SRS11_HUMAN - dbPTM
SRS11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRS11_HUMAN
UniProt AC Q05519
Protein Name Serine/arginine-rich splicing factor 11
Gene Name SRSF11
Organism Homo sapiens (Human).
Sequence Length 484
Subcellular Localization Nucleus. Colocalizes with spliceosome components.
Protein Description May function in pre-mRNA splicing..
Protein Sequence MSNTTVVPSTAGPGPSGGPGGGGGGGGGGGGTEVIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVSSRVCFVKFHDPDSAVVAQHLTNTVFVDRALIVVPYAEGVIPDEAKALSLLAPANAVAGLLPGGGLLPTPNPLTQIGAVPLAALGAPTLDPALAALGLPGANLNSQSLAADQLLKLMSTVDPKLNHVAAGLVSPSLKSDTSSKEIEEAMKRVREAQSLISAAIEPDKKEEKRRHSRSRSRSRRRRTPSSSRHRRSRSRSRRRSHSKSRSRRRSKSPRRRRSHSRERGRRSRSTSKTRDKKKEDKEKKRSKTPPKSYSTARRSRSASRERRRRRSRSGTRSPKKPRSPKRKLSRSPSPRRHKKEKKKDKDKERSRDERERSTSKKKKSKDKEKDRERKSESDKDVKQVTRDYDEEEQGYDSEKEKKEEKKPIETGSPKTKECSVEKGTGDSLRESKVNGDDHHEEDMDMSD
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
2Acetylation------MSNTTVVPS
------CCCCEECCC		42.7722814378
5Phosphorylation---MSNTTVVPSTAG
---CCCCEECCCCCC		24.6118491316
7Ubiquitination-MSNTTVVPSTAGPG
-CCCCEECCCCCCCC		2.6623000965
17PhosphorylationTAGPGPSGGPGGGGG
CCCCCCCCCCCCCCC		49.8232142685
21UbiquitinationGPSGGPGGGGGGGGG
CCCCCCCCCCCCCCC		34.4032015554
27UbiquitinationGGGGGGGGGGGGTEV
CCCCCCCCCCCCCCE		34.5433845483
32PhosphorylationGGGGGGGTEVIQVTN
CCCCCCCCCEEEEEE		30.2918491316
38PhosphorylationGTEVIQVTNVSPSAS
CCCEEEEEEECCCCC		17.3322210691
51PhosphorylationASSEQMRTLFGFLGK
CCHHHHHHHHHHHHC		22.5421712546
51UbiquitinationASSEQMRTLFGFLGK
CCHHHHHHHHHHHHC		22.5424816145
58AcetylationTLFGFLGKIDELRLF
HHHHHHHCCCEEEEC		49.4826051181
58UbiquitinationTLFGFLGKIDELRLF
HHHHHHHCCCEEEEC		49.4822817900
58UbiquitinationTLFGFLGKIDELRLF
HHHHHHHCCCEEEEC		49.4821890473
70PhosphorylationRLFPPDDSPLPVSSR
EECCCCCCCCCCCCC		35.4021815630
79S-nitrosocysteineLPVSSRVCFVKFHDP
CCCCCCEEEEEECCC		2.93-
79S-nitrosylationLPVSSRVCFVKFHDP
CCCCCCEEEEEECCC		2.9319483679
82AcetylationSSRVCFVKFHDPDSA
CCCEEEEEECCCCHH		19.4126051181
82UbiquitinationSSRVCFVKFHDPDSA
CCCEEEEEECCCCHH		19.4121963094
137UbiquitinationAVAGLLPGGGLLPTP
HHCCCCCCCCCCCCC		42.6521890473
143PhosphorylationPGGGLLPTPNPLTQI
CCCCCCCCCCCCCCC		35.3526853621
150PhosphorylationTPNPLTQIGAVPLAA
CCCCCCCCCCCCHHH		3.0133259812
180PhosphorylationPGANLNSQSLAADQL
CCCCCCCHHHHHHHH		41.2032645325
181UbiquitinationGANLNSQSLAADQLL
CCCCCCHHHHHHHHH		21.5724816145
187PhosphorylationQSLAADQLLKLMSTV
HHHHHHHHHHHHHHC		4.7232645325
197SumoylationLMSTVDPKLNHVAAG
HHHHCCHHHCHHHHH		58.4128112733
197UbiquitinationLMSTVDPKLNHVAAG
HHHHCCHHHCHHHHH		58.4123000965
197UbiquitinationLMSTVDPKLNHVAAG
HHHHCCHHHCHHHHH		58.4121890473
207PhosphorylationHVAAGLVSPSLKSDT
HHHHHCCCCCCCCCC		17.5129255136
207 (in isoform 2)Phosphorylation-17.5124719451
209PhosphorylationAAGLVSPSLKSDTSS
HHHCCCCCCCCCCCH		40.7129255136
209 (in isoform 2)Phosphorylation-40.7124719451
2112-HydroxyisobutyrylationGLVSPSLKSDTSSKE
HCCCCCCCCCCCHHH		51.10-
211SumoylationGLVSPSLKSDTSSKE
HCCCCCCCCCCCHHH		51.1028112733
211UbiquitinationGLVSPSLKSDTSSKE
HCCCCCCCCCCCHHH		51.1032015554
212PhosphorylationLVSPSLKSDTSSKEI
CCCCCCCCCCCHHHH		51.9523401153
212 (in isoform 2)Phosphorylation-51.9524719451
214PhosphorylationSPSLKSDTSSKEIEE
CCCCCCCCCHHHHHH		41.8323927012
215PhosphorylationPSLKSDTSSKEIEEA
CCCCCCCCHHHHHHH		44.3923927012
216PhosphorylationSLKSDTSSKEIEEAM
CCCCCCCHHHHHHHH		36.0823927012
217UbiquitinationLKSDTSSKEIEEAMK
CCCCCCHHHHHHHHH		63.5833845483
221UbiquitinationTSSKEIEEAMKRVRE
CCHHHHHHHHHHHHH		60.7824816145
224UbiquitinationKEIEEAMKRVREAQS
HHHHHHHHHHHHHHH		55.58-
228UbiquitinationEAMKRVREAQSLISA
HHHHHHHHHHHHHHH		48.4824816145
231PhosphorylationKRVREAQSLISAAIE
HHHHHHHHHHHHHHC		34.4230266825
234PhosphorylationREAQSLISAAIEPDK
HHHHHHHHHHHCCCH		19.5530266825
241UbiquitinationSAAIEPDKKEEKRRH
HHHHCCCHHHHHHHH		73.1824816145
243PhosphorylationAIEPDKKEEKRRHSR
HHCCCHHHHHHHHHH		74.6032142685
244PhosphorylationIEPDKKEEKRRHSRS
HCCCHHHHHHHHHHH		61.8232142685
249PhosphorylationKEEKRRHSRSRSRSR
HHHHHHHHHHHHHHH		30.0920068231
250PhosphorylationEEKRRHSRSRSRSRR
HHHHHHHHHHHHHHH		29.9332142685
251PhosphorylationEKRRHSRSRSRSRRR
HHHHHHHHHHHHHHH		37.3120068231
258PhosphorylationSRSRSRRRRTPSSSR
HHHHHHHHCCCCHHH		45.7932142685
259PhosphorylationRSRSRRRRTPSSSRH
HHHHHHHCCCCHHHH		49.5332142685
260PhosphorylationSRSRRRRTPSSSRHR
HHHHHHCCCCHHHHH		26.2227362937
262PhosphorylationSRRRRTPSSSRHRRS
HHHHCCCCHHHHHHH		40.0920363803
263PhosphorylationRRRRTPSSSRHRRSR
HHHCCCCHHHHHHHH		32.3720363803
264PhosphorylationRRRTPSSSRHRRSRS
HHCCCCHHHHHHHHH		36.1227362937
265PhosphorylationRRTPSSSRHRRSRSR
HCCCCHHHHHHHHHH		29.3132142685
266PhosphorylationRTPSSSRHRRSRSRS
CCCCHHHHHHHHHHH		31.3032142685
268UbiquitinationPSSSRHRRSRSRSRR
CCHHHHHHHHHHHHH		30.2333845483
269PhosphorylationSSSRHRRSRSRSRRR
CHHHHHHHHHHHHHH		34.2729449344
269UbiquitinationSSSRHRRSRSRSRRR
CHHHHHHHHHHHHHH		34.2733845483
275UbiquitinationRSRSRSRRRSHSKSR
HHHHHHHHHHHHHHH		45.7833845483
276UbiquitinationSRSRSRRRSHSKSRS
HHHHHHHHHHHHHHH		37.3033845483
277PhosphorylationRSRSRRRSHSKSRSR
HHHHHHHHHHHHHHH		30.2420068231
279PhosphorylationRSRRRSHSKSRSRRR
HHHHHHHHHHHHHHH		33.3120068231
281PhosphorylationRRRSHSKSRSRRRSK
HHHHHHHHHHHHHCC		38.2026074081
283PhosphorylationRSHSKSRSRRRSKSP
HHHHHHHHHHHCCCH		36.9126074081
287PhosphorylationKSRSRRRSKSPRRRR
HHHHHHHCCCHHHHH		35.3626074081
289PhosphorylationRSRRRSKSPRRRRSH
HHHHHCCCHHHHHHH		25.5322817900
295PhosphorylationKSPRRRRSHSRERGR
CCHHHHHHHHHHHHH		24.8120068231
297O-linked_GlycosylationPRRRRSHSRERGRRS
HHHHHHHHHHHHHHH		36.7630379171
297PhosphorylationPRRRRSHSRERGRRS
HHHHHHHHHHHHHHH		36.7620068231
304PhosphorylationSRERGRRSRSTSKTR
HHHHHHHHHHHCHHC		29.2624144214
306PhosphorylationERGRRSRSTSKTRDK
HHHHHHHHHCHHCCH		37.9826552605
307PhosphorylationRGRRSRSTSKTRDKK
HHHHHHHHCHHCCHH		32.8826552605
308PhosphorylationGRRSRSTSKTRDKKK
HHHHHHHCHHCCHHH		33.0224144214
310PhosphorylationRSRSTSKTRDKKKED
HHHHHCHHCCHHHHH		43.8224144214
323PhosphorylationEDKEKKRSKTPPKSY
HHHHHHHCCCCCCHH		50.1623401153
323 (in isoform 2)Phosphorylation-50.1624719451
325PhosphorylationKEKKRSKTPPKSYST
HHHHHCCCCCCHHHH		46.1823927012
325 (in isoform 2)Phosphorylation-46.1824719451
328AcetylationKRSKTPPKSYSTARR
HHCCCCCCHHHHHHH		64.3390419
329PhosphorylationRSKTPPKSYSTARRS
HCCCCCCHHHHHHHH		30.0428796482
330PhosphorylationSKTPPKSYSTARRSR
CCCCCCHHHHHHHHH		19.0328796482
331PhosphorylationKTPPKSYSTARRSRS
CCCCCHHHHHHHHHH		23.7628796482
332PhosphorylationTPPKSYSTARRSRSA
CCCCHHHHHHHHHHH		18.8928796482
336PhosphorylationSYSTARRSRSASRER
HHHHHHHHHHHHHHH		25.6530576142
338PhosphorylationSTARRSRSASRERRR
HHHHHHHHHHHHHHH		31.6630576142
340PhosphorylationARRSRSASRERRRRR
HHHHHHHHHHHHHHH		35.6030576142
348PhosphorylationRERRRRRSRSGTRSP
HHHHHHHHCCCCCCC		29.0526074081
350PhosphorylationRRRRRSRSGTRSPKK
HHHHHHCCCCCCCCC		45.8426074081
352PhosphorylationRRRSRSGTRSPKKPR
HHHHCCCCCCCCCCC		29.2626074081
354PhosphorylationRSRSGTRSPKKPRSP
HHCCCCCCCCCCCCC		40.6926074081
358UbiquitinationGTRSPKKPRSPKRKL
CCCCCCCCCCCCCCC		48.3724816145
360PhosphorylationRSPKKPRSPKRKLSR
CCCCCCCCCCCCCCC		43.2130278072
366PhosphorylationRSPKRKLSRSPSPRR
CCCCCCCCCCCCCHH		33.4726846344
368PhosphorylationPKRKLSRSPSPRRHK
CCCCCCCCCCCHHHH		26.7626846344
368 (in isoform 2)Phosphorylation-26.7624719451
370O-linked_GlycosylationRKLSRSPSPRRHKKE
CCCCCCCCCHHHHHH		32.0830379171
370PhosphorylationRKLSRSPSPRRHKKE
CCCCCCCCCHHHHHH		32.0826846344
370 (in isoform 2)Phosphorylation-32.0824719451
377PhosphorylationSPRRHKKEKKKDKDK
CCHHHHHHHHHHHHH		74.9432645325
394PhosphorylationSRDERERSTSKKKKS
HHHHHHHHHHHHHHH		32.0730576142
395PhosphorylationRDERERSTSKKKKSK
HHHHHHHHHHHHHHH		51.27-
396PhosphorylationDERERSTSKKKKSKD
HHHHHHHHHHHHHHH		43.6630576142
411UbiquitinationKEKDRERKSESDKDV
HHHHHHHHHHCHHHH		54.5524816145
412PhosphorylationEKDRERKSESDKDVK
HHHHHHHHHCHHHHH		48.8629632367
412 (in isoform 2)Phosphorylation-48.8624719451
414PhosphorylationDRERKSESDKDVKQV
HHHHHHHCHHHHHHH		57.9928176443
414 (in isoform 2)Phosphorylation-57.9924719451
418UbiquitinationKSESDKDVKQVTRDY
HHHCHHHHHHHHHCC		6.0224816145
422PhosphorylationDKDVKQVTRDYDEEE
HHHHHHHHHCCCHHH		18.4820363803
425PhosphorylationVKQVTRDYDEEEQGY
HHHHHHCCCHHHCCC		23.2023927012
432PhosphorylationYDEEEQGYDSEKEKK
CCHHHCCCCCHHHHH		18.9130278072
433PhosphorylationDEEEQGYDSEKEKKE
CHHHCCCCCHHHHHH		58.0832142685
433 (in isoform 2)Phosphorylation-58.0825849741
434PhosphorylationEEEQGYDSEKEKKEE
HHHCCCCCHHHHHHC		41.9229255136
440PhosphorylationDSEKEKKEEKKPIET
CCHHHHHHCCCCCCC		82.9332142685
441PhosphorylationSEKEKKEEKKPIETG
CHHHHHHCCCCCCCC		75.2232142685
446 (in isoform 2)Phosphorylation-56.4924719451
447PhosphorylationEEKKPIETGSPKTKE
HCCCCCCCCCCCCCC		43.6223927012
448PhosphorylationEKKPIETGSPKTKEC
CCCCCCCCCCCCCCC		29.2132142685
448 (in isoform 2)Phosphorylation-29.2124719451
449PhosphorylationKKPIETGSPKTKECS
CCCCCCCCCCCCCCE		30.5529255136
452PhosphorylationIETGSPKTKECSVEK
CCCCCCCCCCCEECC		35.1423927012
455PhosphorylationGSPKTKECSVEKGTG
CCCCCCCCEECCCCC		6.1832142685
455 (in isoform 2)Phosphorylation-6.1824719451
456PhosphorylationSPKTKECSVEKGTGD
CCCCCCCEECCCCCC		34.1123927012
458UbiquitinationKTKECSVEKGTGDSL
CCCCCEECCCCCCCH		29.4933845483
459AcetylationTKECSVEKGTGDSLR
CCCCEECCCCCCCHH		60.6623749302
459UbiquitinationTKECSVEKGTGDSLR
CCCCEECCCCCCCHH		60.6633845483
461PhosphorylationECSVEKGTGDSLRES
CCEECCCCCCCHHHH		49.2123927012
463 (in isoform 2)Phosphorylation-44.3224719451
464PhosphorylationVEKGTGDSLRESKVN
ECCCCCCCHHHHCCC		30.5823401153
465UbiquitinationEKGTGDSLRESKVNG
CCCCCCCHHHHCCCC		9.3033845483
466UbiquitinationKGTGDSLRESKVNGD
CCCCCCHHHHCCCCC		50.5233845483
468PhosphorylationTGDSLRESKVNGDDH
CCCCHHHHCCCCCCC		35.1523403867
482 (in isoform 2)Phosphorylation-3.7924719451
483PhosphorylationHEEDMDMSD------
CHHHCCCCC------		35.5823927012
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 SRS11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRS11_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 SRS11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF2_HUMANSRSF2physical
8816452
SRSF1_HUMANSRSF1physical
8816452
U2AF2_HUMANU2AF2physical
8816452
TOP1_HUMANTOP1physical
22939629
SRSF9_HUMANSRSF9physical
22939629
SRSF7_HUMANSRSF7physical
22939629
SNRPA_HUMANSNRPAphysical
22939629
SRSF3_HUMANSRSF3physical
22939629
TCRG1_HUMANTCERG1physical
22939629
SNUT2_HUMANUSP39physical
22939629
SNUT1_HUMANSART1physical
22939629
SMU1_HUMANSMU1physical
22939629
TR112_HUMANTRMT112physical
22939629
TRI55_HUMANTRIM55physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
VTNC_HUMANVTNphysical
22939629
TOX4_HUMANTOX4physical
22939629
TPBG_HUMANTPBGphysical
22939629
SPEB_HUMANAGMATphysical
22939629
SHCBP_HUMANSHCBP1physical
22939629
VASN_HUMANVASNphysical
22939629
ZN592_HUMANZNF592physical
22939629
TR150_HUMANTHRAP3physical
22939629
TFPI1_HUMANTFPIphysical
22939629
SON_HUMANSONphysical
22939629
THA11_HUMANTHAP11physical
21988832
RBM39_HUMANRBM39physical
25416956
TANK_HUMANTANKphysical
25416956
PUF60_HUMANPUF60physical
25416956
AR6P4_HUMANARL6IP4physical
25416956
HYI_HUMANHYIphysical
25416956
SREK1_HUMANSREK1physical
25416956
GATC_HUMANGATCphysical
25416956
ARGL1_HUMANARGLU1physical
26344197
DDX46_HUMANDDX46physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
HEXI1_HUMANHEXIM1physical
26344197
LC7L2_HUMANLUC7L2physical
26344197
PNISR_HUMANPNISRphysical
26344197
PUF60_HUMANPUF60physical
26344197
RBM25_HUMANRBM25physical
26344197
RBM39_HUMANRBM39physical
26344197
RUVB1_HUMANRUVBL1physical
26344197
SF3B2_HUMANSF3B2physical
26344197
SRRM2_HUMANSRRM2physical
26344197
RNPS1_HUMANRNPS1physical
14729963
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 SRS11_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-207 AND SER-483, ANDMASS SPECTROMETRY.
"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-434, 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-207; SER-434 ANDSER-483, 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-207; SER-366; SER-368AND SER-449, 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-207; THR-260; SER-264;SER-295; SER-297; SER-366; SER-368 AND SER-370; SER-434 AND SER-483,AND MASS SPECTROMETRY.

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