SRSF4_HUMAN - dbPTM
SRSF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF4_HUMAN
UniProt AC Q08170
Protein Name Serine/arginine-rich splicing factor 4
Gene Name SRSF4
Organism Homo sapiens (Human).
Sequence Length 494
Subcellular Localization Nucleus speckle .
Protein Description Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10..
Protein Sequence MPRVYIGRLSYQARERDVERFFKGYGKILEVDLKNGYGFVEFDDLRDADDAVYELNGKDLCGERVIVEHARGPRRDGSYGSGRSGYGYRRSGRDKYGPPTRTEYRLIVENLSSRCSWQDLKDYMRQAGEVTYADAHKGRKNEGVIEFVSYSDMKRALEKLDGTEVNGRKIRLVEDKPGSRRRRSYSRSRSHSRSRSRSRHSRKSRSRSGSSKSSHSKSRSRSRSGSRSRSKSRSRSQSRSRSKKEKSRSPSKEKSRSRSHSAGKSRSKSKDQAEEKIQNNDNVGKPKSRSPSRHKSKSKSRSRSQERRVEEEKRGSVSRGRSQEKSLRQSRSRSRSKGGSRSRSRSRSKSKDKRKGRKRSREESRSRSRSRSKSERSRKRGSKRDSKAGSSKKKKKEDTDRSQSRSPSRSVSKEREHAKSESSQREGRGESENAGTNQETRSRSRSNSKSKPNLPSESRSRSKSASKTRSRSKSRSRSASRSPSRSRSRSHSRS
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
8MethylationMPRVYIGRLSYQARE
CCCEEEECCCHHHHH
15.7680702415
23AcetylationRDVERFFKGYGKILE
HHHHHHHHCCCCEEE
48.8126051181
23UbiquitinationRDVERFFKGYGKILE
HHHHHHHHCCCCEEE
48.8123000965
27AcetylationRFFKGYGKILEVDLK
HHHHCCCCEEEEECC
35.3226051181
27UbiquitinationRFFKGYGKILEVDLK
HHHHCCCCEEEEECC
35.3223000965
53PhosphorylationRDADDAVYELNGKDL
CCCCCHHHEECCCCC
19.2030174305
58AcetylationAVYELNGKDLCGERV
HHHEECCCCCCCCEE
46.5926051181
58UbiquitinationAVYELNGKDLCGERV
HHHEECCCCCCCCEE
46.5929967540
71MethylationRVIVEHARGPRRDGS
EEEEECCCCCCCCCC
58.52-
78PhosphorylationRGPRRDGSYGSGRSG
CCCCCCCCCCCCCCC
30.5220363803
79PhosphorylationGPRRDGSYGSGRSGY
CCCCCCCCCCCCCCC
22.3529052541
81PhosphorylationRRDGSYGSGRSGYGY
CCCCCCCCCCCCCCC
23.8526853621
83MethylationDGSYGSGRSGYGYRR
CCCCCCCCCCCCCCC
28.7154559241
84PhosphorylationGSYGSGRSGYGYRRS
CCCCCCCCCCCCCCC
39.6323917254
95AcetylationYRRSGRDKYGPPTRT
CCCCCCCCCCCCCHH
51.2325953088
102PhosphorylationKYGPPTRTEYRLIVE
CCCCCCHHHHHHHHC
39.5928152594
104PhosphorylationGPPTRTEYRLIVENL
CCCCHHHHHHHHCCH
15.3128152594
112PhosphorylationRLIVENLSSRCSWQD
HHHHCCHHHCCCHHH
27.5829255136
113PhosphorylationLIVENLSSRCSWQDL
HHHCCHHHCCCHHHH
40.2419664994
116PhosphorylationENLSSRCSWQDLKDY
CCHHHCCCHHHHHHH
27.0225159151
121AcetylationRCSWQDLKDYMRQAG
CCCHHHHHHHHHHCC
55.9226051181
131PhosphorylationMRQAGEVTYADAHKG
HHHCCCCEEHHCCCC
14.5328152594
132NitrationRQAGEVTYADAHKGR
HHCCCCEEHHCCCCC
13.99-
132PhosphorylationRQAGEVTYADAHKGR
HHCCCCEEHHCCCCC
13.9928152594
149PhosphorylationEGVIEFVSYSDMKRA
CCEEEEECHHHHHHH
25.0026270265
150PhosphorylationGVIEFVSYSDMKRAL
CEEEEECHHHHHHHH
11.9121712546
151PhosphorylationVIEFVSYSDMKRALE
EEEEECHHHHHHHHH
24.5921815630
154AcetylationFVSYSDMKRALEKLD
EECHHHHHHHHHHCC
39.2425953088
159AcetylationDMKRALEKLDGTEVN
HHHHHHHHCCCCEEC
53.3725953088
159UbiquitinationDMKRALEKLDGTEVN
HHHHHHHHCCCCEEC
53.3729967540
176AcetylationKIRLVEDKPGSRRRR
EEEEECCCCCCCCCC
37.4623749302
179PhosphorylationLVEDKPGSRRRRSYS
EECCCCCCCCCCHHH
31.0129255136
184PhosphorylationPGSRRRRSYSRSRSH
CCCCCCCHHHHCCCC
26.1626074081
185PhosphorylationGSRRRRSYSRSRSHS
CCCCCCHHHHCCCCC
13.2917081983
186PhosphorylationSRRRRSYSRSRSHSR
CCCCCHHHHCCCCCC
25.6526074081
188PhosphorylationRRRSYSRSRSHSRSR
CCCHHHHCCCCCCHH
31.9926074081
190PhosphorylationRSYSRSRSHSRSRSR
CHHHHCCCCCCHHHH
27.3626074081
192PhosphorylationYSRSRSHSRSRSRSR
HHHCCCCCCHHHHCH
32.9526074081
206PhosphorylationRHSRKSRSRSGSSKS
HHCHHCCCCCCCCCC
37.5822964224
208PhosphorylationSRKSRSRSGSSKSSH
CHHCCCCCCCCCCCC
44.2522964224
210PhosphorylationKSRSRSGSSKSSHSK
HCCCCCCCCCCCCCC
35.5222964224
211PhosphorylationSRSRSGSSKSSHSKS
CCCCCCCCCCCCCCC
39.8322964224
222PhosphorylationHSKSRSRSRSGSRSR
CCCCCCCCCCCCHHH
31.8522817900
232PhosphorylationGSRSRSKSRSRSQSR
CCHHHHHHHHHHHHH
36.41-
238PhosphorylationKSRSRSQSRSRSKKE
HHHHHHHHHHHHHHH
33.21-
255PhosphorylationRSPSKEKSRSRSHSA
CCCCHHHHHHHHHHH
36.2622817900
257PhosphorylationPSKEKSRSRSHSAGK
CCHHHHHHHHHHHCC
45.27-
259PhosphorylationKEKSRSRSHSAGKSR
HHHHHHHHHHHCCCC
24.0428176443
261PhosphorylationKSRSRSHSAGKSRSK
HHHHHHHHHCCCCCC
39.7120068231
264AcetylationSRSHSAGKSRSKSKD
HHHHHHCCCCCCCHH
42.277431965
265PhosphorylationRSHSAGKSRSKSKDQ
HHHHHCCCCCCCHHH
40.6520068231
267PhosphorylationHSAGKSRSKSKDQAE
HHHCCCCCCCHHHHH
48.6630576142
269PhosphorylationAGKSRSKSKDQAEEK
HCCCCCCCHHHHHHH
42.5929743597
276AcetylationSKDQAEEKIQNNDNV
CHHHHHHHHHCCCCC
40.8926051181
285AcetylationQNNDNVGKPKSRSPS
HCCCCCCCCCCCCCC
45.0125953088
287AcetylationNDNVGKPKSRSPSRH
CCCCCCCCCCCCCHH
63.0819826789
288PhosphorylationDNVGKPKSRSPSRHK
CCCCCCCCCCCCHHH
46.6623911959
290PhosphorylationVGKPKSRSPSRHKSK
CCCCCCCCCCHHHCH
34.0323911959
292PhosphorylationKPKSRSPSRHKSKSK
CCCCCCCCHHHCHHH
48.5423911959
296PhosphorylationRSPSRHKSKSKSRSR
CCCCHHHCHHHHCCH
35.7226074081
298PhosphorylationPSRHKSKSKSRSRSQ
CCHHHCHHHHCCHHH
42.8426074081
300PhosphorylationRHKSKSKSRSRSQER
HHHCHHHHCCHHHHH
42.4529743597
302PhosphorylationKSKSKSRSRSQERRV
HCHHHHCCHHHHHHH
43.2929743597
304PhosphorylationKSKSRSRSQERRVEE
HHHHCCHHHHHHHHH
37.3329743597
316PhosphorylationVEEEKRGSVSRGRSQ
HHHHHHHCCCCCHHH
22.4323401153
318PhosphorylationEEKRGSVSRGRSQEK
HHHHHCCCCCHHHHH
30.6220363803
322PhosphorylationGSVSRGRSQEKSLRQ
HCCCCCHHHHHHHHH
45.5830576142
326PhosphorylationRGRSQEKSLRQSRSR
CCHHHHHHHHHHHHH
28.2128102081
330PhosphorylationQEKSLRQSRSRSRSK
HHHHHHHHHHHHHCC
26.2828102081
332PhosphorylationKSLRQSRSRSRSKGG
HHHHHHHHHHHCCCC
39.5928102081
360PhosphorylationKRKGRKRSREESRSR
HHHHHHHHHHHHHHH
47.26-
364PhosphorylationRKRSREESRSRSRSR
HHHHHHHHHHHHHHC
30.70-
368PhosphorylationREESRSRSRSRSKSE
HHHHHHHHHHCHHHH
35.54-
399PhosphorylationKKKKKEDTDRSQSRS
CCCCHHHCCHHHCCC
34.1130242111
402PhosphorylationKKEDTDRSQSRSPSR
CHHHCCHHHCCCCCC
35.0030242111
404PhosphorylationEDTDRSQSRSPSRSV
HHCCHHHCCCCCCHH
35.6530242111
406PhosphorylationTDRSQSRSPSRSVSK
CCHHHCCCCCCHHHH
32.2627794612
408O-linked_GlycosylationRSQSRSPSRSVSKER
HHHCCCCCCHHHHHH
38.1330379171
408PhosphorylationRSQSRSPSRSVSKER
HHHCCCCCCHHHHHH
38.1327794612
410PhosphorylationQSRSPSRSVSKEREH
HCCCCCCHHHHHHHH
34.7723312004
412PhosphorylationRSPSRSVSKEREHAK
CCCCCHHHHHHHHHH
30.0023312004
420PhosphorylationKEREHAKSESSQREG
HHHHHHHCHHHCCCC
43.4228450419
422PhosphorylationREHAKSESSQREGRG
HHHHHCHHHCCCCCC
38.5728450419
423PhosphorylationEHAKSESSQREGRGE
HHHHCHHHCCCCCCC
29.2525394399
428MethylationESSQREGRGESENAG
HHHCCCCCCCCCCCC
40.74115916761
431PhosphorylationQREGRGESENAGTNQ
CCCCCCCCCCCCCCH
38.6929255136
436PhosphorylationGESENAGTNQETRSR
CCCCCCCCCHHHHHH
31.1723927012
440PhosphorylationNAGTNQETRSRSRSN
CCCCCHHHHHHCCCC
24.9523927012
442PhosphorylationGTNQETRSRSRSNSK
CCCHHHHHHCCCCCC
41.8725159151
444PhosphorylationNQETRSRSRSNSKSK
CHHHHHHCCCCCCCC
41.1130108239
446PhosphorylationETRSRSRSNSKSKPN
HHHHHCCCCCCCCCC
46.8623927012
448PhosphorylationRSRSRSNSKSKPNLP
HHHCCCCCCCCCCCC
39.2823401153
450PhosphorylationRSRSNSKSKPNLPSE
HCCCCCCCCCCCCHH
53.8423927012
456PhosphorylationKSKPNLPSESRSRSK
CCCCCCCHHHHHHCH
51.9030266825
458PhosphorylationKPNLPSESRSRSKSA
CCCCCHHHHHHCHHH
39.6323927012
460PhosphorylationNLPSESRSRSKSASK
CCCHHHHHHCHHHHH
50.6225463755
462PhosphorylationPSESRSRSKSASKTR
CHHHHHHCHHHHHHH
32.0120164059
464PhosphorylationESRSRSKSASKTRSR
HHHHHCHHHHHHHHH
38.7326074081
466PhosphorylationRSRSKSASKTRSRSK
HHHCHHHHHHHHHHH
41.4726074081
470PhosphorylationKSASKTRSRSKSRSR
HHHHHHHHHHHHHHC
46.2526074081
472PhosphorylationASKTRSRSKSRSRSA
HHHHHHHHHHHHCCC
35.9126074081
474PhosphorylationKTRSRSKSRSRSASR
HHHHHHHHHHCCCCC
36.4126074081
476PhosphorylationRSRSKSRSRSASRSP
HHHHHHHHCCCCCCC
37.3626074081
478PhosphorylationRSKSRSRSASRSPSR
HHHHHHCCCCCCCCH
31.6626074081
480PhosphorylationKSRSRSASRSPSRSR
HHHHCCCCCCCCHHH
34.2420363803
482PhosphorylationRSRSASRSPSRSRSR
HHCCCCCCCCHHHCC
25.4026074081
484PhosphorylationRSASRSPSRSRSRSH
CCCCCCCCHHHCCCC
44.1026074081
486PhosphorylationASRSPSRSRSRSHSR
CCCCCCHHHCCCCCC
38.6620363803

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 SRSF4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF4_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 SRSF4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF6_HUMANSRSF6physical
16189514
HAP1_HUMANHAP1physical
16169070
WRIP1_HUMANWRNIP1physical
22939629
HTSF1_HUMANHTATSF1physical
22365833
SRSF1_HUMANSRSF1physical
22365833
SRRM2_HUMANSRRM2physical
22365833
SNUT1_HUMANSART1physical
22365833
PR38A_HUMANPRPF38Aphysical
22365833
RNPS1_HUMANRNPS1physical
22365833
SRSF2_HUMANSRSF2physical
22365833
TRA2B_HUMANTRA2Bphysical
22365833
SRS10_HUMANSRSF10physical
22365833
TCAM1_HUMANTICAM1physical
21988832

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 SRSF4_HUMAN

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Related Literatures of Post-Translational Modification
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-113, 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-113, 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-222; SER-255; SER-300;SER-302; SER-304; SER-316; SER-322; THR-440; SER-448; SER-460 ANDSER-462, 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 SER-458; SER-460 ANDSER-462, AND MASS SPECTROMETRY.
"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-53, AND MASSSPECTROMETRY.

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