dbPTM

SPF45_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPF45_HUMAN
UniProt AC	Q96I25
Protein Name	Splicing factor 45
Gene Name	RBM17
Organism	Homo sapiens (Human).
Sequence Length	401
Subcellular Localization	Nucleus .
Protein Description	Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia..
Protein Sequence	MSLYDDLGVETSDSKTEGWSKNFKLLQSQLQVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIVDTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDATEKDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDEDLEVETKEECEKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGRVVKACFYNLDKFRVLDLAEQV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSLYDDLGV ------CCCCCCCCC	35.32	22223895
2	Phosphorylation	------MSLYDDLGV ------CCCCCCCCC	35.32	25159151
4	Phosphorylation	----MSLYDDLGVET ----CCCCCCCCCCC	10.49	23663014
11	Phosphorylation	YDDLGVETSDSKTEG CCCCCCCCCCCCCCH	35.11	27251275
12	Phosphorylation	DDLGVETSDSKTEGW CCCCCCCCCCCCCHH	26.78	27251275
14	Phosphorylation	LGVETSDSKTEGWSK CCCCCCCCCCCHHHH	41.04	27251275
15	Sumoylation	GVETSDSKTEGWSKN CCCCCCCCCCHHHHH	56.43	28112733
21	Ubiquitination	SKTEGWSKNFKLLQS CCCCHHHHHHHHHHH	60.95	19608861
21	Acetylation	SKTEGWSKNFKLLQS CCCCHHHHHHHHHHH	60.95	19608861
24	Sumoylation	EGWSKNFKLLQSQLQ CHHHHHHHHHHHHHH	58.65	28112733
24	Methylation	EGWSKNFKLLQSQLQ CHHHHHHHHHHHHHH	58.65	115976359
24	Acetylation	EGWSKNFKLLQSQLQ CHHHHHHHHHHHHHH	58.65	25953088
24	Sumoylation	EGWSKNFKLLQSQLQ CHHHHHHHHHHHHHH	58.65	-
28	Phosphorylation	KNFKLLQSQLQVKKA HHHHHHHHHHHHHHH	32.59	25159151
33	Acetylation	LQSQLQVKKAALTQA HHHHHHHHHHHHHHH	24.59	25953088
33	Sumoylation	LQSQLQVKKAALTQA HHHHHHHHHHHHHHH	24.59	28112733
33	Ubiquitination	LQSQLQVKKAALTQA HHHHHHHHHHHHHHH	24.59	-
34	Ubiquitination	QSQLQVKKAALTQAK HHHHHHHHHHHHHHH	39.78	-
41	Acetylation	KAALTQAKSQRTKQS HHHHHHHHHHHHHCC	36.99	25953088
41	Sumoylation	KAALTQAKSQRTKQS HHHHHHHHHHHHHCC	36.99	28112733
41	Ubiquitination	KAALTQAKSQRTKQS HHHHHHHHHHHHHCC	36.99	-
42	Phosphorylation	AALTQAKSQRTKQST HHHHHHHHHHHHCCC	28.10	26434776
45	Phosphorylation	TQAKSQRTKQSTVLA HHHHHHHHHCCCEEE	26.29	27251275
46	Ubiquitination	QAKSQRTKQSTVLAP HHHHHHHHCCCEEEE	44.43	-
48	Phosphorylation	KSQRTKQSTVLAPVI HHHHHHCCCEEEEEE	23.26	21406692
49	Phosphorylation	SQRTKQSTVLAPVID HHHHHCCCEEEEEEE	19.62	21406692
58	Sumoylation	LAPVIDLKRGGSSDD EEEEEECCCCCCCCC	45.29	28112733
58	Acetylation	LAPVIDLKRGGSSDD EEEEEECCCCCCCCC	45.29	7493371
58	Methylation	LAPVIDLKRGGSSDD EEEEEECCCCCCCCC	45.29	7493371
62	Phosphorylation	IDLKRGGSSDDRQIV EECCCCCCCCCCCHH	33.16	25159151
63	Phosphorylation	DLKRGGSSDDRQIVD ECCCCCCCCCCCHHC	46.97	25159151
66	Methylation	RGGSSDDRQIVDTPP CCCCCCCCCHHCCCC	32.87	115490659
71	Phosphorylation	DDRQIVDTPPHVAAG CCCCHHCCCCCHHCC	28.03	25159151
85	Phosphorylation	GLKDPVPSGFSAGEV CCCCCCCCCCCCCCE	53.34	20068231
88	Phosphorylation	DPVPSGFSAGEVLIP CCCCCCCCCCCEEEE	38.60	20068231
100	Phosphorylation	LIPLADEYDPMFPND EEECCCCCCCCCCCH	26.37	28122231
108	Phosphorylation	DPMFPNDYEKVVKRQ CCCCCCHHHHHHHHH	25.04	20068231
129	Acetylation	QRELERQKEIEEREK HHHHHHHHHHHHHHH	67.87	30591777
145	Phosphorylation	RKDRHEASGFARRPD HHHHHHHCCCCCCCC	31.30	26074081
155	Phosphorylation	ARRPDPDSDEDEDYE CCCCCCCCCCCHHHH	48.57	29255136
161	Phosphorylation	DSDEDEDYERERRKR CCCCCHHHHHHHHHH	18.16	27273156
169	Phosphorylation	ERERRKRSMGGAAIA HHHHHHHHHCCCCCC	25.47	29255136
170	Sulfoxidation	RERRKRSMGGAAIAP HHHHHHHHCCCCCCC	7.15	21406390
179	Phosphorylation	GAAIAPPTSLVEKDK CCCCCCCCCHHCCCC	33.36	20068231
180	Phosphorylation	AAIAPPTSLVEKDKE CCCCCCCCHHCCCCC	35.87	20068231
184	Acetylation	PPTSLVEKDKELPRD CCCCHHCCCCCCCCC	67.62	25953088
194	Phosphorylation	ELPRDFPYEEDSRPR CCCCCCCCCCCCCCC	31.76	28796482
198	Phosphorylation	DFPYEEDSRPRSQSS CCCCCCCCCCCCCCC	47.68	25159151
202	Phosphorylation	EEDSRPRSQSSKAAI CCCCCCCCCCCCCCC	36.78	25159151
204	Phosphorylation	DSRPRSQSSKAAIPP CCCCCCCCCCCCCCC	34.74	25159151
205	Phosphorylation	SRPRSQSSKAAIPPP CCCCCCCCCCCCCCC	20.76	25627689
214	Phosphorylation	AAIPPPVYEEQDRPR CCCCCCCCCCCCCCC	21.37	25159151
222	Phosphorylation	EEQDRPRSPTGPSNS CCCCCCCCCCCCCCC	29.51	29255136
224	Phosphorylation	QDRPRSPTGPSNSFL CCCCCCCCCCCCCHH	64.07	29255136
227	Phosphorylation	PRSPTGPSNSFLANM CCCCCCCCCCHHHHC	46.59	22167270
229	Phosphorylation	SPTGPSNSFLANMGG CCCCCCCCHHHHCCH	26.44	22167270
237	Phosphorylation	FLANMGGTVAHKIMQ HHHHCCHHHHHHHHH	14.59	30278072
241	Acetylation	MGGTVAHKIMQKYGF CCHHHHHHHHHHHCC	30.09	25953088
245	Acetylation	VAHKIMQKYGFREGQ HHHHHHHHHCCCCCC	29.93	25953088
245	Ubiquitination	VAHKIMQKYGFREGQ HHHHHHHHHCCCCCC	29.93	-
246	Phosphorylation	AHKIMQKYGFREGQG HHHHHHHHCCCCCCC	12.47	26074081
256	Ubiquitination	REGQGLGKHEQGLST CCCCCCCCCCCCHHH	49.35	-
256	Sumoylation	REGQGLGKHEQGLST CCCCCCCCCCCCHHH	49.35	28112733
256	Acetylation	REGQGLGKHEQGLST CCCCCCCCCCCCHHH	49.35	25953088
262	Phosphorylation	GKHEQGLSTALSVEK CCCCCCHHHEEEEEC	20.61	28450419
263	Phosphorylation	KHEQGLSTALSVEKT CCCCCHHHEEEEECC	36.34	28450419
266	Phosphorylation	QGLSTALSVEKTSKR CCHHHEEEEECCCCC	26.26	28450419
269	Acetylation	STALSVEKTSKRGGK HHEEEEECCCCCCCE	56.81	25953088
273	Methylation	SVEKTSKRGGKIIVG EEECCCCCCCEEEEC	59.88	115388077
276	Sumoylation	KTSKRGGKIIVGDAT CCCCCCCEEEECCCC	31.89	28112733
276	Acetylation	KTSKRGGKIIVGDAT CCCCCCCEEEECCCC	31.89	25953088
285	2-Hydroxyisobutyrylation	IVGDATEKDASKKSD EECCCCHHHCCCCCC	54.99	-
285	Acetylation	IVGDATEKDASKKSD EECCCCHHHCCCCCC	54.99	23749302
288	Phosphorylation	DATEKDASKKSDSNP CCCHHHCCCCCCCCC	51.23	23186163
291	Phosphorylation	EKDASKKSDSNPLTE HHHCCCCCCCCCHHH	50.43	30108239
293	Phosphorylation	DASKKSDSNPLTEIL HCCCCCCCCCHHHHH	47.65	25159151
297	Phosphorylation	KSDSNPLTEILKCPT CCCCCCHHHHHHCCC	23.41	30108239
304	Phosphorylation	TEILKCPTKVVLLRN HHHHHCCCHHEEEEC	46.04	21712546
305	Acetylation	EILKCPTKVVLLRNM HHHHCCCHHEEEECC	18.58	26051181
327	Acetylation	EDLEVETKEECEKYG CCCEECCHHHHHHHC	37.70	26051181
332	Acetylation	ETKEECEKYGKVGKC CCHHHHHHHCCCCEE	71.59	26051181
338	Acetylation	EKYGKVGKCVIFEIP HHHCCCCEEEEEECC	28.46	26051181
339	Glutathionylation	KYGKVGKCVIFEIPG HHCCCCEEEEEECCC	2.03	22555962
391	Acetylation	ACFYNLDKFRVLDLA HHEECCCCCEEHHHH	37.93	25825284
391	2-Hydroxyisobutyrylation	ACFYNLDKFRVLDLA HHEECCCCCEEHHHH	37.93	-

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
48	S	Phosphorylation	Kinase	CLK1	P49759	PSP
62	S	Phosphorylation	Kinase	CLK1	P49759	PSP
71	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
71	T	Phosphorylation	Kinase	JNK1	P45983	PSP
71	T	Phosphorylation	Kinase	P38A	Q16539	PSP
202	S	Phosphorylation	Kinase	CLK1	P49759	PSP
204	S	Phosphorylation	Kinase	CLK1	P49759	PSP
222	S	Phosphorylation	Kinase	CLK1	P49759	PSP
222	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
222	S	Phosphorylation	Kinase	JNK1	P45983	PSP
222	S	Phosphorylation	Kinase	P38A	Q16539	PSP
266	S	Phosphorylation	Kinase	CLK1	P49759	PSP
288	S	Phosphorylation	Kinase	CLK1	P49759	PSP
291	S	Phosphorylation	Kinase	CLK1	P49759	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPF45_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 SPF45_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SF3B1_HUMAN	SF3B1	physical	22365833
DHX15_HUMAN	DHX15	physical	22365833
SR140_HUMAN	U2SURP	physical	22365833
SF01_HUMAN	SF1	physical	22365833
SUGP1_HUMAN	SUGP1	physical	22365833
CWC15_HUMAN	CWC15	physical	22365833
S30BP_HUMAN	SAP30BP	physical	22365833
FAM9B_HUMAN	FAM9B	physical	25416956
SON_HUMAN	SON	physical	26344197
CHERP_HUMAN	CHERP	physical	28514442
SR140_HUMAN	U2SURP	physical	28514442
SFSWA_HUMAN	SFSWAP	physical	28514442
SF3A2_HUMAN	SF3A2	physical	28514442
RBM5_HUMAN	RBM5	physical	28514442
GPT11_HUMAN	GPATCH11	physical	28514442
SF3A3_HUMAN	SF3A3	physical	28514442
SF3A1_HUMAN	SF3A1	physical	28514442
SF3B2_HUMAN	SF3B2	physical	28514442
SF3B1_HUMAN	SF3B1	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
RBM10_HUMAN	RBM10	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 SPF45_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-21, AND MASS SPECTROMETRY.	19608861 [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-155, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-155 AND SER-169, ANDMASS SPECTROMETRY.	19690332 [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-155 AND SER-169, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.	18318008 [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-155, AND MASSSPECTROMETRY.	19367720 [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-169, 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 SER-155 AND SER-204, ANDMASS SPECTROMETRY.	17287340 [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-71 AND SER-155, AND MASSSPECTROMETRY.	17081983 [Abstract]