dbPTM

ROA3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROA3_HUMAN
UniProt AC	P51991
Protein Name	Heterogeneous nuclear ribonucleoprotein A3
Gene Name	HNRNPA3
Organism	Homo sapiens (Human).
Sequence Length	378
Subcellular Localization	Nucleus. Component of ribonucleosomes.
Protein Description	Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing..
Protein Sequence	MEVKPPPGRPQPDSGRRRRRRGEEGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEKWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMCARPHKVDGRVVEPKRAVSREDSVKPGAHLTVKKIFVGGIKEDTEEYNLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQSAGSQRGRGGGSGNFMGRGGNFGGGGGNFGRGGNFGGRGGYGGGGGGSRGSYGGGDGGYNGFGGDGGNYGGGPGYSSRGGYGGGGPGYGNQGGGYGGGGGYDGYNEGGNFGGGNYGGGGNYNDFGNYSGQQQSNYGPMKGGSFGGRSSGSPYGGGYGSGGGSGGYGSRRF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEVKPPPG -------CCCCCCCC	13.91	25944712
1	Sulfoxidation	-------MEVKPPPG -------CCCCCCCC	13.91	28183972
4	Sumoylation	----MEVKPPPGRPQ ----CCCCCCCCCCC	38.20	-
4	Acetylation	----MEVKPPPGRPQ ----CCCCCCCCCCC	38.20	23954790
4	Sumoylation	----MEVKPPPGRPQ ----CCCCCCCCCCC	38.20	28112733
4	Ubiquitination	----MEVKPPPGRPQ ----CCCCCCCCCCC	38.20	21890473
14	Phosphorylation	PGRPQPDSGRRRRRR CCCCCCCCCHHHHHC	40.66	23401153
14 (in isoform 2)	Ubiquitination	-	40.66	21890473
21	Methylation	SGRRRRRRGEEGHDP CCHHHHHCCCCCCCC	55.88	115478979
29	Acetylation	GEEGHDPKEPEQLRK CCCCCCCCCHHHHHH	86.22	25825284
29	Ubiquitination	GEEGHDPKEPEQLRK CCCCCCCCCHHHHHH	86.22	19608861
35	Methylation	PKEPEQLRKLFIGGL CCCHHHHHHHHHCCC	33.07	16289319
35 (in isoform 2)	Ubiquitination	-	33.07	21890473
36	Sumoylation	KEPEQLRKLFIGGLS CCHHHHHHHHHCCCC	57.23	-
36	Sumoylation	KEPEQLRKLFIGGLS CCHHHHHHHHHCCCC	57.23	28112733
36	Ubiquitination	KEPEQLRKLFIGGLS CCHHHHHHHHHCCCC	57.23	21890473
36 (in isoform 1)	Ubiquitination	-	57.23	21890473
43	Phosphorylation	KLFIGGLSFETTDDS HHHHCCCCCCCCCHH	25.06	22617229
46	Phosphorylation	IGGLSFETTDDSLRE HCCCCCCCCCHHHHH	33.25	28450419
47	Phosphorylation	GGLSFETTDDSLREH CCCCCCCCCHHHHHH	30.52	28450419
50	Phosphorylation	SFETTDDSLREHFEK CCCCCCHHHHHHHHH	31.94	28450419
51 (in isoform 2)	Ubiquitination	-	10.82	21890473
52	Dimethylation	ETTDDSLREHFEKWG CCCCHHHHHHHHHHC	39.02	-
52	Methylation	ETTDDSLREHFEKWG CCCCHHHHHHHHHHC	39.02	24390661
57	2-Hydroxyisobutyrylation	SLREHFEKWGTLTDC HHHHHHHHHCCCEEE	50.40	-
57	Acetylation	SLREHFEKWGTLTDC HHHHHHHHHCCCEEE	50.40	25825284
57	Ubiquitination	SLREHFEKWGTLTDC HHHHHHHHHCCCEEE	50.40	21890473
57 (in isoform 1)	Ubiquitination	-	50.40	21890473
60	Phosphorylation	EHFEKWGTLTDCVVM HHHHHHCCCEEEEEE	25.93	28857561
62	Phosphorylation	FEKWGTLTDCVVMRD HHHHCCCEEEEEECC	27.47	20068231
64	Glutathionylation	KWGTLTDCVVMRDPQ HHCCCEEEEEECCCC	1.78	22555962
72	Phosphorylation	VVMRDPQTKRSRGFG EEECCCCCCCCCCCE	33.54	21406692
73	Acetylation	VMRDPQTKRSRGFGF EECCCCCCCCCCCEE	43.03	25953088
73	Ubiquitination	VMRDPQTKRSRGFGF EECCCCCCCCCCCEE	43.03	73
73 (in isoform 1)	Ubiquitination	-	43.03	21890473
76	Methylation	DPQTKRSRGFGFVTY CCCCCCCCCCEEEEE	48.79	24129315
82	O-linked_Glycosylation	SRGFGFVTYSCVEEV CCCCEEEEEECHHHH	13.88	23301498
84	O-linked_Glycosylation	GFGFVTYSCVEEVDA CCEEEEEECHHHHCH	11.43	23301498
96 (in isoform 2)	Ubiquitination	-	29.00	21890473
99	2-Hydroxyisobutyrylation	AMCARPHKVDGRVVE HHHCCCCCCCCEECC	44.71	-
99	Acetylation	AMCARPHKVDGRVVE HHHCCCCCCCCEECC	44.71	26051181
108	Acetylation	DGRVVEPKRAVSRED CCEECCCCCCCCCHH	39.21	30584555
108	Sumoylation	DGRVVEPKRAVSRED CCEECCCCCCCCCHH	39.21	-
108	Ubiquitination	DGRVVEPKRAVSRED CCEECCCCCCCCCHH	39.21	-
112	Phosphorylation	VEPKRAVSREDSVKP CCCCCCCCCHHCCCC	29.03	23401153
112 (in isoform 2)	Ubiquitination	-	29.03	21890473
116	Phosphorylation	RAVSREDSVKPGAHL CCCCCHHCCCCCCEE	27.56	29255136
118	2-Hydroxyisobutyrylation	VSREDSVKPGAHLTV CCCHHCCCCCCEEEE	41.51	-
118	Acetylation	VSREDSVKPGAHLTV CCCHHCCCCCCEEEE	41.51	25953088
118	Sumoylation	VSREDSVKPGAHLTV CCCHHCCCCCCEEEE	41.51	28112733
118	Ubiquitination	VSREDSVKPGAHLTV CCCHHCCCCCCEEEE	41.51	21906983
118 (in isoform 1)	Ubiquitination	-	41.51	21890473
124	Phosphorylation	VKPGAHLTVKKIFVG CCCCCEEEEEEEEEC	22.03	25159151
126	2-Hydroxyisobutyrylation	PGAHLTVKKIFVGGI CCCEEEEEEEEECCC	34.61	-
126	Acetylation	PGAHLTVKKIFVGGI CCCEEEEEEEEECCC	34.61	25953088
126	Ubiquitination	PGAHLTVKKIFVGGI CCCEEEEEEEEECCC	34.61	-
126 (in isoform 2)	Ubiquitination	-	34.61	21890473
127	Methylation	GAHLTVKKIFVGGIK CCEEEEEEEEECCCC	36.72	24624369
127	Ubiquitination	GAHLTVKKIFVGGIK CCEEEEEEEEECCCC	36.72	-
129 (in isoform 2)	Ubiquitination	-	6.00	21890473
134	Sumoylation	KIFVGGIKEDTEEYN EEEECCCCCCCCCCC	53.46	-
134	Acetylation	KIFVGGIKEDTEEYN EEEECCCCCCCCCCC	53.46	19608861
134	Malonylation	KIFVGGIKEDTEEYN EEEECCCCCCCCCCC	53.46	26320211
134	Sumoylation	KIFVGGIKEDTEEYN EEEECCCCCCCCCCC	53.46	28112733
134	Ubiquitination	KIFVGGIKEDTEEYN EEEECCCCCCCCCCC	53.46	21906983
134 (in isoform 1)	Ubiquitination	-	53.46	21890473
137	Phosphorylation	VGGIKEDTEEYNLRD ECCCCCCCCCCCHHH	31.63	28152594
140	Phosphorylation	IKEDTEEYNLRDYFE CCCCCCCCCHHHHHH	17.17	28152594
143	Methylation	DTEEYNLRDYFEKYG CCCCCCHHHHHHHHC	32.71	115478955
145	Phosphorylation	EEYNLRDYFEKYGKI CCCCHHHHHHHHCCE	13.75	-
148	2-Hydroxyisobutyrylation	NLRDYFEKYGKIETI CHHHHHHHHCCEEEE	49.78	-
148	Acetylation	NLRDYFEKYGKIETI CHHHHHHHHCCEEEE	49.78	25825284
148	Malonylation	NLRDYFEKYGKIETI CHHHHHHHHCCEEEE	49.78	26320211
148	Ubiquitination	NLRDYFEKYGKIETI CHHHHHHHHCCEEEE	49.78	21890473
148 (in isoform 1)	Ubiquitination	-	49.78	21890473
149	Phosphorylation	LRDYFEKYGKIETIE HHHHHHHHCCEEEEE	19.22	29438985
151	Sumoylation	DYFEKYGKIETIEVM HHHHHHCCEEEEEEE	33.99	-
151	Acetylation	DYFEKYGKIETIEVM HHHHHHCCEEEEEEE	33.99	19608861
151	Malonylation	DYFEKYGKIETIEVM HHHHHHCCEEEEEEE	33.99	26320211
151	Sumoylation	DYFEKYGKIETIEVM HHHHHHCCEEEEEEE	33.99	28112733
151	Ubiquitination	DYFEKYGKIETIEVM HHHHHHCCEEEEEEE	33.99	21890473
151 (in isoform 1)	Ubiquitination	-	33.99	21890473
158	Sulfoxidation	KIETIEVMEDRQSGK CEEEEEEEEHHHCCC	2.62	21406390
161	Methylation	TIEVMEDRQSGKKRG EEEEEEHHHCCCCCE	21.18	115478971
163	Phosphorylation	EVMEDRQSGKKRGFA EEEEHHHCCCCCEEE	54.17	30108239
167	Methylation	DRQSGKKRGFAFVTF HHHCCCCCEEEEEEC	49.28	115478987
173	O-linked_Glycosylation	KRGFAFVTFDDHDTV CCEEEEEECCCCCCC	18.20	23301498
179	Phosphorylation	VTFDDHDTVDKIVVQ EECCCCCCCEEEEEE	27.47	26546556
182	2-Hydroxyisobutyrylation	DDHDTVDKIVVQKYH CCCCCCEEEEEEEEC	32.82	-
182	Acetylation	DDHDTVDKIVVQKYH CCCCCCEEEEEEEEC	32.82	25953088
182	Sumoylation	DDHDTVDKIVVQKYH CCCCCCEEEEEEEEC	32.82	28112733
182	Ubiquitination	DDHDTVDKIVVQKYH CCCCCCEEEEEEEEC	32.82	-
187	Acetylation	VDKIVVQKYHTINGH CEEEEEEEECCCCCC	27.65	23236377
187	Malonylation	VDKIVVQKYHTINGH CEEEEEEEECCCCCC	27.65	26320211
187	Ubiquitination	VDKIVVQKYHTINGH CEEEEEEEECCCCCC	27.65	-
188	Phosphorylation	DKIVVQKYHTINGHN EEEEEEEECCCCCCC	6.26	28152594
190	Phosphorylation	IVVQKYHTINGHNCE EEEEEECCCCCCCHH	17.04	28152594
199	2-Hydroxyisobutyrylation	NGHNCEVKKALSKQE CCCCHHHHHHCCHHH	15.27	-
199	Acetylation	NGHNCEVKKALSKQE CCCCHHHHHHCCHHH	15.27	23749302
199	Ubiquitination	NGHNCEVKKALSKQE CCCCHHHHHHCCHHH	15.27	-
200	Acetylation	GHNCEVKKALSKQEM CCCHHHHHHCCHHHH	60.79	7613293
200	Ubiquitination	GHNCEVKKALSKQEM CCCHHHHHHCCHHHH	60.79	-
204	Ubiquitination	EVKKALSKQEMQSAG HHHHHCCHHHHHHHC	51.64	-
209	Phosphorylation	LSKQEMQSAGSQRGR CCHHHHHHHCCCCCC	33.03	29449344
212	Phosphorylation	QEMQSAGSQRGRGGG HHHHHHCCCCCCCCC	19.20	24719451
214	Asymmetric dimethylarginine	MQSAGSQRGRGGGSG HHHHCCCCCCCCCCC	38.17	-
214	Methylation	MQSAGSQRGRGGGSG HHHHCCCCCCCCCCC	38.17	24129315
216	Asymmetric dimethylarginine	SAGSQRGRGGGSGNF HHCCCCCCCCCCCCC	42.65	-
216	Methylation	SAGSQRGRGGGSGNF HHCCCCCCCCCCCCC	42.65	12018831
220	Phosphorylation	QRGRGGGSGNFMGRG CCCCCCCCCCCCCCC	33.56	-
226	Asymmetric dimethylarginine	GSGNFMGRGGNFGGG CCCCCCCCCCCCCCC	37.75	-
226	Methylation	GSGNFMGRGGNFGGG CCCCCCCCCCCCCCC	37.75	24129315
239	Asymmetric dimethylarginine	GGGGNFGRGGNFGGR CCCCCCCCCCCCCCC	45.79	-
239	Methylation	GGGGNFGRGGNFGGR CCCCCCCCCCCCCCC	45.79	24129315
246	Asymmetric dimethylarginine	RGGNFGGRGGYGGGG CCCCCCCCCCCCCCC	35.42	-
246	Methylation	RGGNFGGRGGYGGGG CCCCCCCCCCCCCCC	35.42	24129315
257	Methylation	GGGGGGSRGSYGGGD CCCCCCCCCCCCCCC	41.15	12018879
259	Phosphorylation	GGGGSRGSYGGGDGG CCCCCCCCCCCCCCC	21.35	-
260	Phosphorylation	GGGSRGSYGGGDGGY CCCCCCCCCCCCCCC	23.71	-
267	Phosphorylation	YGGGDGGYNGFGGDG CCCCCCCCCCCCCCC	20.03	28985074
284	Phosphorylation	YGGGPGYSSRGGYGG CCCCCCCCCCCCCCC	21.34	28985074
285	Phosphorylation	GGGPGYSSRGGYGGG CCCCCCCCCCCCCCC	26.85	-
286	Asymmetric dimethylarginine	GGPGYSSRGGYGGGG CCCCCCCCCCCCCCC	36.29	-
286	Methylation	GGPGYSSRGGYGGGG CCCCCCCCCCCCCCC	36.29	18600967
336	Phosphorylation	YNDFGNYSGQQQSNY CCCCCCCCCCCCCCC	33.84	29460479
341	Phosphorylation	NYSGQQQSNYGPMKG CCCCCCCCCCCCCCC	27.90	29460479
343	Phosphorylation	SGQQQSNYGPMKGGS CCCCCCCCCCCCCCC	28.05	-
347	Sumoylation	QSNYGPMKGGSFGGR CCCCCCCCCCCCCCC	64.35	-
350	Phosphorylation	YGPMKGGSFGGRSSG CCCCCCCCCCCCCCC	29.41	23927012
354	Methylation	KGGSFGGRSSGSPYG CCCCCCCCCCCCCCC	28.20	24129315
355	Phosphorylation	GGSFGGRSSGSPYGG CCCCCCCCCCCCCCC	42.18	22167270
356	Phosphorylation	GSFGGRSSGSPYGGG CCCCCCCCCCCCCCC	41.76	19664994
358	Phosphorylation	FGGRSSGSPYGGGYG CCCCCCCCCCCCCCC	19.52	22167270
360	Phosphorylation	GRSSGSPYGGGYGSG CCCCCCCCCCCCCCC	30.05	23927012
364	Phosphorylation	GSPYGGGYGSGGGSG CCCCCCCCCCCCCCC	16.05	22167270
366	Phosphorylation	PYGGGYGSGGGSGGY CCCCCCCCCCCCCCC	26.27	22167270
370	Phosphorylation	GYGSGGGSGGYGSRR CCCCCCCCCCCCCCC	32.11	23927012
373	Phosphorylation	SGGGSGGYGSRRF-- CCCCCCCCCCCCC--	18.56	21945579
375	Phosphorylation	GGSGGYGSRRF---- CCCCCCCCCCC----	16.29	21945579
376	Methylation	GSGGYGSRRF----- CCCCCCCCCC-----	39.39	18967029
377	Methylation	SGGYGSRRF------ CCCCCCCCC------	43.24	18966659

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 ROA3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ROA3_HUMAN !!

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 ROA3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRRM2_HUMAN	SRRM2	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RT26_HUMAN	MRPS26	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
AT1B1_HUMAN	ATP1B1	physical	26344197
CHM2A_HUMAN	CHMP2A	physical	26344197
CYB5B_HUMAN	CYB5B	physical	26344197
DDX17_HUMAN	DDX17	physical	26344197
FPPS_HUMAN	FDPS	physical	26344197
ROAA_HUMAN	HNRNPAB	physical	26344197
HNRPF_HUMAN	HNRNPF	physical	26344197
HNRH1_HUMAN	HNRNPH1	physical	26344197
HNRH2_HUMAN	HNRNPH2	physical	26344197
HNRH3_HUMAN	HNRNPH3	physical	26344197
ITPA_HUMAN	ITPA	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
PTBP1_HUMAN	PTBP1	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
RAB7A_HUMAN	RAB7A	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197

Drug and Disease Associations

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

Regulatory Network of ROA3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-355; SER-356; SER-358; TYR-360; TYR-364;SER-366 AND SER-370, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29; LYS-134; LYS-148 ANDLYS-151, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; TYR-360; TYR-364;SER-366 AND SER-370, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-355; SER-356; SER-358; TYR-360; TYR-364;SER-366 AND SER-370, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-360 AND SER-366, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-366, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-358, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-355, ANDMASS SPECTROMETRY.	17287340 [Abstract]