ROAA_MOUSE - dbPTM
ROAA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROAA_MOUSE
UniProt AC Q99020
Protein Name Heterogeneous nuclear ribonucleoprotein A/B
Gene Name Hnrnpab
Organism Mus musculus (Mouse).
Sequence Length 285
Subcellular Localization Nucleus . Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs..
Protein Description Transcriptional repressor. Binds to CArG box motifs, single-stranded and double-stranded DNA, and RNA. It may be that repression by CBF-A is a result of competitive binding of CBF, a putative positive factor, and CBF-A to the same or overlapping motifs around the CArG boxes..
Protein Sequence MSDAAEEQPMETTGATENGHEAAPEGEAPVEPSAAAAAPAASAGSGGGTTTAPSGNQNGAEGDQINASKNEEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFKDSSSVEKVLDQKEHRLDGRVIDPKKAMAMKKDPVKKIFVGGLNPEATEEKIREYFGQFGEIEAIELPIDPKLNKRRGFVFITFKEEDPVKKVLEKKFHTVSGSKCEIKVAQPKEVYQQQQYGSGGRGNRNRGNRGSGGGQGSTNYGKSQRRGGHQNNYKPY
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------MSDAAEEQP
------CCCHHHHCC		35.6425338131
12PhosphorylationAEEQPMETTGATENG
HHHCCCCCCCCCCCC		25.0325338131
76UbiquitinationKNEEDAGKMFVGGLS
CCHHHHHHHCCCEEC		30.77-
83PhosphorylationKMFVGGLSWDTSKKD
HHCCCEECCCCCHHH		26.6126643407
86PhosphorylationVGGLSWDTSKKDLKD
CCEECCCCCHHHHHH		35.8726643407
87PhosphorylationGGLSWDTSKKDLKDY
CEECCCCCHHHHHHH		34.9228725479
88UbiquitinationGLSWDTSKKDLKDYF
EECCCCCHHHHHHHH		53.01-
89UbiquitinationLSWDTSKKDLKDYFT
ECCCCCHHHHHHHHH		68.97-
92UbiquitinationDTSKKDLKDYFTKFG
CCCHHHHHHHHHHHH		61.59-
97UbiquitinationDLKDYFTKFGEVVDC
HHHHHHHHHHCEEEE		41.28-
104S-nitrosocysteineKFGEVVDCTIKMDPN
HHHCEEEEEEEECCC		2.61-
104S-nitrosylationKFGEVVDCTIKMDPN
HHHCEEEEEEEECCC		2.6124926564
105PhosphorylationFGEVVDCTIKMDPNT
HHCEEEEEEEECCCC		21.1125159016
107UbiquitinationEVVDCTIKMDPNTGR
CEEEEEEEECCCCCC		21.06-
107MalonylationEVVDCTIKMDPNTGR
CEEEEEEEECCCCCC		21.0626320211
124UbiquitinationGFGFILFKDSSSVEK
EEEEEEECCCHHHHH		53.94-
131UbiquitinationKDSSSVEKVLDQKEH
CCCHHHHHHHHHCHH		46.04-
136UbiquitinationVEKVLDQKEHRLDGR
HHHHHHHCHHCCCCE		55.97-
154UbiquitinationPKKAMAMKKDPVKKI
HHHHHHCCCCCCCEE		44.48-
160UbiquitinationMKKDPVKKIFVGGLN
CCCCCCCEEEECCCC		41.43-
160MalonylationMKKDPVKKIFVGGLN
CCCCCCCEEEECCCC		41.4326320211
171PhosphorylationGGLNPEATEEKIREY
CCCCHHHHHHHHHHH		42.9129514104
174UbiquitinationNPEATEEKIREYFGQ
CHHHHHHHHHHHHHC		40.61-
195UbiquitinationIELPIDPKLNKRRGF
EECCCCCCCCCCCCE		62.03-
220AcetylationVKKVLEKKFHTVSGS
HHHHHHHHEEECCCC		32.7623806337
223PhosphorylationVLEKKFHTVSGSKCE
HHHHHEEECCCCCCE		21.3525338131
225PhosphorylationEKKFHTVSGSKCEIK
HHHEEECCCCCCEEE		38.2125338131
227PhosphorylationKFHTVSGSKCEIKVA
HEEECCCCCCEEEEC		26.9929514104
228MalonylationFHTVSGSKCEIKVAQ
EEECCCCCCEEEECC		39.1426320211
228UbiquitinationFHTVSGSKCEIKVAQ
EEECCCCCCEEEECC		39.14-
229GlutathionylationHTVSGSKCEIKVAQP
EECCCCCCEEEECCC		7.5724333276
237UbiquitinationEIKVAQPKEVYQQQQ
EEEECCCHHHHHHCC		47.97-
237MalonylationEIKVAQPKEVYQQQQ
EEEECCCHHHHHHCC		47.9726320211
245PhosphorylationEVYQQQQYGSGGRGN
HHHHHCCCCCCCCCC		14.6625619855
247PhosphorylationYQQQQYGSGGRGNRN
HHHCCCCCCCCCCCC		32.8923684622
250DimethylationQQYGSGGRGNRNRGN
CCCCCCCCCCCCCCC		42.62-
250MethylationQQYGSGGRGNRNRGN
CCCCCCCCCCCCCCC		42.6224129315
253MethylationGSGGRGNRNRGNRGS
CCCCCCCCCCCCCCC		36.7312018069
255MethylationGGRGNRNRGNRGSGG
CCCCCCCCCCCCCCC		40.2924129315
258MethylationGNRNRGNRGSGGGQG
CCCCCCCCCCCCCCC		43.4024129315
260PhosphorylationRNRGNRGSGGGQGST
CCCCCCCCCCCCCCC		30.9027087446
266PhosphorylationGSGGGQGSTNYGKSQ
CCCCCCCCCCCCCCC		12.9427149854
267PhosphorylationSGGGQGSTNYGKSQR
CCCCCCCCCCCCCCC		39.0127149854
271AcetylationQGSTNYGKSQRRGGH
CCCCCCCCCCCCCCC		32.8123806337
272PhosphorylationGSTNYGKSQRRGGHQ
CCCCCCCCCCCCCCC		25.2627149854
274DimethylationTNYGKSQRRGGHQNN
CCCCCCCCCCCCCCC		46.43-
274MethylationTNYGKSQRRGGHQNN
CCCCCCCCCCCCCCC		46.4354540481
275MethylationNYGKSQRRGGHQNNY
CCCCCCCCCCCCCCC		48.0524129315
275Asymmetric dimethylarginineNYGKSQRRGGHQNNY
CCCCCCCCCCCCCCC		48.05-
283AcetylationGGHQNNYKPY-----
CCCCCCCCCC-----		39.7122641125
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 ROAA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-83, AND MASSSPECTROMETRY.

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