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UniProtKB/Swiss-Prot entry Q15287

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RNPS1_HUMAN
Primary accession number Q15287
Secondary accession numbers O75308 Q32P25 Q8WY42 Q9NYG3
Integrated into Swiss-Prot on November 22, 2005
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 71)
Name and origin of the protein
Protein name RNA-binding protein with serine-rich domain 1
Synonym SR-related protein LDC2
Gene name
Name: RNPS1
Synonyms: LDC2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
DOI=10.1016/0378-1119(95)00571-4; PubMed=8543184 [NCBI, ExPASy, EBI, Israel, Japan]
Badolato J., Gardiner E., Morrison N., Eisman J.;
"Identification and characterisation of a novel human RNA-binding protein.";
Gene 166:323-327(1995).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC2L1, AND SUBCELLULAR LOCATION.
TISSUE=B-cell;
PubMed=9580558 [NCBI, ExPASy, EBI, Israel, Japan]
Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.;
"The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo.";
J. Cell Sci. 111:1495-1506(1998).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Harada K., Yang D., Yamada A., Shichijo S., Itoh K.;
"Identification of an alternatively spliced form of RNPS1.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
 NUCLEOTIDE SEQUENCE [MRNA] OF 78-305.
TISSUE=Kidney;
Lee D.-C., Ouyang P.;
"Direct interaction of LDC2, a SR-related protein with pinin.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
 FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE SPLICEOSOME, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/18.16.4560; PubMed=10449421 [NCBI, ExPASy, EBI, Israel, Japan]
Mayeda A., Badolato J., Kobayashi R., Zhang M.Q., Gardiner E.M., Krainer A.R.;
"Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing.";
EMBO J. 18:4560-4570(1999).
[7]
 IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; SRRM1 AND THOC4.
DOI=10.1093/emboj/19.24.6860; PubMed=11118221 [NCBI, ExPASy, EBI, Israel, Japan]
Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.;
"The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions.";
EMBO J. 19:6860-6869(2000).
[8]
 INTERACTION WITH SART3, AND SUBCELLULAR LOCATION.
DOI=10.1002/ijc.1391; PubMed=11477570 [NCBI, ExPASy, EBI, Israel, Japan]
Harada K., Yamada A., Yang D., Itoh K., Shichijo S.;
"Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation.";
Int. J. Cancer 93:623-628(2001).
[9]
 FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD), IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; RBM8A; RENT1; RENT2; RENT3A AND RENT3B, RNA-BINDING, AND SUBCELLULAR LOCATION.
DOI=10.1126/science.1062786; PubMed=11546874 [NCBI, ExPASy, EBI, Israel, Japan]
Lykke-Andersen J., Shu M.-D., Steitz J.A.;
"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.";
Science 293:1836-1839(2001).
[10]
 FUNCTION IN MRNA 3'-END FORMATION, AND INTERACTION WITH SRRM1.
DOI=10.1074/jbc.M306856200; PubMed=12944400 [NCBI, ExPASy, EBI, Israel, Japan]
McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
"An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.";
J. Biol. Chem. 278:44153-44160(2003).
[11]
 IDENTIFICATION IN A MRNP COMPLEX WITH PININ, INTERACTION WITH PNN, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.23.20.7363-7376.2003; PubMed=14517304 [NCBI, ExPASy, EBI, Israel, Japan]
Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.;
"Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1.";
Mol. Cell. Biol. 23:7363-7376(2003).
[12]
 FUNCTION IN TRANSLATIONAL ACTIVITY AND NONSENSE-MEDIATED MRNA DECAY (NMD), AND ASSOCIATION WITH POLYSOMES.
DOI=10.1101/gad.1163204; PubMed=14752011 [NCBI, ExPASy, EBI, Israel, Japan]
Nott A., Le Hir H., Moore M.J.;
"Splicing enhances translation in mammalian cells: an additional function of the exon junction complex.";
Genes Dev. 18:210-222(2004).
[13]
 IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RBM8A AND SRRM1.
DOI=10.1074/jbc.M307692200; PubMed=14625303 [NCBI, ExPASy, EBI, Israel, Japan]
Kataoka N., Dreyfuss G.;
"A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex.";
J. Biol. Chem. 279:7009-7013(2004).
[14]
 FUNCTION IN ALTERNATIVE PRE-MRNA SPLICING, INTERACTION WITH PNN; SFRS10 AND SRP54, MUTAGENESIS OF TYR-205 AND TYR-207, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.24.3.1174-1187.2004; PubMed=14729963 [NCBI, ExPASy, EBI, Israel, Japan]
Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.;
"Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo.";
Mol. Cell. Biol. 24:1174-1187(2004).
[15]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-155 AND SER-157, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[16]
 FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVE SPLICEOSOME, PHOSPHORYLATION, PHOSPHORYLATION AT SER-53, MASS SPECTROMETRY, INTERACTION WITH CSNK2A1, MUTAGENESIS OF SER-53, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.25.4.1446-1457.2005; PubMed=15684395 [NCBI, ExPASy, EBI, Israel, Japan]
Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., Suzuki H., Endo H., Kidd V.J., Mayeda A.;
"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation.";
Mol. Cell. Biol. 25:1446-1457(2005).
[17]
 FUNCTION IN A RENT2-DEPENDENT NONSENSE-MEDIATED MRNA DECAY (NMD), AND IDENTIFICATION IN A COMPLEX WITH RENT2 AND RENT3B.
DOI=10.1016/j.molcel.2005.08.012; PubMed=16209946 [NCBI, ExPASy, EBI, Israel, Japan]
Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.;
"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements.";
Mol. Cell 20:65-75(2005).
[18]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[19]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-251; SER-266; SER-287 AND SER-289, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[20]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L37368; AAA92859.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF015608; AAC39791.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF274003; AAL56665.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001659; AAH01659.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001838; AAH01838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108316; AAI08317.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF247662; AAF72519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4525; JC4525.
RefSeq NP_006702.1; -.
NP_542161.1; -.
UniGene Hs.355643
3D structure databases
HSSP Q9V535; 1HL6. [HSSP ENTRY / PDB]
ModBase Q15287.
Protein-protein interaction databases
IntAct Q15287; -.
PTM databases
PhosphoSite Q15287; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_1788; Transcription.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.
Organism-specific databases
H-InvDB HIX0012719; -.
HIX0031789; -.
HGNC HGNC:10080; RNPS1.
GenAtlas RNPS1.
MIM 606447; gene. [NCBI / EBI]
PharmGKB PA34453; -.
GeneCards Q15287.
Gene expression databases
ArrayExpress Q15287; -.
CleanEx HS_RNPS1; -.
GermOnline ENSG00000205937; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (traceable author statement from ProtInc).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
GO:0006350; Biological process: transcription (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
Pfam PF00076; RRM_1; 1.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 1.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q15287.
Genome annotation databases
Ensembl ENSG00000205937; Homo sapiens. [Contig view]
GeneID 10921; -.
KEGG hsa:10921; -.
Phylogenomic databases
HOGENOM Q15287; -.
HOVERGEN Q15287; -.
Other
SOURCE RNPS1; Homo sapiens.
ProtoNet Q15287.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   305  305     RNA-binding protein with serine-rich domain 1. PRO_0000081816
DOMAIN   161   240  80     RRM. 
REGION   1   220  220     Necessary for interaction with the cleaved p110 isoform of CDC2L1. 
REGION   1   161  161     Necessary for interaction with SRP54, nuclear localization and exon-skipping. 
REGION   69   121  53     Necessary for interactions with RENT2 and REN3B and RENT2-dependent NMD. 
REGION   156   242  87     Necessary for interaction with PNN and exon-skipping. 
REGION   238   305  68     Necessary for interaction with SFRS10, nuclear localization and exon-skipping. 
COMPBIAS   7    64  58     Lys-rich. 
COMPBIAS   67   141  75     Ser-rich. 
COMPBIAS   128   154  27     Arg-rich. 
COMPBIAS   241   298  58     Arg/Pro-rich. 
MOD_RES   27    27        Phosphoserine. 
MOD_RES   53    53        Phosphoserine; by CK2. 
MOD_RES   125   125        Phosphoserine. 
MOD_RES   155   155        Phosphoserine. 
MOD_RES   157   157        Phosphoserine. 
MOD_RES   205   205        Phosphotyrosine. 
MOD_RES   251   251        Phosphoserine. 
MOD_RES   266   266        Phosphoserine. 
MOD_RES   287   287        Phosphoserine. 
MOD_RES   289   289        Phosphoserine. 
VAR_SEQ   2    24        Missing (in isoform 2). VSP_016243
MUTAGEN   53    53        S->A: Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. 
MUTAGEN   53    53        S->E: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. 
MUTAGEN   205   205        Y->A: Abolishes exon-skipping. 
MUTAGEN   207   207        Y->A: Abolishes exon-skipping. 
CONFLICT   66    66        R -> G (in Ref. 2; AAC39791). 
Sequence information
Length: 305 AA [This is the length of the unprocessed precursor] Molecular weight: 34208 Da [This is the MW of the unprocessed precursor] CRC64: 930C9D36C2486144 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK ESSEKDRGRD 

        70         80         90        100        110        120 
KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS SASSRSGSSS TSRSSSSSSS 

       130        140        150        160        170        180 
SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI 

       190        200        210        220        230        240 
FSTYGKIKMI DMPVERMHPH LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA 

       250        260        270        280        290        300 
PWPRPPPRRF SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS 


SNSSR
Q15287 in FASTA format

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