dbPTM

RBM15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM15_HUMAN
UniProt AC	Q96T37
Protein Name	RNA-binding protein 15 {ECO:0000305}
Gene Name	RBM15 {ECO:0000303\|PubMed:11431691, ECO:0000312\|HGNC:HGNC:14959}
Organism	Homo sapiens (Human).
Sequence Length	977
Subcellular Localization	Nucleus speckle . Nucleus, nucleoplasm . Nucleus envelope . Nucleus membrane Peripheral membrane protein . Colocalizes at the nuclear pore with DBP5 and NXF1.
Protein Description	RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. [PubMed: 27602518 Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex]
Protein Sequence	MRTAGRDPVPRRSPRWRRAVPLCETSAGRRVTQLRGDDLRRPATMKGKERSPVKAKRSRGGEDSTSRGERSKKLGGSGGSNGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGAEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPPPLPRDLERERDYPFYERVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTESDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDAFGHRAPDPLRGARDRTPPLLYRDRDRDLYPDSDWVPPPPPVRERSTRTAATSVPAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESDRPRKRHCAPSPDRSPELSSSRDRYNSDNDRSSRLLLERPSPIRDRRGSLEKSQGDKRDRKNSASAERDRKHRTTAPTEGKSPLKKEDRSDGSAPSTSTASSKLKSPSQKQDGGTAPVASASPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSAASDTATSTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRGFGFQIGVRYENKKRENLALTLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	RDPVPRRSPRWRRAV CCCCCCCCCCHHHHH	21.79	20068231
26	Phosphorylation	AVPLCETSAGRRVTQ HHCCCCCCCCCCEEE	13.36	24719451
32	Phosphorylation	TSAGRRVTQLRGDDL CCCCCCEEECCCCCC	21.78	23532336
44	Phosphorylation	DDLRRPATMKGKERS CCCCCCCCCCCCCCC	23.30	26074081
51	Phosphorylation	TMKGKERSPVKAKRS CCCCCCCCCCCCCHH	34.83	30576142
77	Phosphorylation	RSKKLGGSGGSNGSS HHHCCCCCCCCCCCC	37.88	21406692
80	Phosphorylation	KLGGSGGSNGSSSGK CCCCCCCCCCCCCCC	41.36	28985074
83	Phosphorylation	GSGGSNGSSSGKTDS CCCCCCCCCCCCCCC	26.11	21406692
84	Phosphorylation	SGGSNGSSSGKTDSG CCCCCCCCCCCCCCC	44.50	21406692
85	Phosphorylation	GGSNGSSSGKTDSGG CCCCCCCCCCCCCCC	46.11	21406692
90	Phosphorylation	SSSGKTDSGGGSRRS CCCCCCCCCCCCCCE	44.56	28634120
94	Phosphorylation	KTDSGGGSRRSLHLD CCCCCCCCCCEEECC	28.00	27282143
97	Phosphorylation	SGGGSRRSLHLDKSS CCCCCCCEEECCCCC	21.02	26055452
103	Phosphorylation	RSLHLDKSSSRGGSR CEEECCCCCCCCCCC	32.96	26055452
104	Phosphorylation	SLHLDKSSSRGGSRE EEECCCCCCCCCCCC	29.78	24732914
105	Phosphorylation	LHLDKSSSRGGSREY EECCCCCCCCCCCCC	41.87	25159151
109	Phosphorylation	KSSSRGGSREYDTGG CCCCCCCCCCCCCCC	25.43	25159151
110	Methylation	SSSRGGSREYDTGGG CCCCCCCCCCCCCCC	50.17	115388197
112	Phosphorylation	SRGGSREYDTGGGSS CCCCCCCCCCCCCCC	20.07	23898821
114	Phosphorylation	GGSREYDTGGGSSSS CCCCCCCCCCCCCCC	36.50	29691806
118	Phosphorylation	EYDTGGGSSSSRLHS CCCCCCCCCCCCCEE	30.26	28450419
119	Phosphorylation	YDTGGGSSSSRLHSY CCCCCCCCCCCCEEC	35.29	28450419
120	Phosphorylation	DTGGGSSSSRLHSYS CCCCCCCCCCCEECC	22.60	28450419
121	Phosphorylation	TGGGSSSSRLHSYSS CCCCCCCCCCEECCC	40.59	28450419
125	Phosphorylation	SSSSRLHSYSSPSTK CCCCCCEECCCCCCC	31.16	30266825
126	Phosphorylation	SSSRLHSYSSPSTKN CCCCCEECCCCCCCC	11.47	22167270
127	Phosphorylation	SSRLHSYSSPSTKNS CCCCEECCCCCCCCC	38.49	22167270
128	Phosphorylation	SRLHSYSSPSTKNSS CCCEECCCCCCCCCC	18.03	22167270
130	Phosphorylation	LHSYSSPSTKNSSGG CEECCCCCCCCCCCC	54.70	30266825
131	Phosphorylation	HSYSSPSTKNSSGGG EECCCCCCCCCCCCC	37.31	30266825
134	Phosphorylation	SSPSTKNSSGGGESR CCCCCCCCCCCCCCC	31.73	28450419
135	Phosphorylation	SPSTKNSSGGGESRS CCCCCCCCCCCCCCC	51.34	28450419
140	Phosphorylation	NSSGGGESRSSSRGG CCCCCCCCCCCCCCC	40.51	28450419
143	Phosphorylation	GGGESRSSSRGGGGE CCCCCCCCCCCCCCC	23.97	-
151	Phosphorylation	SRGGGGESRSSGAAS CCCCCCCCCCCCCCC	40.51	28450419
153	Phosphorylation	GGGGESRSSGAASSA CCCCCCCCCCCCCCC	42.26	25627689
154	Phosphorylation	GGGESRSSGAASSAP CCCCCCCCCCCCCCC	31.20	25159151
158	Phosphorylation	SRSSGAASSAPGGGD CCCCCCCCCCCCCCC	26.88	28450419
159	Phosphorylation	RSSGAASSAPGGGDG CCCCCCCCCCCCCCC	33.48	28450419
169	Phosphorylation	GGGDGAEYKTLKISE CCCCCHHEEEEEHHH	14.56	23186163
170	Sumoylation	GGDGAEYKTLKISEL CCCCHHEEEEEHHHH	38.60	-
170	Acetylation	GGDGAEYKTLKISEL CCCCHHEEEEEHHHH	38.60	26051181
170	Sumoylation	GGDGAEYKTLKISEL CCCCHHEEEEEHHHH	38.60	-
170	Ubiquitination	GGDGAEYKTLKISEL CCCCHHEEEEEHHHH	38.60	29967540
175	Phosphorylation	EYKTLKISELGSQLS HEEEEEHHHHHHHCC	25.78	22617229
179	Phosphorylation	LKISELGSQLSDEAV EEHHHHHHHCCHHHH	40.34	17525332
182	Phosphorylation	SELGSQLSDEAVEDG HHHHHHCCHHHHHCC	26.26	22617229
195	Acetylation	DGLFHEFKRFGDVSV CCHHHCCHHHCCEEE	43.78	26051181
195	Ubiquitination	DGLFHEFKRFGDVSV CCHHHCCHHHCCEEE	43.78	29967540
201	Phosphorylation	FKRFGDVSVKISHLS CHHHCCEEEEEEECC	23.56	23186163
205	Phosphorylation	GDVSVKISHLSGSGS CCEEEEEEECCCCCC	16.80	29255136
208	Phosphorylation	SVKISHLSGSGSGDE EEEEEECCCCCCCCC	26.03	29255136
210	Phosphorylation	KISHLSGSGSGDERV EEEECCCCCCCCCEE	26.81	29255136
212	Phosphorylation	SHLSGSGSGDERVAF EECCCCCCCCCEEEE	44.78	23401153
241	Phosphorylation	ARGRLVLYDRPLKIE HCCCEEEECCCCCEE	11.48	27642862
246	Sumoylation	VLYDRPLKIEAVYVS EEECCCCCEEEEEEC	40.98	28112733
251	Phosphorylation	PLKIEAVYVSRRRSR CCCEEEEEECCCCCC	10.35	28152594
253	Phosphorylation	KIEAVYVSRRRSRSP CEEEEEECCCCCCCC	11.46	21815630
257	Phosphorylation	VYVSRRRSRSPLDKD EEECCCCCCCCCCCC	34.99	22167270
259	Phosphorylation	VSRRRSRSPLDKDTY ECCCCCCCCCCCCCC	30.94	22167270
265	Phosphorylation	RSPLDKDTYPPSASV CCCCCCCCCCCCCCE	43.60	22167270
266	Phosphorylation	SPLDKDTYPPSASVV CCCCCCCCCCCCCEE	24.23	22167270
269	Phosphorylation	DKDTYPPSASVVGAS CCCCCCCCCCEEEEE	28.77	23927012
271	Phosphorylation	DTYPPSASVVGASVG CCCCCCCCEEEEEEC	22.98	23927012
276	Phosphorylation	SASVVGASVGGHRHP CCCEEEEEECCCCCC	18.50	23927012
292	Phosphorylation	GGGGGQRSLSPGGAA CCCCCCCCCCCCCCC	25.88	22167270
294	Phosphorylation	GGGQRSLSPGGAALG CCCCCCCCCCCCCCC	23.81	19664994
302	Phosphorylation	PGGAALGYRDYRLQQ CCCCCCCCCCHHHHH	10.93	23927012
305	Phosphorylation	AALGYRDYRLQQLAL CCCCCCCHHHHHHHH	12.29	23403867
333	Phosphorylation	DLERERDYPFYERVR CHHHHCCCCCHHCCC	11.06	28152594
336	Phosphorylation	RERDYPFYERVRPAY HHCCCCCHHCCCCCC	9.79	28796482
340	Methylation	YPFYERVRPAYSLEP CCCHHCCCCCCCCCC	19.16	115490619
343	Phosphorylation	YERVRPAYSLEPRVG HHCCCCCCCCCCCCC	19.23	21945579
344	Phosphorylation	ERVRPAYSLEPRVGA HCCCCCCCCCCCCCC	28.50	21945579
348	Methylation	PAYSLEPRVGAGAGA CCCCCCCCCCCCCCC	30.08	115490611
365	Phosphorylation	FREVDEISPEDDQRA CCCCCCCCHHHHHHH	21.86	23401153
384	Phosphorylation	FLGNLDITVTESDLR EECEEEEEECHHHHH	22.50	22817900
401	O-linked_Glycosylation	FDRFGVITEVDIKRP HHHCCCEEEEEECCC	27.78	30620550
406	Sumoylation	VITEVDIKRPSRGQT CEEEEEECCCCCCCC	54.51	28112733
406	Ubiquitination	VITEVDIKRPSRGQT CEEEEEECCCCCCCC	54.51	-
409	Phosphorylation	EVDIKRPSRGQTSTY EEEECCCCCCCCCEE	53.74	28555341
414	Phosphorylation	RPSRGQTSTYGFLKF CCCCCCCCEEEEEEE	16.25	28555341
416	Phosphorylation	SRGQTSTYGFLKFEN CCCCCCEEEEEEECC	12.97	20090780
420	Methylation	TSTYGFLKFENLDMS CCEEEEEEECCCCCC	48.66	115976351
420	Sumoylation	TSTYGFLKFENLDMS CCEEEEEEECCCCCC	48.66	28112733
445	Sumoylation	IIIRNPIKIGYGKAT EEECCCEEECCCCCC	31.19	28112733
445	Ubiquitination	IIIRNPIKIGYGKAT EEECCCEEECCCCCC	31.19	29967540
450	Acetylation	PIKIGYGKATPTTRL CEEECCCCCCCCCEE	40.37	19608861
452	Phosphorylation	KIGYGKATPTTRLWV EECCCCCCCCCEEEC	25.34	26714015
537	Phosphorylation	EHRYQQQYLQPLPLT HHHHHHHHCCCCCCC	11.72	17360941
544	Phosphorylation	YLQPLPLTHYELVTD HCCCCCCCCHHHHHH	22.07	28796482
546	Phosphorylation	QPLPLTHYELVTDAF CCCCCCCHHHHHHHC	13.01	28796482
550	Phosphorylation	LTHYELVTDAFGHRA CCCHHHHHHHCCCCC	33.95	28796482
568	Phosphorylation	LRGARDRTPPLLYRD CCCCCCCCCCCEECC	33.28	29255136
573	Phosphorylation	DRTPPLLYRDRDRDL CCCCCCEECCCCCCC	20.39	23927012
578	Dimethylation	LLYRDRDRDLYPDSD CEECCCCCCCCCCCC	36.41	-
578	Methylation	LLYRDRDRDLYPDSD CEECCCCCCCCCCCC	36.41	26575292
581	Phosphorylation	RDRDRDLYPDSDWVP CCCCCCCCCCCCCCC	14.85	30576142
584	Phosphorylation	DRDLYPDSDWVPPPP CCCCCCCCCCCCCCC	28.94	30576142
597	Phosphorylation	PPPVRERSTRTAATS CCCCCCCCCCCCCCC	19.93	26074081
598	Phosphorylation	PPVRERSTRTAATSV CCCCCCCCCCCCCCC	37.96	26074081
600	Phosphorylation	VRERSTRTAATSVPA CCCCCCCCCCCCCCC	22.26	26074081
603	Phosphorylation	RSTRTAATSVPAYEP CCCCCCCCCCCCCCC	28.00	21945579
604	Phosphorylation	STRTAATSVPAYEPL CCCCCCCCCCCCCCC	22.75	21945579
608	Phosphorylation	AATSVPAYEPLDSLD CCCCCCCCCCCCCCC	16.41	21945579
613	Phosphorylation	PAYEPLDSLDRRRDG CCCCCCCCCCCCCCC	39.59	21945579
622	Phosphorylation	DRRRDGWSLDRDRGD CCCCCCCCCCCCCCC	26.39	23401153
634	Phosphorylation	RGDRDLPSSRDQPRK CCCCCCCCCCCCCCH	45.35	30576142
635	Phosphorylation	GDRDLPSSRDQPRKR CCCCCCCCCCCCCHH	37.63	30576142
648	Phosphorylation	KRRLPEESGGRHLDR HHCCCCCCCCCCCCC	44.90	21815630
656	Phosphorylation	GGRHLDRSPESDRPR CCCCCCCCCCCCCCC	32.46	29255136
659	Phosphorylation	HLDRSPESDRPRKRH CCCCCCCCCCCCCCC	42.16	29255136
670	Phosphorylation	RKRHCAPSPDRSPEL CCCCCCCCCCCCCCC	22.40	29255136
674	Phosphorylation	CAPSPDRSPELSSSR CCCCCCCCCCCCCCC	30.06	29255136
678	Phosphorylation	PDRSPELSSSRDRYN CCCCCCCCCCCCCCC	25.30	22167270
679	Phosphorylation	DRSPELSSSRDRYNS CCCCCCCCCCCCCCC	41.85	22167270
680	Phosphorylation	RSPELSSSRDRYNSD CCCCCCCCCCCCCCC	34.52	22167270
684	Phosphorylation	LSSSRDRYNSDNDRS CCCCCCCCCCCCCHH	24.25	27273156
686	Phosphorylation	SSRDRYNSDNDRSSR CCCCCCCCCCCHHHH	28.93	25884760
691	Phosphorylation	YNSDNDRSSRLLLER CCCCCCHHHHHHHCC	23.75	26074081
692	O-linked_Glycosylation	NSDNDRSSRLLLERP CCCCCHHHHHHHCCC	28.04	30620550
692	Phosphorylation	NSDNDRSSRLLLERP CCCCCHHHHHHHCCC	28.04	26074081
700	Phosphorylation	RLLLERPSPIRDRRG HHHHCCCCCCCCCCC	38.90	29255136
708	Phosphorylation	PIRDRRGSLEKSQGD CCCCCCCCHHCCCCC	31.38	28176443
712	Phosphorylation	RRGSLEKSQGDKRDR CCCCHHCCCCCHHCC	29.98	23312004
722	Phosphorylation	DKRDRKNSASAERDR CHHCCCCCHHHHHHH	27.00	30576142
724	Phosphorylation	RDRKNSASAERDRKH HCCCCCHHHHHHHCC	30.40	26329039
733	Phosphorylation	ERDRKHRTTAPTEGK HHHHCCCCCCCCCCC	27.33	23927012
734	Phosphorylation	RDRKHRTTAPTEGKS HHHCCCCCCCCCCCC	30.51	23927012
737	Phosphorylation	KHRTTAPTEGKSPLK CCCCCCCCCCCCCCC	55.71	23927012
741	Phosphorylation	TAPTEGKSPLKKEDR CCCCCCCCCCCCCCC	46.45	20201521
744	Sumoylation	TEGKSPLKKEDRSDG CCCCCCCCCCCCCCC	58.46	28112733
744	Ubiquitination	TEGKSPLKKEDRSDG CCCCCCCCCCCCCCC	58.46	24816145
749	Phosphorylation	PLKKEDRSDGSAPST CCCCCCCCCCCCCCC	59.66	28985074
752	Phosphorylation	KEDRSDGSAPSTSTA CCCCCCCCCCCCCCC	41.83	25849741
755	Phosphorylation	RSDGSAPSTSTASSK CCCCCCCCCCCCCHH	34.41	26074081
756	Phosphorylation	SDGSAPSTSTASSKL CCCCCCCCCCCCHHC	29.10	26074081
757	O-linked_Glycosylation	DGSAPSTSTASSKLK CCCCCCCCCCCHHCC	26.72	30620550
757	Phosphorylation	DGSAPSTSTASSKLK CCCCCCCCCCCHHCC	26.72	26074081
758	Phosphorylation	GSAPSTSTASSKLKS CCCCCCCCCCHHCCC	30.55	26074081
760	Phosphorylation	APSTSTASSKLKSPS CCCCCCCCHHCCCCC	28.26	22210691
761	Phosphorylation	PSTSTASSKLKSPSQ CCCCCCCHHCCCCCC	39.27	26074081
762	Acetylation	STSTASSKLKSPSQK CCCCCCHHCCCCCCC	58.39	26822725
765	Phosphorylation	TASSKLKSPSQKQDG CCCHHCCCCCCCCCC	39.97	23927012
767	Phosphorylation	SSKLKSPSQKQDGGT CHHCCCCCCCCCCCC	58.04	23927012
774	Phosphorylation	SQKQDGGTAPVASAS CCCCCCCCCCCCCCC	33.06	23927012
779	Phosphorylation	GGTAPVASASPKLCL CCCCCCCCCCHHHHH	29.52	25159151
781	Phosphorylation	TAPVASASPKLCLAW CCCCCCCCHHHHHHH	21.77	23401153
830	Acetylation	GGKVAQLKITQRLRL CCCEEEEEEEHHHCC	31.46	25953088
841	Ubiquitination	RLRLDQPKLDEVTRR HHCCCCCCHHHHHHH	64.04	24816145
850	Ubiquitination	DEVTRRIKVAGPNGY HHHHHHEEECCCCCE	24.99	-
857	Phosphorylation	KVAGPNGYAILLAVP EECCCCCEEEEEEEC	9.34	25867546
866	Phosphorylation	ILLAVPGSSDSRSSS EEEEECCCCCCCCCC	25.54	25867546
867	Phosphorylation	LLAVPGSSDSRSSSS EEEECCCCCCCCCCC	45.58	25867546
869	Phosphorylation	AVPGSSDSRSSSSSA EECCCCCCCCCCCCC	35.69	25867546
871	Phosphorylation	PGSSDSRSSSSSAAS CCCCCCCCCCCCCCC	38.22	29116813
872	Phosphorylation	GSSDSRSSSSSAASD CCCCCCCCCCCCCCC	32.88	29116813
873	Phosphorylation	SSDSRSSSSSAASDT CCCCCCCCCCCCCCC	29.56	29116813
874	Phosphorylation	SDSRSSSSSAASDTA CCCCCCCCCCCCCCC	26.41	27732954
875	Phosphorylation	DSRSSSSSAASDTAT CCCCCCCCCCCCCCC	29.78	27732954
878	Phosphorylation	SSSSSAASDTATSTQ CCCCCCCCCCCCCCH	34.90	23312004
880	Phosphorylation	SSSAASDTATSTQRP CCCCCCCCCCCCHHH	29.37	23186163
882	Phosphorylation	SAASDTATSTQRPLR CCCCCCCCCCHHHHH	34.11	23186163
883	Phosphorylation	AASDTATSTQRPLRN CCCCCCCCCHHHHHH	21.78	23186163
884	Phosphorylation	ASDTATSTQRPLRNL CCCCCCCCHHHHHHH	25.01	23186163
893	Phosphorylation	RPLRNLVSYLKQKQA HHHHHHHHHHHHHCC	28.10	-
917	Phosphorylation	GNKDKENTGVLHAFP CCCCCCCCCCCEECC	29.74	26074081
929	Phosphorylation	AFPPCEFSQQFLDSP ECCCCHHHHHHHHCH	10.77	30266825
935	Phosphorylation	FSQQFLDSPAKALAK HHHHHHHCHHHHHHC	28.98	30266825
938	Ubiquitination	QFLDSPAKALAKSEE HHHHCHHHHHHCCCC	47.52	29967540

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
-	K	Ubiquitination	E3 ubiquitin ligase	CNOT4	O95628	PMID:26575292

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
578	R	Methylation	26575292
Methylated at Arg-578 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.
578	R	Methylation	26575292
Ubiquitinated by CNOT4 following methylation at Arg-578 by PRMT1.
578	R	ubiquitylation	26575292
Methylated at Arg-578 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.
578	R	ubiquitylation	26575292
Ubiquitinated by CNOT4 following methylation at Arg-578 by PRMT1.

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 RBM15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC3_HUMAN	HDAC3	physical	18667423
THOC4_HUMAN	ALYREF	physical	19586903
NXF1_HUMAN	NXF1	physical	19586903
NXF1_HUMAN	NXF1	physical	17001072
TPM1_HUMAN	TPM1	physical	22939629
UBE3C_HUMAN	UBE3C	physical	22939629
RRN3_HUMAN	RRN3	physical	22939629
CEP44_HUMAN	CEP44	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
NAV2_HUMAN	NAV2	physical	25416956
ANM1_HUMAN	PRMT1	physical	26575292
CNOT4_HUMAN	CNOT4	physical	26575292
SF3B1_HUMAN	SF3B1	physical	26575292

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 RBM15_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 LYS-450, AND MASS SPECTROMETRY.	19608861 [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-294; SER-670 ANDSER-674, AND MASS SPECTROMETRY.	19690332 [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-154; SER-292; SER-294AND SER-781, AND MASS 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-257; SER-259; SER-292;SER-294; THR-568; SER-656; SER-659; SER-670; SER-674; SER-700; SER-741AND SER-935, 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-294 AND SER-700, ANDMASS SPECTROMETRY.	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-292; SER-294; THR-568;SER-670 AND SER-674, AND MASS SPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASSSPECTROMETRY.	17525332 [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-656 AND SER-741, ANDMASS 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-659, AND MASSSPECTROMETRY.	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-294 AND SER-365, 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-51; SER-292; SER-294;THR-568; SER-622; SER-670; SER-674; SER-700; SER-708 AND SER-724, ANDMASS 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-83; SER-125; SER-128 ANDSER-294, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.	15302935 [Abstract]

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