RBM25_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RBM25_HUMAN
• UniProt AC: P49756
• Protein Name: RNA-binding protein 25
• Gene Name: RBM25
• Organism: Homo sapiens (Human).
• Sequence Length: 843
• Subcellular Localization: Nucleus speckle. Cytoplasm. Colocalizes predominantly, with SFRS2 and LUC7L3 splicing factors, in nuclear speckles. Cytoplasmic localization is faint.
• Protein Description: RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and truncated splice form of SCN5A in heart failure..
• Protein Sequence: MSFPPHLNRPPMGIPALPPGIPPPQFPGFPPPVPPGTPMIPVPMSIMAPAPTVLVPTVSMVGKHLGARKDHPGLKAKENDENCGPTTTVFVGNISEKASDMLIRQLLAKCGLVLSWKRVQGASGKLQAFGFCEYKEPESTLRALRLLHDLQIGEKKLLVKVDAKTKAQLDEWKAKKKASNGNARPETVTNDDEEALDEETKRRDQMIKGAIEVLIREYSSELNAPSQESDSHPRKKKKEKKEDIFRRFPVAPLIPYPLITKEDINAIEMEEDKRDLISREISKFRDTHKKLEEEKGKKEKERQEIEKERRERERERERERERREREREREREREREKEKERERERERDRDRDRTKERDRDRDRERDRDRDRERSSDRNKDRSRSREKSRDREREREREREREREREREREREREREREREREREREKDKKRDREEDEEDAYERRKLERKLREKEAAYQERLKNWEIRERKKTREYEKEAEREEERRREMAKEAKRLKEFLEDYDDDRDDPKYYRGSALQKRLRDREKEMEADERDRKREKEELEEIRQRLLAEGHPDPDAELQRMEQEAERRRQPQIKQEPESEEEEEEKQEKEEKREEPMEEEEEPEQKPCLKPTLRPISSAPSVSSASGNATPNTPGDESPCGIIIPHENSPDQQQPEEHRPKIGLSLKLGASNSPGQPNSVKRKKLPVDSVFNKFEDEDSDDVPRKRKLVPLDYGEDDKNATKGTVNTEEKRKHIKSLIEKIPTAKPELFAYPLDWSIVDSILMERRIRPWINKKIIEYIGEEEATLVDFVCSKVMAHSSPQSILDDVAMVLDEEAEVFIVKMWRLLIYETEAKKIGLVK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Ubiquitination	FPPPVPPGTPMIPVP CCCCCCCCCCCCCCC	36.06	24816145
63	Acetylation	PTVSMVGKHLGARKD CCHHHHHHHCCCCCC	25.01	30591799
77	Methylation	DHPGLKAKENDENCG CCCCCCCCCCCCCCC	56.30	23583077
77	Acetylation	DHPGLKAKENDENCG CCCCCCCCCCCCCCC	56.30	26051181
83	Glutathionylation	AKENDENCGPTTTVF CCCCCCCCCCCEEEE	6.94	22555962
90	Ubiquitination	CGPTTTVFVGNISEK CCCCEEEEECCCCHH	5.67	24816145
101	Sulfoxidation	ISEKASDMLIRQLLA CCHHHHHHHHHHHHH	2.88	21406390
117	Acetylation	CGLVLSWKRVQGASG CCCEEEEEECCCCCC	39.04	26051181
125	Acetylation	RVQGASGKLQAFGFC ECCCCCCCEEEECCC	34.62	23749302
135	Acetylation	AFGFCEYKEPESTLR EECCCCCCCCHHHHH	44.49	23954790
135	Malonylation	AFGFCEYKEPESTLR EECCCCCCCCHHHHH	44.49	26320211
155	Acetylation	HDLQIGEKKLLVKVD HHHCCCCCEEEEEEC	43.43	26051181
160	Ubiquitination	GEKKLLVKVDAKTKA CCCEEEEEECCCCHH	34.07	29967540
160	Malonylation	GEKKLLVKVDAKTKA CCCEEEEEECCCCHH	34.07	26320211
160	Acetylation	GEKKLLVKVDAKTKA CCCEEEEEECCCCHH	34.07	23236377
166	2-Hydroxyisobutyrylation	VKVDAKTKAQLDEWK EEECCCCHHHHHHHH	33.17	-
172	Phosphorylation	TKAQLDEWKAKKKAS CHHHHHHHHHHHHHC	12.94	18669648
173	Methylation	KAQLDEWKAKKKASN HHHHHHHHHHHHHCC	48.56	115976405
173	2-Hydroxyisobutyrylation	KAQLDEWKAKKKASN HHHHHHHHHHHHHCC	48.56	-
179	Phosphorylation	WKAKKKASNGNARPE HHHHHHHCCCCCCCC	54.90	-
187	Phosphorylation	NGNARPETVTNDDEE CCCCCCCCCCCCCHH	35.00	-
189	Phosphorylation	NARPETVTNDDEEAL CCCCCCCCCCCHHHC	40.11	-
200	Phosphorylation	EEALDEETKRRDQMI HHHCCHHHHHHHHHH	28.01	-
201	Acetylation	EALDEETKRRDQMIK HHCCHHHHHHHHHHH	49.03	26051181
218	Phosphorylation	IEVLIREYSSELNAP HHHHHHHHHHHHCCC	13.98	28152594
219	Phosphorylation	EVLIREYSSELNAPS HHHHHHHHHHHCCCC	16.75	28152594
220	Phosphorylation	VLIREYSSELNAPSQ HHHHHHHHHHCCCCC	45.24	28152594
224	Ubiquitination	EYSSELNAPSQESDS HHHHHHCCCCCCCCC	20.11	24816145
226	Phosphorylation	SSELNAPSQESDSHP HHHHCCCCCCCCCCC	44.14	28985074
229	Phosphorylation	LNAPSQESDSHPRKK HCCCCCCCCCCCCCC	36.45	25159151
231	Phosphorylation	APSQESDSHPRKKKK CCCCCCCCCCCCCHH	44.67	25159151
241	Ubiquitination	RKKKKEKKEDIFRRF CCCHHHHHHHHHHHC	62.81	24816145
256	Phosphorylation	PVAPLIPYPLITKED CCCCCCCCCCCCHHH	12.04	17360941
261	Acetylation	IPYPLITKEDINAIE CCCCCCCHHHHCCCC	46.53	18527743
261	Ubiquitination	IPYPLITKEDINAIE CCCCCCCHHHHCCCC	46.53	32015554
261	Sumoylation	IPYPLITKEDINAIE CCCCCCCHHHHCCCC	46.53	28112733
269	Sulfoxidation	EDINAIEMEEDKRDL HHHCCCCCCHHHHHH	5.81	21406390
272	Ubiquitination	NAIEMEEDKRDLISR CCCCCCHHHHHHHHH	37.67	22817900
273	Ubiquitination	AIEMEEDKRDLISRE CCCCCHHHHHHHHHH	51.60	29967540
273	Acetylation	AIEMEEDKRDLISRE CCCCCHHHHHHHHHH	51.60	26051181
273	Sumoylation	AIEMEEDKRDLISRE CCCCCHHHHHHHHHH	51.60	28112733
295	Ubiquitination	HKKLEEEKGKKEKER HHHHHHHHCHHHHHH	78.35	24816145
306	Ubiquitination	EKERQEIEKERRERE HHHHHHHHHHHHHHH	48.38	24816145
335	Ubiquitination	EREREREREKEKERE HHHHHHHHHHHHHHH	67.52	24816145
374	Phosphorylation	RDRDRERSSDRNKDR HHHHHHHHHHHHHHH	31.66	-
382	Phosphorylation	SDRNKDRSRSREKSR HHHHHHHHHHHHHHH	44.75	-
384	Phosphorylation	RNKDRSRSREKSRDR HHHHHHHHHHHHHHH	46.14	-
388	Phosphorylation	RSRSREKSRDRERER HHHHHHHHHHHHHHH	34.36	30576142
429	Ubiquitination	EREREKDKKRDREED HHHHHHHHHHCHHHH	61.86	24816145
430	Sumoylation	REREKDKKRDREEDE HHHHHHHHHCHHHHH	70.44	28112733
441	Phosphorylation	EEDEEDAYERRKLER HHHHHHHHHHHHHHH	23.45	25839225
457	Phosphorylation	LREKEAAYQERLKNW HHHHHHHHHHHHHHH	20.25	22817900
475	Phosphorylation	ERKKTREYEKEAERE HHHHHHHHHHHHHHH	29.07	29759185
477	Ubiquitination	KKTREYEKEAEREEE HHHHHHHHHHHHHHH	62.41	22817900
480	Ubiquitination	REYEKEAEREEERRR HHHHHHHHHHHHHHH	62.81	27667366
483	Ubiquitination	EKEAEREEERRREMA HHHHHHHHHHHHHHH	64.13	24816145
491	Ubiquitination	ERRREMAKEAKRLKE HHHHHHHHHHHHHHH	57.82	-
511	Ubiquitination	DDDRDDPKYYRGSAL CCCCCCCCHHCHHHH	63.01	24816145
511	2-Hydroxyisobutyrylation	DDDRDDPKYYRGSAL CCCCCCCCHHCHHHH	63.01	-
511	Acetylation	DDDRDDPKYYRGSAL CCCCCCCCHHCHHHH	63.01	26051181
514	Methylation	RDDPKYYRGSALQKR CCCCCHHCHHHHHHH	29.51	115490681
516	Phosphorylation	DPKYYRGSALQKRLR CCCHHCHHHHHHHHH	19.46	20068231
517	Ubiquitination	PKYYRGSALQKRLRD CCHHCHHHHHHHHHH	19.48	24816145
521	Ubiquitination	RGSALQKRLRDREKE CHHHHHHHHHHHHHH	23.22	27667366
540	Ubiquitination	ERDRKREKEELEEIR HHHHHHHHHHHHHHH	61.60	24816145
540	Acetylation	ERDRKREKEELEEIR HHHHHHHHHHHHHHH	61.60	25953088
578	Sumoylation	RRRQPQIKQEPESEE HHHCHHHHCCCCCHH	43.28	-
578	Sumoylation	RRRQPQIKQEPESEE HHHCHHHHCCCCCHH	43.28	28112733
583	Phosphorylation	QIKQEPESEEEEEEK HHHCCCCCHHHHHHH	62.11	29255136
616	Phosphorylation	QKPCLKPTLRPISSA CCCCCCCCCCCCCCC	33.54	18669648
618	Phosphorylation	PCLKPTLRPISSAPS CCCCCCCCCCCCCCC	29.05	18669648
621	Phosphorylation	KPTLRPISSAPSVSS CCCCCCCCCCCCCCC	24.11	20873877
622	Phosphorylation	PTLRPISSAPSVSSA CCCCCCCCCCCCCCC	44.94	20873877
624	Phosphorylation	LRPISSAPSVSSASG CCCCCCCCCCCCCCC	36.89	18669648
625	Phosphorylation	RPISSAPSVSSASGN CCCCCCCCCCCCCCC	34.06	20873877
627	Phosphorylation	ISSAPSVSSASGNAT CCCCCCCCCCCCCCC	25.23	20873877
628	Phosphorylation	SSAPSVSSASGNATP CCCCCCCCCCCCCCC	25.05	20873877
630	Phosphorylation	APSVSSASGNATPNT CCCCCCCCCCCCCCC	34.23	20873877
634	Phosphorylation	SSASGNATPNTPGDE CCCCCCCCCCCCCCC	22.52	20873877
637	Phosphorylation	SGNATPNTPGDESPC CCCCCCCCCCCCCCC	29.83	20873877
642	Phosphorylation	PNTPGDESPCGIIIP CCCCCCCCCCEEEEC	30.17	26074081
644	Phosphorylation	TPGDESPCGIIIPHE CCCCCCCCEEEECCC	9.47	18669648
653	Phosphorylation	IIIPHENSPDQQQPE EEECCCCCCCCCCCC	27.20	26074081
669	Phosphorylation	HRPKIGLSLKLGASN CCCCCCEEEECCCCC	20.46	23312004
671	Acetylation	PKIGLSLKLGASNSP CCCCEEEECCCCCCC	41.31	26051181
671	Sumoylation	PKIGLSLKLGASNSP CCCCEEEECCCCCCC	41.31	28112733
675	Phosphorylation	LSLKLGASNSPGQPN EEEECCCCCCCCCCC	35.72	22167270
677	Phosphorylation	LKLGASNSPGQPNSV EECCCCCCCCCCCCC	28.10	19664994
683	Phosphorylation	NSPGQPNSVKRKKLP CCCCCCCCCCCCCCC	35.38	23927012
685	Ubiquitination	PGQPNSVKRKKLPVD CCCCCCCCCCCCCHH	59.32	32015554
685	Acetylation	PGQPNSVKRKKLPVD CCCCCCCCCCCCCHH	59.32	25953088
688	Ubiquitination	PNSVKRKKLPVDSVF CCCCCCCCCCHHHHH	63.15	24816145
688	Sumoylation	PNSVKRKKLPVDSVF CCCCCCCCCCHHHHH	63.15	28112733
693	Phosphorylation	RKKLPVDSVFNKFED CCCCCHHHHHHHCCC	28.92	23927012
697	Ubiquitination	PVDSVFNKFEDEDSD CHHHHHHHCCCCCCC	38.37	29967540
697	Acetylation	PVDSVFNKFEDEDSD CHHHHHHHCCCCCCC	38.37	26051181
697	Sumoylation	PVDSVFNKFEDEDSD CHHHHHHHCCCCCCC	38.37	28112733
703	Phosphorylation	NKFEDEDSDDVPRKR HHCCCCCCCCCCCCC	33.39	29255136
711	Ubiquitination	DDVPRKRKLVPLDYG CCCCCCCCEEECCCC	57.80	32142685
717	Phosphorylation	RKLVPLDYGEDDKNA CCEEECCCCCCCCCC	30.05	-
722	Sumoylation	LDYGEDDKNATKGTV CCCCCCCCCCCCCCC	61.88	28112733
722	Ubiquitination	LDYGEDDKNATKGTV CCCCCCCCCCCCCCC	61.88	33845483
722	Acetylation	LDYGEDDKNATKGTV CCCCCCCCCCCCCCC	61.88	26051181
726	Ubiquitination	EDDKNATKGTVNTEE CCCCCCCCCCCCHHH	50.61	33845483
728	Phosphorylation	DKNATKGTVNTEEKR CCCCCCCCCCHHHHH	16.49	19664995
731	Phosphorylation	ATKGTVNTEEKRKHI CCCCCCCHHHHHHHH	40.98	28985074
739	Ubiquitination	EEKRKHIKSLIEKIP HHHHHHHHHHHHHCC	38.64	29967540
739	Malonylation	EEKRKHIKSLIEKIP HHHHHHHHHHHHHCC	38.64	26320211
739	Acetylation	EEKRKHIKSLIEKIP HHHHHHHHHHHHHCC	38.64	26051181
740	Phosphorylation	EKRKHIKSLIEKIPT HHHHHHHHHHHHCCC	33.70	24719451
747	Phosphorylation	SLIEKIPTAKPELFA HHHHHCCCCCHHHHC	51.27	24719451
749	Acetylation	IEKIPTAKPELFAYP HHHCCCCCHHHHCCC	41.31	6570247
777	Acetylation	RIRPWINKKIIEYIG CCHHHHCHHHHHHHC	35.89	25953088
802	Phosphorylation	CSKVMAHSSPQSILD HHHHHCCCCCHHHHH	33.89	25627689
803	Phosphorylation	SKVMAHSSPQSILDD HHHHCCCCCHHHHHH	19.66	25159151
806	Phosphorylation	MAHSSPQSILDDVAM HCCCCCHHHHHHHHH	28.62	25627689
832	Phosphorylation	KMWRLLIYETEAKKI HHHHHHHHHCCHHHH	19.44	24275569
837	2-Hydroxyisobutyrylation	LIYETEAKKIGLVK- HHHHCCHHHHCCCC-	38.40	-
837	Acetylation	LIYETEAKKIGLVK- HHHHCCHHHHCCCC-	38.40	25953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RBM25_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RBM25_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RBM25_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRRM1_HUMAN	SRRM1	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
TRA2A_HUMAN	TRA2A	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
TCEA1_HUMAN	TCEA1	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
VRK1_HUMAN	VRK1	physical	22939629
SEPT7_HUMAN	SEPT7	physical	22939629
SIR1_HUMAN	SIRT1	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
SP16H_HUMAN	SUPT16H	physical	22939629
SMN_HUMAN	SMN1	physical	22939629
RBM23_HUMAN	RBM23	physical	22365833
RBM39_HUMAN	RBM39	physical	22365833
PRP31_HUMAN	PRPF31	physical	22365833
SNUT1_HUMAN	SART1	physical	22365833
PR40A_HUMAN	PRPF40A	physical	26344197
PR40B_HUMAN	PRPF40B	physical	26344197
PUF60_HUMAN	PUF60	physical	26344197
SNUT1_HUMAN	SART1	physical	26344197
SREK1_HUMAN	SREK1	physical	26344197
SRRM1_HUMAN	SRRM1	physical	26344197
SRRM2_HUMAN	SRRM2	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-677 AND SER-703, ANDMASS SPECTROMETRY.
PubMed: 19690332

"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-583; SER-675; SER-677AND SER-683, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-675; SER-677; SER-683AND SER-703, AND MASS SPECTROMETRY.
PubMed: 18669648

"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASSSPECTROMETRY.
PubMed: 19367720

"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-677, AND MASSSPECTROMETRY.
PubMed: 19007248

"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-677, AND MASSSPECTROMETRY.
PubMed: 17287340

"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-677 AND SER-683, ANDMASS SPECTROMETRY.
PubMed: 17924679

"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-677 AND SER-683, ANDMASS SPECTROMETRY.
PubMed: 16964243

"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-677 AND SER-683, ANDMASS SPECTROMETRY.
PubMed: 17081983

"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-677, AND MASSSPECTROMETRY.
PubMed: 15302935

Ubiquitylation

"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-477, AND MASSSPECTROMETRY.
PubMed: 17370265