCIR1physical
15652350
U2AF1_HUMANU2AF1physical
21988832
GROA_HUMANCXCL1physical
21822258
RNPS1_HUMANRNPS1physical
26344197
TRA2B_HUMANTRA2Bphysical
26344197
PRP4B_HUMANPRPF4Bphysical
11418604
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 SRSF1_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-38 AND LYS-179, AND MASSSPECTROMETRY.
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-93; ARG-97 AND ARG-109, ANDMASS SPECTROMETRY.
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-199; SER-201; TYR-202;SER-205; SER-231; SER-234; TYR-237 AND SER-238, AND MASS SPECTROMETRY.
"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-199; SER-201 ANDSER-205, 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-199, 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-199; SER-201 ANDSER-205, 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-199, 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-2; SER-199 AND SER-205,AND MASS SPECTROMETRY.
"Processive phosphorylation of alternative splicing factor/splicingfactor 2.";
Aubol B.E., Chakrabarti S., Ngo J., Shaffer J., Nolen B., Fu X.-D.,Ghosh G., Adams J.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003).
Cited for: PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION, ANDINTERACTION WITH SRPK1.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-189, AND MASSSPECTROMETRY.

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