dbPTM

SPF45_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPF45_MOUSE
UniProt AC	Q8JZX4
Protein Name	Splicing factor 45
Gene Name	Rbm17
Organism	Mus musculus (Mouse).
Sequence Length	405
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 (By similarity)..
Protein Sequence	MSLYDDLGVETSDSKTEGWSKNFKLLQSQLQVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIADTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFSRRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEPDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDATEKGEAQDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDEDLEVETKEECEKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGRVVKACFYNLDKFRVLDLAEQV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLYDDLGV ------CCCCCCCCC	35.32	-
2	Acetylation	------MSLYDDLGV ------CCCCCCCCC	35.32	-
11	Phosphorylation	YDDLGVETSDSKTEG CCCCCCCCCCCCCCH	35.11	-
12	Phosphorylation	DDLGVETSDSKTEGW CCCCCCCCCCCCCHH	26.78	-
14	Phosphorylation	LGVETSDSKTEGWSK CCCCCCCCCCCHHHH	41.04	-
21	Acetylation	SKTEGWSKNFKLLQS CCCCHHHHHHHHHHH	60.95	-
24	Acetylation	EGWSKNFKLLQSQLQ CHHHHHHHHHHHHHH	58.65	22826441
41	Malonylation	KAALTQAKSQRTKQS HHHHHHHHHHHHHCC	36.99	26320211
41	Acetylation	KAALTQAKSQRTKQS HHHHHHHHHHHHHCC	36.99	23806337
58	Acetylation	LAPVIDLKRGGSSDD EEEEEECCCCCCCCC	45.29	7493375
62	Phosphorylation	IDLKRGGSSDDRQIA EECCCCCCCCCCHHC	33.16	26643407
63	Phosphorylation	DLKRGGSSDDRQIAD ECCCCCCCCCCHHCC	46.97	26643407
71	Phosphorylation	DDRQIADTPPHVAAG CCCHHCCCCCCHHCC	29.69	25521595
155	Phosphorylation	SRRPDPDSDEDEDYE CCCCCCCCCCCHHHH	48.57	27087446
161	Phosphorylation	DSDEDEDYERERRKR CCCCCHHHHHHHHHH	18.16	25619855
169	Phosphorylation	ERERRKRSMGGAAIA HHHHHHHHHCCCCCC	25.47	21082442
179	Phosphorylation	GAAIAPPTSLVEKDK CCCCCCCCCHHCCCC	33.36	28833060
180	Phosphorylation	AAIAPPTSLVEKDKE CCCCCCCCHHCCCCC	35.87	28833060
194	Phosphorylation	ELPRDFPYEEDSRPR CCCCCCCCCCCCCCC	31.76	25159016
198	Phosphorylation	DFPYEEDSRPRSQSS CCCCCCCCCCCCCCC	47.68	25159016
214	Phosphorylation	AAIPPPVYEEPDRPR CCCCCCCCCCCCCCC	21.98	26239621
222	Phosphorylation	EEPDRPRSPTGPSNS CCCCCCCCCCCCCCC	29.51	25521595
224	Phosphorylation	PDRPRSPTGPSNSFL CCCCCCCCCCCCCHH	64.07	25521595
227	Phosphorylation	PRSPTGPSNSFLANM CCCCCCCCCCHHHHC	46.59	25521595
229	Phosphorylation	SPTGPSNSFLANMGG CCCCCCCCHHHHCCH	26.44	24925903
237	Phosphorylation	FLANMGGTVAHKIMQ HHHHCCHHHHHHHHH	14.59	25619855
256	Acetylation	REGQGLGKHEQGLST CCCCCCCCCCCCHHH	49.35	22826441
262	Phosphorylation	GKHEQGLSTALSVEK CCCCCCHHHCEEEEC	20.61	26643407
263	Phosphorylation	KHEQGLSTALSVEKT CCCCCHHHCEEEECC	36.34	26643407
266	Phosphorylation	QGLSTALSVEKTSKR CCHHHCEEEECCCCC	26.26	26643407
295	Phosphorylation	AQDASKKSDSNPLTE HHCCCCCCCCCCHHH	50.43	-
297	Phosphorylation	DASKKSDSNPLTEIL CCCCCCCCCCHHHHH	47.65	25338131
331	Acetylation	EDLEVETKEECEKYG CCCEECCHHHHHHHC	37.70	19865061
336	Acetylation	ETKEECEKYGKVGKC CCHHHHHHHCCCCEE	71.59	19865071
342	Acetylation	EKYGKVGKCVIFEIP HHHCCCCEEEEEECC	28.46	19865081
343	S-nitrosocysteine	KYGKVGKCVIFEIPG HHCCCCEEEEEECCC	2.03	-
343	S-nitrosylation	KYGKVGKCVIFEIPG HHCCCCEEEEEECCC	2.03	20925432
395	Acetylation	ACFYNLDKFRVLDLA HHEECCCCCEEHHHH	37.93	22826441

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 SPF45_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPF45_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SPF45_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SPF45_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.	19367708 [Abstract]