RBM33_HUMAN - dbPTM
RBM33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM33_HUMAN
UniProt AC Q96EV2
Protein Name RNA-binding protein 33
Gene Name RBM33
Organism Homo sapiens (Human).
Sequence Length 1170
Subcellular Localization
Protein Description
Protein Sequence MAAALGASGGAGAGDDDFDQFDKPGAERSWRRRAADEDWDSELEDDLLGEDLLSGKKNQSDLSDEELNDDLLQSDNEDEENFSSQGVTISLNATSGMVTSFELSDNTNDQSGEQESEYEQEQGEDELVYHKSDGSELYTQEYPEEGQYEGHEAELTEDQIEYVEEPEEEQLYTDEVLDIEINEPLDEFTGGMETLELQKDIKEESDEEEEDDEESGRLRFKTERKEGTIIRLSDVTRERRNIPETLELSAEAKAALLEFEERERQHKQGRYSSRRGGRRGGPLMCRGVGDQRRESTERGRMKDHRPALLPTQPPVVPQAPPPPPPPPQQQPIRSLFQPQPLQPLLPVQHPHHPSPPQGMHMPPQLETPRMMMTPPPVTPQQPKNIHINPHFKGTVVTPVQVPLLPVPSQPRPAVGPQRFPGPPEFPQHTPGPVPNSFSQPPRLPLQDQWRAPPPPQDRDPFFLGVSGEPRFPSHLFLEQRSPPPPPPPPTLLNSSHPVPTQSPLPFTQPGPAFNQQGQQPVFPRERPVRPALQPPGPVGILHFSQPGSATTRPFIPPRQPFLPGPGQPFLPTHTQPNLQGPLHPPLPPPHQPQPQQPQQQPPPQHQPPHQPPHQPPPQHQPPPQHPPQHPPQHQHHHHHHHLSVPPPPLMPMSQPQFRPHVQTAQPQASSSRMQCPQRQGLRHNTTSQNVSKRPMQQMQPTAPRNSNLRELPIAPSHVIEMSSSRCSATPSAQVKPIVSASPPSRAVAGSRSSQGKTEVKVKPASPVAQPKEEAKTETEFPDEDEETRLYRLKIEEQKRLREEILKQKELRRQQQAGARKKELLERLAQQQQQLYAPPPPAEQEEQALSPSPTNGNPLLPFPGAQVRQNVKNRLLVKNQDVSISNVQPKTSNFVPSSANMQYQGQQMKALKHLRQTRTVPQSQTQPLHKVLPIKPADVEEPAVPQTPRVASIQGRPQDTKPGVKRTVTHRTNSGGGDGPHISSKVRVIKLSGGGGESDGFFHPEGQPQRLPQPPEVGPQPARKVTLTRGGLQQPPHLPAGPHAHSPVPPGIKSIQGIHPAKKAIMHGRGRGVAGPMGRGRLMPNKQNLRVVECKPQPCVVSVEGLSSSTTDAQLKSLLMSVGPIQSLQMLPQQRKAIAKFKEPAHALAFQQKFHRHMIDLSHINVALIVE
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------MAAALGASG
------CCCCCCCCC
16.8522814378
8PhosphorylationMAAALGASGGAGAGD
CCCCCCCCCCCCCCC
35.6429743597
23AcetylationDDFDQFDKPGAERSW
CCHHHCCCCCHHHHH
46.7925953088
29PhosphorylationDKPGAERSWRRRAAD
CCCCHHHHHHHHHCC
19.2127251275
41PhosphorylationAADEDWDSELEDDLL
HCCCCCCHHHHHCCC
39.5719664994
54PhosphorylationLLGEDLLSGKKNQSD
CCCHHHHCCCCCHHH
56.7323403867
56AcetylationGEDLLSGKKNQSDLS
CHHHHCCCCCHHHCC
45.2126051181
148PhosphorylationEYPEEGQYEGHEAEL
ECCCCCCCCCCCEEC
34.43-
171PhosphorylationEEPEEEQLYTDEVLD
CCCHHHHCCCCCEEE
5.8615302935
185PhosphorylationDIEINEPLDEFTGGM
EEEECCCHHHHCCCH
8.8715302935
202SumoylationLELQKDIKEESDEEE
HHHHHHHHHHCCCCC
66.61-
205PhosphorylationQKDIKEESDEEEEDD
HHHHHHHCCCCCCCC
51.9522167270
215PhosphorylationEEEDDEESGRLRFKT
CCCCCHHHCCEEEEE
27.4522167270
224DimethylationRLRFKTERKEGTIIR
CEEEEEEECCCEEEE
47.78-
224MethylationRLRFKTERKEGTIIR
CEEEEEEECCCEEEE
47.7824379947
228PhosphorylationKTERKEGTIIRLSDV
EEEECCCEEEEHHHH
17.8320068231
231DimethylationRKEGTIIRLSDVTRE
ECCCEEEEHHHHCHH
25.04-
231MethylationRKEGTIIRLSDVTRE
ECCCEEEEHHHHCHH
25.0424379957
233PhosphorylationEGTIIRLSDVTRERR
CCEEEEHHHHCHHHC
21.8625159151
236PhosphorylationIIRLSDVTRERRNIP
EEEHHHHCHHHCCCC
31.6320068231
237DimethylationIRLSDVTRERRNIPE
EEHHHHCHHHCCCCC
34.96-
237MethylationIRLSDVTRERRNIPE
EEHHHHCHHHCCCCC
34.9624379967
245PhosphorylationERRNIPETLELSAEA
HHCCCCCHHHHCHHH
21.8527251275
245 (in isoform 2)Phosphorylation-21.8519845377
249PhosphorylationIPETLELSAEAKAAL
CCCHHHHCHHHHHHH
18.0629396449
253UbiquitinationLELSAEAKAALLEFE
HHHCHHHHHHHHHHH
26.2029967540
256 (in isoform 2)Phosphorylation-5.8619845377
258 (in isoform 2)Phosphorylation-52.4419845377
261 (in isoform 2)Phosphorylation-66.2319845377
271PhosphorylationRQHKQGRYSSRRGGR
HHHHCCCCCCCCCCC
20.1626074081
272PhosphorylationQHKQGRYSSRRGGRR
HHHCCCCCCCCCCCC
18.9326074081
273PhosphorylationHKQGRYSSRRGGRRG
HHCCCCCCCCCCCCC
19.6426074081
279MethylationSSRRGGRRGGPLMCR
CCCCCCCCCCCCCCC
58.6616289391
286MethylationRGGPLMCRGVGDQRR
CCCCCCCCCCCHHCH
28.9430988979
295PhosphorylationVGDQRRESTERGRMK
CCHHCHHHCCCCCCC
33.4826074081
296PhosphorylationGDQRRESTERGRMKD
CHHCHHHCCCCCCCC
25.5826074081
302MethylationSTERGRMKDHRPALL
HCCCCCCCCCCCCCC
49.3624129315
311PhosphorylationHRPALLPTQPPVVPQ
CCCCCCCCCCCCCCC
54.39-
373PhosphorylationETPRMMMTPPPVTPQ
CCCCCCCCCCCCCCC
18.1028985074
378PhosphorylationMMTPPPVTPQQPKNI
CCCCCCCCCCCCCCC
22.5823186163
394PhosphorylationINPHFKGTVVTPVQV
CCCCCCCCEEECCCC
16.6428122231
397PhosphorylationHFKGTVVTPVQVPLL
CCCCCEEECCCCCCC
17.2628348404
442DimethylationNSFSQPPRLPLQDQW
CCCCCCCCCCCCCCC
56.47-
442MethylationNSFSQPPRLPLQDQW
CCCCCCCCCCCCCCC
56.4752717395
450DimethylationLPLQDQWRAPPPPQD
CCCCCCCCCCCCCCC
31.42-
450MethylationLPLQDQWRAPPPPQD
CCCCCCCCCCCCCCC
31.4254549455
470Asymmetric dimethylarginineLGVSGEPRFPSHLFL
EECCCCCCCCCCCCC
52.37-
470MethylationLGVSGEPRFPSHLFL
EECCCCCCCCCCCCC
52.3724129315
481PhosphorylationHLFLEQRSPPPPPPP
CCCCCCCCCCCCCCC
41.2626074081
490PhosphorylationPPPPPPPTLLNSSHP
CCCCCCCCCCCCCCC
50.0426434776
494PhosphorylationPPPTLLNSSHPVPTQ
CCCCCCCCCCCCCCC
29.9626434776
495PhosphorylationPPTLLNSSHPVPTQS
CCCCCCCCCCCCCCC
30.6426434776
500PhosphorylationNSSHPVPTQSPLPFT
CCCCCCCCCCCCCCC
41.7426074081
502PhosphorylationSHPVPTQSPLPFTQP
CCCCCCCCCCCCCCC
30.7726074081
507PhosphorylationTQSPLPFTQPGPAFN
CCCCCCCCCCCCCCC
31.7325002506
524MethylationGQQPVFPRERPVRPA
CCCCCCCCCCCCCCC
40.8881452797
658DimethylationPMSQPQFRPHVQTAQ
CCCCCCCCCCCCCCC
18.37-
658MethylationPMSQPQFRPHVQTAQ
CCCCCCCCCCCCCCC
18.3754561675
672DimethylationQPQASSSRMQCPQRQ
CCCCCCCCCCCCHHH
22.57-
672MethylationQPQASSSRMQCPQRQ
CCCCCCCCCCCCHHH
22.5754561667
678DimethylationSRMQCPQRQGLRHNT
CCCCCCHHHCCCCCC
20.06-
678MethylationSRMQCPQRQGLRHNT
CCCCCCHHHCCCCCC
20.0654561691
682DimethylationCPQRQGLRHNTTSQN
CCHHHCCCCCCCCCC
28.03-
682MethylationCPQRQGLRHNTTSQN
CCHHHCCCCCCCCCC
28.0354558599
692AcetylationTTSQNVSKRPMQQMQ
CCCCCCCCCCHHHCC
57.1324469647
693MethylationTSQNVSKRPMQQMQP
CCCCCCCCCHHHCCC
25.15115490743
706PhosphorylationQPTAPRNSNLRELPI
CCCCCCCCCCCCCCC
38.2228555341
722PhosphorylationPSHVIEMSSSRCSAT
HHHEEEECCCCCCCC
16.6328555341
724O-linked_GlycosylationHVIEMSSSRCSATPS
HEEEECCCCCCCCCC
29.9630379171
724PhosphorylationHVIEMSSSRCSATPS
HEEEECCCCCCCCCC
29.96-
727PhosphorylationEMSSSRCSATPSAQV
EECCCCCCCCCCCCC
33.7823403867
729PhosphorylationSSSRCSATPSAQVKP
CCCCCCCCCCCCCCC
11.0723663014
731PhosphorylationSRCSATPSAQVKPIV
CCCCCCCCCCCCCCE
27.2923927012
735AcetylationATPSAQVKPIVSASP
CCCCCCCCCCEECCC
19.5625953088
739O-linked_GlycosylationAQVKPIVSASPPSRA
CCCCCCEECCCCCCC
24.6130379171
739PhosphorylationAQVKPIVSASPPSRA
CCCCCCEECCCCCCC
24.6123401153
741PhosphorylationVKPIVSASPPSRAVA
CCCCEECCCCCCCCC
29.8219664994
744PhosphorylationIVSASPPSRAVAGSR
CEECCCCCCCCCCCC
35.9330266825
750PhosphorylationPSRAVAGSRSSQGKT
CCCCCCCCCCCCCCC
21.1726074081
752PhosphorylationRAVAGSRSSQGKTEV
CCCCCCCCCCCCCEE
28.8026074081
753PhosphorylationAVAGSRSSQGKTEVK
CCCCCCCCCCCCEEE
41.6726074081
756AcetylationGSRSSQGKTEVKVKP
CCCCCCCCCEEEEEC
33.6026051181
757PhosphorylationSRSSQGKTEVKVKPA
CCCCCCCCEEEEECC
53.4823312004
765PhosphorylationEVKVKPASPVAQPKE
EEEEECCCCCCCCHH
28.5629255136
776PhosphorylationQPKEEAKTETEFPDE
CCHHHHCCCCCCCCC
56.0123403867
778PhosphorylationKEEAKTETEFPDEDE
HHHHCCCCCCCCCCH
48.4328270605
793SumoylationETRLYRLKIEEQKRL
HHHHHHHHHHHHHHH
38.79-
798UbiquitinationRLKIEEQKRLREEIL
HHHHHHHHHHHHHHH
57.5924816145
808UbiquitinationREEILKQKELRRQQQ
HHHHHHHHHHHHHHH
58.0724816145
835PhosphorylationAQQQQQLYAPPPPAE
HHHHHHHHCCCCCHH
16.8430108239
838UbiquitinationQQQLYAPPPPAEQEE
HHHHHCCCCCHHHHH
39.0624816145
848UbiquitinationAEQEEQALSPSPTNG
HHHHHHHCCCCCCCC
8.4824816145
849PhosphorylationEQEEQALSPSPTNGN
HHHHHHCCCCCCCCC
26.7525022875
851PhosphorylationEEQALSPSPTNGNPL
HHHHCCCCCCCCCCC
40.7730108239
853PhosphorylationQALSPSPTNGNPLLP
HHCCCCCCCCCCCCC
61.1630108239
877SumoylationVKNRLLVKNQDVSIS
HHHCEEECCCCEECC
49.19-
877SumoylationVKNRLLVKNQDVSIS
HHHCEEECCCCEECC
49.19-
882O-linked_GlycosylationLVKNQDVSISNVQPK
EECCCCEECCCCCCC
28.7030379171
882PhosphorylationLVKNQDVSISNVQPK
EECCCCEECCCCCCC
28.7028176443
884PhosphorylationKNQDVSISNVQPKTS
CCCCEECCCCCCCCC
24.3628176443
889MethylationSISNVQPKTSNFVPS
ECCCCCCCCCCCCCC
47.7124129315
934SumoylationLHKVLPIKPADVEEP
HHCCCCCCCCCCCCC
32.01-
934AcetylationLHKVLPIKPADVEEP
HHCCCCCCCCCCCCC
32.0126051181
934SumoylationLHKVLPIKPADVEEP
HHCCCCCCCCCCCCC
32.01-
934UbiquitinationLHKVLPIKPADVEEP
HHCCCCCCCCCCCCC
32.0129967540
946PhosphorylationEEPAVPQTPRVASIQ
CCCCCCCCCCEEEEC
13.6429255136
951PhosphorylationPQTPRVASIQGRPQD
CCCCCEEEECCCCCC
16.7623917254
960AcetylationQGRPQDTKPGVKRTV
CCCCCCCCCCCEEEE
48.3323749302
960SumoylationQGRPQDTKPGVKRTV
CCCCCCCCCCCEEEE
48.3328112733
960UbiquitinationQGRPQDTKPGVKRTV
CCCCCCCCCCCEEEE
48.3324816145
964MethylationQDTKPGVKRTVTHRT
CCCCCCCEEEEEECC
48.55116253411
966PhosphorylationTKPGVKRTVTHRTNS
CCCCCEEEEEECCCC
24.8429514088
968PhosphorylationPGVKRTVTHRTNSGG
CCCEEEEEECCCCCC
12.6729514088
970UbiquitinationVKRTVTHRTNSGGGD
CEEEEEECCCCCCCC
26.6624816145
971PhosphorylationKRTVTHRTNSGGGDG
EEEEEECCCCCCCCC
26.5721955146
973PhosphorylationTVTHRTNSGGGDGPH
EEEECCCCCCCCCCC
37.9025159151
982PhosphorylationGGDGPHISSKVRVIK
CCCCCCCCCEEEEEE
22.5223403867
983PhosphorylationGDGPHISSKVRVIKL
CCCCCCCCEEEEEEE
34.2723403867
984AcetylationDGPHISSKVRVIKLS
CCCCCCCEEEEEEEC
27.5425953088
991PhosphorylationKVRVIKLSGGGGESD
EEEEEEECCCCCCCC
30.3225159151
1000UbiquitinationGGGESDGFFHPEGQP
CCCCCCCCCCCCCCC
6.4524816145
1010UbiquitinationPEGQPQRLPQPPEVG
CCCCCCCCCCCCCCC
3.7824816145
1028Asymmetric dimethylarginineARKVTLTRGGLQQPP
CCEEEEECCCCCCCC
40.05-
1028MethylationARKVTLTRGGLQQPP
CCEEEEECCCCCCCC
40.0524129315
1045PhosphorylationPAGPHAHSPVPPGIK
CCCCCCCCCCCCCCC
28.5129255136
1061AcetylationIQGIHPAKKAIMHGR
HCCCCHHHHHHHCCC
47.3825953088
1070DimethylationAIMHGRGRGVAGPMG
HHHCCCCCCCCCCCC
34.74-
1070MethylationAIMHGRGRGVAGPMG
HHHCCCCCCCCCCCC
34.7426494771
1078DimethylationGVAGPMGRGRLMPNK
CCCCCCCCCCCCCCC
22.32-
1078MethylationGVAGPMGRGRLMPNK
CCCCCCCCCCCCCCC
22.3254558623
1085AcetylationRGRLMPNKQNLRVVE
CCCCCCCCCCEEEEE
34.3919821601
1085UbiquitinationRGRLMPNKQNLRVVE
CCCCCCCCCCEEEEE
34.3929967540
1094AcetylationNLRVVECKPQPCVVS
CEEEEECCCCCEEEE
32.9325953088
1106PhosphorylationVVSVEGLSSSTTDAQ
EEEEECCCCCCCHHH
32.8527251275
1107PhosphorylationVSVEGLSSSTTDAQL
EEEECCCCCCCHHHH
36.4227251275
1108PhosphorylationSVEGLSSSTTDAQLK
EEECCCCCCCHHHHH
31.7627251275
1109PhosphorylationVEGLSSSTTDAQLKS
EECCCCCCCHHHHHH
30.5527251275
1141UbiquitinationRKAIAKFKEPAHALA
HHHHHHHCCHHHHHH
63.1829967540

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 RBM33_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM33_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 RBM33_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOM34_HUMANTOMM34physical
22939629
SORC3_HUMANSORCS3physical
22939629
MYO9B_HUMANMYO9Bphysical
26186194
TRM2A_HUMANTRMT2Aphysical
26186194
EME1_HUMANEME1physical
26186194
ATF6B_HUMANATF6Bphysical
26186194
KPTN_HUMANKPTNphysical
26186194
EME1_HUMANEME1physical
28514442
KPTN_HUMANKPTNphysical
28514442
MYO9B_HUMANMYO9Bphysical
28514442

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 RBM33_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-41 AND SER-205, 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-205, 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-41; SER-205 AND SER-765,AND MASS SPECTROMETRY.
"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-741 AND SER-765, ANDMASS 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-765, 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-41 AND SER-205, AND MASSSPECTROMETRY.

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