ROA1_MOUSE - dbPTM
ROA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROA1_MOUSE
UniProt AC P49312
Protein Name Heterogeneous nuclear ribonucleoprotein A1
Gene Name Hnrnpa1
Organism Mus musculus (Mouse).
Sequence Length 320
Subcellular Localization Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes.
Protein Description Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection (By similarity). May bind to specific miRNA hairpins (By similarity)..
Protein Sequence MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
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-------MSKSESPK
-------CCCCCCCC		11.68-
2Phosphorylation------MSKSESPKE
------CCCCCCCCC		44.9126824392
2Acetylation------MSKSESPKE
------CCCCCCCCC		44.91-
3Acetylation-----MSKSESPKEP
-----CCCCCCCCCH		57.8723806337
4Phosphorylation----MSKSESPKEPE
----CCCCCCCCCHH		35.6827087446
6Phosphorylation--MSKSESPKEPEQL
--CCCCCCCCCHHHH		48.6527087446
8UbiquitinationMSKSESPKEPEQLRK
CCCCCCCCCHHHHHH		87.79-
8AcetylationMSKSESPKEPEQLRK
CCCCCCCCCHHHHHH		87.7923806337
22PhosphorylationKLFIGGLSFETTDES
HHHHCCCCCCCCCHH		25.0626824392
25PhosphorylationIGGLSFETTDESLRS
HCCCCCCCCCHHHHH		37.2223984901
26PhosphorylationGGLSFETTDESLRSH
CCCCCCCCCHHHHHH		30.4823984901
43S-nitrosocysteineQWGTLTDCVVMRDPN
HHCCEEEEEEEECCC		1.78-
43S-nitrosylationQWGTLTDCVVMRDPN
HHCCEEEEEEEECCC		1.7820925432
52AcetylationVMRDPNTKRSRGFGF
EEECCCCCCCCCCEE		55.8223236377
91PhosphorylationVEPKRAVSREDSQRP
CCCCCCCCCCCCCCC		29.0326824392
95PhosphorylationRAVSREDSQRPGAHL
CCCCCCCCCCCCCEE		24.2826824392
103PhosphorylationQRPGAHLTVKKIFVG
CCCCCEEEEEEEEEC		22.0328725479
105AcetylationPGAHLTVKKIFVGGI
CCCEEEEEEEEECCC		34.6122826441
106AcetylationGAHLTVKKIFVGGIK
CCEEEEEEEEECCCC		36.7222826441
113AcetylationKIFVGGIKEDTEEHH
EEEECCCCCCCCHHH		53.4623236377
113MalonylationKIFVGGIKEDTEEHH
EEEECCCCCCCCHHH		53.4626073543
116PhosphorylationVGGIKEDTEEHHLRD
ECCCCCCCCHHHHHH		44.3524899341
138PhosphorylationIEVIEIMTDRGSGKK
EEEEEEEEECCCCCC		28.3619854140
142PhosphorylationEIMTDRGSGKKRGFA
EEEEECCCCCCCEEE		48.6219854140
144AcetylationMTDRGSGKKRGFAFV
EEECCCCCCCEEEEE		40.78129629
145AcetylationTDRGSGKKRGFAFVT
EECCCCCCCEEEEEE		62.377379923
166AcetylationVDKIVIQKYHTVNGH
CCEEEEEEECCCCCC		28.0722826441
167PhosphorylationDKIVIQKYHTVNGHN
CEEEEEEECCCCCCC		6.0729514104
175S-nitrosylationHTVNGHNCEVRKALS
CCCCCCCHHHHHHHC		4.1920925432
175S-nitrosocysteineHTVNGHNCEVRKALS
CCCCCCCHHHHHHHC		4.19-
192PhosphorylationEMASASSSQRGRSGS
HHHHCCCCCCCCCCC		22.77-
194Asymmetric dimethylarginineASASSSQRGRSGSGN
HHCCCCCCCCCCCCC		44.43-
194MethylationASASSSQRGRSGSGN
HHCCCCCCCCCCCCC		44.43136635
196MethylationASSSQRGRSGSGNFG
CCCCCCCCCCCCCCC		39.7816288417
197PhosphorylationSSSQRGRSGSGNFGG
CCCCCCCCCCCCCCC		39.8826643407
199PhosphorylationSQRGRSGSGNFGGGR
CCCCCCCCCCCCCCC		31.6325266776
206MethylationSGNFGGGRGGGFGGN
CCCCCCCCCCCCCCC		43.8124129315
206Asymmetric dimethylarginineSGNFGGGRGGGFGGN
CCCCCCCCCCCCCCC		43.81-
218MethylationGGNDNFGRGGNFSGR
CCCCCCCCCCCCCCC		45.7924129315
218Asymmetric dimethylarginineGGNDNFGRGGNFSGR
CCCCCCCCCCCCCCC		45.79-
223PhosphorylationFGRGGNFSGRGGFGG
CCCCCCCCCCCCCCC		31.4225890499
225MethylationRGGNFSGRGGFGGSR
CCCCCCCCCCCCCCC		40.6424129315
225Asymmetric dimethylarginineRGGNFSGRGGFGGSR
CCCCCCCCCCCCCCC		40.64-
232MethylationRGGFGGSRGGGGYGG
CCCCCCCCCCCCCCC		51.5624129315
232Asymmetric dimethylarginineRGGFGGSRGGGGYGG
CCCCCCCCCCCCCCC		51.56-
259PhosphorylationSNFGGGGSYNDFGNY
CCCCCCCCCCCCCCC		24.84-
260PhosphorylationNFGGGGSYNDFGNYN
CCCCCCCCCCCCCCC		23.25-
266PhosphorylationSYNDFGNYNNQSSNF
CCCCCCCCCCCCCCC		18.83-
284MethylationKGGNFGGRSSGPYGG
CCCCCCCCCCCCCCC		28.2024129315
285PhosphorylationGGNFGGRSSGPYGGG
CCCCCCCCCCCCCCC		42.8121082442
286PhosphorylationGNFGGRSSGPYGGGG
CCCCCCCCCCCCCCC		42.2922942356
289PhosphorylationGGRSSGPYGGGGQYF
CCCCCCCCCCCCCCC		31.7428833060
295PhosphorylationPYGGGGQYFAKPRNQ
CCCCCCCCCCCCCCC		14.5820116462
298UbiquitinationGGGQYFAKPRNQGGY
CCCCCCCCCCCCCCC		34.31-
298AcetylationGGGQYFAKPRNQGGY
CCCCCCCCCCCCCCC		34.3123806337
298MalonylationGGGQYFAKPRNQGGY
CCCCCCCCCCCCCCC		34.3126320211
300DimethylationGQYFAKPRNQGGYGG
CCCCCCCCCCCCCCC		47.61-
300MethylationGQYFAKPRNQGGYGG
CCCCCCCCCCCCCCC		47.6124129315
305PhosphorylationKPRNQGGYGGSSSSS
CCCCCCCCCCCCCCC		25.7425159016
308PhosphorylationNQGGYGGSSSSSSYG
CCCCCCCCCCCCCCC		23.7623527152
309PhosphorylationQGGYGGSSSSSSYGS
CCCCCCCCCCCCCCC		37.2023684622
310PhosphorylationGGYGGSSSSSSYGSG
CCCCCCCCCCCCCCC		35.6223527152
311PhosphorylationGYGGSSSSSSYGSGR
CCCCCCCCCCCCCCC		25.8327087446
312PhosphorylationYGGSSSSSSYGSGRR
CCCCCCCCCCCCCCC		29.5327087446
313PhosphorylationGGSSSSSSYGSGRRF
CCCCCCCCCCCCCCC		35.1523684622
314PhosphorylationGSSSSSSYGSGRRF-
CCCCCCCCCCCCCC-		19.7725159016
316PhosphorylationSSSSSYGSGRRF---
CCCCCCCCCCCC---		22.3923684622
318MethylationSSSYGSGRRF-----
CCCCCCCCCC-----		38.2324381473
319MethylationSSYGSGRRF------
CCCCCCCCC------		45.1930759943
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
192SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
310SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
311SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
312SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROA1_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 ROA1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ROA1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROA1_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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-6, AND MASSSPECTROMETRY.
"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-6, 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-4, 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-6, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-313, AND MASSSPECTROMETRY.

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