NSRP1_HUMAN - dbPTM
NSRP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSRP1_HUMAN
UniProt AC Q9H0G5
Protein Name Nuclear speckle splicing regulatory protein 1
Gene Name NSRP1
Organism Homo sapiens (Human).
Sequence Length 558
Subcellular Localization Nucleus . Nucleus speckle . Colocalizes with splicing factors SRSF1 and SRSF2 in speckles.
Protein Description RNA-binding protein that mediates pre-mRNA alternative splicing regulation..
Protein Sequence MAIPGRQYGLILPKKTQQLHPVLQKPSVFGNDSDDDDETSVSESLQREAAKKQAMKQTKLEIQKALAEDATVYEYDSIYDEMQKKKEENNPKLLLGKDRKPKYIHNLLKAVEIRKKEQEKRMEKKIQREREMEKGEFDDKEAFVTSAYKKKLQERAEEEEREKRAAALEACLDVTKQKDLSGFYRHLLNQAVGEEEVPKCSFREARSGIKEEKSRGFSNEVSSKNRIPQEKCILQTDVKVEENPDADSDFDAKSSADDEIEETRVNCRREKVIETPENDFKHHRSQNHSRSPSEERGHSTRHHTKGSRTSRGHEKREDQHQQKQSRDQENHYTDRDYRKERDSHRHREASHRDSHWKRHEQEDKPRARDQRERSDRVWKREKDREKYSQREQERDRQQNDQNRPSEKGEKEEKSKAKEEHMKVRKERYENNDKYRDREKREVGVQSSERNQDRKESSPNSRAKDKFLDQERSNKMRNMAKDKERNQEKPSNSESSLGAKHRLTEEGQEKGKEQERPPEAVSKFAKRNNEETVMSARDRYLARQMARVNAKTYIEKEDD
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
8PhosphorylationMAIPGRQYGLILPKK
CCCCCCCCEEECCCC		16.7329978859
16PhosphorylationGLILPKKTQQLHPVL
EEECCCCCCCCCCCC		27.8923927012
25AcetylationQLHPVLQKPSVFGND
CCCCCCCCCCCCCCC		34.7923236377
27PhosphorylationHPVLQKPSVFGNDSD
CCCCCCCCCCCCCCC		36.7923927012
33PhosphorylationPSVFGNDSDDDDETS
CCCCCCCCCCCCCCC		47.1129255136
39PhosphorylationDSDDDDETSVSESLQ
CCCCCCCCCHHHHHH		41.2323927012
40PhosphorylationSDDDDETSVSESLQR
CCCCCCCCHHHHHHH		22.9223927012
42PhosphorylationDDDETSVSESLQREA
CCCCCCHHHHHHHHH		22.6423403867
44PhosphorylationDETSVSESLQREAAK
CCCCHHHHHHHHHHH		23.4623403867
73PhosphorylationLAEDATVYEYDSIYD
HHCCCCHHHHHHHHH		12.3829978859
75PhosphorylationEDATVYEYDSIYDEM
CCCCHHHHHHHHHHH		9.4127642862
79PhosphorylationVYEYDSIYDEMQKKK
HHHHHHHHHHHHHHH		15.1427642862
103PhosphorylationGKDRKPKYIHNLLKA
CCCCCHHHHHHHHHH		18.8828674419
145PhosphorylationDDKEAFVTSAYKKKL
CCHHHHHHHHHHHHH		10.9429396449
146PhosphorylationDKEAFVTSAYKKKLQ
CHHHHHHHHHHHHHH		25.0525159151
178UbiquitinationCLDVTKQKDLSGFYR
HHHHHHCCCHHHHHH		63.29-
181PhosphorylationVTKQKDLSGFYRHLL
HHHCCCHHHHHHHHH		36.6727134283
199SumoylationVGEEEVPKCSFREAR
HCCCCCCCCCHHHHH		47.9228112733
201PhosphorylationEEEVPKCSFREARSG
CCCCCCCCHHHHHHC		33.2026434776
207PhosphorylationCSFREARSGIKEEKS
CCHHHHHHCCCHHHH		52.50-
210SumoylationREARSGIKEEKSRGF
HHHHHCCCHHHHCCC		64.44-
210SumoylationREARSGIKEEKSRGF
HHHHHCCCHHHHCCC		64.4425218447
214PhosphorylationSGIKEEKSRGFSNEV
HCCCHHHHCCCCCCH		40.7025159151
224AcetylationFSNEVSSKNRIPQEK
CCCCHHHCCCCCHHH		42.6225953088
231AcetylationKNRIPQEKCILQTDV
CCCCCHHHEEEEECC		22.7125953088
248PhosphorylationEENPDADSDFDAKSS
CCCCCCCCCCCCCCC		41.7329255136
254PhosphorylationDSDFDAKSSADDEIE
CCCCCCCCCCCHHHH		32.2629255136
255PhosphorylationSDFDAKSSADDEIEE
CCCCCCCCCCHHHHH		34.7029255136
263PhosphorylationADDEIEETRVNCRRE
CCHHHHHHHHHHCHH		27.4222167270
275PhosphorylationRREKVIETPENDFKH
CHHHEECCCCCHHCH		25.4419664994
281SumoylationETPENDFKHHRSQNH
CCCCCHHCHHHHCCC		41.1728112733
285PhosphorylationNDFKHHRSQNHSRSP
CHHCHHHHCCCCCCC		30.8620068231
289PhosphorylationHHRSQNHSRSPSEER
HHHHCCCCCCCCHHC		41.8421955146
291PhosphorylationRSQNHSRSPSEERGH
HHCCCCCCCCHHCCC		35.4726055452
293PhosphorylationQNHSRSPSEERGHST
CCCCCCCCHHCCCCC		54.0221955146
299PhosphorylationPSEERGHSTRHHTKG
CCHHCCCCCCCCCCC		29.9320068231
300PhosphorylationSEERGHSTRHHTKGS
CHHCCCCCCCCCCCC		28.4820068231
325PhosphorylationDQHQQKQSRDQENHY
HHHHHHHHHHHHHHC		44.88-
332PhosphorylationSRDQENHYTDRDYRK
HHHHHHHCCCHHHHH		23.1724719451
333PhosphorylationRDQENHYTDRDYRKE
HHHHHHCCCHHHHHH		19.6024719451
337PhosphorylationNHYTDRDYRKERDSH
HHCCCHHHHHHHHHH		25.2028796482
350PhosphorylationSHRHREASHRDSHWK
HHHHHHHHHHHHHHH		17.8224719451
407UbiquitinationDQNRPSEKGEKEEKS
HCCCCCHHHHHHHHH		76.37-
413UbiquitinationEKGEKEEKSKAKEEH
HHHHHHHHHHHHHHH		59.35-
415UbiquitinationGEKEEKSKAKEEHMK
HHHHHHHHHHHHHHH		74.64-
425AcetylationEEHMKVRKERYENND
HHHHHHHHHHHCCCC		49.9111921507
428PhosphorylationMKVRKERYENNDKYR
HHHHHHHHCCCCCCC		24.89-
446PhosphorylationKREVGVQSSERNQDR
HHHHCCCCHHHCCCC		31.5925627689
454AcetylationSERNQDRKESSPNSR
HHHCCCCCCCCCCHH		70.9511688555
456PhosphorylationRNQDRKESSPNSRAK
HCCCCCCCCCCHHHH		54.8828985074
457PhosphorylationNQDRKESSPNSRAKD
CCCCCCCCCCHHHHH		29.2326074081
460PhosphorylationRKESSPNSRAKDKFL
CCCCCCCHHHHHHHH		36.6826074081
463MethylationSSPNSRAKDKFLDQE
CCCCHHHHHHHHHHH		61.41-
472PhosphorylationKFLDQERSNKMRNMA
HHHHHHHHHHHHHHH		39.8026714015
499AcetylationSESSLGAKHRLTEEG
CCCHHHHHHHCCHHH		27.7116916647
503PhosphorylationLGAKHRLTEEGQEKG
HHHHHHCCHHHHHCC		31.7628985074
531PhosphorylationAKRNNEETVMSARDR
HHHCCHHHHHHHHHH		18.48-
534PhosphorylationNNEETVMSARDRYLA
CCHHHHHHHHHHHHH		18.80-
539PhosphorylationVMSARDRYLARQMAR
HHHHHHHHHHHHHHH		14.7026074081
550AcetylationQMARVNAKTYIEKED
HHHHHHHHHHHCCCC		36.3425953088
551PhosphorylationMARVNAKTYIEKEDD
HHHHHHHHHHCCCCC		27.5926074081
552PhosphorylationARVNAKTYIEKEDD-
HHHHHHHHHCCCCC-		13.3326074081
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 NSRP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSRP1_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 NSRP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CTBL1_HUMANCTNNBL1physical
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 NSRP1_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-248; SER-254; SER-255AND THR-275, AND MASS 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-33 AND THR-275, 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-33; SER-248; SER-254;SER-255 AND THR-275, 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-33, 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-33; THR-39; SER-248;SER-254 AND SER-255, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275, AND MASSSPECTROMETRY.

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