CPLM-012040

Genbank Nucleotide ID

Serine/arginine-rich splicing factor 9

Protein Synonyms/Alias

Pre-mRNA-splicing factor SRp30C; Splicing factor, arginine/serine-rich 9

Homo sapiens (Human)

Position	Peptide	Type	References
28	LPTDVREKDLEDLFY	ubiquitination	[1, 2, 3, 4]
36	DLEDLFYKYGRIREI	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
46	RIREIELKNRHGLVP	ubiquitination	[3, 4]
128	SGSWQDLKDHMREAG	ubiquitination	[1, 2, 3, 4]
144	VCYADVQKDGVGMVE	ubiquitination	[3]
155	GMVEYLRKEDMEYAL	ubiquitination	[2, 3]
164	DMEYALRKLDDTKFR	ubiquitination	[3]
169	LRKLDDTKFRSHEGE	ubiquitination	[1, 3, 6]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10.

DOMAIN 14 89 RRM 1.
DOMAIN 111 187 RRM 2.
REGION 188 200 Interacts with SAFB1.
MOD_RES 189 189 Phosphoserine.
MOD_RES 192 192 Phosphotyrosine.
MOD_RES 193 193 Phosphoserine.
MOD_RES 195 195 Phosphoserine.
MOD_RES 204 204 Phosphoserine.
MOD_RES 208 208 Phosphoserine.
MOD_RES 211 211 Phosphoserine.
MOD_RES 216 216 Phosphoserine.

Complete proteome; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005730; C:nucleolus; IDA:HPA.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO:0006376; P:mRNA splice site selection; TAS:ProtInc.
GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.

IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.