dbPTM

ROA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROA2_MOUSE
UniProt AC	O88569
Protein Name	Heterogeneous nuclear ribonucleoproteins A2/B1
Gene Name	Hnrnpa2b1
Organism	Mus musculus (Mouse).
Sequence Length	353
Subcellular Localization	Nucleus, nucleoplasm . Cytoplasmic granule . Secreted, exosome . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes follwong sumoylation.
Protein Description	Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity)..
Protein Sequence	MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGSYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEKTLETV -------CCCCCCCC	12.29	-
4	Phosphorylation	----MEKTLETVPLE ----CCCCCCCCCCH	19.27	29514104
17 (in isoform 3)	Phosphorylation	-	61.93	29514104
17 (in isoform 2)	Phosphorylation	-	61.93	29514104
17	Ubiquitination	LERKKREKEQFRKLF CHHHHHHHHHHHHHH	61.93	27667366
22	Ubiquitination	REKEQFRKLFIGGLS HHHHHHHHHHCCCCC	49.38	22790023
29	Phosphorylation	KLFIGGLSFETTEES HHHCCCCCCCCCHHH	25.06	26239621
32	Phosphorylation	IGGLSFETTEESLRN CCCCCCCCCHHHHHH	37.18	26239621
33	Phosphorylation	GGLSFETTEESLRNY CCCCCCCCHHHHHHH	30.47	26239621
38	Methylation	ETTEESLRNYYEQWG CCCHHHHHHHHHHHC	38.08	24129315
46	Acetylation	NYYEQWGKLTDCVVM HHHHHHCCCEEEEEE	45.30	22826441
46	Ubiquitination	NYYEQWGKLTDCVVM HHHHHHCCCEEEEEE	45.30	22790023
50	S-nitrosocysteine	QWGKLTDCVVMRDPA HHCCCEEEEEECCCC	1.78	-
50	S-palmitoylation	QWGKLTDCVVMRDPA HHCCCEEEEEECCCC	1.78	28526873
50	S-nitrosylation	QWGKLTDCVVMRDPA HHCCCEEEEEECCCC	1.78	24926564
59	Ubiquitination	VMRDPASKRSRGFGF EECCCCCCCCCCCEE	57.40	22790023
59	Acetylation	VMRDPASKRSRGFGF EECCCCCCCCCCCEE	57.40	68671
68	Phosphorylation	SRGFGFVTFSSMAEV CCCCEEEEEHHHHHH	18.62	25890499
70	Phosphorylation	GFGFVTFSSMAEVDA CCEEEEEHHHHHHHH	15.16	25777480
71	Phosphorylation	FGFVTFSSMAEVDAA CEEEEEHHHHHHHHH	20.16	25777480
85	Phosphorylation	AMAARPHSIDGRVVE HHHCCCCCCCCEECC	25.67	23684622
99	Methylation	EPKRAVAREESGKPG CCCCHHHHHHCCCCC	41.43	58857861
100	Ubiquitination	PKRAVAREESGKPGA CCCHHHHHHCCCCCC	46.94	27667366
102	Phosphorylation	RAVAREESGKPGAHV CHHHHHHCCCCCCEE	47.57	23684622
104	Methylation	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	-
104	Malonylation	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	26320211
104	Acetylation	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	23806337
104	Ubiquitination	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	-
104	"N6,N6-dimethyllysine"	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	-
112	Ubiquitination	PGAHVTVKKLFVGGI CCCEEEEEEEEECCC	34.10	22790023
112	Acetylation	PGAHVTVKKLFVGGI CCCEEEEEEEEECCC	34.10	22826441
113	Acetylation	GAHVTVKKLFVGGIK CCEEEEEEEEECCCC	42.70	22826441
113	Ubiquitination	GAHVTVKKLFVGGIK CCEEEEEEEEECCCC	42.70	22790023
120	Ubiquitination	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	-
120	Acetylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	23806337
120	Succinylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	-
120	Malonylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	26320211
123	Phosphorylation	VGGIKEDTEEHHLRD ECCCCCCCCHHHHHH	44.35	24899341
137	Ubiquitination	DYFEEYGKIDTIEII HHHHHHCCCCEEEEE	36.19	-
140	Phosphorylation	EEYGKIDTIEIITDR HHHCCCCEEEEEECC	24.79	29514104
145	Phosphorylation	IDTIEIITDRQSGKK CCEEEEEECCCCCCC	30.69	28066266
149	Phosphorylation	EIITDRQSGKKRGFG EEEECCCCCCCCEEE	54.17	28066266
152	Ubiquitination	TDRQSGKKRGFGFVT ECCCCCCCCEEEEEE	62.37	22790023
159	Phosphorylation	KRGFGFVTFDDHDPV CCEEEEEEECCCCCH	21.05	29514104
168	Ubiquitination	DDHDPVDKIVLQKYH CCCCCHHHHHHEEEC	34.64	22790023
168	Acetylation	DDHDPVDKIVLQKYH CCCCCHHHHHHEEEC	34.64	23806337
173	Ubiquitination	VDKIVLQKYHTINGH HHHHHHEEECHHCCC	34.53	22790023
173	Acetylation	VDKIVLQKYHTINGH HHHHHHEEECHHCCC	34.53	22826441
174	Phosphorylation	DKIVLQKYHTINGHN HHHHHEEECHHCCCC	7.40	25367039
176	Phosphorylation	IVLQKYHTINGHNAE HHHEEECHHCCCCHH	17.04	23684622
189	Phosphorylation	AEVRKALSRQEMQEV HHHHHHHCHHHHHHH	36.46	29176673
198	Phosphorylation	QEMQEVQSSRSGRGG HHHHHHHHHCCCCCC	32.66	24899341
199	Phosphorylation	EMQEVQSSRSGRGGN HHHHHHHHCCCCCCC	17.24	27742792
200	Methylation	MQEVQSSRSGRGGNF HHHHHHHCCCCCCCC	48.67	58857851
201	Phosphorylation	QEVQSSRSGRGGNFG HHHHHHCCCCCCCCC	34.49	22324799
203	Asymmetric dimethylarginine	VQSSRSGRGGNFGFG HHHHCCCCCCCCCCC	51.60	-
203	Methylation	VQSSRSGRGGNFGFG HHHHCCCCCCCCCCC	51.60	24129315
212	Phosphorylation	GNFGFGDSRGGGGNF CCCCCCCCCCCCCCC	32.95	23684622
213	Asymmetric dimethylarginine	NFGFGDSRGGGGNFG CCCCCCCCCCCCCCC	53.14	-
213	Methylation	NFGFGDSRGGGGNFG CCCCCCCCCCCCCCC	53.14	24129315
225	Phosphorylation	NFGPGPGSNFRGGSD CCCCCCCCCCCCCCC	35.61	26824392
228	Methylation	PGPGSNFRGGSDGYG CCCCCCCCCCCCCCC	53.46	24129315
231	Phosphorylation	GSNFRGGSDGYGSGR CCCCCCCCCCCCCCC	30.59	23684622
234	Phosphorylation	FRGGSDGYGSGRGFG CCCCCCCCCCCCCCC	17.07	26160508
236	Phosphorylation	GGSDGYGSGRGFGDG CCCCCCCCCCCCCCC	19.48	26160508
238	Methylation	SDGYGSGRGFGDGYN CCCCCCCCCCCCCCC	38.68	24129315
244	Phosphorylation	GRGFGDGYNGYGGGP CCCCCCCCCCCCCCC	15.34	25619855
245 (in isoform 3)	Phosphorylation	-	42.62	-
247	Phosphorylation	FGDGYNGYGGGPGGG CCCCCCCCCCCCCCC	14.68	25619855
259	Phosphorylation	GGGNFGGSPGYGGGR CCCCCCCCCCCCCCC	18.61	27087446
262	Phosphorylation	NFGGSPGYGGGRGGY CCCCCCCCCCCCCCC	18.91	25619855
266	Methylation	SPGYGGGRGGYGGGG CCCCCCCCCCCCCCC	38.34	24129315
266	Asymmetric dimethylarginine	SPGYGGGRGGYGGGG CCCCCCCCCCCCCCC	38.34	-
306	Phosphorylation	SYNDFGNYNQQPSNY CCCCCCCCCCCCCCC	18.09	-
312 (in isoform 2)	Phosphorylation	-	53.08	19144319
318	Phosphorylation	SNYGPMKSGNFGGSR CCCCCCCCCCCCCCC	32.49	26643407
324	Phosphorylation	KSGNFGGSRNMGGPY CCCCCCCCCCCCCCC	22.36	19144319
325	Methylation	SGNFGGSRNMGGPYG CCCCCCCCCCCCCCC	40.19	24129315
331	Phosphorylation	SRNMGGPYGGGNYGP CCCCCCCCCCCCCCC	31.51	25619855
336	Phosphorylation	GPYGGGNYGPGGSGG CCCCCCCCCCCCCCC	28.15	25619855
341	Phosphorylation	GNYGPGGSGGSGGYG CCCCCCCCCCCCCCC	45.99	25521595
344	Phosphorylation	GPGGSGGSGGYGGRS CCCCCCCCCCCCCCC	32.35	23684622
347	Phosphorylation	GSGGSGGYGGRSRY- CCCCCCCCCCCCCC-	21.67	27149854
350	Methylation	GSGGYGGRSRY---- CCCCCCCCCCC----	17.38	24129315
351	Phosphorylation	SGGYGGRSRY----- CCCCCCCCCC-----	38.92	22705319
352	Methylation	GGYGGRSRY------ CCCCCCCCC------	39.56	18966523
353	Phosphorylation	GYGGRSRY------- CCCCCCCC-------	24.93	26643407

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 ROA2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
266	R	Methylation	24129315
According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity).
266	R	Methylation	24129315
Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity).

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 ROA2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SET_MOUSE	Set	physical	16170352
PP2AA_MOUSE	Ppp2ca	physical	16170352

Drug and Disease Associations

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

Regulatory Network of ROA2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASSSPECTROMETRY.	19144319 [Abstract]
"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-85, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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-259, AND MASSSPECTROMETRY.	18630941 [Abstract]

show

show