dbPTM

ROA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROA2_HUMAN
UniProt AC	P22626
Protein Name	Heterogeneous nuclear ribonucleoproteins A2/B1
Gene Name	HNRNPA2B1
Organism	Homo sapiens (Human).
Sequence Length	353
Subcellular Localization	Nucleus, nucleoplasm . Cytoplasmic granule . Secreted, exosome . Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). Component of ribonucleosomes (PubMed:17289661). Not found in the nucleolus (PubMed:17289661). Fou
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. [PubMed: 19099192 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]
Protein Sequence	MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEKTLETV -------CCCCCCCC	12.29	22814378
3	Acetylation	-----MEKTLETVPL -----CCCCCCCCCC	58.05	23749302
3	Ubiquitination	-----MEKTLETVPL -----CCCCCCCCCC	58.05	23000965
4	Phosphorylation	----MEKTLETVPLE ----CCCCCCCCCCH	19.27	25159151
5	Ubiquitination	---MEKTLETVPLER ---CCCCCCCCCCHH	8.44	23000965
5 (in isoform 2)	Sumoylation	-	8.44	-
7	Phosphorylation	-MEKTLETVPLERKK -CCCCCCCCCCHHHH	30.45	23403867
10	Ubiquitination	KTLETVPLERKKREK CCCCCCCCHHHHHHH	9.63	21890473
10 (in isoform 2)	Ubiquitination	-	9.63	21890473
13	Sumoylation	ETVPLERKKREKEQF CCCCCHHHHHHHHHH	46.97	-
13	Ubiquitination	ETVPLERKKREKEQF CCCCCHHHHHHHHHH	46.97	29967540
17	Acetylation	LERKKREKEQFRKLF CHHHHHHHHHHHHHH	61.93	25953088
17	Ubiquitination	LERKKREKEQFRKLF CHHHHHHHHHHHHHH	61.93	23000965
22	Acetylation	REKEQFRKLFIGGLS HHHHHHHHHHCCCCC	49.38	25825284
22	Sumoylation	REKEQFRKLFIGGLS HHHHHHHHHHCCCCC	49.38	28112733
22	Ubiquitination	REKEQFRKLFIGGLS HHHHHHHHHHCCCCC	49.38	21890473
22 (in isoform 1)	Ubiquitination	-	49.38	21890473
29	Phosphorylation	KLFIGGLSFETTEES HHHCCCCCCCCCHHH	25.06	22617229
32	Phosphorylation	IGGLSFETTEESLRN CCCCCCCCCHHHHHH	37.18	30108239
33	Phosphorylation	GGLSFETTEESLRNY CCCCCCCCHHHHHHH	30.47	20873877
34	Ubiquitination	GLSFETTEESLRNYY CCCCCCCHHHHHHHH	53.67	23000965
34 (in isoform 2)	Ubiquitination	-	53.67	21890473
36	Phosphorylation	SFETTEESLRNYYEQ CCCCCHHHHHHHHHH	26.79	21712546
38	Methylation	ETTEESLRNYYEQWG CCCHHHHHHHHHHHC	38.08	58857875
40	Phosphorylation	TEESLRNYYEQWGKL CHHHHHHHHHHHCCC	11.27	28152594
41	Phosphorylation	EESLRNYYEQWGKLT HHHHHHHHHHHCCCE	12.75	28152594
46	Acetylation	NYYEQWGKLTDCVVM HHHHHHCCCEEEEEE	45.30	25825284
46	Methylation	NYYEQWGKLTDCVVM HHHHHHCCCEEEEEE	45.30	30582813
46	Sumoylation	NYYEQWGKLTDCVVM HHHHHHCCCEEEEEE	45.30	-
46	Ubiquitination	NYYEQWGKLTDCVVM HHHHHHCCCEEEEEE	45.30	23000965
46 (in isoform 1)	Ubiquitination	-	45.30	21890473
47	Ubiquitination	YYEQWGKLTDCVVMR HHHHHCCCEEEEEEC	4.26	23000965
47 (in isoform 2)	Ubiquitination	-	4.26	21890473
48	O-linked_Glycosylation	YEQWGKLTDCVVMRD HHHHCCCEEEEEECC	30.73	30059200
48	Phosphorylation	YEQWGKLTDCVVMRD HHHHCCCEEEEEECC	30.73	20068231
53	Sulfoxidation	KLTDCVVMRDPASKR CCEEEEEECCCCCCC	1.68	21406390
58	Phosphorylation	VVMRDPASKRSRGFG EEECCCCCCCCCCCE	33.71	23898821
59	Acetylation	VMRDPASKRSRGFGF EECCCCCCCCCCCEE	57.40	23749302
59	Ubiquitination	VMRDPASKRSRGFGF EECCCCCCCCCCCEE	57.40	23000965
59 (in isoform 1)	Ubiquitination	-	57.40	21890473
68	Phosphorylation	SRGFGFVTFSSMAEV CCCCEEEEEHHHHHH	18.62	27251275
70	Phosphorylation	GFGFVTFSSMAEVDA CCEEEEEHHHHHHHH	15.16	23898821
71	Phosphorylation	FGFVTFSSMAEVDAA CEEEEEHHHHHHHHH	20.16	23836654
73	Phosphorylation	FVTFSSMAEVDAAMA EEEEHHHHHHHHHHH	18.66	32645325
73 (in isoform 2)	Phosphorylation	-	18.66	-
85	Phosphorylation	AMAARPHSIDGRVVE HHHCCCCCCCCEECC	25.67	30266825
92	Ubiquitination	SIDGRVVEPKRAVAR CCCCEECCCCCHHHH	42.10	23000965
92 (in isoform 2)	Ubiquitination	-	42.10	21890473
94	Acetylation	DGRVVEPKRAVAREE CCEECCCCCHHHHHH	39.21	30582801
94	Ubiquitination	DGRVVEPKRAVAREE CCEECCCCCHHHHHH	39.21	-
100	Neddylation	PKRAVAREESGKPGA CCCHHHHHHCCCCCC	46.94	32015554
100	Ubiquitination	PKRAVAREESGKPGA CCCHHHHHHCCCCCC	46.94	27667366
100 (in isoform 2)	Ubiquitination	-	46.94	21890473
101	Acetylation	KRAVAREESGKPGAH CCHHHHHHCCCCCCE	60.27	19413330
101	Ubiquitination	KRAVAREESGKPGAH CCHHHHHHCCCCCCE	60.27	19413330
101 (in isoform 2)	Acetylation	-	60.27	-
102	Phosphorylation	RAVAREESGKPGAHV CHHHHHHCCCCCCEE	47.57	23401153
104	"N6,N6-dimethyllysine"	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	-
104	Acetylation	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	25953088
104	Methylation	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	23161681
104	Sumoylation	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	28112733
104	Ubiquitination	VAREESGKPGAHVTV HHHHHCCCCCCEEEE	49.94	23000965
104 (in isoform 1)	Ubiquitination	-	49.94	21890473
108	Neddylation	ESGKPGAHVTVKKLF HCCCCCCEEEEEEEE	22.99	32015554
108	Ubiquitination	ESGKPGAHVTVKKLF HCCCCCCEEEEEEEE	22.99	21890473
108 (in isoform 2)	Ubiquitination	-	22.99	21890473
110	Phosphorylation	GKPGAHVTVKKLFVG CCCCCEEEEEEEEEC	19.42	21406692
112	Acetylation	PGAHVTVKKLFVGGI CCCEEEEEEEEECCC	34.10	23749302
112	Neddylation	PGAHVTVKKLFVGGI CCCEEEEEEEEECCC	34.10	32015554
112	Sumoylation	PGAHVTVKKLFVGGI CCCEEEEEEEEECCC	34.10	28112733
112	Ubiquitination	PGAHVTVKKLFVGGI CCCEEEEEEEEECCC	34.10	21906983
112 (in isoform 1)	Ubiquitination	-	34.10	21890473
113	Acetylation	GAHVTVKKLFVGGIK CCEEEEEEEEECCCC	42.70	19413330
113	Malonylation	GAHVTVKKLFVGGIK CCEEEEEEEEECCCC	42.70	26320211
113	Ubiquitination	GAHVTVKKLFVGGIK CCEEEEEEEEECCCC	42.70	19413330
120	Sumoylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	-
120	Acetylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	23954790
120	Malonylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	26320211
120	Neddylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	32015554
120	Sumoylation	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	28112733
120	Ubiquitination	KLFVGGIKEDTEEHH EEEECCCCCCCCHHH	53.46	23000965
120 (in isoform 1)	Ubiquitination	-	53.46	21890473
125	Ubiquitination	GIKEDTEEHHLRDYF CCCCCCCHHHHHHHH	38.40	32015554
125 (in isoform 2)	Ubiquitination	-	38.40	21890473
129	Methylation	DTEEHHLRDYFEEYG CCCHHHHHHHHHHHC	32.02	115478939
131	Phosphorylation	EEHHLRDYFEEYGKI CHHHHHHHHHHHCCC	13.37	-
135	Phosphorylation	LRDYFEEYGKIDTIE HHHHHHHHCCCCEEE	19.27	25159151
137	Sumoylation	DYFEEYGKIDTIEII HHHHHHCCCCEEEEE	36.19	28112733
137	Ubiquitination	DYFEEYGKIDTIEII HHHHHHCCCCEEEEE	36.19	21906983
137 (in isoform 1)	Ubiquitination	-	36.19	21890473
137 (in isoform 2)	Phosphorylation	-	36.19	-
139	Neddylation	FEEYGKIDTIEIITD HHHHCCCCEEEEEEC	45.15	32015554
139	Ubiquitination	FEEYGKIDTIEIITD HHHHCCCCEEEEEEC	45.15	29967540
140	Phosphorylation	EEYGKIDTIEIITDR HHHCCCCEEEEEECC	24.79	21815630
145	Phosphorylation	IDTIEIITDRQSGKK CCEEEEEECCCCCCC	30.69	30266825
147	Methylation	TIEIITDRQSGKKRG EEEEEECCCCCCCCE	24.74	115478947
149	Phosphorylation	EIITDRQSGKKRGFG EEEECCCCCCCCEEE	54.17	30266825
151	Neddylation	ITDRQSGKKRGFGFV EECCCCCCCCEEEEE	44.54	32015554
151	Sumoylation	ITDRQSGKKRGFGFV EECCCCCCCCEEEEE	44.54	-
151	Ubiquitination	ITDRQSGKKRGFGFV EECCCCCCCCEEEEE	44.54	29967540
152	Sumoylation	TDRQSGKKRGFGFVT ECCCCCCCCEEEEEE	62.37	28112733
153	Dimethylation	DRQSGKKRGFGFVTF CCCCCCCCEEEEEEE	49.51	-
153	Methylation	DRQSGKKRGFGFVTF CCCCCCCCEEEEEEE	49.51	81453655
156	Acetylation	SGKKRGFGFVTFDDH CCCCCEEEEEEECCC	20.95	19608861
156	Ubiquitination	SGKKRGFGFVTFDDH CCCCCEEEEEEECCC	20.95	23000965
156 (in isoform 2)	Acetylation	-	20.95	-
156 (in isoform 2)	Ubiquitination	-	20.95	21890473
159	Phosphorylation	KRGFGFVTFDDHDPV CCEEEEEEECCCCCH	21.05	28450419
161	Acetylation	GFGFVTFDDHDPVDK EEEEEEECCCCCHHH	42.86	19608861
161	Ubiquitination	GFGFVTFDDHDPVDK EEEEEEECCCCCHHH	42.86	23000965
161 (in isoform 2)	Acetylation	-	42.86	-
161 (in isoform 2)	Ubiquitination	-	42.86	21890473
164 (in isoform 2)	Phosphorylation	-	52.49	-
168	Sumoylation	DDHDPVDKIVLQKYH CCCCCHHHHHHEEEC	34.64	-
168	Acetylation	DDHDPVDKIVLQKYH CCCCCHHHHHHEEEC	34.64	19608861
168	Sumoylation	DDHDPVDKIVLQKYH CCCCCHHHHHHEEEC	34.64	28112733
168	Ubiquitination	DDHDPVDKIVLQKYH CCCCCHHHHHHEEEC	34.64	23000965
168 (in isoform 1)	Ubiquitination	-	34.64	21890473
173	Sumoylation	VDKIVLQKYHTINGH HHHHHHEEECHHCCC	34.53	-
173	Acetylation	VDKIVLQKYHTINGH HHHHHHEEECHHCCC	34.53	19608861
173	Sumoylation	VDKIVLQKYHTINGH HHHHHHEEECHHCCC	34.53	28112733
173	Ubiquitination	VDKIVLQKYHTINGH HHHHHHEEECHHCCC	34.53	23000965
173 (in isoform 1)	Ubiquitination	-	34.53	21890473
174	Phosphorylation	DKIVLQKYHTINGHN HHHHHEEECHHCCCC	7.40	27155012
176	Phosphorylation	IVLQKYHTINGHNAE HHHEEECHHCCCCHH	17.04	27696853
177 (in isoform 2)	Phosphorylation	-	3.56	-
186	Sumoylation	GHNAEVRKALSRQEM CCCHHHHHHHCHHHH	59.87	-
186	Sumoylation	GHNAEVRKALSRQEM CCCHHHHHHHCHHHH	59.87	25218447
189	Phosphorylation	AEVRKALSRQEMQEV HHHHHHHCHHHHHHH	36.46	23927012
189 (in isoform 2)	Phosphorylation	-	36.46	-
191	Methylation	VRKALSRQEMQEVQS HHHHHCHHHHHHHHH	47.33	12509629
191 (in isoform 2)	Methylation	-	47.33	-
193	Sulfoxidation	KALSRQEMQEVQSSR HHHCHHHHHHHHHHC	2.89	28183972
198	Phosphorylation	QEMQEVQSSRSGRGG HHHHHHHHHCCCCCC	32.66	29255136
199	O-linked_Glycosylation	EMQEVQSSRSGRGGN HHHHHHHHCCCCCCC	17.24	30059200
199	Phosphorylation	EMQEVQSSRSGRGGN HHHHHHHHCCCCCCC	17.24	29255136
200	Methylation	MQEVQSSRSGRGGNF HHHHHHHCCCCCCCC	48.67	58857855
200 (in isoform 2)	Phosphorylation	-	48.67	-
201	Phosphorylation	QEVQSSRSGRGGNFG HHHHHHCCCCCCCCC	34.49	25159151
203	Asymmetric dimethylarginine	VQSSRSGRGGNFGFG HHHHCCCCCCCCCCC	51.60	-
203	Methylation	VQSSRSGRGGNFGFG HHHHCCCCCCCCCCC	51.60	136605
212	Phosphorylation	GNFGFGDSRGGGGNF CCCCCCCCCCCCCCC	32.95	29255136
213	Asymmetric dimethylarginine	NFGFGDSRGGGGNFG CCCCCCCCCCCCCCC	53.14	-
213	Methylation	NFGFGDSRGGGGNFG CCCCCCCCCCCCCCC	53.14	12018583
213	Phosphorylation	NFGFGDSRGGGGNFG CCCCCCCCCCCCCCC	53.14	32142685
213 (in isoform 2)	Phosphorylation	-	53.14	-
219 (in isoform 2)	Phosphorylation	-	16.47	-
225	Phosphorylation	NFGPGPGSNFRGGSD CCCCCCCCCCCCCCC	35.61	25159151
228	Dimethylation	PGPGSNFRGGSDGYG CCCCCCCCCCCCCCC	53.46	-
228	Methylation	PGPGSNFRGGSDGYG CCCCCCCCCCCCCCC	53.46	24129315
231	Phosphorylation	GSNFRGGSDGYGSGR CCCCCCCCCCCCCCC	30.59	28355574
232 (in isoform 2)	Phosphorylation	-	58.57	-
234	Phosphorylation	FRGGSDGYGSGRGFG CCCCCCCCCCCCCCC	17.07	28152594
236	Phosphorylation	GGSDGYGSGRGFGDG CCCCCCCCCCCCCCC	19.48	21712546
238	Methylation	SDGYGSGRGFGDGYN CCCCCCCCCCCCCCC	38.68	24129315
244	Phosphorylation	GRGFGDGYNGYGGGP CCCCCCCCCCCCCCC	15.34	21945579
247	Phosphorylation	FGDGYNGYGGGPGGG CCCCCCCCCCCCCCC	14.68	21945579
247 (in isoform 2)	Phosphorylation	-	14.68	-
250 (in isoform 2)	Phosphorylation	-	17.20	-
259	Phosphorylation	GGGNFGGSPGYGGGR CCCCCCCCCCCCCCC	18.61	22167270
262	Phosphorylation	NFGGSPGYGGGRGGY CCCCCCCCCCCCCCC	18.91	21945579
266	Asymmetric dimethylarginine	SPGYGGGRGGYGGGG CCCCCCCCCCCCCCC	38.34	-
266	Methylation	SPGYGGGRGGYGGGG CCCCCCCCCCCCCCC	38.34	24129315
269	Phosphorylation	YGGGRGGYGGGGPGY CCCCCCCCCCCCCCC	18.54	26074081
287	Phosphorylation	GGGYGGGYDNYGGGN CCCCCCCCCCCCCCC	12.32	-
290	Phosphorylation	YGGGYDNYGGGNYGS CCCCCCCCCCCCCCC	17.78	20007894
295	Phosphorylation	DNYGGGNYGSGNYND CCCCCCCCCCCCCCC	18.88	20007894
297	Phosphorylation	YGGGNYGSGNYNDFG CCCCCCCCCCCCCCC	17.32	-
300	Phosphorylation	GNYGSGNYNDFGNYN CCCCCCCCCCCCCCC	21.45	-
306	Acetylation	NYNDFGNYNQQPSNY CCCCCCCCCCCCCCC	18.09	19413330
306	Phosphorylation	NYNDFGNYNQQPSNY CCCCCCCCCCCCCCC	18.09	-
306 (in isoform 2)	Acetylation	-	18.09	-
311	Phosphorylation	GNYNQQPSNYGPMKS CCCCCCCCCCCCCCC	38.04	-
312 (in isoform 2)	Phosphorylation	-	53.08	-
313	Phosphorylation	YNQQPSNYGPMKSGN CCCCCCCCCCCCCCC	27.26	-
317	Sumoylation	PSNYGPMKSGNFGGS CCCCCCCCCCCCCCC	59.34	-
318	Acetylation	SNYGPMKSGNFGGSR CCCCCCCCCCCCCCC	32.49	19413330
318	Phosphorylation	SNYGPMKSGNFGGSR CCCCCCCCCCCCCCC	32.49	22115753
324	Phosphorylation	KSGNFGGSRNMGGPY CCCCCCCCCCCCCCC	22.36	25159151
325	Methylation	SGNFGGSRNMGGPYG CCCCCCCCCCCCCCC	40.19	24129315
327	Sulfoxidation	NFGGSRNMGGPYGGG CCCCCCCCCCCCCCC	6.80	28465586
329	Phosphorylation	GGSRNMGGPYGGGNY CCCCCCCCCCCCCCC	11.07	32142685
329 (in isoform 2)	Phosphorylation	-	11.07	-
331	Phosphorylation	SRNMGGPYGGGNYGP CCCCCCCCCCCCCCC	31.51	21945579
332	Phosphorylation	RNMGGPYGGGNYGPG CCCCCCCCCCCCCCC	40.44	32142685
332 (in isoform 2)	Phosphorylation	-	40.44	-
335 (in isoform 2)	Phosphorylation	-	41.69	-
336	Phosphorylation	GPYGGGNYGPGGSGG CCCCCCCCCCCCCCC	28.15	21945579
341	Phosphorylation	GNYGPGGSGGSGGYG CCCCCCCCCCCCCCC	45.99	22167270
344	Phosphorylation	GPGGSGGSGGYGGRS CCCCCCCCCCCCCCC	32.35	22167270
347	Phosphorylation	GSGGSGGYGGRSRY- CCCCCCCCCCCCCC-	21.67	23927012
350	Methylation	GSGGYGGRSRY---- CCCCCCCCCCC----	17.38	24129315
351	Phosphorylation	SGGYGGRSRY----- CCCCCCCCCC-----	38.92	27422710
352	Methylation	GGYGGRSRY------ CCCCCCCCC------	39.56	18966529
353	Acetylation	GYGGRSRY------- CCCCCCCC-------	24.93	19608861
353	Phosphorylation	GYGGRSRY------- CCCCCCCC-------	24.93	26074081

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
159	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
176	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSK21_HUMAN	CSNK2A1	physical	10381337
HNRPL_HUMAN	HNRNPL	physical	10441480
VHL_HUMAN	VHL	physical	11517223
ZMAT3_HUMAN	ZMAT3	physical	18519039
ROA3_HUMAN	HNRNPA3	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SRSF9_HUMAN	SRSF9	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
YBOX1_HUMAN	YBX1	physical	22939629
SRSF2_HUMAN	SRSF2	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RL40_HUMAN	UBA52	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
ROAA_HUMAN	HNRNPAB	physical	22939629
TPR_HUMAN	TPR	physical	22939629
TIM13_HUMAN	TIMM13	physical	22939629
SQSTM_HUMAN	SQSTM1	physical	22939629
S10AG_HUMAN	S100A16	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
ROA1_HUMAN	HNRNPA1	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
MRE11_HUMAN	MRE11A	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
RU2B_HUMAN	SNRPB2	physical	22863883
HNRPL_HUMAN	HNRNPL	physical	23976881
THIM_HUMAN	ACAA2	physical	26344197
AT1B1_HUMAN	ATP1B1	physical	26344197
4EBP2_HUMAN	EIF4EBP2	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
ROAA_HUMAN	HNRNPAB	physical	26344197
HNRPD_HUMAN	HNRNPD	physical	26344197
HNRDL_HUMAN	HNRNPDL	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
SERPH_HUMAN	SERPINH1	physical	26344197
EP300_HUMAN	EP300	physical	26774881
SPTA1_HUMAN	SPTA1	physical	16889989

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615422	Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ROA2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1; LYS-3; LYS-168 ANDLYS-173, AND MASS SPECTROMETRY.	19608861 [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-203, AND MASS SPECTROMETRY.	15782174 [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-85; SER-212; SER-259 ANDSER-344, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY.	19369195 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-344, ANDMASS 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 SER-212; SER-225; SER-259;SER-341 AND SER-344, AND MASS 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-259, 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-259 AND SER-341, ANDMASS SPECTROMETRY.	18220336 [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 THR-176; SER-212; SER-259;SER-341; SER-344 AND TYR-347, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.	15302935 [Abstract]

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