CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012528
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding protein with serine-rich domain 1 
Protein Synonyms/Alias
 SR-related protein LDC2 
Gene Name
 RNPS1 
Gene Synonyms/Alias
 LDC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
188FSTYGKIKMIDMPVEubiquitination[1]
203RMHPHLSKGYAYVEFubiquitination[2]
218ENPDEAEKALKHMDGacetylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Part of pre- and post- splicing multiprotein mRNP complexes. 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. 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. 
Sequence Annotation
 DOMAIN 161 240 RRM.
 REGION 1 220 Necessary for interaction with the
 REGION 1 161 Necessary for interaction with SRP54,
 REGION 69 121 Necessary for interactions with UPF2 and
 REGION 156 242 Necessary for interaction with PNN and
 REGION 238 305 Necessary for interaction with TRA2B,
 MOD_RES 53 53 Phosphoserine; by CK2.
 MOD_RES 155 155 Phosphoserine.
 MOD_RES 157 157 Phosphoserine.
 MOD_RES 161 161 Phosphothreonine.
 MOD_RES 218 218 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; mRNA processing; mRNA splicing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 305 AA 
Protein Sequence
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK ESSEKDRGRD 60
KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS SASSRSGSSS TSRSSSSSSS 120
SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI 180
FSTYGKIKMI DMPVERMHPH LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA 240
PWPRPPPRRF SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS 300
SNSSR 305 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS