RBMX_RAT - dbPTM
RBMX_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBMX_RAT
UniProt AC Q4V898
Protein Name RNA-binding motif protein, X chromosome
Gene Name Rbmx
Organism Rattus norvegicus (Rat).
Sequence Length 390
Subcellular Localization Nucleus. Component of ribonucleosomes (By similarity). Localizes in numerous small granules in the nucleus..
Protein Description RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment..
Protein Sequence MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGLPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFTLSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDGYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRERDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYTSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGRSRY
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
1Acetylation-------MVEADRPG
-------CCCCCCCC		5.77-
2Acetylation------MVEADRPGK
------CCCCCCCCC		9.26-
9AcetylationVEADRPGKLFIGGLN
CCCCCCCCEEECCCC		42.7972597475
22UbiquitinationLNTETNEKALEAVFG
CCCCCCHHHHHHHHH		61.41-
30AcetylationALEAVFGKYGRIVEV
HHHHHHHHHHHHHEE		32.8225447713
55PhosphorylationSRGFAFVTFESPADA
CCCEEEEEECCCCHH		18.4128689409
58PhosphorylationFAFVTFESPADAKDA
EEEEEECCCCHHHHH		22.6127097102
63AcetylationFESPADAKDAARDMN
ECCCCHHHHHHHHHC		48.7422902405
80AcetylationSLDGKAIKVEQATKP
CCCCCEEEEEECCCC		44.5872593265
85PhosphorylationAIKVEQATKPSFESG
EEEEEECCCCCCCCC		43.0927097102
86AcetylationIKVEQATKPSFESGR
EEEEECCCCCCCCCC		41.5072596129
88PhosphorylationVEQATKPSFESGRRG
EEECCCCCCCCCCCC		43.1127097102
91PhosphorylationATKPSFESGRRGLPP
CCCCCCCCCCCCCCC		35.2727097102
116PhosphorylationLRGGRGGSGGTRGPP
CCCCCCCCCCCCCCC		36.5525532521
125Asymmetric dimethylarginineGTRGPPSRGGHMDDG
CCCCCCCCCCCCCCC		61.97-
125MethylationGTRGPPSRGGHMDDG
CCCCCCCCCCCCCCC		61.9725447705
144MethylationNFTLSSSRGPLPVKR
EEEEECCCCCCCCCC		53.34-
150AcetylationSRGPLPVKRGPPPRS
CCCCCCCCCCCCCCC		50.0925447703
157PhosphorylationKRGPPPRSGGPPPKR
CCCCCCCCCCCCCCC		54.6025575281
164MethylationSGGPPPKRSAPSGPV
CCCCCCCCCCCCCCC		43.7725447711
165PhosphorylationGGPPPKRSAPSGPVR
CCCCCCCCCCCCCCC		51.1316396499
172MethylationSAPSGPVRSSSGMGG
CCCCCCCCCCCCCCC		33.6725447683
174PhosphorylationPSGPVRSSSGMGGRA
CCCCCCCCCCCCCCC		21.98-
185MethylationGGRAPVSRGRDGYGG
CCCCCCCCCCCCCCC		44.38-
206PhosphorylationLPSRRDVYLSPRDDG
CCCCCCCEECCCCCC		13.0225403869
208PhosphorylationSRRDVYLSPRDDGYS
CCCCCEECCCCCCCC		10.5323712012
214PhosphorylationLSPRDDGYSTKDSYS
ECCCCCCCCCCCCCC		21.8423984901
215PhosphorylationSPRDDGYSTKDSYSS
CCCCCCCCCCCCCCC		34.2125403869
216PhosphorylationPRDDGYSTKDSYSSR
CCCCCCCCCCCCCCC		30.3225403869
219PhosphorylationDGYSTKDSYSSRDYP
CCCCCCCCCCCCCCC		28.5928432305
220PhosphorylationGYSTKDSYSSRDYPS
CCCCCCCCCCCCCCC		22.3127097102
221PhosphorylationYSTKDSYSSRDYPSS
CCCCCCCCCCCCCCC		23.8928432305
222PhosphorylationSTKDSYSSRDYPSSR
CCCCCCCCCCCCCCC		22.4227097102
225PhosphorylationDSYSSRDYPSSRDTR
CCCCCCCCCCCCCCC		12.1427097102
227PhosphorylationYSSRDYPSSRDTRDY
CCCCCCCCCCCCCCC		31.6028432305
228PhosphorylationSSRDYPSSRDTRDYA
CCCCCCCCCCCCCCC		29.6628432305
231PhosphorylationDYPSSRDTRDYAPPP
CCCCCCCCCCCCCCC		25.0828432305
246PhosphorylationRDYTYRDYGHSSSRD
CCCCCCCCCCCCCCC		14.0327097102
249PhosphorylationTYRDYGHSSSRDDYP
CCCCCCCCCCCCCCC		26.1627097102
250PhosphorylationYRDYGHSSSRDDYPS
CCCCCCCCCCCCCCC		24.5827097102
251PhosphorylationRDYGHSSSRDDYPSR
CCCCCCCCCCCCCCC		42.6227097102
255PhosphorylationHSSSRDDYPSRGYSD
CCCCCCCCCCCCCCC		13.8527097102
257PhosphorylationSSRDDYPSRGYSDRD
CCCCCCCCCCCCCCC		31.9127097102
261PhosphorylationDYPSRGYSDRDGYGR
CCCCCCCCCCCCCCC		29.0628432305
277PhosphorylationRDYSDHPSGGSYRDS
CCCCCCCCCCCCCCC		52.9827097102
280PhosphorylationSDHPSGGSYRDSYES
CCCCCCCCCCCCHHH		22.1127097102
287PhosphorylationSYRDSYESYGNSRSA
CCCCCHHHCCCCCCC		30.0627097102
303PhosphorylationPTRGPPPSYGGSSRY
CCCCCCCCCCCCCCC		42.0327097102
307PhosphorylationPPPSYGGSSRYDDYS
CCCCCCCCCCCCCCC		13.7927097102
308PhosphorylationPPSYGGSSRYDDYSS
CCCCCCCCCCCCCCC		37.8327097102
313PhosphorylationGSSRYDDYSSSRDGY
CCCCCCCCCCCCCCC		13.9327097102
314PhosphorylationSSRYDDYSSSRDGYG
CCCCCCCCCCCCCCC		28.9123984901
315PhosphorylationSRYDDYSSSRDGYGG
CCCCCCCCCCCCCCC		24.1423984901
316PhosphorylationRYDDYSSSRDGYGGS
CCCCCCCCCCCCCCC		28.5723984901
323PhosphorylationSRDGYGGSRDSYTSS
CCCCCCCCCCCCCCC		28.6628432305
326PhosphorylationGYGGSRDSYTSSRSD
CCCCCCCCCCCCHHH		29.2427097102
327PhosphorylationYGGSRDSYTSSRSDL
CCCCCCCCCCCHHHH		18.2227097102
328PhosphorylationGGSRDSYTSSRSDLY
CCCCCCCCCCHHHHH		24.9528432305
329PhosphorylationGSRDSYTSSRSDLYS
CCCCCCCCCHHHHHH		18.6028432305
330PhosphorylationSRDSYTSSRSDLYSS
CCCCCCCCHHHHHHC		28.1828432305
332PhosphorylationDSYTSSRSDLYSSGR
CCCCCCHHHHHHCCC		33.6428432305
335PhosphorylationTSSRSDLYSSGRDRV
CCCHHHHHHCCCCCC		13.0428432305
336PhosphorylationSSRSDLYSSGRDRVG
CCHHHHHHCCCCCCC		33.3528432305
337PhosphorylationSRSDLYSSGRDRVGR
CHHHHHHCCCCCCCC		25.0430181290
352PhosphorylationQERGLPPSMERGYPP
CCCCCCCHHHCCCCC		31.1929779826
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 RBMX_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
182RMethylation

-
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 RBMX_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-208, ANDMASS SPECTROMETRY.

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