U520_HUMAN - dbPTM
U520_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U520_HUMAN
UniProt AC O75643
Protein Name U5 small nuclear ribonucleoprotein 200 kDa helicase
Gene Name SNRNP200
Organism Homo sapiens (Human).
Sequence Length 2136
Subcellular Localization Nucleus .
Protein Description RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome..
Protein Sequence MADVTARSLQYEYKANSNLVLQADRSLIDRTRRDEPTGEVLSLVGKLEGTRMGDKAQRTKPQMQEERRAKRRKRDEDRHDINKMKGYTLLSEGIDEMVGIIYKPKTKETRETYEVLLSFIQAALGDQPRDILCGAADEVLAVLKNEKLRDKERRKEIDLLLGQTDDTRYHVLVNLGKKITDYGGDKEIQNMDDNIDETYGVNVQFESDEEEGDEDVYGEVREEASDDDMEGDEAVVRCTLSANLVASGELMSSKKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDDRECENQLVLLLGFNTFDFIKVLRQHRMMILYCTLLASAQSEAEKERIMGKMEADPELSKFLYQLHETEKEDLIREERSRRERVRQSRMDTDLETMDLDQGGEALAPRQVLDLEDLVFTQGSHFMANKRCQLPDGSFRRQRKGYEEVHVPALKPKPFGSEEQLLPVEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEALVARAIRNIEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFDNSFRPVPLEQTYVGITEKKAIKRFQIMNEIVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEVLRTEAEQCKNLELKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRWTELGALDILQMLGRAGRPQYDTKGEGILITSHGELQYYLSLLNQQLPIESQMVSKLPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRMLRSPTLYGISHDDLKGDPLLDQRRLDLVHTAALMLDKNNLVKYDKKTGNFQVTELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINVLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPEEVVKKIEKKNFPFERLYDLNHNEIGELIRMPKMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSEAFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSFRHLILPEKYPPPTELLDLQPLPVSALRNSAFESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHTQTRLLSMAKPVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILTTCAADIQRQRFLHCTEKDLIPYLEKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGKIHAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQGSKKDFFKKFLYEPLPVESHLDHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRRMTQNPNYYNLQGISHRHLSDHLSELVEQTLSDLEQSKCISIEDEMDVAPLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVKTNLLLQAHLSRMQLSAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFTSEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVVDKDSIRSGGPVVVLVQLEREEEVTGPVIAPLFPQKREEGWWVVIGDAKSNSLISIKRLTLQQKAKVKLDFVAPATGAHNYTLYFMSDAYMGCDQEYKFSVDVKEAETDSDSD
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
5O-linked_Glycosylation---MADVTARSLQYE
---CCCCCHHHHHEE
19.5323301498
8PhosphorylationMADVTARSLQYEYKA
CCCCCHHHHHEEECC
19.8420068231
11PhosphorylationVTARSLQYEYKANSN
CCHHHHHEEECCCCC
26.9028796482
13PhosphorylationARSLQYEYKANSNLV
HHHHHEEECCCCCEE
15.5128796482
14MethylationRSLQYEYKANSNLVL
HHHHEEECCCCCEEE
29.20115979297
14UbiquitinationRSLQYEYKANSNLVL
HHHHEEECCCCCEEE
29.2032015554
17PhosphorylationQYEYKANSNLVLQAD
HEEECCCCCEEEEEC
36.0830266825
25MethylationNLVLQADRSLIDRTR
CEEEEECHHHHHCCC
36.06115919225
26PhosphorylationLVLQADRSLIDRTRR
EEEEECHHHHHCCCC
30.1725159151
37PhosphorylationRTRRDEPTGEVLSLV
CCCCCCCCCHHHHHH
43.8827732954
42PhosphorylationEPTGEVLSLVGKLEG
CCCCHHHHHHHHHHC
26.6120873877
462-HydroxyisobutyrylationEVLSLVGKLEGTRMG
HHHHHHHHHHCCCCC
35.57-
46AcetylationEVLSLVGKLEGTRMG
HHHHHHHHHHCCCCC
35.5723954790
46SumoylationEVLSLVGKLEGTRMG
HHHHHHHHHHCCCCC
35.5728112733
46UbiquitinationEVLSLVGKLEGTRMG
HHHHHHHHHHCCCCC
35.5732015554
50PhosphorylationLVGKLEGTRMGDKAQ
HHHHHHCCCCCCHHH
14.2223312004
59PhosphorylationMGDKAQRTKPQMQEE
CCCHHHHCCHHHHHH
34.6923312004
832-HydroxyisobutyrylationEDRHDINKMKGYTLL
HHHHHHHHHHHHHHH
42.18-
102PhosphorylationDEMVGIIYKPKTKET
HHHCEEEECCCCCCC
21.22-
133GlutathionylationDQPRDILCGAADEVL
CCCCHHHHCCHHHHH
3.3922555962
155AcetylationLRDKERRKEIDLLLG
HCCHHHHHHHCCCCC
66.3026051181
169PhosphorylationGQTDDTRYHVLVNLG
CCCCCCCEEEEEECC
9.8124532841
1772-HydroxyisobutyrylationHVLVNLGKKITDYGG
EEEEECCCCEECCCC
44.14-
177AcetylationHVLVNLGKKITDYGG
EEEEECCCCEECCCC
44.1425953088
177UbiquitinationHVLVNLGKKITDYGG
EEEEECCCCEECCCC
44.1433845483
182PhosphorylationLGKKITDYGGDKEIQ
CCCCEECCCCCHHCC
17.8522817900
198PhosphorylationMDDNIDETYGVNVQF
CCCCCCCCCCEEEEE
23.1026657352
199PhosphorylationDDNIDETYGVNVQFE
CCCCCCCCCEEEEEE
19.6127732954
207PhosphorylationGVNVQFESDEEEGDE
CEEEEEECCCCCCCC
52.1626657352
217PhosphorylationEEGDEDVYGEVREEA
CCCCCCCHHHHHCCC
21.6425137130
225PhosphorylationGEVREEASDDDMEGD
HHHHCCCCCCCCCCC
44.8719664994
239PhosphorylationDEAVVRCTLSANLVA
CCEEEEEEECCCEEE
17.1223090842
241PhosphorylationAVVRCTLSANLVASG
EEEEEEECCCEEECC
9.2820068231
247PhosphorylationLSANLVASGELMSSK
ECCCEEECCCCCCCC
25.8920068231
252PhosphorylationVASGELMSSKKKDLH
EECCCCCCCCCCCCC
52.1823090842
253PhosphorylationASGELMSSKKKDLHP
ECCCCCCCCCCCCCH
34.2327251275
276PhosphorylationQRQLSRFYDDAIVSQ
HHHHHHHHHHHHHCH
16.2929052541
282PhosphorylationFYDDAIVSQKKADEV
HHHHHHHCHHHHHHH
30.1229052541
2842-HydroxyisobutyrylationDDAIVSQKKADEVLE
HHHHHCHHHHHHHHH
42.28-
284AcetylationDDAIVSQKKADEVLE
HHHHHCHHHHHHHHH
42.2825953088
284UbiquitinationDDAIVSQKKADEVLE
HHHHHCHHHHHHHHH
42.2821906983
284 (in isoform 1)Ubiquitination-42.2821890473
284 (in isoform 2)Ubiquitination-42.2821890473
2852-HydroxyisobutyrylationDAIVSQKKADEVLEI
HHHHCHHHHHHHHHH
54.13-
285AcetylationDAIVSQKKADEVLEI
HHHHCHHHHHHHHHH
54.1326051181
285UbiquitinationDAIVSQKKADEVLEI
HHHHCHHHHHHHHHH
54.1322817900
294UbiquitinationDEVLEILKTASDDRE
HHHHHHHHHCCCCHH
47.94-
295O-linked_GlycosylationEVLEILKTASDDREC
HHHHHHHHCCCCHHH
28.1323301498
339PhosphorylationTLLASAQSEAEKERI
HHHHHHCCHHHHHHH
38.1926546556
349AcetylationEKERIMGKMEADPEL
HHHHHHHHHHCCHHH
19.0423236377
349UbiquitinationEKERIMGKMEADPEL
HHHHHHHHHHCCHHH
19.0433845483
350SulfoxidationKERIMGKMEADPELS
HHHHHHHHHCCHHHH
4.2028183972
358UbiquitinationEADPELSKFLYQLHE
HCCHHHHHHHHHHHH
52.6022817900
358 (in isoform 1)Ubiquitination-52.6021890473
358 (in isoform 2)Ubiquitination-52.6021890473
361PhosphorylationPELSKFLYQLHETEK
HHHHHHHHHHHHHHH
16.5020068231
3682-HydroxyisobutyrylationYQLHETEKEDLIREE
HHHHHHHHHHHHHHH
65.04-
368AcetylationYQLHETEKEDLIREE
HHHHHHHHHHHHHHH
65.0426822725
368UbiquitinationYQLHETEKEDLIREE
HHHHHHHHHHHHHHH
65.0433845483
385PhosphorylationRRERVRQSRMDTDLE
HHHHHHHHHCCCCCC
21.0029214152
389PhosphorylationVRQSRMDTDLETMDL
HHHHHCCCCCCCCCC
32.8926074081
393PhosphorylationRMDTDLETMDLDQGG
HCCCCCCCCCCCCCC
24.2326074081
417PhosphorylationDLEDLVFTQGSHFMA
CHHHHEECCCCHHHC
25.25-
426AcetylationGSHFMANKRCQLPDG
CCHHHCCCCCCCCCC
45.0423954790
426UbiquitinationGSHFMANKRCQLPDG
CCHHHCCCCCCCCCC
45.0422817900
426 (in isoform 1)Ubiquitination-45.0421890473
426 (in isoform 2)Ubiquitination-45.0421890473
427MethylationSHFMANKRCQLPDGS
CHHHCCCCCCCCCCC
17.14115919229
434PhosphorylationRCQLPDGSFRRQRKG
CCCCCCCCHHHCCCC
23.9827080861
440UbiquitinationGSFRRQRKGYEEVHV
CCHHHCCCCCCCCCC
58.4633845483
451AcetylationEVHVPALKPKPFGSE
CCCCCCCCCCCCCCH
53.7725953088
451UbiquitinationEVHVPALKPKPFGSE
CCCCCCCCCCCCCCH
53.7733845483
453UbiquitinationHVPALKPKPFGSEEQ
CCCCCCCCCCCCHHH
51.9329967540
457PhosphorylationLKPKPFGSEEQLLPV
CCCCCCCCHHHCCCH
38.0429255136
466UbiquitinationEQLLPVEKLPKYAQA
HHCCCHHHCHHHHHH
71.0323000965
469AcetylationLPVEKLPKYAQAGFE
CCHHHCHHHHHHCCC
64.7519608861
469UbiquitinationLPVEKLPKYAQAGFE
CCHHHCHHHHHHCCC
64.7523000965
469 (in isoform 1)Ubiquitination-64.7521890473
469 (in isoform 2)Ubiquitination-64.7521890473
479AcetylationQAGFEGFKTLNRIQS
HHCCCHHHHHHHHHH
64.0625953088
479MethylationQAGFEGFKTLNRIQS
HHCCCHHHHHHHHHH
64.0612433335
479UbiquitinationQAGFEGFKTLNRIQS
HHCCCHHHHHHHHHH
64.0623000965
479 (in isoform 1)Ubiquitination-64.0621890473
479 (in isoform 2)Ubiquitination-64.0621890473
487AcetylationTLNRIQSKLYRAALE
HHHHHHHHHHHHHHH
32.9125953088
487UbiquitinationTLNRIQSKLYRAALE
HHHHHHHHHHHHHHH
32.9129967540
502GlutathionylationTDENLLLCAPTGAGK
CCCCEEEECCCCCCH
4.2622555962
510PhosphorylationAPTGAGKTNVALMCM
CCCCCCHHHHHHHHH
33.73-
516GlutathionylationKTNVALMCMLREIGK
HHHHHHHHHHHHHHH
2.1222555962
523AcetylationCMLREIGKHINMDGT
HHHHHHHHHCCCCCC
47.1526051181
527SulfoxidationEIGKHINMDGTINVD
HHHHHCCCCCCCCCC
5.0728183972
540PhosphorylationVDDFKIIYIAPMRSL
CCCCEEEEEECCHHH
8.4320068231
546PhosphorylationIYIAPMRSLVQEMVG
EEEECCHHHHHHHHH
27.0021712546
551SulfoxidationMRSLVQEMVGSFGKR
CHHHHHHHHHHHHHH
2.0121406390
554PhosphorylationLVQEMVGSFGKRLAT
HHHHHHHHHHHHHHH
21.2921712546
557AcetylationEMVGSFGKRLATYGI
HHHHHHHHHHHHHCE
42.0825953088
557UbiquitinationEMVGSFGKRLATYGI
HHHHHHHHHHHHHCE
42.0823000965
557 (in isoform 1)Ubiquitination-42.0821890473
557 (in isoform 2)Ubiquitination-42.0821890473
569 (in isoform 2)Ubiquitination-4.7121890473
604PhosphorylationTRKGGERTYTQLVRL
EECCCCCHHHHHHHH
26.9828152594
605PhosphorylationRKGGERTYTQLVRLI
ECCCCCHHHHHHHHH
9.9428152594
606PhosphorylationKGGERTYTQLVRLII
CCCCCHHHHHHHHHH
18.14-
641SulfoxidationRAIRNIEMTQEDVRL
HHHHCCCCCHHHHHH
4.0821406390
652PhosphorylationDVRLIGLSATLPNYE
HHHHHEEECCCCCHH
17.6228270605
654PhosphorylationRLIGLSATLPNYEDV
HHHEEECCCCCHHHH
39.1028270605
658PhosphorylationLSATLPNYEDVATFL
EECCCCCHHHHHHHE
16.1528270605
663PhosphorylationPNYEDVATFLRVDPA
CCHHHHHHHEEEECC
24.0528270605
6952-HydroxyisobutyrylationTYVGITEKKAIKRFQ
EEEEEECHHHHHHHH
38.56-
709PhosphorylationQIMNEIVYEKIMEHA
HHHHHHHHHHHHHHC
19.71-
7112-HydroxyisobutyrylationMNEIVYEKIMEHAGK
HHHHHHHHHHHHCCC
29.66-
711AcetylationMNEIVYEKIMEHAGK
HHHHHHHHHHHHCCC
29.6627452117
711UbiquitinationMNEIVYEKIMEHAGK
HHHHHHHHHHHHCCC
29.6621906983
711 (in isoform 1)Ubiquitination-29.6621890473
729AcetylationLVFVHSRKETGKTAR
EEEEECCCCCCHHHH
63.74134129
731PhosphorylationFVHSRKETGKTARAI
EEECCCCCCHHHHHH
47.1925954137
742GlutathionylationARAIRDMCLEKDTLG
HHHHHHHHCCCCCHH
5.3422555962
7452-HydroxyisobutyrylationIRDMCLEKDTLGLFL
HHHHHCCCCCHHHHH
42.96-
745AcetylationIRDMCLEKDTLGLFL
HHHHHCCCCCHHHHH
42.9626051181
745UbiquitinationIRDMCLEKDTLGLFL
HHHHHCCCCCHHHHH
42.9629967540
747PhosphorylationDMCLEKDTLGLFLRE
HHHCCCCCHHHHHCC
33.5221712546
756PhosphorylationGLFLREGSASTEVLR
HHHHCCCCCCHHHHH
17.8129255136
758PhosphorylationFLREGSASTEVLRTE
HHCCCCCCHHHHHHH
27.1429255136
759PhosphorylationLREGSASTEVLRTEA
HCCCCCCHHHHHHHH
29.8129255136
764PhosphorylationASTEVLRTEAEQCKN
CCHHHHHHHHHHHCC
35.0723312004
7702-HydroxyisobutyrylationRTEAEQCKNLELKDL
HHHHHHHCCCCHHHH
65.35-
770AcetylationRTEAEQCKNLELKDL
HHHHHHHCCCCHHHH
65.3525953088
770UbiquitinationRTEAEQCKNLELKDL
HHHHHHHCCCCHHHH
65.3523000965
770 (in isoform 1)Ubiquitination-65.3521890473
775UbiquitinationQCKNLELKDLLPYGF
HHCCCCHHHHHCCCH
36.6323000965
795PhosphorylationGMTRVDRTLVEDLFA
CCCCCCCHHHHHHHC
30.6021712546
804MethylationVEDLFADKHIQVLVS
HHHHHCCCCHHHEEH
38.90-
829MethylationPAHTVIIKGTQVYSP
CCCEEEEECCEEECC
44.7924129315
834PhosphorylationIIKGTQVYSPEKGRW
EEECCEEECCCCCCC
14.5323312004
835PhosphorylationIKGTQVYSPEKGRWT
EECCEEECCCCCCCE
27.9428985074
8382-HydroxyisobutyrylationTQVYSPEKGRWTELG
CEEECCCCCCCEEHH
58.10-
838AcetylationTQVYSPEKGRWTELG
CEEECCCCCCCEEHH
58.1027452117
838UbiquitinationTQVYSPEKGRWTELG
CEEECCCCCCCEEHH
58.1033845483
922PhosphorylationDAVNWLGYAYLYIRM
HHHHHHHHHHHHHHH
7.0117053785
924PhosphorylationVNWLGYAYLYIRMLR
HHHHHHHHHHHHHHC
7.4917053785
926PhosphorylationWLGYAYLYIRMLRSP
HHHHHHHHHHHHCCC
3.6217053785
932PhosphorylationLYIRMLRSPTLYGIS
HHHHHHCCCCEECCC
20.4828152594
934PhosphorylationIRMLRSPTLYGISHD
HHHHCCCCEECCCHH
33.5827811184
936PhosphorylationMLRSPTLYGISHDDL
HHCCCCEECCCHHHC
18.1927811184
939PhosphorylationSPTLYGISHDDLKGD
CCCEECCCHHHCCCC
19.2528152594
944SumoylationGISHDDLKGDPLLDQ
CCCHHHCCCCCCCCH
69.16-
944AcetylationGISHDDLKGDPLLDQ
CCCHHHCCCCCCCCH
69.1623954790
944MalonylationGISHDDLKGDPLLDQ
CCCHHHCCCCCCCCH
69.1626320211
944UbiquitinationGISHDDLKGDPLLDQ
CCCHHHCCCCCCCCH
69.1621963094
944 (in isoform 1)Ubiquitination-69.1621890473
966AcetylationTAALMLDKNNLVKYD
HHHHHHCCCCCEEEE
43.7225953088
966UbiquitinationTAALMLDKNNLVKYD
HHHHHHCCCCCEEEE
43.7229967540
971SumoylationLDKNNLVKYDKKTGN
HCCCCCEEEECCCCC
51.39-
971AcetylationLDKNNLVKYDKKTGN
HCCCCCEEEECCCCC
51.3919608861
971UbiquitinationLDKNNLVKYDKKTGN
HCCCCCEEEECCCCC
51.3919608861
974UbiquitinationNNLVKYDKKTGNFQV
CCCEEEECCCCCEEE
49.50-
9752-HydroxyisobutyrylationNLVKYDKKTGNFQVT
CCEEEECCCCCEEEE
59.78-
975UbiquitinationNLVKYDKKTGNFQVT
CCEEEECCCCCEEEE
59.7833845483
989PhosphorylationTELGRIASHYYITND
EEHHEEEEEEEECCH
15.0627732954
991PhosphorylationLGRIASHYYITNDTV
HHEEEEEEEECCHHH
8.2827732954
992PhosphorylationGRIASHYYITNDTVQ
HEEEEEEEECCHHHH
8.8827732954
994PhosphorylationIASHYYITNDTVQTY
EEEEEEECCHHHHHH
15.7727732954
997PhosphorylationHYYITNDTVQTYNQL
EEEECCHHHHHHHHH
19.3127732954
1000PhosphorylationITNDTVQTYNQLLKP
ECCHHHHHHHHHHCC
21.8027732954
1001PhosphorylationTNDTVQTYNQLLKPT
CCHHHHHHHHHHCCC
5.4827732954
1021PhosphorylationLFRVFSLSSEFKNIT
HHHHHCCCHHHCCCC
26.9921712546
1022PhosphorylationFRVFSLSSEFKNITV
HHHHCCCHHHCCCCC
52.9621712546
1025UbiquitinationFSLSSEFKNITVREE
HCCCHHHCCCCCCHH
43.3133845483
1034AcetylationITVREEEKLELQKLL
CCCCHHHHHHHHHHH
51.0126051181
1034UbiquitinationITVREEEKLELQKLL
CCCCHHHHHHHHHHH
51.0123000965
1039AcetylationEEKLELQKLLERVPI
HHHHHHHHHHHCCCC
68.6026051181
1039UbiquitinationEEKLELQKLLERVPI
HHHHHHHHHHHCCCC
68.6023000965
1039 (in isoform 1)Ubiquitination-68.6021890473
10492-HydroxyisobutyrylationERVPIPVKESIEEPS
HCCCCCCCCCCCCCC
40.15-
1049AcetylationERVPIPVKESIEEPS
HCCCCCCCCCCCCCC
40.1526051181
1049UbiquitinationERVPIPVKESIEEPS
HCCCCCCCCCCCCCC
40.1521906983
1049 (in isoform 1)Ubiquitination-40.1521890473
1056PhosphorylationKESIEEPSAKINVLL
CCCCCCCCHHHHHHH
45.5322817900
1068PhosphorylationVLLQAFISQLKLEGF
HHHHHHHHHHCCCCC
24.0124719451
1071SumoylationQAFISQLKLEGFALM
HHHHHHHCCCCCEEE
36.53-
11102-HydroxyisobutyrylationGWAQLTDKTLNLCKM
CHHHCCHHHHHHHHH
50.07-
1125PhosphorylationIDKRMWQSMCPLRQF
HCHHHHHHHCCHHHH
13.5723401153
1134MalonylationCPLRQFRKLPEEVVK
CCHHHHHCCCHHHHH
70.4526320211
1134UbiquitinationCPLRQFRKLPEEVVK
CCHHHHHCCCHHHHH
70.4529967540
1141AcetylationKLPEEVVKKIEKKNF
CCCHHHHHHHHHCCC
53.8926051181
1141UbiquitinationKLPEEVVKKIEKKNF
CCCHHHHHHHHHCCC
53.89-
11462-HydroxyisobutyrylationVVKKIEKKNFPFERL
HHHHHHHCCCCHHHH
51.54-
1146UbiquitinationVVKKIEKKNFPFERL
HHHHHHHCCCCHHHH
51.5433845483
1154PhosphorylationNFPFERLYDLNHNEI
CCCHHHHCCCCCCHH
25.3027642862
1173PhosphorylationRMPKMGKTIHKYVHL
CCCCCCCCHHHHHHH
23.6824719451
1176AcetylationKMGKTIHKYVHLFPK
CCCCCHHHHHHHHHC
45.1519608861
1176MalonylationKMGKTIHKYVHLFPK
CCCCCHHHHHHHHHC
45.1526320211
1176UbiquitinationKMGKTIHKYVHLFPK
CCCCCHHHHHHHHHC
45.1519608861
1177PhosphorylationMGKTIHKYVHLFPKL
CCCCHHHHHHHHHCC
4.4828152594
1183UbiquitinationKYVHLFPKLELSVHL
HHHHHHHCCEEEEEE
47.4633845483
1199SumoylationPITRSTLKVELTITP
ECCCCEEEEEEEECC
33.48-
1238PhosphorylationEVILHHEYFLLKAKY
HHEEEEEEEHHHHHH
8.65-
1294UbiquitinationRHLILPEKYPPPTEL
EEECCCCCCCCCCHH
62.2033845483
1319PhosphorylationLRNSAFESLYQDKFP
HHCHHHHHHHCCCCC
26.3921601212
1321PhosphorylationNSAFESLYQDKFPFF
CHHHHHHHCCCCCCC
24.76-
1367SulfoxidationAEFAILRMLLQSSEG
HHHHHHHHHHHCCCC
3.8221406390
1371PhosphorylationILRMLLQSSEGRCVY
HHHHHHHCCCCCEEE
30.2627174698
1372PhosphorylationLRMLLQSSEGRCVYI
HHHHHHCCCCCEEEE
30.9827174698
1378PhosphorylationSSEGRCVYITPMEAL
CCCCCEEEECCHHHH
11.6027174698
1380PhosphorylationEGRCVYITPMEALAE
CCCEEEECCHHHHHH
10.0127174698
1390PhosphorylationEALAEQVYMDWYEKF
HHHHHHHHHHHHHHH
6.7727174698
1394PhosphorylationEQVYMDWYEKFQDRL
HHHHHHHHHHHHHHH
12.6527174698
1403UbiquitinationKFQDRLNKKVVLLTG
HHHHHHCCCEEEEEC
52.0823000965
1404UbiquitinationFQDRLNKKVVLLTGE
HHHHHCCCEEEEECC
36.1823000965
1409PhosphorylationNKKVVLLTGETSTDL
CCCEEEEECCCCCCE
28.8924670416
1412PhosphorylationVVLLTGETSTDLKLL
EEEEECCCCCCEEEC
37.9724670416
1414PhosphorylationLLTGETSTDLKLLGK
EEECCCCCCEEECCC
53.4224670416
1417AcetylationGETSTDLKLLGKGNI
CCCCCCEEECCCCCE
44.4625953088
1417UbiquitinationGETSTDLKLLGKGNI
CCCCCCEEECCCCCE
44.4623000965
14212-HydroxyisobutyrylationTDLKLLGKGNIIIST
CCEEECCCCCEEEEC
49.07-
1421MalonylationTDLKLLGKGNIIIST
CCEEECCCCCEEEEC
49.0726320211
1421UbiquitinationTDLKLLGKGNIIIST
CCEEECCCCCEEEEC
49.0723000965
1421 (in isoform 1)Ubiquitination-49.0721890473
1427PhosphorylationGKGNIIISTPEKWDI
CCCCEEEECHHHHHH
27.7427050516
1428PhosphorylationKGNIIISTPEKWDIL
CCCEEEECHHHHHHH
25.6730624053
1431AcetylationIIISTPEKWDILSRR
EEEECHHHHHHHHHH
51.9026051181
1431UbiquitinationIIISTPEKWDILSRR
EEEECHHHHHHHHHH
51.9023000965
1431 (in isoform 1)Ubiquitination-51.9021890473
1443SumoylationSRRWKQRKNVQNINL
HHHHHHCCCCCCEEE
60.00-
1491PhosphorylationPIRIVALSSSLSNAK
CCEEEEECCCCCCHH
14.2421406692
1492PhosphorylationIRIVALSSSLSNAKD
CEEEEECCCCCCHHH
35.8321406692
1493PhosphorylationRIVALSSSLSNAKDV
EEEEECCCCCCHHHH
32.2321406692
1495PhosphorylationVALSSSLSNAKDVAH
EEECCCCCCHHHHHH
36.3721406692
1541PhosphorylationHTQTRLLSMAKPVYH
HHHHHHHHHHHHHHH
22.68-
1544AcetylationTRLLSMAKPVYHAIT
HHHHHHHHHHHHHHH
26.7826051181
1544UbiquitinationTRLLSMAKPVYHAIT
HHHHHHHHHHHHHHH
26.7823000965
1544 (in isoform 1)Ubiquitination-26.7821890473
1552AcetylationPVYHAITKHSPKKPV
HHHHHHHCCCCCCCE
35.6525953088
1552UbiquitinationPVYHAITKHSPKKPV
HHHHHHHCCCCCCCE
35.6523000965
1556UbiquitinationAITKHSPKKPVIVFV
HHHCCCCCCCEEEEE
73.1223000965
1557UbiquitinationITKHSPKKPVIVFVP
HHCCCCCCCEEEEEC
48.1523000965
1569PhosphorylationFVPSRKQTRLTAIDI
EECCCCCCHHHHHHH
30.5924719451
1572PhosphorylationSRKQTRLTAIDILTT
CCCCCHHHHHHHHHH
20.48-
1579PhosphorylationTAIDILTTCAADIQR
HHHHHHHHHHHHHHH
9.1924719451
1580GlutathionylationAIDILTTCAADIQRQ
HHHHHHHHHHHHHHH
2.1822555962
1593PhosphorylationRQRFLHCTEKDLIPY
HHHHHCCCHHHHHHH
35.0124719451
1595AcetylationRFLHCTEKDLIPYLE
HHHCCCHHHHHHHHH
39.4225825284
1595UbiquitinationRFLHCTEKDLIPYLE
HHHCCCHHHHHHHHH
39.4223000965
1600PhosphorylationTEKDLIPYLEKLSDS
CHHHHHHHHHHCCCC
22.0929083192
16032-HydroxyisobutyrylationDLIPYLEKLSDSTLK
HHHHHHHHCCCCHHH
51.17-
1603UbiquitinationDLIPYLEKLSDSTLK
HHHHHHHHCCCCHHH
51.1721906983
1603 (in isoform 1)Ubiquitination-51.1721890473
1605PhosphorylationIPYLEKLSDSTLKET
HHHHHHCCCCHHHHH
40.3527251275
1607PhosphorylationYLEKLSDSTLKETLL
HHHHCCCCHHHHHHH
32.0630266825
1608PhosphorylationLEKLSDSTLKETLLN
HHHCCCCHHHHHHHH
47.0030266825
1625PhosphorylationGYLHEGLSPMERRLV
CHHCCCCCHHHHHHH
32.81-
1637PhosphorylationRLVEQLFSSGAIQVV
HHHHHHHCCCCCEEE
36.1329978859
1638PhosphorylationLVEQLFSSGAIQVVV
HHHHHHCCCCCEEEE
25.5529978859
1647PhosphorylationAIQVVVASRSLCWGM
CCEEEEECCCHHHCC
15.7029978859
1648DimethylationIQVVVASRSLCWGMN
CEEEEECCCHHHCCC
24.74-
1648MethylationIQVVVASRSLCWGMN
CEEEEECCCHHHCCC
24.74115390075
1679PhosphorylationKIHAYVDYPIYDVLQ
EEEEEEECCHHHHHH
4.98-
1682PhosphorylationAYVDYPIYDVLQMVG
EEEECCHHHHHHHHC
8.7628064214
1711UbiquitinationIMCQGSKKDFFKKFL
EEECCCCHHHHHHHC
62.56-
1743UbiquitinationFNAEIVTKTIENKQD
CCCEEHHHHHCCCHH
36.2922817900
1748UbiquitinationVTKTIENKQDAVDYL
HHHHHCCCHHHHHHH
36.4421963094
1754PhosphorylationNKQDAVDYLTWTFLY
CCHHHHHHHHHHHHH
10.2222817900
1765PhosphorylationTFLYRRMTQNPNYYN
HHHHHHHCCCCCCCC
24.3124043423
1770PhosphorylationRMTQNPNYYNLQGIS
HHCCCCCCCCCCCCC
8.5917360941
1771PhosphorylationMTQNPNYYNLQGISH
HCCCCCCCCCCCCCH
18.9424043423
1777PhosphorylationYYNLQGISHRHLSDH
CCCCCCCCHHHHHHH
22.6924043423
1782PhosphorylationGISHRHLSDHLSELV
CCCHHHHHHHHHHHH
19.5028450419
1786PhosphorylationRHLSDHLSELVEQTL
HHHHHHHHHHHHHHH
26.0128450419
1792PhosphorylationLSELVEQTLSDLEQS
HHHHHHHHHHHHHHH
18.0928122231
1794PhosphorylationELVEQTLSDLEQSKC
HHHHHHHHHHHHHCC
43.4628122231
1855PhosphorylationIISNAAEYENIPIRH
HHHCCHHHCCCCCCC
15.00-
1874AcetylationLLRQLAQKVPHKLNN
HHHHHHHHCCHHHCC
52.7225953088
1874UbiquitinationLLRQLAQKVPHKLNN
HHHHHHHHCCHHHCC
52.7229967540
1878AcetylationLAQKVPHKLNNPKFN
HHHHCCHHHCCCCCC
47.0025953088
1878UbiquitinationLAQKVPHKLNNPKFN
HHHHCCHHHCCCCCC
47.0029967540
1883AcetylationPHKLNNPKFNDPHVK
CHHHCCCCCCCHHHH
59.9525953088
1883UbiquitinationPHKLNNPKFNDPHVK
CHHHCCCCCCCHHHH
59.9529967540
1890UbiquitinationKFNDPHVKTNLLLQA
CCCCHHHHHHHHHHH
28.7633845483
1891PhosphorylationFNDPHVKTNLLLQAH
CCCHHHHHHHHHHHH
29.9721406692
1900PhosphorylationLLLQAHLSRMQLSAE
HHHHHHHHHHHHHHH
18.8121406692
1910PhosphorylationQLSAELQSDTEEILS
HHHHHHCCCHHHHHH
60.15-
1918UbiquitinationDTEEILSKAIRLIQA
CHHHHHHHHHHHHHH
44.3733845483
1931PhosphorylationQACVDVLSSNGWLSP
HHHHHHHHCCCCCCH
22.9322210691
1932PhosphorylationACVDVLSSNGWLSPA
HHHHHHHCCCCCCHH
34.8922210691
1937PhosphorylationLSSNGWLSPALAAME
HHCCCCCCHHHHHHH
11.1322210691
1955PhosphorylationMVTQAMWSKDSYLKQ
HHHHHHHCCCHHHHH
17.32-
1956UbiquitinationVTQAMWSKDSYLKQL
HHHHHHCCCHHHHHC
34.8722817900
1958PhosphorylationQAMWSKDSYLKQLPH
HHHHCCCHHHHHCCC
35.78-
1959PhosphorylationAMWSKDSYLKQLPHF
HHHCCCHHHHHCCCC
28.22-
1961UbiquitinationWSKDSYLKQLPHFTS
HCCCHHHHHCCCCCH
41.3722817900
1961 (in isoform 1)Ubiquitination-41.3721890473
1972UbiquitinationHFTSEHIKRCTDKGV
CCCHHHHHHHCCCCC
43.2433845483
2000PhosphorylationRNALLQLTDSQIADV
HHHHHHCCHHHHHHH
22.2030266825
2002PhosphorylationALLQLTDSQIADVAR
HHHHCCHHHHHHHHH
20.4630266825
2020PhosphorylationRYPNIELSYEVVDKD
CCCCEEEEEEEECHH
13.37-
2021PhosphorylationYPNIELSYEVVDKDS
CCCEEEEEEEECHHH
25.9317360941
2059UbiquitinationIAPLFPQKREEGWWV
EECCCCCCCCCCEEE
63.1121906983
2059 (in isoform 1)Ubiquitination-63.1121890473
2075PhosphorylationIGDAKSNSLISIKRL
EEECCCCCEEEEEEE
33.8821210654
20802-HydroxyisobutyrylationSNSLISIKRLTLQQK
CCCEEEEEEEECHHC
34.27-
2080AcetylationSNSLISIKRLTLQQK
CCCEEEEEEEECHHC
34.2725953088
2080UbiquitinationSNSLISIKRLTLQQK
CCCEEEEEEEECHHC
34.2721906983
2080 (in isoform 1)Ubiquitination-34.2721890473
2087AcetylationKRLTLQQKAKVKLDF
EEEECHHCCCEEEEE
36.8925953088
2087UbiquitinationKRLTLQQKAKVKLDF
EEEECHHCCCEEEEE
36.8932142685
2091SumoylationLQQKAKVKLDFVAPA
CHHCCCEEEEEEECC
41.45-
2123PhosphorylationCDQEYKFSVDVKEAE
CCCEEEEEEEHHHCC
17.1628634120
2131PhosphorylationVDVKEAETDSDSD--
EEHHHCCCCCCCC--
48.1026503892
2133PhosphorylationVKEAETDSDSD----
HHHCCCCCCCC----
46.5726503892
2135PhosphorylationEAETDSDSD------
HCCCCCCCC------
49.5326503892

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 U520_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U520_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 U520_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U5S1_HUMANEFTUD2physical
16723661
U520_HUMANSNRNP200physical
16723661
PRP8_HUMANPRPF8physical
16723661
SNR40_HUMANSNRNP40physical
16723661
U5S1_HUMANEFTUD2physical
22939629
YBOX1_HUMANYBX1physical
22939629
VIR_HUMANKIAA1429physical
22939629
YETS2_HUMANYEATS2physical
22939629
UBR4_HUMANUBR4physical
22939629
ZBT10_HUMANZBTB10physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
SF3B2_HUMANSF3B2physical
22365833
U520_HUMANSNRNP200physical
22365833
LSM8_HUMANLSM8physical
22365833
R113A_HUMANRNF113Aphysical
22365833
WASC4_HUMANKIAA1033physical
22863883
RPAB3_HUMANPOLR2Hphysical
22863883
T22D1_HUMANTSC22D1physical
22863883
UBP34_HUMANUSP34physical
22863883
WDHD1_HUMANWDHD1physical
22863883
PRP8_HUMANPRPF8physical
23704370
PRP8_HUMANPRPF8physical
17317632
BPTF_HUMANBPTFphysical
26344197
CD2B2_HUMANCD2BP2physical
26344197
U5S1_HUMANEFTUD2physical
26344197
RBP2_HUMANRANBP2physical
26344197
SNUT1_HUMANSART1physical
26344197
SF3A3_HUMANSF3A3physical
26344197
SMD1_HUMANSNRPD1physical
26344197
RUXE_HUMANSNRPEphysical
26344197
SRRM2_HUMANSRRM2physical
26344197
SMU1_HUMANSMU1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610359Retinitis pigmentosa 33 (RP33)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of U520_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-469; LYS-971 AND LYS-1176,AND MASS SPECTROMETRY.
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-225; THR-2131; SER-2133AND SER-2135, 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-225, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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-26; SER-225; THR-2131;SER-2133 AND SER-2135, 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-225, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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-225 AND SER-1056, ANDMASS 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-225 AND SER-756, ANDMASS SPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-922; TYR-924 ANDTYR-926, AND MASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"A proteomic study of SUMO-2 target proteins.";
Vertegaal A.C.O., Ogg S.C., Jaffray E., Rodriguez M.S., Hay R.T.,Andersen J.S., Mann M., Lamond A.I.;
J. Biol. Chem. 279:33791-33798(2004).
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-944; LYS-971; LYS-1071;LYS-1199 AND LYS-2091, AND MASS SPECTROMETRY.

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