dbPTM

ROA0_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROA0_HUMAN
UniProt AC	Q13151
Protein Name	Heterogeneous nuclear ribonucleoprotein A0
Gene Name	HNRNPA0
Organism	Homo sapiens (Human).
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	MENSQLCKLFIGGLNVQTSESGLRGHFEAFGTLTDCVVVVNPQTKRSRCFGFVTYSNVEEADAAMAASPHAVDGNTVELKRAVSREDSARPGAHAKVKKLFVGGLKGDVAEGDLIEHFSQFGTVEKAEIIADKQSGKKRGFGFVYFQNHDAADKAAVVKFHPIQGHRVEVKKAVPKEDIYSGGGGGGSRSSRGGRGGRGRGGGRDQNGLSKGGGGGYNSYGGYGGGGGGGYNAYGGGGGGSSYGGSDYGNGFGGFGSYSQHQSSYGPMKSGGGGGGGGSSWGGRSNSGPYRGGYGGGGGYGGSSF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MENSQLCK -------CCHHHHHH	11.25	22223895
4	Phosphorylation	----MENSQLCKLFI ----CCHHHHHHHHH	15.95	28857561
8	Ubiquitination	MENSQLCKLFIGGLN CCHHHHHHHHHCCCC	55.83	22505724
18	Phosphorylation	IGGLNVQTSESGLRG HCCCCCCCCCCCHHC	30.13	30266825
19	O-linked_Glycosylation	GGLNVQTSESGLRGH CCCCCCCCCCCHHCC	16.81	30059200
19	Phosphorylation	GGLNVQTSESGLRGH CCCCCCCCCCCHHCC	16.81	30266825
21	O-linked_Glycosylation	LNVQTSESGLRGHFE CCCCCCCCCHHCCEE	42.78	30059200
21	Phosphorylation	LNVQTSESGLRGHFE CCCCCCCCCHHCCEE	42.78	30266825
36	Glutathionylation	AFGTLTDCVVVVNPQ EECEECCEEEEECCC	1.79	22555962
45	Acetylation	VVVNPQTKRSRCFGF EEECCCCCCCCEEEE	43.03	26051181
45	Ubiquitination	VVVNPQTKRSRCFGF EEECCCCCCCCEEEE	43.03	21906983
47	Phosphorylation	VNPQTKRSRCFGFVT ECCCCCCCCEEEEEE	34.65	-
49	Glutathionylation	PQTKRSRCFGFVTYS CCCCCCCEEEEEEEC	4.05	22555962
54	Phosphorylation	SRCFGFVTYSNVEEA CCEEEEEEECCHHHH	20.97	21406692
55	Phosphorylation	RCFGFVTYSNVEEAD CEEEEEEECCHHHHH	7.92	21406692
56	Phosphorylation	CFGFVTYSNVEEADA EEEEEEECCHHHHHH	25.65	22210691
68	Phosphorylation	ADAAMAASPHAVDGN HHHHHHCCCCCCCCC	14.00	17001009
76	Phosphorylation	PHAVDGNTVELKRAV CCCCCCCCCHHHHHH	22.38	21406692
80	Ubiquitination	DGNTVELKRAVSRED CCCCCHHHHHHCCHH	25.46	21963094
80	Sumoylation	DGNTVELKRAVSRED CCCCCHHHHHHCCHH	25.46	28112733
84	Phosphorylation	VELKRAVSREDSARP CHHHHHHCCHHHCCC	29.03	23401153
88	Phosphorylation	RAVSREDSARPGAHA HHHCCHHHCCCCCCH	22.79	26055452
96	Sumoylation	ARPGAHAKVKKLFVG CCCCCCHHHEEEEEC	44.73	-
96	Ubiquitination	ARPGAHAKVKKLFVG CCCCCCHHHEEEEEC	44.73	23000965
96	Acetylation	ARPGAHAKVKKLFVG CCCCCCHHHEEEEEC	44.73	23749302
96	Sumoylation	ARPGAHAKVKKLFVG CCCCCCHHHEEEEEC	44.73	28112733
98	Sumoylation	PGAHAKVKKLFVGGL CCCCHHHEEEEECCC	42.95	28112733
98	Ubiquitination	PGAHAKVKKLFVGGL CCCCHHHEEEEECCC	42.95	23000965
99	Ubiquitination	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	23000965
99	Sumoylation	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	-
99	Sumoylation	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	28112733
99	Malonylation	GAHAKVKKLFVGGLK CCCHHHEEEEECCCC	50.58	26320211
106	Sumoylation	KLFVGGLKGDVAEGD EEEECCCCCCCCCCC	57.23	-
106	Neddylation	KLFVGGLKGDVAEGD EEEECCCCCCCCCCC	57.23	32015554
106	Ubiquitination	KLFVGGLKGDVAEGD EEEECCCCCCCCCCC	57.23	21906983
106	Sumoylation	KLFVGGLKGDVAEGD EEEECCCCCCCCCCC	57.23	28112733
106	Acetylation	KLFVGGLKGDVAEGD EEEECCCCCCCCCCC	57.23	25953088
119	Phosphorylation	GDLIEHFSQFGTVEK CCHHHHHHHCCCEEE	26.89	28857561
123	Phosphorylation	EHFSQFGTVEKAEII HHHHHCCCEEEEEEE	27.12	28555341
126	Sumoylation	SQFGTVEKAEIIADK HHCCCEEEEEEEEEC	47.16	-
126	Sumoylation	SQFGTVEKAEIIADK HHCCCEEEEEEEEEC	47.16	-
126	Ubiquitination	SQFGTVEKAEIIADK HHCCCEEEEEEEEEC	47.16	32015554
133	Acetylation	KAEIIADKQSGKKRG EEEEEEECCCCCCCE	37.02	23749302
133	Ubiquitination	KAEIIADKQSGKKRG EEEEEEECCCCCCCE	37.02	27667366
133	Sumoylation	KAEIIADKQSGKKRG EEEEEEECCCCCCCE	37.02	-
133	Sumoylation	KAEIIADKQSGKKRG EEEEEEECCCCCCCE	37.02	-
133	Malonylation	KAEIIADKQSGKKRG EEEEEEECCCCCCCE	37.02	26320211
135	Phosphorylation	EIIADKQSGKKRGFG EEEEECCCCCCCEEE	59.32	25159151
137	Ubiquitination	IADKQSGKKRGFGFV EEECCCCCCCEEEEE	44.54	22817900
138	Ubiquitination	ADKQSGKKRGFGFVY EECCCCCCCEEEEEE	62.37	22817900
138	Sumoylation	ADKQSGKKRGFGFVY EECCCCCCCEEEEEE	62.37	-
138	Sumoylation	ADKQSGKKRGFGFVY EECCCCCCCEEEEEE	62.37	-
139	Methylation	DKQSGKKRGFGFVYF ECCCCCCCEEEEEEE	49.51	24129315
145	Phosphorylation	KRGFGFVYFQNHDAA CCEEEEEEEECCCCC	9.37	20090780
154	Ubiquitination	QNHDAADKAAVVKFH ECCCCCCCEEEEEEE	33.25	22505724
154	Sumoylation	QNHDAADKAAVVKFH ECCCCCCCEEEEEEE	33.25	-
154	Sumoylation	QNHDAADKAAVVKFH ECCCCCCCEEEEEEE	33.25	28112733
154	Acetylation	QNHDAADKAAVVKFH ECCCCCCCEEEEEEE	33.25	25953088
159	Sumoylation	ADKAAVVKFHPIQGH CCCEEEEEEECCCCC	31.21	28112733
159	Acetylation	ADKAAVVKFHPIQGH CCCEEEEEEECCCCC	31.21	25825284
159	Sumoylation	ADKAAVVKFHPIQGH CCCEEEEEEECCCCC	31.21	-
159	Ubiquitination	ADKAAVVKFHPIQGH CCCEEEEEEECCCCC	31.21	32015554
171	Sumoylation	QGHRVEVKKAVPKED CCCCEEEEECCCHHH	22.85	-
171	Sumoylation	QGHRVEVKKAVPKED CCCCEEEEECCCHHH	22.85	-
172	Sumoylation	GHRVEVKKAVPKEDI CCCEEEEECCCHHHC	60.85	-
172	Sumoylation	GHRVEVKKAVPKEDI CCCEEEEECCCHHHC	60.85	25218447
172	Ubiquitination	GHRVEVKKAVPKEDI CCCEEEEECCCHHHC	60.85	22505724
176	Sumoylation	EVKKAVPKEDIYSGG EEEECCCHHHCCCCC	62.51	-
176	Acetylation	EVKKAVPKEDIYSGG EEEECCCHHHCCCCC	62.51	26051181
176	Ubiquitination	EVKKAVPKEDIYSGG EEEECCCHHHCCCCC	62.51	24816145
176	Sumoylation	EVKKAVPKEDIYSGG EEEECCCHHHCCCCC	62.51	28112733
180	Phosphorylation	AVPKEDIYSGGGGGG CCCHHHCCCCCCCCC	17.37	27273156
181	Phosphorylation	VPKEDIYSGGGGGGS CCHHHCCCCCCCCCC	31.15	28102081
188	Phosphorylation	SGGGGGGSRSSRGGR CCCCCCCCCCCCCCC	32.06	23401153
189	Methylation	GGGGGGSRSSRGGRG CCCCCCCCCCCCCCC	41.76	18601045
190	Phosphorylation	GGGGGSRSSRGGRGG CCCCCCCCCCCCCCC	26.53	29438985
191	Phosphorylation	GGGGSRSSRGGRGGR CCCCCCCCCCCCCCC	33.56	29438985
192	Methylation	GGGSRSSRGGRGGRG CCCCCCCCCCCCCCC	53.48	115478887
195	Methylation	SRSSRGGRGGRGRGG CCCCCCCCCCCCCCC	47.41	115478891
198	Methylation	SRGGRGGRGRGGGRD CCCCCCCCCCCCCCC	34.16	115478897
200	Methylation	GGRGGRGRGGGRDQN CCCCCCCCCCCCCCC	38.94	115478903
204	Methylation	GRGRGGGRDQNGLSK CCCCCCCCCCCCCCC	45.69	115478909
211	Sumoylation	RDQNGLSKGGGGGYN CCCCCCCCCCCCCCC	67.62	-
217	Phosphorylation	SKGGGGGYNSYGGYG CCCCCCCCCCCCCCC	12.29	-
231	Phosphorylation	GGGGGGGYNAYGGGG CCCCCCCCCCCCCCC	10.41	-
234	Phosphorylation	GGGGYNAYGGGGGGS CCCCCCCCCCCCCCC	16.80	-
265	Phosphorylation	YSQHQSSYGPMKSGG CCCCCCCCCCCCCCC	30.41	-
269	Sumoylation	QSSYGPMKSGGGGGG CCCCCCCCCCCCCCC	49.43	-
270	Phosphorylation	SSYGPMKSGGGGGGG CCCCCCCCCCCCCCC	36.10	22199227
279	Phosphorylation	GGGGGGGSSWGGRSN CCCCCCCCCCCCCCC	26.62	28450419
280	Phosphorylation	GGGGGGSSWGGRSNS CCCCCCCCCCCCCCC	32.77	28450419
284	Methylation	GGSSWGGRSNSGPYR CCCCCCCCCCCCCCC	28.82	24129315
291	Asymmetric dimethylarginine	RSNSGPYRGGYGGGG CCCCCCCCCCCCCCC	34.88	-
291	Methylation	RSNSGPYRGGYGGGG CCCCCCCCCCCCCCC	34.88	24129315
303	Phosphorylation	GGGGYGGSSF----- CCCCCCCCCC-----	24.98	-

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	P49137	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
84	S	Phosphorylation	20932473
Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA.
291	R	Methylation
Arg-291 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRSF5_HUMAN	SRSF5	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
SPF27_HUMAN	BCAS2	physical	22939629
THOC6_HUMAN	THOC6	physical	22939629
ROAA_HUMAN	HNRNPAB	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22365833
SRSF1_HUMAN	SRSF1	physical	22365833
DDX5_HUMAN	DDX5	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
CIRBP_HUMAN	CIRBP	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
HNRH2_HUMAN	HNRNPH2	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
GA45A_HUMAN	GADD45A	physical	20932473
DHX9_HUMAN	DHX9	physical	22863883
DC1I2_HUMAN	DYNC1I2	physical	22863883
PSD13_HUMAN	PSMD13	physical	22863883
PSMD8_HUMAN	PSMD8	physical	22863883

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 ROA0_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, AND MASS SPECTROMETRY.	19413330 [Abstract]
Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-291, AND MASS SPECTROMETRY.	15782174 [Abstract]
Phosphorylation
Reference	PubMed
"DNA damage activates a spatially distinct late cytoplasmic cell-cyclecheckpoint network controlled by MK2-mediated RNA stabilization."; Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S.,van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A.,Yaffe M.B.; Mol. Cell 40:34-49(2010). Cited for: RNA-BINDING, AND PHOSPHORYLATION AT SER-84 BY MAPKAPK2.	20932473 [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-84, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND MASSSPECTROMETRY.	15592455 [Abstract]

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