dbPTM

TRA2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRA2B_HUMAN
UniProt AC	P62995
Protein Name	Transformer-2 protein homolog beta
Gene Name	TRA2B
Organism	Homo sapiens (Human).
Sequence Length	288
Subcellular Localization	Nucleus .
Protein Description	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA..
Protein Sequence	MSDSGEQNYGERESRSASRSGSAHGSGKSARHTPARSRSKEDSRRSRSKSRSRSESRSRSRRSSRRHYTRSRSRSRSHRRSRSRSYSRDYRRRHSHSHSPMSTRRRHVGNRANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHTPTPGIYMGRPTYGSSRRRDYYDRGYDRGYDDRDYYSRSYRGGGGGGGGWRAAQDRDQIYRRRSPSPYYSRGGYRSRSRSRSYSPRRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDSGEQNY ------CCCCCCCCC	40.25	21406692
2	Phosphorylation	------MSDSGEQNY ------CCCCCCCCC	40.25	29255136
4	Phosphorylation	----MSDSGEQNYGE ----CCCCCCCCCCC	36.60	23401153
9	Phosphorylation	SDSGEQNYGERESRS CCCCCCCCCCCCCCC	21.76	17081983
14	Phosphorylation	QNYGERESRSASRSG CCCCCCCCCCCCCCC	37.44	29255136
16	Phosphorylation	YGERESRSASRSGSA CCCCCCCCCCCCCCC	39.62	25159151
18	Phosphorylation	ERESRSASRSGSAHG CCCCCCCCCCCCCCC	28.38	25159151
20	Phosphorylation	ESRSASRSGSAHGSG CCCCCCCCCCCCCCC	34.31	30576142
22	Phosphorylation	RSASRSGSAHGSGKS CCCCCCCCCCCCCCC	20.52	25849741
26	Phosphorylation	RSGSAHGSGKSARHT CCCCCCCCCCCCCCC	32.93	26055452
29	Phosphorylation	SAHGSGKSARHTPAR CCCCCCCCCCCCCCC	33.78	26055452
33	Phosphorylation	SGKSARHTPARSRSK CCCCCCCCCCCCCCH	17.06	26055452
37	Phosphorylation	ARHTPARSRSKEDSR CCCCCCCCCCHHHHH	42.91	26055452
39	Phosphorylation	HTPARSRSKEDSRRS CCCCCCCCHHHHHHH	41.46	22167270
40	Ubiquitination	TPARSRSKEDSRRSR CCCCCCCHHHHHHHH	65.51	23000965
40 (in isoform 3)	Ubiquitination	-	65.51	21890473
43	Phosphorylation	RSRSKEDSRRSRSKS CCCCHHHHHHHHHHH	30.59	22167270
46	Phosphorylation	SKEDSRRSRSKSRSR CHHHHHHHHHHHHHH	39.53	24719451
63	Phosphorylation	SRSRSRRSSRRHYTR HHHHHHHHHHHHHHH	27.38	17081983
68	Phosphorylation	RRSSRRHYTRSRSRS HHHHHHHHHHHHHHC	11.31	23663014
69	Phosphorylation	RSSRRHYTRSRSRSR HHHHHHHHHHHHHCH	18.95	20363803
71	Phosphorylation	SRRHYTRSRSRSRSH HHHHHHHHHHHCHHH	27.14	20363803
73	Ubiquitination	RHYTRSRSRSRSHRR HHHHHHHHHCHHHHH	35.54	33845483
73 (in isoform 3)	Ubiquitination	-	35.54	21890473
81	Phosphorylation	RSRSHRRSRSRSYSR HCHHHHHHHCHHCCH	34.27	22798277
83	Phosphorylation	RSHRRSRSRSYSRDY HHHHHHHCHHCCHHH	27.16	22167270
85	Phosphorylation	HRRSRSRSYSRDYRR HHHHHCHHCCHHHHH	28.80	22167270
86	Phosphorylation	RRSRSRSYSRDYRRR HHHHCHHCCHHHHHH	13.45	22167270
87	Phosphorylation	RSRSRSYSRDYRRRH HHHCHHCCHHHHHHH	21.66	22167270
90	Phosphorylation	SRSYSRDYRRRHSHS CHHCCHHHHHHHCCC	12.62	22167270
95	Phosphorylation	RDYRRRHSHSHSPMS HHHHHHHCCCCCCCC	25.52	29255136
97	Phosphorylation	YRRRHSHSHSPMSTR HHHHHCCCCCCCCHH	28.77	22167270
97	Ubiquitination	YRRRHSHSHSPMSTR HHHHHCCCCCCCCHH	28.77	23000965
97 (in isoform 3)	Ubiquitination	-	28.77	21890473
99	Phosphorylation	RRHSHSHSPMSTRRR HHHCCCCCCCCHHCC	25.88	29255136
101	Phosphorylation	HSHSHSPMSTRRRHV HCCCCCCCCHHCCCC	7.77	32645325
102	Phosphorylation	SHSHSPMSTRRRHVG CCCCCCCCHHCCCCC	23.34	29255136
103	Phosphorylation	HSHSPMSTRRRHVGN CCCCCCCHHCCCCCC	23.18	29255136
119	Glutathionylation	ANPDPNCCLGVFGLS CCCCCCCEEHHHCEE	4.75	22555962
140	Acetylation	DLREVFSKYGPIADV HHHHHHHHHCCCCEE	42.64	26051181
140	Ubiquitination	DLREVFSKYGPIADV HHHHHHHHHCCCCEE	42.64	23000965
140 (in isoform 1)	Ubiquitination	-	42.64	21890473
141	Methylation	LREVFSKYGPIADVS HHHHHHHHCCCCEEE	27.25	15782174
141	Phosphorylation	LREVFSKYGPIADVS HHHHHHHHCCCCEEE	27.25	28152594
148	Phosphorylation	YGPIADVSIVYDQQS HCCCCEEEEEEECCC	13.59	28555341
155	Phosphorylation	SIVYDQQSRRSRGFA EEEEECCCCCCCCEE	24.83	21712546
164	Phosphorylation	RSRGFAFVYFENVDD CCCCEEEEEEECCCC	4.86	32142685
166	Phosphorylation	RGFAFVYFENVDDAK CCEEEEEEECCCCHH	4.65	32142685
173	2-Hydroxyisobutyrylation	FENVDDAKEAKERAN EECCCCHHHHHHHHC	66.26	-
173	Acetylation	FENVDDAKEAKERAN EECCCCHHHHHHHHC	66.26	26051181
173	Ubiquitination	FENVDDAKEAKERAN EECCCCHHHHHHHHC	66.26	33845483
173 (in isoform 1)	Ubiquitination	-	66.26	21890473
176	Ubiquitination	VDDAKEAKERANGME CCCHHHHHHHHCCCE	49.15	-
187	Methylation	NGMELDGRRIRVDFS CCCEECCEEEEEEEE	30.44	-
194	Phosphorylation	RRIRVDFSITKRPHT EEEEEEEEEECCCCC	25.53	26074081
196	Phosphorylation	IRVDFSITKRPHTPT EEEEEEEECCCCCCC	21.58	26074081
197	2-Hydroxyisobutyrylation	RVDFSITKRPHTPTP EEEEEEECCCCCCCC	63.36	-
197	Acetylation	RVDFSITKRPHTPTP EEEEEEECCCCCCCC	63.36	25953088
197	Sumoylation	RVDFSITKRPHTPTP EEEEEEECCCCCCCC	63.36	28112733
197	Ubiquitination	RVDFSITKRPHTPTP EEEEEEECCCCCCCC	63.36	23000965
197 (in isoform 1)	Ubiquitination	-	63.36	21890473
201	Phosphorylation	SITKRPHTPTPGIYM EEECCCCCCCCCEEC	31.38	29255136
203	Phosphorylation	TKRPHTPTPGIYMGR ECCCCCCCCCEECCC	34.99	22167270
207	Phosphorylation	HTPTPGIYMGRPTYG CCCCCCEECCCCCCC	10.22	23927012
210	Methylation	TPGIYMGRPTYGSSR CCCEECCCCCCCCCC	12.12	54559211
212	Phosphorylation	GIYMGRPTYGSSRRR CEECCCCCCCCCCCC	38.87	25159151
213	Phosphorylation	IYMGRPTYGSSRRRD EECCCCCCCCCCCCC	20.07	23927012
215	Phosphorylation	MGRPTYGSSRRRDYY CCCCCCCCCCCCCCH	15.40	23927012
216	Phosphorylation	GRPTYGSSRRRDYYD CCCCCCCCCCCCCHH	25.99	23927012
217	Methylation	RPTYGSSRRRDYYDR CCCCCCCCCCCCHHC	39.07	-
221	Phosphorylation	GSSRRRDYYDRGYDR CCCCCCCCHHCCCCC	12.88	25367160
222	Phosphorylation	SSRRRDYYDRGYDRG CCCCCCCHHCCCCCC	11.94	25367160
224	Methylation	RRRDYYDRGYDRGYD CCCCCHHCCCCCCCC	29.47	81453753
226	Phosphorylation	RDYYDRGYDRGYDDR CCCHHCCCCCCCCCC	11.89	28152594
228	Methylation	YYDRGYDRGYDDRDY CHHCCCCCCCCCCCC	36.77	80701933
230	Phosphorylation	DRGYDRGYDDRDYYS HCCCCCCCCCCCCCC	18.63	28796482
233	Methylation	YDRGYDDRDYYSRSY CCCCCCCCCCCCCCC	30.82	81121037
235	Phosphorylation	RGYDDRDYYSRSYRG CCCCCCCCCCCCCCC	12.30	27273156
236	Phosphorylation	GYDDRDYYSRSYRGG CCCCCCCCCCCCCCC	11.25	28796482
237	Phosphorylation	YDDRDYYSRSYRGGG CCCCCCCCCCCCCCC	14.44	28796482
238	Methylation	DDRDYYSRSYRGGGG CCCCCCCCCCCCCCC	22.91	80701925
240	Phosphorylation	RDYYSRSYRGGGGGG CCCCCCCCCCCCCCC	16.50	-
241	Asymmetric dimethylarginine	DYYSRSYRGGGGGGG CCCCCCCCCCCCCCC	38.23	-
241	Methylation	DYYSRSYRGGGGGGG CCCCCCCCCCCCCCC	38.23	24129315
251	Methylation	GGGGGGWRAAQDRDQ CCCCCCCHHCCCHHH	24.26	80701941
256	Methylation	GWRAAQDRDQIYRRR CCHHCCCHHHHHHCC	26.17	115918885
260	Phosphorylation	AQDRDQIYRRRSPSP CCCHHHHHHCCCCCC	7.76	21609022
264	Phosphorylation	DQIYRRRSPSPYYSR HHHHHCCCCCCCCCC	28.11	26846344
266	Phosphorylation	IYRRRSPSPYYSRGG HHHCCCCCCCCCCCC	27.12	19664994
268	Phosphorylation	RRRSPSPYYSRGGYR HCCCCCCCCCCCCCC	20.57	20201521
269	Phosphorylation	RRSPSPYYSRGGYRS CCCCCCCCCCCCCCC	8.69	23927012
270	Phosphorylation	RSPSPYYSRGGYRSR CCCCCCCCCCCCCCC	20.71	26846344
271	Methylation	SPSPYYSRGGYRSRS CCCCCCCCCCCCCCC	26.83	115367923
274	Phosphorylation	PYYSRGGYRSRSRSR CCCCCCCCCCCCCCC	14.29	29116813
276	Phosphorylation	YSRGGYRSRSRSRSY CCCCCCCCCCCCCCC	26.56	29116813
278	Phosphorylation	RGGYRSRSRSRSYSP CCCCCCCCCCCCCCC	35.54	26846344
280	Phosphorylation	GYRSRSRSRSYSPRR CCCCCCCCCCCCCCC	27.16	26846344
282	Phosphorylation	RSRSRSRSYSPRRY- CCCCCCCCCCCCCC-	31.07	26846344
283	Phosphorylation	SRSRSRSYSPRRY-- CCCCCCCCCCCCC--	22.91	26846344
284	Phosphorylation	RSRSRSYSPRRY--- CCCCCCCCCCCC---	17.12	28355574
288	Phosphorylation	RSYSPRRY------- CCCCCCCC-------	24.96	21406692

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 TRA2B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
241	R	Methylation
Dimethylation at Arg-241 is probably asymmetric.

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 TRA2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBMX_HUMAN	RBMX	physical	12165565
SRSF9_HUMAN	SRSF9	physical	11875052
SAFB1_RAT	Safb	physical	9671816
SRSF3_HUMAN	SRSF3	physical	22365833
SRSF6_HUMAN	SRSF6	physical	22365833
ROA1_HUMAN	HNRNPA1	physical	22365833
SRSF4_HUMAN	SRSF4	physical	22365833
SRSF2_HUMAN	SRSF2	physical	22365833
RBMX_HUMAN	RBMX	physical	22365833
SRS10_HUMAN	SRSF10	physical	22365833
RNPS1_HUMAN	RNPS1	physical	14729963
YTDC1_HUMAN	YTHDC1	physical	21988832
DDX47_HUMAN	DDX47	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
4F2_HUMAN	SLC3A2	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 TRA2B_HUMAN

Related Literatures of Post-Translational Modification

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-241, AND MASS SPECTROMETRY.	15782174 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-14, AND MASSSPECTROMETRY.	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-83; SER-85; SER-87;THR-201 AND THR-212, 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-2; SER-14; SER-264 ANDSER-266, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.	19007248 [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-201; TYR-207; SER-215AND SER-216, AND MASS SPECTROMETRY.	17287340 [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-264 AND SER-266, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-29; THR-33;SER-37; SER-39; THR-69; SER-71; SER-95; SER-97; SER-99; SER-264;SER-266 AND SER-276, AND MASS SPECTROMETRY.	17081983 [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-264 AND SER-266, ANDMASS SPECTROMETRY.	15302935 [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-268 AND TYR-269, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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