RNPS1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNPS1_MOUSE
• UniProt AC: Q99M28
• Protein Name: RNA-binding protein with serine-rich domain 1
• Gene Name: Rnps1
• Organism: Mus musculus (Mouse).
• Sequence Length: 305
• Subcellular Localization: Nucleus. Nucleus speckle. Cytoplasm. Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity)..
• Protein Description: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions (By similarity)..
• Protein Sequence: MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKERKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPHLSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRFSPPRRMLPPPPMWRRSPPRMRRRSRSPRRRSPVRRRSRSPGRRRHRSRSSSNSSR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4 (in isoform 2)	Phosphorylation	-	36.96	29895711
4	Phosphorylation	----MDLSGVKKKSL ----CCCCCCCCHHH	36.96	24719451
6 (in isoform 2)	Phosphorylation	-	8.05	25367039
9	Acetylation	DLSGVKKKSLLGVKE CCCCCCCHHHCCCCC	40.39	7614525
10	Phosphorylation	LSGVKKKSLLGVKEN CCCCCCHHHCCCCCC	37.39	27600695
19	Acetylation	LGVKENNKKSSTRAP CCCCCCCCCCCCCCC	66.66	7614535
21	Phosphorylation	VKENNKKSSTRAPSP CCCCCCCCCCCCCCC	38.25	25266776
22	Phosphorylation	KENNKKSSTRAPSPT CCCCCCCCCCCCCCC	30.69	26745281
23	Phosphorylation	ENNKKSSTRAPSPTK CCCCCCCCCCCCCCC	37.63	26745281
27	Phosphorylation	KSSTRAPSPTKRKDR CCCCCCCCCCCCCCC	44.19	26824392
29	Phosphorylation	STRAPSPTKRKDRSD CCCCCCCCCCCCCCC	48.06	24453211
49	Phosphorylation	RSKDKGATKESSEKD HHHCCCCCHHHHHHH	43.97	20531401
52	Phosphorylation	DKGATKESSEKDRGR CCCCCHHHHHHHHCC	45.40	23684622
53	Phosphorylation	KGATKESSEKDRGRD CCCCHHHHHHHHCCC	50.16	23684622
75	Phosphorylation	ASSGSSSTRSRSSST CCCCCCCCCCCCCCC	34.31	22802335
80	Phosphorylation	SSTRSRSSSTSSSGS CCCCCCCCCCCCCCC	36.20	-
93	Phosphorylation	GSSTSTGSSSGSSSS CCCCCCCCCCCCCCC	22.78	-
94	Phosphorylation	SSTSTGSSSGSSSSS CCCCCCCCCCCCCCC	39.81	-
103	Phosphorylation	GSSSSSASSRSGSSS CCCCCCCCCCCCCCC	28.38	-
119	Phosphorylation	SRSSSSSSSSGSPSP CCCCCCCCCCCCCCC	30.39	23684622
120	Phosphorylation	RSSSSSSSSGSPSPS CCCCCCCCCCCCCCC	40.44	23684622
125	Phosphorylation	SSSSGSPSPSRRRHD CCCCCCCCCCHHHHH	36.89	23684622
155	Phosphorylation	EKERKRRSPSPKPTK HHHHHHCCCCCCCCE	33.49	23684622
157	Phosphorylation	ERKRRSPSPKPTKVH HHHHCCCCCCCCEEE	46.96	23684622
161	Phosphorylation	RSPSPKPTKVHIGRL CCCCCCCCEEEHHHH	52.40	23335269
173	Phosphorylation	GRLTRNVTKDHIMEI HHHCCCCCHHHHHHH	34.01	29895711
174	Acetylation	RLTRNVTKDHIMEIF HHCCCCCHHHHHHHH	42.92	22826441
182	Phosphorylation	DHIMEIFSTYGKIKM HHHHHHHHHCCCEEE	26.78	29895711
183	Phosphorylation	HIMEIFSTYGKIKMI HHHHHHHHCCCEEEE	26.08	29895711
186	Acetylation	EIFSTYGKIKMIDMP HHHHHCCCEEEEECC	28.83	22826441
205	Phosphorylation	HPHLSKGYAYVEFEN CCCCCCCEEEEEECC	9.86	-
218	Acetylation	ENPDEAEKALKHMDG CCHHHHHHHHHHCCC	67.10	23806337
218	Ubiquitination	ENPDEAEKALKHMDG CCHHHHHHHHHHCCC	67.10	-
251	Phosphorylation	RPPPRRFSPPRRMLP CCCCCCCCCCHHCCC	31.98	26824392
266	Phosphorylation	PPPMWRRSPPRMRRR CCCHHHCCCHHHHHC	30.59	26239621
274	Phosphorylation	PPRMRRRSRSPRRRS CHHHHHCCCCCCCCC	34.99	20450229
276	Phosphorylation	RMRRRSRSPRRRSPV HHHHCCCCCCCCCCC	24.81	20450229
281	Phosphorylation	SRSPRRRSPVRRRSR CCCCCCCCCCHHHCC	26.40	23384938
287	Phosphorylation	RSPVRRRSRSPGRRR CCCCHHHCCCCCCCC	34.99	23737553
289	Phosphorylation	PVRRRSRSPGRRRHR CCHHHCCCCCCCCCC	32.71	23737553

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RNPS1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
43	S	Phosphorylation	Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).	-
49	T	Phosphorylation	Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).	-
52	S	Phosphorylation	Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).	-
53	S	Phosphorylation	Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53).	-
53	S	Phosphorylation	Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RNPS1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FOXE3_MOUSE	Foxe3	physical	20211142

Drug and Disease Associations

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