ROA1_RAT - dbPTM
ROA1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROA1_RAT
UniProt AC P04256
Protein Name Heterogeneous nuclear ribonucleoprotein A1
Gene Name Hnrnpa1
Organism Rattus norvegicus (Rat).
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 MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALCKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
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		44.9127097102
2Acetylation------MSKSESPKE
------CCCCCCCCC		44.91-
3Acetylation-----MSKSESPKEP
-----CCCCCCCCCH		57.8722902405
4Phosphorylation----MSKSESPKEPE
----CCCCCCCCCHH		35.6823712012
6Phosphorylation--MSKSESPKEPEQL
--CCCCCCCCCHHHH		48.6523712012
22PhosphorylationKLFIGGLSFETTDES
HHHHCCCCCCCCCHH		25.0628432305
25PhosphorylationIGGLSFETTDESLRS
HCCCCCCCCCHHHHH		37.2228432305
26PhosphorylationGGLSFETTDESLRSH
CCCCCCCCCHHHHHH		30.4828432305
52AcetylationVMRDPNTKRSRGFGF
EEECCCCCCCCCCEE		55.8222902405
95PhosphorylationRAVSREDSQRPGAHL
CCCCCCCCCCCCCEE		24.2827097102
103PhosphorylationQRPGAHLTVKKIFVG
CCCCCEEEEEEEEEC		22.0325575281
105AcetylationPGAHLTVKKIFVGGI
CCCEEEEEEEEECCC		34.6122902405
138PhosphorylationIEVIEIMTDRGSGKK
EEEEEEEEECCCCCC		28.3623984901
142PhosphorylationEIMTDRGSGKKRGFA
EEEEECCCCCCCEEE		48.6223984901
158PhosphorylationVTFDDHDSVDKIVIQ
EEECCCCCCCEEEEE		28.8823984901
169PhosphorylationIVIQKYHTVNGHNCE
EEEEEEECCCCCCHH		16.7523984901
192PhosphorylationEMASASSSQRGRSGS
HHHHCCCCCCCCCCC		22.7722668510
194MethylationASASSSQRGRSGSGN
HHCCCCCCCCCCCCC		44.4324098712
194Asymmetric dimethylarginineASASSSQRGRSGSGN
HHCCCCCCCCCCCCC		44.43-
197PhosphorylationSSSQRGRSGSGNFGG
CCCCCCCCCCCCCCC		39.8825403869
199PhosphorylationSQRGRSGSGNFGGGR
CCCCCCCCCCCCCCC		31.6329779826
206Asymmetric dimethylarginineSGNFGGGRGGGFGGN
CCCCCCCCCCCCCCC		43.81-
206MethylationSGNFGGGRGGGFGGN
CCCCCCCCCCCCCCC		43.8124098712
218Asymmetric dimethylarginineGGNDNFGRGGNFSGR
CCCCCCCCCCCCCCC		45.79-
218MethylationGGNDNFGRGGNFSGR
CCCCCCCCCCCCCCC		45.7924098712
223PhosphorylationFGRGGNFSGRGGFGG
CCCCCCCCCCCCCCC		31.427727389
225Asymmetric dimethylarginineRGGNFSGRGGFGGSR
CCCCCCCCCCCCCCC		40.64-
225MethylationRGGNFSGRGGFGGSR
CCCCCCCCCCCCCCC		40.6424098712
231PhosphorylationGRGGFGGSRGGGGYG
CCCCCCCCCCCCCCC		28.297727389
232MethylationRGGFGGSRGGGGYGG
CCCCCCCCCCCCCCC		51.5624098712
232Asymmetric dimethylarginineRGGFGGSRGGGGYGG
CCCCCCCCCCCCCCC		51.56-
237PhosphorylationGSRGGGGYGGSGDGY
CCCCCCCCCCCCCCC		22.9123712012
240PhosphorylationGGGGYGGSGDGYNGF
CCCCCCCCCCCCCCC		29.3723712012
284MethylationKGGNFGGRSSGPYGG
CCCCCCCCCCCCCCC		28.2018600467
285PhosphorylationGGNFGGRSSGPYGGG
CCCCCCCCCCCCCCC		42.8127097102
286PhosphorylationGNFGGRSSGPYGGGG
CCCCCCCCCCCCCCC		42.2927097102
289PhosphorylationGGRSSGPYGGGGQYF
CCCCCCCCCCCCCCC		31.7427097102
298AcetylationGGGQYFAKPRNQGGY
CCCCCCCCCCCCCCC		34.3125786129
300MethylationGQYFAKPRNQGGYGG
CCCCCCCCCCCCCCC		47.6118600823
305PhosphorylationKPRNQGGYGGSSSSS
CCCCCCCCCCCCCCC		25.7427097102
308PhosphorylationNQGGYGGSSSSSSYG
CCCCCCCCCCCCCCC		23.7623984901
309PhosphorylationQGGYGGSSSSSSYGS
CCCCCCCCCCCCCCC		37.2027097102
310PhosphorylationGGYGGSSSSSSYGSG
CCCCCCCCCCCCCCC		35.6227097102
311PhosphorylationGYGGSSSSSSYGSGR
CCCCCCCCCCCCCCC		25.8327097102
312PhosphorylationYGGSSSSSSYGSGRR
CCCCCCCCCCCCCCC		29.5327097102
313PhosphorylationGGSSSSSSYGSGRRF
CCCCCCCCCCCCCCC		35.1527097102
314PhosphorylationGSSSSSSYGSGRRF-
CCCCCCCCCCCCCC-		19.7723984901
316PhosphorylationSSSSSYGSGRRF---
CCCCCCCCCCCC---		22.3927097102
318MethylationSSSYGSGRRF-----
CCCCCCCCCC-----		38.2324381477
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
95SPhosphorylationKinasePRKCAP17252
GPS
103TPhosphorylationKinasePRKCAP17252
GPS
192SPhosphorylationKinasePRKCAP17252
GPS
192SPhosphorylationKinaseMKNK2Q5U2N4
Uniprot
197SPhosphorylationKinasePRKCAP17252
GPS
199SPhosphorylationKinasePRKCAP17252
GPS
223SPhosphorylationKinasePRKCAP17252
GPS
231SPhosphorylationKinasePRKCAP17252
GPS
310SPhosphorylationKinaseMKNK2Q5U2N4
Uniprot
311SPhosphorylationKinaseMKNK2Q5U2N4
Uniprot
312SPhosphorylationKinaseMKNK2Q5U2N4
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROA1_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ROA1_RAT !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROA1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.
"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-6, AND MASSSPECTROMETRY.

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