dbPTM

ROA0_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROA0_MOUSE
UniProt AC	Q9CX86
Protein Name	Heterogeneous nuclear ribonucleoprotein A0
Gene Name	Hnrnpa0
Organism	Mus musculus (Mouse).
Sequence Length	305
Subcellular Localization	Nucleus. Component of ribonucleosomes..
Protein Description	mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs..
Protein Sequence	MENSQLCKLFIGGLNVQTSESGLRGHFEAFGTLTDCVVVVNPQTKRSRCFGFVTYSNVEEADAAMAASPHAVDGNTVELKRAVSREDSARPGAHAKVKKLFVGGLKGDVAEGDLIEHFSQFGAVEKAEIIADKQSGKKRGFGFVYFQSHDAADKAAVVKFHPIQGHRVEVKKAVPKEDIHAGGGGARAARGGRGGGRGRGGGGGGGGRDQNGLAKGGGGGGGGYNSYGGYGGYGAYGGGGGGGGSYGGSDYGNGFGGFGSYSQHQSSYGPMKSGGGGGGGGSWGGRSNSGPYRGGYGGGYGGGSF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MENSQLCK -------CCHHHHHH	11.25	-
18	Phosphorylation	IGGLNVQTSESGLRG HCCCCCCCCCCCHHC	30.13	23737553
19	Phosphorylation	GGLNVQTSESGLRGH CCCCCCCCCCCHHCC	16.81	23737553
21	Phosphorylation	LNVQTSESGLRGHFE CCCCCCCCCHHCCEE	42.78	23737553
36	S-nitrosocysteine	AFGTLTDCVVVVNPQ EECEECCEEEEECCC	1.79	-
55	Phosphorylation	RCFGFVTYSNVEEAD CEEEEEEECCHHHHH	7.92	26745281
56	Phosphorylation	CFGFVTYSNVEEADA EEEEEEECCHHHHHH	25.65	26745281
68	Phosphorylation	ADAAMAASPHAVDGN HHHHHHCCCCCCCCC	14.00	26745281
84	Phosphorylation	VELKRAVSREDSARP CHHHHHHCCHHHCCC	29.03	26824392
88	Phosphorylation	RAVSREDSARPGAHA HHHCCHHHCCCCCCH	22.79	25521595
99	Succinylation	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	-
99	Ubiquitination	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	-
99	Malonylation	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	26320211
99	Acetylation	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	23806337
133	Acetylation	KAEIIADKQSGKKRG EEEEEEECCCCCCCC	37.02	23806337
133	Ubiquitination	KAEIIADKQSGKKRG EEEEEEECCCCCCCC	37.02	-
135	Phosphorylation	EIIADKQSGKKRGFG EEEEECCCCCCCCCE	59.32	29176673
139	Methylation	DKQSGKKRGFGFVYF ECCCCCCCCCEEEEE	49.51	24129315
145	Phosphorylation	KRGFGFVYFQSHDAA CCCCEEEEEECCCCC	8.14	29514104
148	Phosphorylation	FGFVYFQSHDAADKA CEEEEEECCCCCCCE	17.28	22817900
187	Methylation	HAGGGGARAARGGRG CCCCCCHHHCCCCCC	31.86	30987661
224	Phosphorylation	GGGGGGGYNSYGGYG CCCCCCCCCCCCCCC	12.29	-
226	Phosphorylation	GGGGGYNSYGGYGGY CCCCCCCCCCCCCCC	19.37	-
227	Phosphorylation	GGGGYNSYGGYGGYG CCCCCCCCCCCCCCC	15.78	-
273	Phosphorylation	SSYGPMKSGGGGGGG CCCCCCCCCCCCCCC	36.10	29514104
282	Phosphorylation	GGGGGGGSWGGRSNS CCCCCCCCCCCCCCC	26.31	23684622
286	Methylation	GGGSWGGRSNSGPYR CCCCCCCCCCCCCCC	28.82	24129315
293	Methylation	RSNSGPYRGGYGGGY CCCCCCCCCCCCCCC	34.88	24129315
293	Asymmetric dimethylarginine	RSNSGPYRGGYGGGY CCCCCCCCCCCCCCC	34.88	-
304	Phosphorylation	GGGYGGGSF------ CCCCCCCCC------	30.93	19854140

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
84	S	Phosphorylation	Kinase	MAPKAPK2	P49138	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
84	S	Phosphorylation	12456657
Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA.
293	R	Methylation	24129315
Arg-293 is dimethylated, probably to asymmetric dimethylarginine.

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 ROA0_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CXCL2_MOUSE	Cxcl2	physical	12456657
PGH2_MOUSE	Ptgs2	physical	12456657
TNFA_MOUSE	Tnf	physical	12456657

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ROA0_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs."; Rousseau S., Morrice N., Peggie M., Campbell D.G., Gaestel M.,Cohen P.; EMBO J. 21:6505-6514(2002). Cited for: FUNCTION, RNA-BINDING, AND PHOSPHORYLATION AT SER-84 BY MAPKAPK2.	12456657 [Abstract]

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