RBM10_HUMAN - dbPTM
RBM10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM10_HUMAN
UniProt AC P98175
Protein Name RNA-binding protein 10 {ECO:0000305}
Gene Name RBM10 {ECO:0000312|HGNC:HGNC:9896}
Organism Homo sapiens (Human).
Sequence Length 930
Subcellular Localization Nucleus . In the extranucleolar nucleoplasm constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, the nuclear bodies enlarge and decrease in
Protein Description May be involved in post-transcriptional processing, most probably in mRNA splicing. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). May bind to specific miRNA hairpins. [PubMed: 28431233]
Protein Sequence MEYERRGGRGDRTGRYGATDRSQDDGGENRSRDHDYRDMDYRSYPREYGSQEGKHDYDDSSEEQSAEDSYEASPGSETQRRRRRRHRHSPTGPPGFPRDGDYRDQDYRTEQGEEEEEEEDEEEEEKASNIVMLRMLPQAATEDDIRGQLQSHGVQAREVRLMRNKSSGQSRGFAFVEFSHLQDATRWMEANQHSLNILGQKVSMHYSDPKPKINEDWLCNKCGVQNFKRREKCFKCGVPKSEAEQKLPLGTRLDQQTLPLGGRELSQGLLPLPQPYQAQGVLASQALSQGSEPSSENANDTIILRNLNPHSTMDSILGALAPYAVLSSSNVRVIKDKQTQLNRGFAFIQLSTIVEAAQLLQILQALHPPLTIDGKTINVEFAKGSKRDMASNEGSRISAASVASTAIAAAQWAISQASQGGEGTWATSEEPPVDYSYYQQDEGYGNSQGTESSLYAHGYLKGTKGPGITGTKGDPTGAGPEASLEPGADSVSMQAFSRAQPGAAPGIYQQSAEASSSQGTAANSQSYTIMSPAVLKSELQSPTHPSSALPPATSPTAQESYSQYPVPDVSTYQYDETSGYYYDPQTGLYYDPNSQYYYNAQSQQYLYWDGERRTYVPALEQSADGHKETGAPSKEGKEKKEKHKTKTAQQIAKDMERWARSLNKQKENFKNSFQPISSLRDDERRESATADAGYAILEKKGALAERQHTSMDLPKLASDDRPSPPRGLVAAYSGESDSEEEQERGGPEREEKLTDWQKLACLLCRRQFPSKEALIRHQQLSGLHKQNLEIHRRAHLSENELEALEKNDMEQMKYRDRAAERREKYGIPEPPEPKRRKYGGISTASVDFEQPTRDGLGSDNIGSRMLQAMGWKEGSGLGRKKQGIVTPIEAQTRVRGSGLGARGSSYGVTSTESYKETLHKTMVTRFNEAQ
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
2Phosphorylation------MEYERRGGR
------CCCCCCCCC
56.9823090842
2Phosphorylation------MEYERRGGR
------CCCCCCCCC
56.9823090842
2 (in isoform 5)Acetylation-56.9821406692
2 (in isoform 5)Phosphorylation-56.9823663014
4Phosphorylation----MEYERRGGRGD
----CCCCCCCCCCC
23.6923090842
4Phosphorylation----MEYERRGGRGD
----CCCCCCCCCCC
23.6920068231
4 (in isoform 5)Phosphorylation-23.6928355574
6Phosphorylation--MEYERRGGRGDRT
--CCCCCCCCCCCCC
39.7222199227
6Phosphorylation--MEYERRGGRGDRT
--CCCCCCCCCCCCC
39.7222199227
6 (in isoform 5)Phosphorylation-39.7223663014
8PhosphorylationMEYERRGGRGDRTGR
CCCCCCCCCCCCCCC
28.6927251275
8 (in isoform 5)Phosphorylation-28.6927251275
15PhosphorylationGRGDRTGRYGATDRS
CCCCCCCCCCCCCCC
26.5427251275
15 (in isoform 5)Phosphorylation-26.5427251275
16PhosphorylationRGDRTGRYGATDRSQ
CCCCCCCCCCCCCCC
16.6822817900
19PhosphorylationRTGRYGATDRSQDDG
CCCCCCCCCCCCCCC
27.8129496963
22PhosphorylationRYGATDRSQDDGGEN
CCCCCCCCCCCCCCC
40.5525159151
25PhosphorylationATDRSQDDGGENRSR
CCCCCCCCCCCCCCC
60.40-
25PhosphorylationATDRSQDDGGENRSR
CCCCCCCCCCCCCCC
60.40-
25 (in isoform 5)Phosphorylation-60.4029978859
30PhosphorylationQDDGGENRSRDHDYR
CCCCCCCCCCCCCCC
28.8522199227
30PhosphorylationQDDGGENRSRDHDYR
CCCCCCCCCCCCCCC
28.8522199227
30 (in isoform 5)Phosphorylation-28.8521955146
31PhosphorylationDDGGENRSRDHDYRD
CCCCCCCCCCCCCCC
54.3522817900
36PhosphorylationNRSRDHDYRDMDYRS
CCCCCCCCCCCCCCC
12.7022817900
38PhosphorylationSRDHDYRDMDYRSYP
CCCCCCCCCCCCCCC
28.2420068231
38PhosphorylationSRDHDYRDMDYRSYP
CCCCCCCCCCCCCCC
28.2424719451
38 (in isoform 5)Phosphorylation-28.2420068231
39PhosphorylationRDHDYRDMDYRSYPR
CCCCCCCCCCCCCCH
3.4527251275
39 (in isoform 5)Phosphorylation-3.4528348404
40PhosphorylationDHDYRDMDYRSYPRE
CCCCCCCCCCCCCHH
39.7321857030
40PhosphorylationDHDYRDMDYRSYPRE
CCCCCCCCCCCCCHH
39.7321857030
40 (in isoform 5)Phosphorylation-39.7320068231
41PhosphorylationHDYRDMDYRSYPREY
CCCCCCCCCCCCHHH
8.5322817900
43PhosphorylationYRDMDYRSYPREYGS
CCCCCCCCCCHHHCC
33.0123090842
44PhosphorylationRDMDYRSYPREYGSQ
CCCCCCCCCHHHCCC
9.4130576142
48PhosphorylationYRSYPREYGSQEGKH
CCCCCHHHCCCCCCC
24.2925137130
48 (in isoform 3)Phosphorylation-24.2928450419
48 (in isoform 4)Phosphorylation-24.2928450419
50PhosphorylationSYPREYGSQEGKHDY
CCCHHHCCCCCCCCC
24.9417525332
50 (in isoform 3)Phosphorylation-24.9424719451
50 (in isoform 4)Phosphorylation-24.9424719451
57PhosphorylationSQEGKHDYDDSSEEQ
CCCCCCCCCCCCCHH
22.7523401153
57 (in isoform 3)Phosphorylation-22.7528450419
57 (in isoform 4)Phosphorylation-22.7528450419
57 (in isoform 5)Phosphorylation-22.7528176443
58PhosphorylationQEGKHDYDDSSEEQS
CCCCCCCCCCCCHHC
56.2124719451
58 (in isoform 5)Phosphorylation-56.2128176443
60PhosphorylationGKHDYDDSSEEQSAE
CCCCCCCCCCHHCHH
36.4317525332
60 (in isoform 3)Phosphorylation-36.4325849741
60 (in isoform 4)Phosphorylation-36.4325849741
61PhosphorylationKHDYDDSSEEQSAED
CCCCCCCCCHHCHHH
52.7423927012
61 (in isoform 3)Phosphorylation-52.7423663014
61 (in isoform 4)Phosphorylation-52.7423663014
63 (in isoform 5)Phosphorylation-52.3528102081
65PhosphorylationDDSSEEQSAEDSYEA
CCCCCHHCHHHHCCC
36.5823927012
65 (in isoform 3)Phosphorylation-36.5830108239
65 (in isoform 4)Phosphorylation-36.5830108239
68PhosphorylationSEEQSAEDSYEASPG
CCHHCHHHHCCCCCC
57.12-
68PhosphorylationSEEQSAEDSYEASPG
CCHHCHHHHCCCCCC
57.12-
68 (in isoform 5)Phosphorylation-57.12-
69PhosphorylationEEQSAEDSYEASPGS
CHHCHHHHCCCCCCC
19.1723927012
70PhosphorylationEQSAEDSYEASPGSE
HHCHHHHCCCCCCCH
28.0323927012
73PhosphorylationAEDSYEASPGSETQR
HHHHCCCCCCCHHHH
20.1823927012
76PhosphorylationSYEASPGSETQRRRR
HCCCCCCCHHHHHHH
40.6323927012
78PhosphorylationEASPGSETQRRRRRR
CCCCCCHHHHHHHHH
29.1330576142
87PhosphorylationRRRRRRHRHSPTGPP
HHHHHHHCCCCCCCC
30.1224719451
89PhosphorylationRRRRHRHSPTGPPGF
HHHHHCCCCCCCCCC
24.9029255136
91PhosphorylationRRHRHSPTGPPGFPR
HHHCCCCCCCCCCCC
66.3922167270
102PhosphorylationGFPRDGDYRDQDYRT
CCCCCCCCCCCCCCC
22.9427642862
107PhosphorylationGDYRDQDYRTEQGEE
CCCCCCCCCCCCCCH
17.5030576142
109PhosphorylationYRDQDYRTEQGEEEE
CCCCCCCCCCCCHHH
26.8230576142
125PhosphorylationEEDEEEEEKASNIVM
HCCHHHHHHHHHHHH
58.1427251275
126PhosphorylationEDEEEEEKASNIVML
CCHHHHHHHHHHHHE
61.4724719451
126SumoylationEDEEEEEKASNIVML
CCHHHHHHHHHHHHE
61.47-
128PhosphorylationEEEEEKASNIVMLRM
HHHHHHHHHHHHEEE
37.8530576142
130PhosphorylationEEEKASNIVMLRMLP
HHHHHHHHHHEEECC
1.4627251275
134MethylationASNIVMLRMLPQAAT
HHHHHHEEECCCCCC
13.39115490479
135PhosphorylationSNIVMLRMLPQAATE
HHHHHEEECCCCCCC
5.8827251275
135SulfoxidationSNIVMLRMLPQAATE
HHHHHEEECCCCCCC
5.8821406390
138PhosphorylationVMLRMLPQAATEDDI
HHEEECCCCCCCCHH
39.4027251275
141PhosphorylationRMLPQAATEDDIRGQ
EECCCCCCCCHHHHH
42.8530576142
146MethylationAATEDDIRGQLQSHG
CCCCCHHHHHHHHCC
33.52115490483
154PhosphorylationGQLQSHGVQAREVRL
HHHHHCCCCHHEEEE
3.1724719451
166PhosphorylationVRLMRNKSSGQSRGF
EEEECCCCCCCCCCE
43.16-
171MethylationNKSSGQSRGFAFVEF
CCCCCCCCCEEEEEE
36.04115490491
194PhosphorylationWMEANQHSLNILGQK
HHHHHHHHHHHHCCE
17.2225159151
203PhosphorylationNILGQKVSMHYSDPK
HHHCCEEECCCCCCC
13.5825599653
206PhosphorylationGQKVSMHYSDPKPKI
CCEEECCCCCCCCCC
13.2130631047
207PhosphorylationQKVSMHYSDPKPKIN
CEEECCCCCCCCCCC
32.5325159151
228AcetylationKCGVQNFKRREKCFK
HHCCCCHHHHHHHHH
59.0825953088
246SumoylationPKSEAEQKLPLGTRL
CHHHHHHHCCCCCCC
43.51-
246SumoylationPKSEAEQKLPLGTRL
CHHHHHHHCCCCCCC
43.51-
246UbiquitinationPKSEAEQKLPLGTRL
CHHHHHHHCCCCCCC
43.51-
257PhosphorylationGTRLDQQTLPLGGRE
CCCCCCCCCCCCCCC
25.3928555341
266PhosphorylationPLGGRELSQGLLPLP
CCCCCCHHCCCCCCC
19.9027251275
276PhosphorylationLLPLPQPYQAQGVLA
CCCCCCCCCHHHHHH
15.95-
288PhosphorylationVLASQALSQGSEPSS
HHHHHHHHCCCCCCC
35.2017525332
312PhosphorylationRNLNPHSTMDSILGA
ECCCCCCCHHHHHHH
23.20-
331PhosphorylationAVLSSSNVRVIKDKQ
HHHCCCCEEEECCCC
5.8127251275
3372-HydroxyisobutyrylationNVRVIKDKQTQLNRG
CEEEECCCCCHHHCC
50.68-
382AcetylationKTINVEFAKGSKRDM
EEEEEEECCCCHHHC
11.2019608861
383AcetylationTINVEFAKGSKRDMA
EEEEEECCCCHHHCC
69.8719608861
383MalonylationTINVEFAKGSKRDMA
EEEEEECCCCHHHCC
69.8726320211
383UbiquitinationTINVEFAKGSKRDMA
EEEEEECCCCHHHCC
69.8719608861
435PhosphorylationSEEPPVDYSYYQQDE
CCCCCCCCCEEECCC
9.98-
447PhosphorylationQDEGYGNSQGTESSL
CCCCCCCCCCCCCCH
26.14-
469PhosphorylationGTKGPGITGTKGDPT
CCCCCCCCCCCCCCC
44.72-
471PhosphorylationKGPGITGTKGDPTGA
CCCCCCCCCCCCCCC
24.17-
472AcetylationGPGITGTKGDPTGAG
CCCCCCCCCCCCCCC
63.7626051181
476PhosphorylationTGTKGDPTGAGPEAS
CCCCCCCCCCCCCCC
44.39-
483PhosphorylationTGAGPEASLEPGADS
CCCCCCCCCCCCCCC
31.4428555341
490PhosphorylationSLEPGADSVSMQAFS
CCCCCCCCCCHHHHH
18.6328555341
492PhosphorylationEPGADSVSMQAFSRA
CCCCCCCCHHHHHHC
14.7728555341
497PhosphorylationSVSMQAFSRAQPGAA
CCCHHHHHHCCCCCC
29.71-
515PhosphorylationYQQSAEASSSQGTAA
CCCCCHHHCCCCCCC
23.2528348404
516PhosphorylationQQSAEASSSQGTAAN
CCCCHHHCCCCCCCC
33.4627251275
517PhosphorylationQSAEASSSQGTAANS
CCCHHHCCCCCCCCC
30.0817525332
520PhosphorylationEASSSQGTAANSQSY
HHHCCCCCCCCCCCE
18.2427251275
524PhosphorylationSQGTAANSQSYTIMS
CCCCCCCCCCEEEEC
18.7722199227
526PhosphorylationGTAANSQSYTIMSPA
CCCCCCCCEEEECHH
24.8630576142
527PhosphorylationTAANSQSYTIMSPAV
CCCCCCCEEEECHHH
7.8328634298
528PhosphorylationAANSQSYTIMSPAVL
CCCCCCEEEECHHHH
18.5622199227
531PhosphorylationSQSYTIMSPAVLKSE
CCCEEEECHHHHHHH
13.0729496963
536SumoylationIMSPAVLKSELQSPT
EECHHHHHHHHCCCC
34.97-
537PhosphorylationMSPAVLKSELQSPTH
ECHHHHHHHHCCCCC
39.1026074081
541PhosphorylationVLKSELQSPTHPSSA
HHHHHHCCCCCCHHC
44.3726074081
543PhosphorylationKSELQSPTHPSSALP
HHHHCCCCCCHHCCC
52.2226074081
546PhosphorylationLQSPTHPSSALPPAT
HCCCCCCHHCCCCCC
22.1926074081
547PhosphorylationQSPTHPSSALPPATS
CCCCCCHHCCCCCCC
37.9726074081
553PhosphorylationSSALPPATSPTAQES
HHCCCCCCCCCCCHH
40.8026074081
554PhosphorylationSALPPATSPTAQESY
HCCCCCCCCCCCHHH
23.5126074081
556PhosphorylationLPPATSPTAQESYSQ
CCCCCCCCCCHHHCC
40.5125137130
560PhosphorylationTSPTAQESYSQYPVP
CCCCCCHHHCCCCCC
20.2926074081
561PhosphorylationSPTAQESYSQYPVPD
CCCCCHHHCCCCCCC
10.0726074081
596PhosphorylationYYDPNSQYYYNAQSQ
EECCCCCEEEEEECC
14.0327251275
622PhosphorylationYVPALEQSADGHKET
CCCCEECCCCCCCCC
20.9625159151
629PhosphorylationSADGHKETGAPSKEG
CCCCCCCCCCCCCCC
43.3728555341
633PhosphorylationHKETGAPSKEGKEKK
CCCCCCCCCCCHHHH
42.69-
647PhosphorylationKEKHKTKTAQQIAKD
HHHHHHHHHHHHHHH
34.6221601212
653AcetylationKTAQQIAKDMERWAR
HHHHHHHHHHHHHHH
60.2722990431
661PhosphorylationDMERWARSLNKQKEN
HHHHHHHHHHHHHHH
28.6618669648
672PhosphorylationQKENFKNSFQPISSL
HHHHHHHCCCCHHHC
26.3321406692
677PhosphorylationKNSFQPISSLRDDER
HHCCCCHHHCCCHHH
29.9728258704
678PhosphorylationNSFQPISSLRDDERR
HCCCCHHHCCCHHHH
28.3025954137
687PhosphorylationRDDERRESATADAGY
CCHHHHHHHHHHHHH
29.1620873877
689PhosphorylationDERRESATADAGYAI
HHHHHHHHHHHHHHH
34.0629978859
694PhosphorylationSATADAGYAILEKKG
HHHHHHHHHHHHHHC
7.6828796482
709PhosphorylationALAERQHTSMDLPKL
HHHHCCCCCCCHHHH
19.8728450419
710PhosphorylationLAERQHTSMDLPKLA
HHHCCCCCCCHHHHC
14.2628450419
718PhosphorylationMDLPKLASDDRPSPP
CCHHHHCCCCCCCCC
50.9429255136
722PhosphorylationKLASDDRPSPPRGLV
HHCCCCCCCCCCCEE
59.1717287340
723O-linked_GlycosylationLASDDRPSPPRGLVA
HCCCCCCCCCCCEEE
48.7230379171
723PhosphorylationLASDDRPSPPRGLVA
HCCCCCCCCCCCEEE
48.7229255136
732PhosphorylationPRGLVAAYSGESDSE
CCCEEEEECCCCCCH
13.8929255136
733PhosphorylationRGLVAAYSGESDSEE
CCEEEEECCCCCCHH
31.2129255136
735PhosphorylationLVAAYSGESDSEEEQ
EEEEECCCCCCHHHH
45.4915302935
736PhosphorylationVAAYSGESDSEEEQE
EEEECCCCCCHHHHH
50.3829255136
737PhosphorylationAAYSGESDSEEEQER
EEECCCCCCHHHHHH
56.6215302935
738PhosphorylationAYSGESDSEEEQERG
EECCCCCCHHHHHHC
57.0729255136
754PhosphorylationPEREEKLTDWQKLAC
CHHHHHHCHHHHHHH
46.3824719451
758AcetylationEKLTDWQKLACLLCR
HHHCHHHHHHHHHHH
33.5226051181
771AcetylationCRRQFPSKEALIRHQ
HHCCCCCHHHHHHHH
47.4426051181
774PhosphorylationQFPSKEALIRHQQLS
CCCCHHHHHHHHHHH
3.5724719451
781PhosphorylationLIRHQQLSGLHKQNL
HHHHHHHHHHHHHCH
34.6620068231
788PhosphorylationSGLHKQNLEIHRRAH
HHHHHHCHHHHHHHC
6.4024719451
797PhosphorylationIHRRAHLSENELEAL
HHHHHCCCHHHHHHH
28.6329255136
798PhosphorylationHRRAHLSENELEALE
HHHHCCCHHHHHHHH
62.1724719451
801PhosphorylationAHLSENELEALEKND
HCCCHHHHHHHHHCC
7.6124719451
803PhosphorylationLSENELEALEKNDME
CCHHHHHHHHHCCHH
33.3824719451
825PhosphorylationAAERREKYGIPEPPE
HHHHHHHHCCCCCCC
18.6117192257
838PhosphorylationPEPKRRKYGGISTAS
CCCCCCCCCCCCCCE
20.8320873877
842PhosphorylationRRKYGGISTASVDFE
CCCCCCCCCCEECCC
22.6120873877
843PhosphorylationRKYGGISTASVDFEQ
CCCCCCCCCEECCCC
22.4920873877
845PhosphorylationYGGISTASVDFEQPT
CCCCCCCEECCCCCC
23.4721712546
852PhosphorylationSVDFEQPTRDGLGSD
EECCCCCCCCCCCCC
40.8826074081
858PhosphorylationPTRDGLGSDNIGSRM
CCCCCCCCCCHHHHH
32.3120873877
862PhosphorylationGLGSDNIGSRMLQAM
CCCCCCHHHHHHHHH
18.5624719451
872AcetylationMLQAMGWKEGSGLGR
HHHHHCCCCCCCCCC
46.6026051181
881SumoylationGSGLGRKKQGIVTPI
CCCCCCCCCCEECCC
53.01-
881MethylationGSGLGRKKQGIVTPI
CCCCCCCCCCEECCC
53.0124129315
881SumoylationGSGLGRKKQGIVTPI
CCCCCCCCCCEECCC
53.01-
881UbiquitinationGSGLGRKKQGIVTPI
CCCCCCCCCCEECCC
53.01-
886PhosphorylationRKKQGIVTPIEAQTR
CCCCCEECCCEEECC
19.3420068231
892PhosphorylationVTPIEAQTRVRGSGL
ECCCEEECCCCCCCC
37.8720068231
895MethylationIEAQTRVRGSGLGAR
CEEECCCCCCCCCCC
30.2154558535
897PhosphorylationAQTRVRGSGLGARGS
EECCCCCCCCCCCCC
21.9328555341
902MethylationRGSGLGARGSSYGVT
CCCCCCCCCCCCCCC
43.6724129315
904PhosphorylationSGLGARGSSYGVTST
CCCCCCCCCCCCCCC
18.1623401153
905PhosphorylationGLGARGSSYGVTSTE
CCCCCCCCCCCCCCH
28.8225159151
906PhosphorylationLGARGSSYGVTSTES
CCCCCCCCCCCCCHH
19.8128555341
908PhosphorylationARGSSYGVTSTESYK
CCCCCCCCCCCHHHH
2.6527251275
909PhosphorylationRGSSYGVTSTESYKE
CCCCCCCCCCHHHHH
26.1026714015
910PhosphorylationGSSYGVTSTESYKET
CCCCCCCCCHHHHHH
27.9824719451
911O-linked_GlycosylationSSYGVTSTESYKETL
CCCCCCCCHHHHHHH
21.4230379171
911PhosphorylationSSYGVTSTESYKETL
CCCCCCCCHHHHHHH
21.4228555341
913PhosphorylationYGVTSTESYKETLHK
CCCCCCHHHHHHHHH
41.4129507054
915AcetylationVTSTESYKETLHKTM
CCCCHHHHHHHHHHH
54.2026051181
917PhosphorylationSTESYKETLHKTMVT
CCHHHHHHHHHHHHH
29.9728152594
920AcetylationSYKETLHKTMVTRFN
HHHHHHHHHHHHHHH
41.2425953088
921PhosphorylationYKETLHKTMVTRFNE
HHHHHHHHHHHHHHH
13.2128152594
924PhosphorylationTLHKTMVTRFNEAQ-
HHHHHHHHHHHHCC-
20.7928152594
951Phosphorylation----------------------------
----------------------------
27251275
969Phosphorylation----------------------------------------------
----------------------------------------------
27251275

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 RBM10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM10_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 RBM10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTBP2_HUMANPTBP2physical
16189514
F124A_HUMANFAM124Aphysical
16189514
RU1C_HUMANSNRPCphysical
22365833
SF3A1_HUMANSF3A1physical
22365833
SF3B4_HUMANSF3B4physical
22365833
DHX15_HUMANDHX15physical
22365833
U2AF2_HUMANU2AF2physical
22365833
U2AF1_HUMANU2AF1physical
22365833
SR140_HUMANU2SURPphysical
22365833
CCAR1_HUMANCCAR1physical
22365833
RBM10_HUMANRBM10physical
22365833
SF01_HUMANSF1physical
22365833
SUGP1_HUMANSUGP1physical
22365833
SRSF6_HUMANSRSF6physical
22365833
PRP19_HUMANPRPF19physical
22365833
PRCC_HUMANPRCCphysical
22365833
RED_HUMANIKphysical
22365833
PRP16_HUMANDHX38physical
22365833
DDX5_HUMANDDX5physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
RBM4_HUMANRBM4physical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
GPKOW_HUMANGPKOWphysical
22365833
PTBP1_HUMANPTBP1physical
22365833
PTBP2_HUMANPTBP2physical
22365833
TB22B_HUMANTBC1D22Bphysical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
311900TARP syndrome (TARPS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBM10_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-383, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-60; SER-61; SER-65;SER-723; SER-733; SER-736; SER-738 AND SER-797, 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-723; SER-733; SER-736AND SER-738, 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-723, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-60 AND SER-288,AND MASS SPECTROMETRY.
"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-723, AND MASSSPECTROMETRY.
"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-89; SER-733; SER-736;SER-738 AND SER-797, 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-733; SER-736 ANDSER-738, 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 THR-91; SER-733; SER-736;SER-738 AND SER-797, AND MASS 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-736 AND SER-738, ANDMASS SPECTROMETRY.

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