RBMX2_HUMAN - dbPTM
RBMX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBMX2_HUMAN
UniProt AC Q9Y388
Protein Name RNA-binding motif protein, X-linked 2
Gene Name RBMX2
Organism Homo sapiens (Human).
Sequence Length 322
Subcellular Localization
Protein Description
Protein Sequence MNPLTKVKLINELNEREVQLGVADKVSWHSEYKDSAWIFLGGLPYELTEGDIICVFSQYGEIVNINLVRDKKTGKSKGFCFLCYEDQRSTILAVDNFNGIKIKGRTIRVDHVSNYRAPKDSEEIDDVTRQLQEKGCGARTPSPSLSESSEDEKPTKKHKKDKKEKKKKKKEKEKADREVQAEQPSSSSPRRKTVKEKDDTGPKKHSSKNSERAQKSEPREGQKLPKSRTAYSGGAEDLERELKKEKPKHEHKSSSRREAREEKTRIRDRGRSSDAHSSWYNGRSEGRSYRSRSRSRDKSHRHKRARRSRERESSNPSDRWRH
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
8AcetylationMNPLTKVKLINELNE
CCHHHHHHHHHHHCH		45.2525953088
8SumoylationMNPLTKVKLINELNE
CCHHHHHHHHHHHCH		45.2528112733
8UbiquitinationMNPLTKVKLINELNE
CCHHHHHHHHHHHCH		45.2529967540
8SumoylationMNPLTKVKLINELNE
CCHHHHHHHHHHHCH		45.25-
77AcetylationDKKTGKSKGFCFLCY
ECCCCCCCCEEEEEE		60.5426051181
115PhosphorylationRVDHVSNYRAPKDSE
EEEECCCCCCCCCHH		10.7229214152
119UbiquitinationVSNYRAPKDSEEIDD
CCCCCCCCCHHHHHH		73.2724816145
121PhosphorylationNYRAPKDSEEIDDVT
CCCCCCCHHHHHHHH		43.1630108239
134UbiquitinationVTRQLQEKGCGARTP
HHHHHHHCCCCCCCC		46.6829967540
140PhosphorylationEKGCGARTPSPSLSE
HCCCCCCCCCCCCCC		27.8126552605
142PhosphorylationGCGARTPSPSLSESS
CCCCCCCCCCCCCCC		26.8920873877
144PhosphorylationGARTPSPSLSESSED
CCCCCCCCCCCCCCC		49.1920873877
146PhosphorylationRTPSPSLSESSEDEK
CCCCCCCCCCCCCCC		39.5120363803
148PhosphorylationPSPSLSESSEDEKPT
CCCCCCCCCCCCCCC		35.3320363803
149PhosphorylationSPSLSESSEDEKPTK
CCCCCCCCCCCCCCH		45.0420363803
155PhosphorylationSSEDEKPTKKHKKDK
CCCCCCCCHHHHHHH		64.8920873877
185PhosphorylationEVQAEQPSSSSPRRK
HHHHHCCCCCCCCCC		42.4129255136
186PhosphorylationVQAEQPSSSSPRRKT
HHHHCCCCCCCCCCC		41.3329255136
187PhosphorylationQAEQPSSSSPRRKTV
HHHCCCCCCCCCCCC		49.0129255136
188PhosphorylationAEQPSSSSPRRKTVK
HHCCCCCCCCCCCCC		25.1119664994
193PhosphorylationSSSPRRKTVKEKDDT
CCCCCCCCCCCCCCC		34.6926074081
210PhosphorylationKKHSSKNSERAQKSE
CCCCCCCCHHHHHCC		32.0026074081
216PhosphorylationNSERAQKSEPREGQK
CCHHHHHCCCCCCCC		40.5330576142
223UbiquitinationSEPREGQKLPKSRTA
CCCCCCCCCCCCCCC		77.0724816145
229PhosphorylationQKLPKSRTAYSGGAE
CCCCCCCCCCCCCHH		36.7228152594
231PhosphorylationLPKSRTAYSGGAEDL
CCCCCCCCCCCHHHH		13.7730001349
232PhosphorylationPKSRTAYSGGAEDLE
CCCCCCCCCCHHHHH		28.4325159151
243SumoylationEDLERELKKEKPKHE
HHHHHHHHHHCCCCC		54.8828112733
272PhosphorylationRIRDRGRSSDAHSSW
HHHHCCCCCCCCCCC		35.0823401153
273PhosphorylationIRDRGRSSDAHSSWY
HHHCCCCCCCCCCCC		37.1423927012
277PhosphorylationGRSSDAHSSWYNGRS
CCCCCCCCCCCCCCC		25.0423403867
278PhosphorylationRSSDAHSSWYNGRSE
CCCCCCCCCCCCCCC		24.5823403867
280PhosphorylationSDAHSSWYNGRSEGR
CCCCCCCCCCCCCCC		15.08-
284PhosphorylationSSWYNGRSEGRSYRS
CCCCCCCCCCCCHHC		45.8922210691
293PhosphorylationGRSYRSRSRSRDKSH
CCCHHCCCCCCCHHH		35.5420068231
295PhosphorylationSYRSRSRSRDKSHRH
CHHCCCCCCCHHHHH		46.1820068231
308PhosphorylationRHKRARRSRERESSN
HHHHHHHHHHHHHCC		32.7030576142
313PhosphorylationRRSRERESSNPSDRW
HHHHHHHHCCCCCCC		41.4523927012
314PhosphorylationRSRERESSNPSDRWR
HHHHHHHCCCCCCCC		48.2725159151
317PhosphorylationERESSNPSDRWRH--
HHHHCCCCCCCCC--		44.0223403867
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 RBMX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBMX2_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 RBMX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PR40A_HUMANPRPF40Aphysical
22365833
BUD13_HUMANBUD13physical
22365833
DHX8_HUMANDHX8physical
22365833
NKAP_HUMANNKAPphysical
22365833
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 RBMX2_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-188, AND MASSSPECTROMETRY.
"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-185 AND SER-188, ANDMASS SPECTROMETRY.
"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-186 AND SER-188, ANDMASS 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-188, AND MASSSPECTROMETRY.
"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-188, 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-188, AND MASSSPECTROMETRY.
"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-188, AND MASSSPECTROMETRY.

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