dbPTM

RB15B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RB15B_HUMAN
UniProt AC	Q8NDT2
Protein Name	Putative RNA-binding protein 15B {ECO:0000305}
Gene Name	RBM15B {ECO:0000303\|PubMed:16129689, ECO:0000303\|PubMed:19586903, ECO:0000312\|HGNC:HGNC:24303}
Organism	Homo sapiens (Human).
Sequence Length	890
Subcellular Localization	Nucleus, nucleoplasm . Nucleus speckle . Nucleus envelope . Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli.
Protein Description	RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. [PubMed: 16129689]
Protein Sequence	MKRQSERDSSPSGRGSSSSAKRPREREREAEAGGRRAAHKASGGAKHPVPARARDKPRGSGSGGGGHRDGRGTGDANHRASSGRSSGSGAGGGGRGGKASGDPGASGMSPRASPLPPPPPPPGAEPACPGSSAAAPEYKTLLISSLSPALPAEHLEDRLFHQFKRFGEISLRLSHTPELGRVAYVNFRHPQDAREARQHALARQLLLYDRPLKVEPVYLRGGGGSSRRSSSSSAAASTPPPGPPAPADPLGYLPLHGGYQYKQRSLSPVAAPPLREPRARHAAAAFALDAAAAAAVGLSRERALDYYGLYDDRGRPYGYPAVCEEDLMPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGRVIGRNPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGGPDRRLRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLVRDRTPPHLLYSDRDRTFLEGDWTSPSKSSDRRNSLEGYSRSVRSRSGERWGADGDRGLPKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGSGQQSERGSDRTPERSRKENHSSEGTKESSSNSLSNSRHGAEERGHHHHHHEAADSSHGKKARDSERNHRTTEAEPKPLEEPKHETKKLKNLSEYAQTLQLGWNGLLVLKNSCFPTSMHILEGDQGVISSLLKDHTSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLATQATPSGLGTEGMPTVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDGTGMLYAFPPCDFSQQYLQSALRTLGKLEEEHMVIVIVRDTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MKRQSERDSSPS ---CCCCCCCCCCCC	38.34	30576142
9	Phosphorylation	KRQSERDSSPSGRGS CCCCCCCCCCCCCCC	50.82	30576142
10	Phosphorylation	RQSERDSSPSGRGSS CCCCCCCCCCCCCCC	27.63	30576142
12	Phosphorylation	SERDSSPSGRGSSSS CCCCCCCCCCCCCCC	42.97	30242111
16	Phosphorylation	SSPSGRGSSSSAKRP CCCCCCCCCCCCCCH	26.20	26074081
17	Phosphorylation	SPSGRGSSSSAKRPR CCCCCCCCCCCCCHH	31.01	26074081
18	Phosphorylation	PSGRGSSSSAKRPRE CCCCCCCCCCCCHHH	35.69	21406692
19	Phosphorylation	SGRGSSSSAKRPRER CCCCCCCCCCCHHHH	39.49	21406692
42	Phosphorylation	RRAAHKASGGAKHPV HHHHHHHCCCCCCCC	42.43	-
46	Acetylation	HKASGGAKHPVPARA HHHCCCCCCCCCCCC	52.28	25953088
58	Methylation	ARARDKPRGSGSGGG CCCCCCCCCCCCCCC	58.62	81452785
60	O-linked_Glycosylation	ARDKPRGSGSGGGGH CCCCCCCCCCCCCCC	30.94	30379171
73	Phosphorylation	GHRDGRGTGDANHRA CCCCCCCCCCCCCCC	30.44	-
81	Phosphorylation	GDANHRASSGRSSGS CCCCCCCCCCCCCCC	33.03	30576142
86	Phosphorylation	RASSGRSSGSGAGGG CCCCCCCCCCCCCCC	35.30	22964224
88	Phosphorylation	SSGRSSGSGAGGGGR CCCCCCCCCCCCCCC	27.67	22964224
95	Methylation	SGAGGGGRGGKASGD CCCCCCCCCCCCCCC	54.70	80700909
100	Phosphorylation	GGRGGKASGDPGASG CCCCCCCCCCCCCCC	47.41	23927012
106	Phosphorylation	ASGDPGASGMSPRAS CCCCCCCCCCCCCCC	40.73	29255136
109	Phosphorylation	DPGASGMSPRASPLP CCCCCCCCCCCCCCC	18.11	29255136
113	Phosphorylation	SGMSPRASPLPPPPP CCCCCCCCCCCCCCC	28.40	23401153
131	Phosphorylation	AEPACPGSSAAAPEY CCCCCCCCCCCCCCH	11.27	22199227
132	Phosphorylation	EPACPGSSAAAPEYK CCCCCCCCCCCCCHH	28.04	22199227
138	Phosphorylation	SSAAAPEYKTLLISS CCCCCCCHHHHHHHH	14.28	22199227
140	Phosphorylation	AAAPEYKTLLISSLS CCCCCHHHHHHHHCC	26.37	24732914
144	Phosphorylation	EYKTLLISSLSPALP CHHHHHHHHCCCCCC	25.79	28102081
145	Phosphorylation	YKTLLISSLSPALPA HHHHHHHHCCCCCCH	26.35	28102081
147	Phosphorylation	TLLISSLSPALPAEH HHHHHHCCCCCCHHH	15.29	25159151
170	Phosphorylation	FKRFGEISLRLSHTP HHHHCEEEEEEECCC	11.79	28857561
174	Phosphorylation	GEISLRLSHTPELGR CEEEEEEECCCCCCC	20.91	28674419
176	Phosphorylation	ISLRLSHTPELGRVA EEEEEECCCCCCCEE	18.32	28674419
177	Phosphorylation	SLRLSHTPELGRVAY EEEEECCCCCCCEEE	29.41	18220336
205	Phosphorylation	QHALARQLLLYDRPL HHHHHHHHHHHCCCC	2.72	18220336
208	Phosphorylation	LARQLLLYDRPLKVE HHHHHHHHCCCCCEE	15.18	-
212	Phosphorylation	LLLYDRPLKVEPVYL HHHHCCCCCEECEEE	11.48	18220336
213	Sumoylation	LLYDRPLKVEPVYLR HHHCCCCCEECEEEC	47.43	-
213	Sumoylation	LLYDRPLKVEPVYLR HHHCCCCCEECEEEC	47.43	28112733
220	Methylation	KVEPVYLRGGGGSSR CEECEEECCCCCCCC	24.83	80700917
225	Phosphorylation	YLRGGGGSSRRSSSS EECCCCCCCCCCCCC	24.77	18669648
226	Phosphorylation	LRGGGGSSRRSSSSS ECCCCCCCCCCCCCC	34.68	24144214
227	Methylation	RGGGGSSRRSSSSSA CCCCCCCCCCCCCCC	44.17	115387739
229	Phosphorylation	GGGSSRRSSSSSAAA CCCCCCCCCCCCCCC	33.20	24043423
230	Phosphorylation	GGSSRRSSSSSAAAS CCCCCCCCCCCCCCC	32.21	24043423
231	Phosphorylation	GSSRRSSSSSAAAST CCCCCCCCCCCCCCC	29.56	24043423
232	Phosphorylation	SSRRSSSSSAAASTP CCCCCCCCCCCCCCC	26.41	25159151
233	Phosphorylation	SRRSSSSSAAASTPP CCCCCCCCCCCCCCC	24.71	24043423
235	Phosphorylation	RSSSSSAAASTPPPG CCCCCCCCCCCCCCC	12.14	18220336
237	Phosphorylation	SSSSAAASTPPPGPP CCCCCCCCCCCCCCC	36.40	24043423
238	Phosphorylation	SSSAAASTPPPGPPA CCCCCCCCCCCCCCC	34.78	24043423
252	Phosphorylation	APADPLGYLPLHGGY CCCCCCCCCCCCCCC	16.90	28450419
259	Phosphorylation	YLPLHGGYQYKQRSL CCCCCCCCEEECCCC	17.17	28450419
261	Phosphorylation	PLHGGYQYKQRSLSP CCCCCCEEECCCCCC	10.70	28450419
265	Phosphorylation	GYQYKQRSLSPVAAP CCEEECCCCCCCCCC	30.61	29255136
267	Phosphorylation	QYKQRSLSPVAAPPL EEECCCCCCCCCCCC	20.69	19664994
271	Phosphorylation	RSLSPVAAPPLREPR CCCCCCCCCCCCCHH	13.38	17287340
273	Phosphorylation	LSPVAAPPLREPRAR CCCCCCCCCCCHHHH	39.05	17287340
274	Phosphorylation	SPVAAPPLREPRARH CCCCCCCCCCHHHHH	10.62	17287340
282	Phosphorylation	REPRARHAAAAFALD CCHHHHHHHHHHHHH	8.01	17287340
306	Phosphorylation	SRERALDYYGLYDDR CHHHHHHHCCCCCCC	10.57	27642862
307	Phosphorylation	RERALDYYGLYDDRG HHHHHHHCCCCCCCC	10.58	27642862
347	Phosphorylation	FIGNLDHSVSEVELR EECCCCCCCCHHHHH	27.31	18491316
349	Phosphorylation	GNLDHSVSEVELRRA CCCCCCCCHHHHHHH	38.65	28122231
360	Phosphorylation	LRRAFEKYGIIEEVV HHHHHHHHCCEEEEE	13.32	20090780
379	Phosphorylation	ARGQGGAYAFLKFQN CCCCCCEEEEEEECC	10.93	20090780
408	Acetylation	VIGRNPIKIGYGKAN CCCCCCEEECCCCCC	31.19	25953088
408	Ubiquitination	VIGRNPIKIGYGKAN CCCCCCEEECCCCCC	31.19	-
417	Phosphorylation	GYGKANPTTRLWVGG CCCCCCCCCEEEECC	25.10	-
418	Phosphorylation	YGKANPTTRLWVGGL CCCCCCCCEEEECCC	25.64	-
443	Phosphorylation	REFDRFGSIRTIDHV HHHHCCCCEEEECCC	13.24	24719451
495	Phosphorylation	DFAKAEETRYPQQYQ EHHHHHHCCCCCCCC	27.32	26074081
497	Phosphorylation	AKAEETRYPQQYQPS HHHHHCCCCCCCCCC	16.89	22199227
501	Phosphorylation	ETRYPQQYQPSPLPV HCCCCCCCCCCCCCC	19.69	28450419
504	Phosphorylation	YPQQYQPSPLPVHYE CCCCCCCCCCCCEEE	24.44	25159151
510	Phosphorylation	PSPLPVHYELLTDGY CCCCCCEEEECCCCC	14.43	28796482
514	Phosphorylation	PVHYELLTDGYTRHR CCEEEECCCCCCCCC	39.75	28450419
517	Phosphorylation	YELLTDGYTRHRNLD EEECCCCCCCCCCCC	11.92	29978859
518	Phosphorylation	ELLTDGYTRHRNLDA EECCCCCCCCCCCCH	26.06	29978859
532	Phosphorylation	ADLVRDRTPPHLLYS HHHHCCCCCCCEEEC	45.52	29255136
538	Phosphorylation	RTPPHLLYSDRDRTF CCCCCEEECCCCCCC	18.19	23403867
539	Phosphorylation	TPPHLLYSDRDRTFL CCCCEEECCCCCCCC	26.58	23927012
544	Phosphorylation	LYSDRDRTFLEGDWT EECCCCCCCCCCCCC	36.54	23403867
551	Phosphorylation	TFLEGDWTSPSKSSD CCCCCCCCCCCCCCC	35.18	30266825
552	Phosphorylation	FLEGDWTSPSKSSDR CCCCCCCCCCCCCCC	23.95	19664994
554	Phosphorylation	EGDWTSPSKSSDRRN CCCCCCCCCCCCCCC	44.96	25159151
556	Phosphorylation	DWTSPSKSSDRRNSL CCCCCCCCCCCCCCC	41.63	25159151
557	Phosphorylation	WTSPSKSSDRRNSLE CCCCCCCCCCCCCCC	38.58	23403867
562	Phosphorylation	KSSDRRNSLEGYSRS CCCCCCCCCCCCCHH	26.45	25159151
566	Phosphorylation	RRNSLEGYSRSVRSR CCCCCCCCCHHHHCC	7.49	26074081
567	Phosphorylation	RNSLEGYSRSVRSRS CCCCCCCCHHHHCCC	29.01	23403867
569	Phosphorylation	SLEGYSRSVRSRSGE CCCCCCHHHHCCCCC	18.88	26074081
572	Phosphorylation	GYSRSVRSRSGERWG CCCHHHHCCCCCCCC	28.74	26074081
574	Phosphorylation	SRSVRSRSGERWGAD CHHHHCCCCCCCCCC	46.37	26074081
598	Phosphorylation	EERRKRRSLSSDRGR HHHHHHHCCCCCCCC	36.31	26055452
600	Phosphorylation	RRKRRSLSSDRGRTT HHHHHCCCCCCCCCC	31.29	26055452
601	Phosphorylation	RKRRSLSSDRGRTTH HHHHCCCCCCCCCCC	36.30	17287340
606	Phosphorylation	LSSDRGRTTHSPYEE CCCCCCCCCCCCHHH	31.52	30266825
607	Phosphorylation	SSDRGRTTHSPYEER CCCCCCCCCCCHHHH	20.99	30266825
609	Phosphorylation	DRGRTTHSPYEERSR CCCCCCCCCHHHHCC	27.38	23401153
611	Phosphorylation	GRTTHSPYEERSRTK CCCCCCCHHHHCCCC	33.18	21955146
617	Phosphorylation	PYEERSRTKGSGQQS CHHHHCCCCCCCCCC	40.79	-
624	Phosphorylation	TKGSGQQSERGSDRT CCCCCCCCCCCCCCC	22.75	26074081
628	Phosphorylation	GQQSERGSDRTPERS CCCCCCCCCCCCCHH	30.09	26074081
631	Phosphorylation	SERGSDRTPERSRKE CCCCCCCCCCHHHCC	34.20	26074081
635	Phosphorylation	SDRTPERSRKENHSS CCCCCCHHHCCCCCC	46.15	26074081
641	Phosphorylation	RSRKENHSSEGTKES HHHCCCCCCCCCCCC	41.49	28387310
642	Phosphorylation	SRKENHSSEGTKESS HHCCCCCCCCCCCCC	32.28	-
648	Phosphorylation	SSEGTKESSSNSLSN CCCCCCCCCCCCCCC	40.39	21406692
649	Phosphorylation	SEGTKESSSNSLSNS CCCCCCCCCCCCCCC	34.33	21406692
650	Phosphorylation	EGTKESSSNSLSNSR CCCCCCCCCCCCCCC	39.45	21406692
652	Phosphorylation	TKESSSNSLSNSRHG CCCCCCCCCCCCCCC	34.81	21406692
654	Phosphorylation	ESSSNSLSNSRHGAE CCCCCCCCCCCCCHH	32.36	30576142
656	Phosphorylation	SSNSLSNSRHGAEER CCCCCCCCCCCHHHC	23.44	25159151
679	Acetylation	AADSSHGKKARDSER HCCCCCCCCHHHHHH	37.52	24431515
684	Phosphorylation	HGKKARDSERNHRTT CCCCHHHHHHCCCCC	32.66	27251275
702	Sumoylation	PKPLEEPKHETKKLK CCCCCCCCCHHHHCC	58.30	28112733
749	Phosphorylation	GDQGVISSLLKDHTS CCHHHHHHHHCCCCC	26.96	24719451
759	Acetylation	KDHTSGSKLTQLKIA CCCCCCCHHHHHHHH	60.11	25953088
759	Ubiquitination	KDHTSGSKLTQLKIA CCCCCCCHHHHHHHH	60.11	29967540
764	Ubiquitination	GSKLTQLKIAQRLRL CCHHHHHHHHHHHCC	26.61	29967540
775	Ubiquitination	RLRLDQPKLDEVTRR HHCCCCCCHHHHHHH	64.04	24816145
826	Phosphorylation	RLLRNLVSYLKQKQA HHHHHHHHHHHHHHC	28.10	20068231
827	Phosphorylation	LLRNLVSYLKQKQAA HHHHHHHHHHHHHCC	15.50	20068231
829	Acetylation	RNLVSYLKQKQAAGV HHHHHHHHHHHCCCE	47.41	25953088
838	Phosphorylation	KQAAGVISLPVGGSK HHCCCEEEEEECCCC	24.98	20068231
844	Phosphorylation	ISLPVGGSKGRDGTG EEEEECCCCCCCCCC	26.47	28857561
889	Phosphorylation	VIVIVRDTA------ EEEEEECCC------	24.57	-

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 RB15B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RB15B_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 RB15B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THOC4_HUMAN	ALYREF	physical	19586903
RBM15_HUMAN	RBM15	physical	19586903
NXF1_HUMAN	NXF1	physical	19586903
UBP11_HUMAN	USP11	physical	22939629
TNNC1_HUMAN	TNNC1	physical	21988832
NAV2_HUMAN	NAV2	physical	25416956
DDX47_HUMAN	DDX47	physical	26344197
RBM15_HUMAN	RBM15	physical	28514442
KLH22_HUMAN	KLHL22	physical	28514442

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 RB15B_HUMAN

Related Literatures of Post-Translational Modification

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-267 AND SER-552, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-562, AND MASSSPECTROMETRY.	19367720 [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 THR-532 AND SER-562, 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 SER-598; SER-600; SER-601AND SER-609, AND MASS SPECTROMETRY.	17287340 [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-552, AND MASSSPECTROMETRY.	15302935 [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 THR-532, AND MASSSPECTROMETRY.	17081983 [Abstract]