RBM10_MOUSE - dbPTM
RBM10_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM10_MOUSE
UniProt AC Q99KG3
Protein Name RNA-binding protein 10 {ECO:0000305}
Gene Name Rbm10 {ECO:0000312|MGI:MGI:2384310}
Organism Mus musculus (Mouse).
Sequence Length 930
Subcellular Localization Nucleus.
Protein Description Not known. 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 (By similarity)..
Protein Sequence MEYERRGGRGDRTGRYGATDRSQDDSGENRSRDHDYRDMDYRSYPREYGSQEGKHEYDDSSEEQSAEDSYEASPGSETQRRRRRRHRHSPTGPPGFPRDGDYRDQDYRTEQGEEEEEEDEEEEEEKASNIVMLRMLPQAATEDDIRGQLQSHGVQAREVRLMRNKSSGQSRGFAFVEFSHLQDATRWMEANQHSLNILGQKVSMHYSDPKPKINEDWLCNKCGVQNFKRREKCFKCGVPKSEAEQKLPLGTRLDQQALPLGGRELSQGLLPLPQPYQAQGVLTSQALSQGSEPSSENANDTIILRNLNPHSTMDSILGALAPYAVLSSSNVRVIKDKQTQLNRGFAFIQLSTIVEAAQLLQILQALHPPLTIDGKTINVEFAKGSKRDMASNEGSRINAASVASTAIAAAQWAISQASQGGESAWAAPEEPPVDYSYYQQDEGYGSSQGTDSLYAHGYLKNSKGPGMTGTKGDPAGTGPEASLEAGADSVSLQAFSRAQPGAAPGLYQQSAEGSSGQSTATNSQSYTIISPAVLKAELQSPTQPSSSAFPPATSPTAPEAYSQYPVPDVSTYQYDETSGYYYDPQTGLYYDPNSQYYYNAQSQQYLYWDGERRTYIPALEQSADGHKDTGASSKEGKEKKEKHKTKTAQQIAKDMERWARSLNKQKENFKNSFQPISALRDDERRESATADAGYAILEKKGALAERQHTSMDLPKLASDDRPSPPRGLVAAYSGESDSEEEQERGGPEREEKLTDWQKLACLLCRRQFPSKEALIRHQQLSGLHKQNLEIHRRAHLSENELEALEKNDMEQMKYRDRAAERREKYGIPEPPEPKRRKYGGISTASVDFEQPTRDGLGSDNIGSRMLQAMGWKEGSGLGRKKQGIVTPIEAQTRVRGSGLGARGSSYGVTSTESYKETLHKTMVTRFNEAQ
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
22PhosphorylationRYGATDRSQDDSGEN
CCCCCCCCCCCCCCC		40.5529899451
48 (in isoform 2)Phosphorylation-24.2925777480
48PhosphorylationYRSYPREYGSQEGKH
CCCCCHHHCCCCCCC		24.2929899451
50PhosphorylationSYPREYGSQEGKHEY
CCCHHHCCCCCCCCC		24.9423684622
50 (in isoform 2)Phosphorylation-24.9423684622
54AcetylationEYGSQEGKHEYDDSS
HHCCCCCCCCCCCCC		32.2922826441
54 (in isoform 2)Acetylation-32.29-
57 (in isoform 2)Phosphorylation-25.4425777480
57PhosphorylationSQEGKHEYDDSSEEQ
CCCCCCCCCCCCCHH		25.4429899451
60PhosphorylationGKHEYDDSSEEQSAE
CCCCCCCCCCHHCHH		36.4321149613
60 (in isoform 2)Phosphorylation-36.4323684622
61 (in isoform 2)Phosphorylation-52.7423684622
61PhosphorylationKHEYDDSSEEQSAED
CCCCCCCCCHHCHHH		52.7421149613
65 (in isoform 2)Phosphorylation-36.5825777480
65PhosphorylationDDSSEEQSAEDSYEA
CCCCCHHCHHHHCCC		36.5829899451
69PhosphorylationEEQSAEDSYEASPGS
CHHCHHHHCCCCCCC		19.1721149613
70PhosphorylationEQSAEDSYEASPGSE
HHCHHHHCCCCCCCH		28.0321149613
73PhosphorylationAEDSYEASPGSETQR
HHHHCCCCCCCHHHH		20.1825338131
89PhosphorylationRRRRHRHSPTGPPGF
HHHHHCCCCCCCCCC		24.9026824392
91PhosphorylationRRHRHSPTGPPGFPR
HHHCCCCCCCCCCCC		66.3923684622
228SuccinylationKCGVQNFKRREKCFK
HHCCCCHHHHHHHHH		59.0824315375
383AcetylationTINVEFAKGSKRDMA
EEEEEECCCCHHHCC		69.87-
515PhosphorylationQQSAEGSSGQSTATN
ECCCCCCCCCCCCCC		52.2726745281
518PhosphorylationAEGSSGQSTATNSQS
CCCCCCCCCCCCCCC		24.4326745281
519PhosphorylationEGSSGQSTATNSQSY
CCCCCCCCCCCCCCE		29.6126745281
521PhosphorylationSSGQSTATNSQSYTI
CCCCCCCCCCCCEEE		35.1826745281
523PhosphorylationGQSTATNSQSYTIIS
CCCCCCCCCCEEEEC		19.0226745281
525PhosphorylationSTATNSQSYTIISPA
CCCCCCCCEEEECHH		24.8626745281
526PhosphorylationTATNSQSYTIISPAV
CCCCCCCEEEECHHH		8.3626745281
527PhosphorylationATNSQSYTIISPAVL
CCCCCCEEEECHHHH		19.6526745281
530PhosphorylationSQSYTIISPAVLKAE
CCCEEEECHHHHHHH		11.7129514104
646AcetylationKKEKHKTKTAQQIAK
HHHHHHHHHHHHHHH		46.826569005
653AcetylationKTAQQIAKDMERWAR
HHHHHHHHHHHHHHH		60.2722636265
661PhosphorylationDMERWARSLNKQKEN
HHHHHHHHHHHHHHH		28.6615345747
687PhosphorylationRDDERRESATADAGY
CCHHHHHHHHHHHHH		29.1628833060
689PhosphorylationDERRESATADAGYAI
HHHHHHHHHHHHHHH		34.0628833060
709PhosphorylationALAERQHTSMDLPKL
HHHHCCCCCCCHHHH		19.8726643407
710PhosphorylationLAERQHTSMDLPKLA
HHHCCCCCCCHHHHC		14.2626643407
718PhosphorylationMDLPKLASDDRPSPP
CCHHHHCCCCCCCCC		50.9424925903
723PhosphorylationLASDDRPSPPRGLVA
HCCCCCCCCCCCEEE		48.7224925903
732PhosphorylationPRGLVAAYSGESDSE
CCCEEEEECCCCCCH		13.8924925903
733PhosphorylationRGLVAAYSGESDSEE
CCEEEEECCCCCCHH		31.2125521595
736PhosphorylationVAAYSGESDSEEEQE
EEEECCCCCCHHHHH		50.3827087446
738PhosphorylationAYSGESDSEEEQERG
EECCCCCCHHHHHHC		57.0724925903
781PhosphorylationLIRHQQLSGLHKQNL
HHHHHHHHHHHHHCH		34.6627841257
797PhosphorylationIHRRAHLSENELEAL
HHHHHCCCHHHHHHH		28.6325521595
838PhosphorylationPEPKRRKYGGISTAS
CCCCCCCCCCCCCCE		20.8326643407
842PhosphorylationRRKYGGISTASVDFE
CCCCCCCCCCEECCC		22.6126643407
843PhosphorylationRKYGGISTASVDFEQ
CCCCCCCCCEECCCC		22.4926643407
845PhosphorylationYGGISTASVDFEQPT
CCCCCCCEECCCCCC		23.4726239621
872AcetylationMLQAMGWKEGSGLGR
HHHHHCCCCCCCCCC		46.6022826441
897PhosphorylationAQTRVRGSGLGARGS
EECCCCCCCCCCCCC		21.9329514104
902MethylationRGSGLGARGSSYGVT
CCCCCCCCCCCCCCC		43.6724129315
904PhosphorylationSGLGARGSSYGVTST
CCCCCCCCCCCCCCC		18.1627149854
905PhosphorylationGLGARGSSYGVTSTE
CCCCCCCCCCCCCCH		28.8227149854
906PhosphorylationLGARGSSYGVTSTES
CCCCCCCCCCCCCHH		19.8127149854
909PhosphorylationRGSSYGVTSTESYKE
CCCCCCCCCCHHHHH		26.1027149854
910PhosphorylationGSSYGVTSTESYKET
CCCCCCCCCHHHHHH		27.9827149854
911PhosphorylationSSYGVTSTESYKETL
CCCCCCCCHHHHHHH		21.4227149854
913PhosphorylationYGVTSTESYKETLHK
CCCCCCHHHHHHHHH		41.4127149854
914PhosphorylationGVTSTESYKETLHKT
CCCCCHHHHHHHHHH		13.4527149854
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM10_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RBM10_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBM10_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736 ANDSER-738, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, ANDMASS SPECTROMETRY.

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