Tag | Content |
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CPLM ID | CPLM-014858 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | RNA-binding protein with serine-rich domain 1 |
Protein Synonyms/Alias | |
Gene Name | Rnps1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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218 | ENPDEAEKALKHMDG | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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 (By similarity). |
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 similarity). MOD_RES 155 155 Phosphoserine (By similarity). MOD_RES 157 157 Phosphoserine (By similarity). MOD_RES 161 161 Phosphothreonine (By similarity). MOD_RES 218 218 N6-acetyllysine (By similarity). |
Keyword | Acetylation; 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 DRSKDKGTTK 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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. GO:0000166; F:nucleotide binding; IEA:InterPro. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW. GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |