ROA3_MOUSE - dbPTM
ROA3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROA3_MOUSE
UniProt AC Q8BG05
Protein Name Heterogeneous nuclear ribonucleoprotein A3
Gene Name Hnrnpa3
Organism Mus musculus (Mouse).
Sequence Length 379
Subcellular Localization Nucleus. Component of ribonucleosomes..
Protein Description Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing (By similarity)..
Protein Sequence MEVKPPPGRPQPDSGRRRRRRGEEGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEKWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMCARPHKVDGRVVEPKRAVSREDSVKPGAHLTVKKIFVGGIKEDTEEYNLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQSAGSQRGRGGGSGNFMGRGGNFGGGGGNFGRGGNFGGRGGYGGGGGGSRGSYGGGDGGYNGFGGDGGNYGGGPGYSSRGGYGGGGPGYGNQGGGYGGGGGGYDGYNEGGNFGGGNYGGGGNYNDFGNYSGQQQSNYGPMKGGSFGGRSSGSPYGGGYGSGGGSGGYGSRRF
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-------MEVKPPPG
-------CCCCCCCC		13.91-
4Acetylation----MEVKPPPGRPQ
----CCCCCCCCCCC		38.2022733758
14PhosphorylationPGRPQPDSGRRRRRR
CCCCCCCCCHHHHHC		40.6625338131
29UbiquitinationGEEGHDPKEPEQLRK
CCCCCCCCCHHHHHH		86.22-
43PhosphorylationKLFIGGLSFETTDDS
HHHHCCCCCCCCCHH		25.0624925903
46PhosphorylationIGGLSFETTDDSLRE
HCCCCCCCCCHHHHH		33.2524925903
47PhosphorylationGGLSFETTDDSLREH
CCCCCCCCCHHHHHH		30.5223984901
50PhosphorylationSFETTDDSLREHFEK
CCCCCCHHHHHHHHH		31.9424759943
52MethylationETTDDSLREHFEKWG
CCCCHHHHHHHHHHC		39.02-
57MalonylationSLREHFEKWGTLTDC
HHHHHHHHHCCCEEE		50.4026320211
57UbiquitinationSLREHFEKWGTLTDC
HHHHHHHHHCCCEEE		50.40-
57AcetylationSLREHFEKWGTLTDC
HHHHHHHHHCCCEEE		50.4022826441
64S-palmitoylationKWGTLTDCVVMRDPQ
HHCCCEEEEEECCCC		1.7828526873
64S-nitrosylationKWGTLTDCVVMRDPQ
HHCCCEEEEEECCCC		1.7820925432
64GlutathionylationKWGTLTDCVVMRDPQ
HHCCCEEEEEECCCC		1.7824333276
64S-nitrosocysteineKWGTLTDCVVMRDPQ
HHCCCEEEEEECCCC		1.78-
76MethylationDPQTKRSRGFGFVTY
CCCCCCCCCCEEEEE		48.7954556577
85GlutathionylationFGFVTYSCVEEVDAA
CEEEEEECHHHHCHH		2.9224333276
94GlutathionylationEEVDAAMCARPHKVD
HHHCHHHHCCCCCCC		2.2024333276
112PhosphorylationVEPKRAVSREDSVKP
CCCCCCCCCHHCCCC		29.0326824392
116PhosphorylationRAVSREDSVKPGAHL
CCCCCHHCCCCCCEE		27.5626824392
118UbiquitinationVSREDSVKPGAHLTV
CCCHHCCCCCCEEEE		41.51-
124PhosphorylationVKPGAHLTVKKIFVG
CCCCCEEEEEEEEEC		22.0319854140
126UbiquitinationPGAHLTVKKIFVGGI
CCCEEEEEEEEECCC		34.61-
127UbiquitinationGAHLTVKKIFVGGIK
CCEEEEEEEEECCCC		36.72-
134SuccinylationKIFVGGIKEDTEEYN
EEEECCCCCCCCCCC		53.4623806337
134MalonylationKIFVGGIKEDTEEYN
EEEECCCCCCCCCCC		53.4626320211
134AcetylationKIFVGGIKEDTEEYN
EEEECCCCCCCCCCC		53.4623806337
134UbiquitinationKIFVGGIKEDTEEYN
EEEECCCCCCCCCCC		53.46-
148AcetylationNLRDYFEKYGKIETI
CHHHHHHHHCCEEEE		49.7823806337
148UbiquitinationNLRDYFEKYGKIETI
CHHHHHHHHCCEEEE		49.78-
151AcetylationDYFEKYGKIETIEVM
HHHHHHCCEEEEEEE		33.9922826441
151UbiquitinationDYFEKYGKIETIEVM
HHHHHHCCEEEEEEE		33.99-
163PhosphorylationEVMEDRQSGKKRGFA
EEEEHHHCCCCCEEE		54.1729176673
173PhosphorylationKRGFAFVTFDDHDTV
CCEEEEEECCCCCCC		18.2026643407
187AcetylationVDKIVVQKYHTINGH
CEEEEEEEECCCCCC		27.6522826441
188PhosphorylationDKIVVQKYHTINGHN
EEEEEEEECCCCCCC		6.2625367039
190PhosphorylationIVVQKYHTINGHNCE
EEEEEECCCCCCCHH		17.0423375375
196S-nitrosylationHTINGHNCEVKKALS
CCCCCCCHHHHHHCC		5.4420925432
196S-nitrosocysteineHTINGHNCEVKKALS
CCCCCCCHHHHHHCC		5.44-
196GlutathionylationHTINGHNCEVKKALS
CCCCCCCHHHHHHCC		5.4424333276
199AcetylationNGHNCEVKKALSKQE
CCCCHHHHHHCCHHH		15.277611783
200AcetylationGHNCEVKKALSKQEM
CCCHHHHHHCCHHHH		60.797613287
204UbiquitinationEVKKALSKQEMQSAG
HHHHHCCHHHHHHHC		51.64-
212PhosphorylationQEMQSAGSQRGRGGG
HHHHHHCCCCCCCCC		19.2025890499
214Asymmetric dimethylarginineMQSAGSQRGRGGGSG
HHHHCCCCCCCCCCC		38.17-
214MethylationMQSAGSQRGRGGGSG
HHHHCCCCCCCCCCC		38.1718600961
216Asymmetric dimethylarginineSAGSQRGRGGGSGNF
HHCCCCCCCCCCCCC		42.65-
216MethylationSAGSQRGRGGGSGNF
HHCCCCCCCCCCCCC		42.6512018835
220PhosphorylationQRGRGGGSGNFMGRG
CCCCCCCCCCCCCCC		33.5625890499
226Asymmetric dimethylarginineGSGNFMGRGGNFGGG
CCCCCCCCCCCCCCC		37.75-
226MethylationGSGNFMGRGGNFGGG
CCCCCCCCCCCCCCC		37.7524129315
239Asymmetric dimethylarginineGGGGNFGRGGNFGGR
CCCCCCCCCCCCCCC		45.79-
239MethylationGGGGNFGRGGNFGGR
CCCCCCCCCCCCCCC		45.7924129315
246MethylationRGGNFGGRGGYGGGG
CCCCCCCCCCCCCCC		35.4224129315
246Asymmetric dimethylarginineRGGNFGGRGGYGGGG
CCCCCCCCCCCCCCC		35.42-
249PhosphorylationNFGGRGGYGGGGGGS
CCCCCCCCCCCCCCC		18.5421183079
257MethylationGGGGGGSRGSYGGGD
CCCCCCCCCCCCCCC		41.1524129315
286MethylationGGPGYSSRGGYGGGG
CCCCCCCCCCCCCCC		36.2918600971
286Asymmetric dimethylarginineGGPGYSSRGGYGGGG
CCCCCCCCCCCCCCC		36.29-
303PhosphorylationYGNQGGGYGGGGGGY
CCCCCCCCCCCCCCC		18.84-
310PhosphorylationYGGGGGGYDGYNEGG
CCCCCCCCCCCCCCC		14.96-
313PhosphorylationGGGGYDGYNEGGNFG
CCCCCCCCCCCCCCC		13.72-
324PhosphorylationGNFGGGNYGGGGNYN
CCCCCCCCCCCCCCC		22.03-
351PhosphorylationYGPMKGGSFGGRSSG
CCCCCCCCCCCCCCC		29.4126239621
355MethylationKGGSFGGRSSGSPYG
CCCCCCCCCCCCCCC		28.2016289313
356PhosphorylationGGSFGGRSSGSPYGG
CCCCCCCCCCCCCCC		42.1824925903
357PhosphorylationGSFGGRSSGSPYGGG
CCCCCCCCCCCCCCC		41.7625521595
359PhosphorylationFGGRSSGSPYGGGYG
CCCCCCCCCCCCCCC		19.5224925903
361PhosphorylationGRSSGSPYGGGYGSG
CCCCCCCCCCCCCCC		30.0525521595
365PhosphorylationGSPYGGGYGSGGGSG
CCCCCCCCCCCCCCC		16.0524925903
367PhosphorylationPYGGGYGSGGGSGGY
CCCCCCCCCCCCCCC		26.2724925903
371PhosphorylationGYGSGGGSGGYGSRR
CCCCCCCCCCCCCCC		32.1125521595
374PhosphorylationSGGGSGGYGSRRF--
CCCCCCCCCCCCC--		18.5624925903
376PhosphorylationGGSGGYGSRRF----
CCCCCCCCCCC----		16.2924925903
377MethylationGSGGYGSRRF-----
CCCCCCCCCC-----		39.3918967023
378MethylationSGGYGSRRF------
CCCCCCCCC------		43.2418966653
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 ROA3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROA3_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 ROA3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHX9_HUMANDHX9physical
26496610
ROA1_HUMANHNRNPA1physical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
ROAA_HUMANHNRNPABphysical
26496610
HNRPC_HUMANHNRNPCphysical
26496610
HNRH3_HUMANHNRNPH3physical
26496610
HNRPM_HUMANHNRNPMphysical
26496610
SAFB1_HUMANSAFBphysical
26496610
ELOC_HUMANTCEB1physical
26496610
BRPF1_HUMANBRPF1physical
26496610
SAFB2_HUMANSAFB2physical
26496610
MATR3_HUMANMATR3physical
26496610
HNRDL_HUMANHNRNPDLphysical
26496610
HNRPR_HUMANHNRNPRphysical
26496610
S35B1_HUMANSLC35B1physical
26496610
RBM14_HUMANRBM14physical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
ROA0_HUMANHNRNPA0physical
26496610
RALY_HUMANRALYphysical
26496610
F120A_HUMANFAM120Aphysical
26496610
FA50B_HUMANFAM50Bphysical
26496610
ZN638_HUMANZNF638physical
26496610
RT10_HUMANMRPS10physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
YLPM1_HUMANYLPM1physical
26496610
STN1_HUMANOBFC1physical
26496610
CE290_HUMANCEP290physical
26496610
GATC_HUMANGATCphysical
26496610
ZN326_HUMANZNF326physical
26496610
RB12B_HUMANRBM12Bphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROA3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASSSPECTROMETRY.
"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-359; TYR-361 ANDSER-371, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASSSPECTROMETRY.

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