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Protein

RNA-binding protein with serine-rich domain 1

Gene

Rnps1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein with serine-rich domain 1
Gene namesi
Name:Rnps1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:97960. Rnps1.

Subcellular locationi

  • Nucleus By similarity
  • Nucleus speckle By similarity
  • Cytoplasm By similarity

  • Note: Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305RNA-binding protein with serine-rich domain 1PRO_0000081817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531PhosphoserineBy similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei157 – 1571PhosphoserineBy similarity
Modified residuei161 – 1611PhosphothreonineBy similarity
Modified residuei218 – 2181N6-acetyllysineCombined sources

Post-translational modificationi

Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99M28.
PaxDbiQ99M28.
PRIDEiQ99M28.

PTM databases

iPTMnetiQ99M28.
PhosphoSiteiQ99M28.

Expressioni

Gene expression databases

BgeeiENSMUSG00000034681.
CleanExiMM_RNPS1.
GenevisibleiQ99M28. MM.

Interactioni

Subunit structurei

Found in mRNA splicing-dependent exon junction complexes (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. Component of the active spliceosome. Associates with polysomes. Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10 (By similarity).By similarity

Protein-protein interaction databases

BioGridi202923. 5 interactions.
IntActiQ99M28. 1 interaction.
MINTiMINT-4124387.
STRINGi10090.ENSMUSP00000085867.

Structurei

3D structure databases

ProteinModelPortaliQ99M28.
SMRiQ99M28. Positions 157-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 24080RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 220220Necessary for interaction with the cleaved p110 isoform of CDC2L1By similarityAdd
BLAST
Regioni1 – 161161Necessary for interaction with SRP54, nuclear localization and exon-skippingBy similarityAdd
BLAST
Regioni69 – 12153Necessary for interactions with UPF2 and UPF3B and UPF2-dependent NMDBy similarityAdd
BLAST
Regioni156 – 24287Necessary for interaction with PNN and exon-skippingBy similarityAdd
BLAST
Regioni159 – 24486Interaction with SAP18 and ACIN1By similarityAdd
BLAST
Regioni238 – 30568Necessary for interaction with TRA2B, nuclear localization and exon-skippingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 6458Lys-richAdd
BLAST
Compositional biasi67 – 14175Ser-richAdd
BLAST
Compositional biasi128 – 15427Arg-richAdd
BLAST
Compositional biasi241 – 29858Arg/Pro-richAdd
BLAST

Domaini

The RRM domain is required for the formation of the ASAP complex.By similarity

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4209. Eukaryota.
ENOG4111PFV. LUCA.
GeneTreeiENSGT00730000111029.
HOGENOMiHOG000044325.
HOVERGENiHBG053138.
InParanoidiQ99M28.
KOiK14325.
OMAiPTKVHLG.
OrthoDBiEOG091G14LV.
PhylomeDBiQ99M28.
TreeFamiTF314165.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99M28-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK
60 70 80 90 100
ESSEKDRGRD KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS
110 120 130 140 150
SASSRSGSSS TSRSSSSSSS SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE
160 170 180 190 200
RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI FSTYGKIKMI DMPVERMHPH
210 220 230 240 250
LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA PWPRPPPRRF
260 270 280 290 300
SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS

SNSSR
Length:305
Mass (Da):34,208
Last modified:June 1, 2001 - v1
Checksum:i930C9D36C2486144
GO
Isoform 2 (identifier: Q99M28-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-24: Missing.

Show »
Length:282
Mass (Da):31,709
Checksum:iD3F7AAD16B6309F4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 2423Missing in isoform 2. 1 PublicationVSP_016244Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146443 mRNA. Translation: BAE27176.1.
AK151150 mRNA. Translation: BAE30156.1.
AK165905 mRNA. Translation: BAE38451.1.
BC002061 mRNA. Translation: AAH02061.1.
BC008089 mRNA. Translation: AAH08089.1.
CCDSiCCDS37487.1. [Q99M28-2]
CCDS37488.1. [Q99M28-1]
RefSeqiNP_001073596.1. NM_001080127.1. [Q99M28-1]
NP_001073597.1. NM_001080128.1. [Q99M28-2]
NP_033096.2. NM_009070.2. [Q99M28-1]
XP_006523984.1. XM_006523921.2. [Q99M28-1]
UniGeneiMm.1951.

Genome annotation databases

EnsembliENSMUST00000088512; ENSMUSP00000085867; ENSMUSG00000034681. [Q99M28-1]
ENSMUST00000115371; ENSMUSP00000111028; ENSMUSG00000034681. [Q99M28-2]
ENSMUST00000163717; ENSMUSP00000126345; ENSMUSG00000034681. [Q99M28-1]
GeneIDi19826.
KEGGimmu:19826.
UCSCiuc008avs.1. mouse. [Q99M28-1]
uc008avu.1. mouse. [Q99M28-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146443 mRNA. Translation: BAE27176.1.
AK151150 mRNA. Translation: BAE30156.1.
AK165905 mRNA. Translation: BAE38451.1.
BC002061 mRNA. Translation: AAH02061.1.
BC008089 mRNA. Translation: AAH08089.1.
CCDSiCCDS37487.1. [Q99M28-2]
CCDS37488.1. [Q99M28-1]
RefSeqiNP_001073596.1. NM_001080127.1. [Q99M28-1]
NP_001073597.1. NM_001080128.1. [Q99M28-2]
NP_033096.2. NM_009070.2. [Q99M28-1]
XP_006523984.1. XM_006523921.2. [Q99M28-1]
UniGeneiMm.1951.

3D structure databases

ProteinModelPortaliQ99M28.
SMRiQ99M28. Positions 157-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202923. 5 interactions.
IntActiQ99M28. 1 interaction.
MINTiMINT-4124387.
STRINGi10090.ENSMUSP00000085867.

PTM databases

iPTMnetiQ99M28.
PhosphoSiteiQ99M28.

Proteomic databases

MaxQBiQ99M28.
PaxDbiQ99M28.
PRIDEiQ99M28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088512; ENSMUSP00000085867; ENSMUSG00000034681. [Q99M28-1]
ENSMUST00000115371; ENSMUSP00000111028; ENSMUSG00000034681. [Q99M28-2]
ENSMUST00000163717; ENSMUSP00000126345; ENSMUSG00000034681. [Q99M28-1]
GeneIDi19826.
KEGGimmu:19826.
UCSCiuc008avs.1. mouse. [Q99M28-1]
uc008avu.1. mouse. [Q99M28-2]

Organism-specific databases

CTDi10921.
MGIiMGI:97960. Rnps1.

Phylogenomic databases

eggNOGiKOG4209. Eukaryota.
ENOG4111PFV. LUCA.
GeneTreeiENSGT00730000111029.
HOGENOMiHOG000044325.
HOVERGENiHBG053138.
InParanoidiQ99M28.
KOiK14325.
OMAiPTKVHLG.
OrthoDBiEOG091G14LV.
PhylomeDBiQ99M28.
TreeFamiTF314165.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRnps1. mouse.
PROiQ99M28.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034681.
CleanExiMM_RNPS1.
GenevisibleiQ99M28. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNPS1_MOUSE
AccessioniPrimary (citable) accession number: Q99M28
Secondary accession number(s): Q3TMJ1, Q922H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.