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RNA-binding protein with serine-rich domain 1

 
Known also as: SR-related protein LDC2

Known abbreviations: RNPS1, LDC2

 

FUNCTION:
 
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. 
 
SUBUNIT STRUCTURE:
 
Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and ALYREF/THOC4. Forms heterodimers with ACIN1. Found in a heterotrimeric complex with ACIN1, RNPS1 and SAP18. Component of the active spliceosome. Associates with polysomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10. 
 
CELLULAR LOCALIZATION:
 
Nucleus. Nucleus speckle. Cytoplasm. Note: Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
 
TISSUE SPECIFICITY:
 
Ubiquitous. 
 
POST-TRANSLATIONAL MODIFICATION:
 
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.



This protein can be a part of a given complexes: Activities in which RNA-binding protein with serine-rich domain 1 is involved: Pathways in which RNA-binding protein with serine-rich domain 1 is involved:

NCBI GI number(s): 6857826
312261235
18379334
312261234
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q15287 Q15287
BRENDA - -
KEGG hsa:10921 hsa:10921
PFAM: PF00076
PF00076
InterPro: IPR012677
IPR000504
IPR012677
IPR000504
CATH: - -
SCOP: - -
Solved crystal structures: 4A8X
[PDB] [details]


Protein sequence:
MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATK
ESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSS
SASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKE
RKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPH
LSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRF
SPPRRMLPPPPMWRRSPPRMRRRSRSPRRRSPVRRRSRSPGRRRHRSRSS
SNSSR

RNA-binding protein with serine-rich domain 1 (Homo sapiens) is product of expression of RNPS1 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements. Gehring NH, Kunz JB, Neu-Yilik G, Breit S, Viegas MH, Hentze MW, Kulozik AE Mol Cell 2005-10-07 (20) 16209946
The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo. Loyer P, Trembley JH, Lahti JM, Kidd VJ J Cell Sci 1998-06-01 (None) 9580558
Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Lykke-Andersen J, Shu MD, Steitz JA Science 2001-09-07 (293) 11546874
Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation. Harada K, Yamada A, Yang D, Itoh K, Shichijo S Int J Cancer 2001-09-01 (93) 11477570
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
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 2009-08-14 (325) 19608861
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ Nat Biotechnol 2005-02-01 (23) 15592455
The sequence and analysis of duplication-rich human chromosome 16. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M Nature 2004-12-23 (432) 15616553
Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core. Tange TO, Shibuya T, Jurica MS, Moore MJ RNA 2005-12-01 (11) 16314458
The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. Le Hir H, Izaurralde E, Maquat LE, Moore MJ EMBO J 2000-12-15 (19) 11118221
An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation. McCracken S, Longman D, Johnstone IL, Caceres JF, Blencowe BJ J Biol Chem 2003-11-07 (278) 12944400
Assembly and mobility of exon-exon junction complexes in living cells. Schmidt U, Im KB, Benzing C, Janjetovic S, Rippe K, Lichter P, Wachsmuth M RNA 2009-05-01 (15) 19324961
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A 2004-08-17 (101) 15302935
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A Proc Natl Acad Sci U S A 2007-01-13 (104) 17287340
A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex. Kataoka N, Dreyfuss G J Biol Chem 2004-01-20 (279) 14625303
Identification and characterisation of a novel human RNA-binding protein. Badolato J, Gardiner E, Morrison N, Eisman J Gene 1995-12-12 (166) 8543184
Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing. Mayeda A, Badolato J, Kobayashi R, Zhang MQ, Gardiner EM, Krainer AR EMBO J 1999-08-16 (18) 10449421
Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1. Li C, Lin RI, Lai MC, Ouyang P, Tarn WY Mol Cell Biol 2003-10-01 (23) 14517304
Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Nott A, Le Hir H, Moore MJ Genes Dev 2004-02-15 (18) 14752011
Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo. Sakashita E, Tatsumi S, Werner D, Endo H, Mayeda A Mol Cell Biol 2004-01-01 (24) 14729963
Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation. Trembley JH, Tatsumi S, Sakashita E, Loyer P, Slaughter CA, Suzuki H, Endo H, Kidd VJ, Mayeda A Mol Cell Biol 2005-01-01 (25) 15684395
The abundance of RNPS1, a protein component of the exon junction complex, can determine the variability in efficiency of the Nonsense Mediated Decay pathway. Viegas MH, Gehring NH, Breit S, Hentze MW, Kulozik AE Nucleic Acids Res 2007-01-01 (35) 17586820



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Last modification of this entry: Sept. 25, 2012.

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