dbPTM

RBM5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM5_HUMAN
UniProt AC	P52756
Protein Name	RNA-binding protein 5
Gene Name	RBM5
Organism	Homo sapiens (Human).
Sequence Length	815
Subcellular Localization	Nucleus .
Protein Description	Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis..
Protein Sequence	MGSDKRVSRTERSGRYGSIIDRDDRDERESRSRRRDSDYKRSSDDRRGDRYDDYRDYDSPERERERRNSDRSEDGYHSDGDYGEHDYRHDISDERESKTIMLRGLPITITESDIREMMESFEGPQPADVRLMKRKTGVSRGFAFVEFYHLQDATSWMEANQKKLVIQGKHIAMHYSNPRPKFEDWLCNKCCLNNFRKRLKCFRCGADKFDSEQEVPPGTTESVQSVDYYCDTIILRNIAPHTVVDSIMTALSPYASLAVNNIRLIKDKQTQQNRGFAFVQLSSAMDASQLLQILQSLHPPLKIDGKTIGVDFAKSARKDLVLSDGNRVSAFSVASTAIAAAQWSSTQSQSGEGGSVDYSYLQPGQDGYAQYAQYSQDYQQFYQQQAGGLESDASSASGTAVTTTSAAVVSQSPQLYNQTSNPPGSPTEEAQPSTSTSTQAPAASPTGVVPGTKYAVPDTSTYQYDESSGYYYDPTTGLYYDPNSQYYYNSLTQQYLYWDGEKETYVPAAESSSHQQSGLPPAKEGKEKKEKPKSKTAQQIAKDMERWAKSLNKQKENFKNSFQPVNSLREEERRESAAADAGFALFEKKGALAERQQLIPELVRNGDEENPLKRGLVAAYSGDSDNEEELVERLESEEEKLADWKKMACLLCRRQFPNKDALVRHQQLSDLHKQNMDIYRRSRLSEQELEALELREREMKYRDRAAERREKYGIPEPPEPKRKKQFDAGTVNYEQPTKDGIDHSNIGNKMLQAMGWREGSGLGRKCQGITAPIEAQVRLKGAGLGAKGSAYGLSGADSYKDAVRKAMFARFTEME

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MGSDKRVSRTERSGR CCCCCCCCCCCCCCC	37.20	20068231
10	Phosphorylation	SDKRVSRTERSGRYG CCCCCCCCCCCCCCC	28.39	20068231
16	Phosphorylation	RTERSGRYGSIIDRD CCCCCCCCCCCCCCC	20.81	26434776
18	Phosphorylation	ERSGRYGSIIDRDDR CCCCCCCCCCCCCCC	13.87	23401153
30	Phosphorylation	DDRDERESRSRRRDS CCCCHHHHHHHHCCH	41.60	28348404
32	Phosphorylation	RDERESRSRRRDSDY CCHHHHHHHHCCHHC	39.14	24719451
37	Phosphorylation	SRSRRRDSDYKRSSD HHHHHCCHHCCCCCC	40.82	30576142
51	Phosphorylation	DDRRGDRYDDYRDYD CCCCCCCCCCCCCCC	20.22	23403867
54	Phosphorylation	RGDRYDDYRDYDSPE CCCCCCCCCCCCCHH	11.50	28796482
57	Phosphorylation	RYDDYRDYDSPERER CCCCCCCCCCHHHHH	14.88	30266825
59 (in isoform 3)	Phosphorylation	-	23.56	25849741
59	Phosphorylation	DDYRDYDSPERERER CCCCCCCCHHHHHHH	23.56	29255136
69	Phosphorylation	RERERRNSDRSEDGY HHHHHHCCCCCCCCC	32.37	23898821
72	Phosphorylation	ERRNSDRSEDGYHSD HHHCCCCCCCCCCCC	45.06	23927012
76	Phosphorylation	SDRSEDGYHSDGDYG CCCCCCCCCCCCCCC	15.52	17081983
78	Phosphorylation	RSEDGYHSDGDYGEH CCCCCCCCCCCCCCC	34.50	23401153
82	Phosphorylation	GYHSDGDYGEHDYRH CCCCCCCCCCCCCCC	29.91	28985074
87	Phosphorylation	GDYGEHDYRHDISDE CCCCCCCCCCCCCCH	16.26	23927012
92	Phosphorylation	HDYRHDISDERESKT CCCCCCCCCHHHCCE	39.20	21406692
97	Phosphorylation	DISDERESKTIMLRG CCCCHHHCCEEEECC	41.12	22210691
99	Phosphorylation	SDERESKTIMLRGLP CCHHHCCEEEECCCC	22.39	22210691
108	Phosphorylation	MLRGLPITITESDIR EECCCCEEEEHHHHH	21.65	30576142
110	Phosphorylation	RGLPITITESDIREM CCCCEEEEHHHHHHH	22.30	30576142
112	Phosphorylation	LPITITESDIREMME CCEEEEHHHHHHHHH	29.68	30576142
189	Ubiquitination	FEDWLCNKCCLNNFR HHHHHCCHHHHCHHH	25.90	-
189	Acetylation	FEDWLCNKCCLNNFR HHHHHCCHHHHCHHH	25.90	26051181
219	Phosphorylation	EQEVPPGTTESVQSV CCCCCCCCCCCHHHC	32.91	29759185
220	Phosphorylation	QEVPPGTTESVQSVD CCCCCCCCCCHHHCC	31.98	29759185
242	Phosphorylation	LRNIAPHTVVDSIMT ECCCCCHHHHHHHHH	22.59	22817900
249	Phosphorylation	TVVDSIMTALSPYAS HHHHHHHHHHHHHHH	23.83	22817900
252	Phosphorylation	DSIMTALSPYASLAV HHHHHHHHHHHHHHH	17.25	22817900
254	Phosphorylation	IMTALSPYASLAVNN HHHHHHHHHHHHHHC	12.87	22817900
256	Phosphorylation	TALSPYASLAVNNIR HHHHHHHHHHHHCEE	15.83	22817900
306	Ubiquitination	PPLKIDGKTIGVDFA CCEEECCEEECHHHH	32.97	-
314	Acetylation	TIGVDFAKSARKDLV EECHHHHHHHCCCEE	44.64	25953088
314	Ubiquitination	TIGVDFAKSARKDLV EECHHHHHHHCCCEE	44.64	-
419	Phosphorylation	SPQLYNQTSNPPGSP CHHHCCCCCCCCCCC	27.17	26074081
420	Phosphorylation	PQLYNQTSNPPGSPT HHHCCCCCCCCCCCC	37.26	26074081
425	Phosphorylation	QTSNPPGSPTEEAQP CCCCCCCCCCCCCCC	34.13	26074081
427	Phosphorylation	SNPPGSPTEEAQPST CCCCCCCCCCCCCCC	48.42	26074081
433	Phosphorylation	PTEEAQPSTSTSTQA CCCCCCCCCCCCCCC	23.94	26074081
434	Phosphorylation	TEEAQPSTSTSTQAP CCCCCCCCCCCCCCC	42.58	26074081
435	Phosphorylation	EEAQPSTSTSTQAPA CCCCCCCCCCCCCCC	25.38	26074081
436	Phosphorylation	EAQPSTSTSTQAPAA CCCCCCCCCCCCCCC	35.56	26074081
437	Phosphorylation	AQPSTSTSTQAPAAS CCCCCCCCCCCCCCC	20.49	26074081
438	Phosphorylation	QPSTSTSTQAPAASP CCCCCCCCCCCCCCC	28.92	26074081
444	Phosphorylation	STQAPAASPTGVVPG CCCCCCCCCCCCCCC	25.71	24275569
446	Phosphorylation	QAPAASPTGVVPGTK CCCCCCCCCCCCCCE	39.86	24275569
542	Acetylation	KTAQQIAKDMERWAK HHHHHHHHHHHHHHH	60.27	23954790
549	Acetylation	KDMERWAKSLNKQKE HHHHHHHHHHHHHHH	48.82	7677699
553	Acetylation	RWAKSLNKQKENFKN HHHHHHHHHHHHHHH	68.95	7677709
561	Phosphorylation	QKENFKNSFQPVNSL HHHHHHHCCCCHHHH	26.33	26270265
567	Phosphorylation	NSFQPVNSLREEERR HCCCCHHHHCHHHHH	29.10	26270265
576	Phosphorylation	REEERRESAAADAGF CHHHHHHHHHHHHHH	22.77	28857561
620	Phosphorylation	KRGLVAAYSGDSDNE CCCCEEEECCCCCCH	11.93	25463755
621	Phosphorylation	RGLVAAYSGDSDNEE CCCEEEECCCCCCHH	31.25	22167270
624	Phosphorylation	VAAYSGDSDNEEELV EEEECCCCCCHHHHH	45.95	19664994
636	Phosphorylation	ELVERLESEEEKLAD HHHHHHHHHHHHHHH	55.70	23898821
669	Phosphorylation	LVRHQQLSDLHKQNM HHHHHHHHHHHHHCH	33.51	20068231
682	Phosphorylation	NMDIYRRSRLSEQEL CHHHHHHHCCCHHHH	28.68	29978859
685	Phosphorylation	IYRRSRLSEQELEAL HHHHHCCCHHHHHHH	35.80	29978859
711	Acetylation	RAAERREKYGIPEPP HHHHHHHHHCCCCCC	47.14	26051181
712	Phosphorylation	AAERREKYGIPEPPE HHHHHHHHCCCCCCC	18.61	17192257
724	Ubiquitination	PPEPKRKKQFDAGTV CCCCCCCCCCCCCCC	61.30	-
730	Phosphorylation	KKQFDAGTVNYEQPT CCCCCCCCCCCCCCC	13.80	30576142
733	Phosphorylation	FDAGTVNYEQPTKDG CCCCCCCCCCCCCCC	16.17	28796482
737	Phosphorylation	TVNYEQPTKDGIDHS CCCCCCCCCCCCCCC	41.27	21406692
744	Phosphorylation	TKDGIDHSNIGNKML CCCCCCCCHHHHHHH	26.79	30576142
749	Acetylation	DHSNIGNKMLQAMGW CCCHHHHHHHHHHCC	35.46	25953088
765	Sumoylation	EGSGLGRKCQGITAP CCCCCCCCCCCCCCC	29.16	-
765	Sumoylation	EGSGLGRKCQGITAP CCCCCCCCCCCCCCC	29.16	-
770	Phosphorylation	GRKCQGITAPIEAQV CCCCCCCCCCCEEEE	32.95	-
778	Methylation	APIEAQVRLKGAGLG CCCEEEEECCCCCCC	20.71	115385883
780	Methylation	IEAQVRLKGAGLGAK CEEEEECCCCCCCCC	35.83	115976455
787	Methylation	KGAGLGAKGSAYGLS CCCCCCCCCCCCCCC	52.15	115976463
789	Phosphorylation	AGLGAKGSAYGLSGA CCCCCCCCCCCCCCC	20.01	23401153
791	Phosphorylation	LGAKGSAYGLSGADS CCCCCCCCCCCCCHH	21.94	22817900
794	Phosphorylation	KGSAYGLSGADSYKD CCCCCCCCCCHHHHH	27.80	24719451
798	Phosphorylation	YGLSGADSYKDAVRK CCCCCCHHHHHHHHH	33.28	24719451
799	Phosphorylation	GLSGADSYKDAVRKA CCCCCHHHHHHHHHH	17.27	22817900
800	Ubiquitination	LSGADSYKDAVRKAM CCCCHHHHHHHHHHH	43.07	-
812	Phosphorylation	KAMFARFTEME---- HHHHHHHHCCC----	28.95	-

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 RBM5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM5_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 RBM5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRIF1_HUMAN	LRIF1	physical	16169070
DHX15_HUMAN	DHX15	physical	22365833
SR140_HUMAN	U2SURP	physical	22365833
ILF3_HUMAN	ILF3	physical	22365833
LSM8_HUMAN	LSM8	physical	22365833
PRP19_HUMAN	PRPF19	physical	22365833
WBP11_HUMAN	WBP11	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
DHX15_HUMAN	DHX15	physical	22569250
PRP19_HUMAN	PRPF19	physical	22569250
PRP8_HUMAN	PRPF8	physical	22569250
U520_HUMAN	SNRNP200	physical	22569250
U2AF2_HUMAN	U2AF2	physical	22569250

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 RBM5_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-542, 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-621 AND SER-624, ANDMASS 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-624, 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-621 AND SER-624, ANDMASS 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-621; SER-624 ANDTYR-712, AND MASS 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-624, AND MASSSPECTROMETRY.	18220336 [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-59 AND SER-624, AND MASSSPECTROMETRY.	17081983 [Abstract]