6ff7

Structural highlights

Disease

[U520_HUMAN] Retinitis pigmentosa. Retinitis pigmentosa 33 (RP33) [MIM:610359]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by mutations affecting the gene represented in this entry.^{[1] [2] [3] [4] [5]} [CDC5L_HUMAN] Note=A chromosomal aberration involving CDC5L is found in multicystic renal dysplasia. Translocation t(6;19)(p21;q13.1) with USF2. [R113A_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. [SNIP1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. [U5S1_HUMAN] Mandibulofacial dysostosis-microcephaly syndrome. The disease is caused by mutations affecting the gene represented in this entry. [PRP8_HUMAN] Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM:600059]. RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP13 inheritance is autosomal dominant.^{[6] [7]} [:]^{[8] [9]}

Function

[SPF27_HUMAN] Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR).^[10] [PRP19_HUMAN] Plays a role in DNA double-strand break (DSB) repair. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.^{[11] [12] [13] [14] [15] [16]} [SF3B2_HUMAN] Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. [CWC15_HUMAN] Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.^[17] [SRRM2_HUMAN] Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity). Binds to RNA.^[18] [SF3A3_HUMAN] Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. [RSMB_HUMAN] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. May have a functional role in the pre-mRNA splicing or in snRNP structure. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner (By similarity). [PHF5A_HUMAN] Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha. Also involved in pre-mRNA splicing.^[19] [SF3B3_HUMAN] Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. [SF3B6_HUMAN] Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA (PubMed:12234937). Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing (PubMed:16432215). Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively (PubMed:16432215).^{[20] [21] [22]} [RUXF_HUMAN] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [CRNL1_HUMAN] Involved in pre-mRNA splicing process. [SRRM1_HUMAN] Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates.^{[23] [24] [25] [26] [27] [28]} [U520_HUMAN] RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.^{[29] [30] [31] [32]} [SF3B1_HUMAN] Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. [SNW1_HUMAN] Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD. Proposed to be involved in transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed promoters. Is recruited by HIV-1 Tat to Tat:P-TEFb:TAR RNA complexes and is involved in Tat transcription by recruitment of MYC, MEN1 and TRRAP to the HIV promoter. Functions as a splicing factor in pre-mRNA splicing. Is required in the specific splicing of CDKN1A pre-mRNA; the function probably involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA.^{[33] [34] [35] [36] [37] [38] [39] [40] [41] [42] [43] [44] [45]} [SNR40_HUMAN] Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs.^[46] [CWC22_HUMAN] Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay.^{[47] [48] [49]} [PLRG1_HUMAN] Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. [DHX16_HUMAN] Involved in pre-mRNA splicing. Contributes to pre-mRNA splicing after spliceosome formation and prior to the first transesterification reaction.^{[50] [51] [52]} [RUXG_HUMAN] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [CWC27_HUMAN] PPIases accelerate the folding of proteins. [PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. [CDC5L_HUMAN] DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.^{[53] [54] [55] [56] [57] [58] [59] [60] [61]} [SNIP1_HUMAN] Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA.^{[62] [63] [64] [65]} [SF3A2_HUMAN] Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. [ISY1_HUMAN] May play a role in pre-mRNA splicing as component of the spliceosome.^{[66] [67]} [SMD2_HUMAN] Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity). [AQR_HUMAN] Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis. Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly. May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing.^[68] [U5S1_HUMAN] Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP. [RUXE_HUMAN] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [PRP17_HUMAN] Associates with the spliceosome late in the splicing pathway and may function in the second step of pre-mRNA splicing.^[69] [SF3A1_HUMAN] Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. [RBM22_HUMAN] Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses.^{[70] [71] [72]} [PRP8_HUMAN] Central component of the spliceosome, which may play a role in aligning the pre-mRNA 5'- and 3'-exons for ligation. Interacts with U5 snRNA, and with pre-mRNA 5'-splice sites in B spliceosomes and 3'-splice sites in C spliceosomes. [RU2B_HUMAN] Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA only in presence of the U2A' protein. [SYF1_HUMAN] Involved in transcription-coupled repair (TCR), transcription and pre-mRNA splicing.^{[73] [74]} [SMD1_HUMAN] May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. [RU2A_HUMAN] This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA. [SMD3_HUMAN] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner.^[75] [PPIL1_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.^[76]

See Also

• Pre-mRNA splicing factors 3D structures

References

1. ↑ Liu S, Rauhut R, Vornlocher HP, Luhrmann R. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. RNA. 2006 Jul;12(7):1418-30. Epub 2006 May 24. PMID:16723661 doi:rna.55406
2. ↑ Santos KF, Jovin SM, Weber G, Pena V, Luhrmann R, Wahl MC. Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045696 doi:10.1073/pnas.1208098109
3. ↑ Zhao C, Bellur DL, Lu S, Zhao F, Grassi MA, Bowne SJ, Sullivan LS, Daiger SP, Chen LJ, Pang CP, Zhao K, Staley JP, Larsson C. Autosomal-dominant retinitis pigmentosa caused by a mutation in SNRNP200, a gene required for unwinding of U4/U6 snRNAs. Am J Hum Genet. 2009 Nov;85(5):617-27. Epub 2009 Oct 29. PMID:19878916 doi:S0002-9297(09)00455-8
4. ↑ Li N, Mei H, MacDonald IM, Jiao X, Hejtmancik JF. Mutations in ASCC3L1 on 2q11.2 are associated with autosomal dominant retinitis pigmentosa in a Chinese family. Invest Ophthalmol Vis Sci. 2010 Feb;51(2):1036-43. doi: 10.1167/iovs.09-3725., Epub 2009 Aug 26. PMID:19710410 doi:10.1167/iovs.09-3725
5. ↑ Benaglio P, McGee TL, Capelli LP, Harper S, Berson EL, Rivolta C. Next generation sequencing of pooled samples reveals new SNRNP200 mutations associated with retinitis pigmentosa. Hum Mutat. 2011 Jun;32(6):E2246-58. doi: 10.1002/humu.21485. Epub 2011 Feb 24. PMID:21618346 doi:10.1002/humu.21485
6. ↑ Pena V, Liu S, Bujnicki JM, Luhrmann R, Wahl MC. Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa. Mol Cell. 2007 Feb 23;25(4):615-24. PMID:17317632 doi:10.1016/j.molcel.2007.01.023
7. ↑ McKie AB, McHale JC, Keen TJ, Tarttelin EE, Goliath R, van Lith-Verhoeven JJ, Greenberg J, Ramesar RS, Hoyng CB, Cremers FP, Mackey DA, Bhattacharya SS, Bird AC, Markham AF, Inglehearn CF. Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal dominant retinitis pigmentosa (RP13). Hum Mol Genet. 2001 Jul 15;10(15):1555-62. PMID:11468273
8. ↑ van Lith-Verhoeven JJ, van der Velde-Visser SD, Sohocki MM, Deutman AF, Brink HM, Cremers FP, Hoyng CB. Clinical characterization, linkage analysis, and PRPC8 mutation analysis of a family with autosomal dominant retinitis pigmentosa type 13 (RP13). Ophthalmic Genet. 2002 Mar;23(1):1-12. PMID:11910553
9. ↑ Martinez-Gimeno M, Gamundi MJ, Hernan I, Maseras M, Milla E, Ayuso C, Garcia-Sandoval B, Beneyto M, Vilela C, Baiget M, Antinolo G, Carballo M. Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31 in Spanish families with autosomal dominant retinitis pigmentosa. Invest Ophthalmol Vis Sci. 2003 May;44(5):2171-7. PMID:12714658
10. ↑ Marechal A, Li JM, Ji XY, Wu CS, Yazinski SA, Nguyen HD, Liu S, Jimenez AE, Jin J, Zou L. PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry. Mol Cell. 2014 Jan 23;53(2):235-46. doi: 10.1016/j.molcel.2013.11.002. Epub 2013 , Dec 12. PMID:24332808 doi:http://dx.doi.org/10.1016/j.molcel.2013.11.002
11. ↑ Gotzmann J, Gerner C, Meissner M, Holzmann K, Grimm R, Mikulits W, Sauermann G. hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions. Exp Cell Res. 2000 Nov 25;261(1):166-79. PMID:11082287 doi:10.1006/excr.2000.5025
12. ↑ Mahajan KN, Mitchell BS. Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase. Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):10746-51. Epub 2003 Sep 5. PMID:12960389 doi:http://dx.doi.org/10.1073/pnas.1631060100
13. ↑ Grillari J, Ajuh P, Stadler G, Loscher M, Voglauer R, Ernst W, Chusainow J, Eisenhaber F, Pokar M, Fortschegger K, Grey M, Lamond AI, Katinger H. SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly. Nucleic Acids Res. 2005 Dec 6;33(21):6868-83. Print 2005. PMID:16332694 doi:33/21/6868
14. ↑ Loscher M, Fortschegger K, Ritter G, Wostry M, Voglauer R, Schmid JA, Watters S, Rivett AJ, Ajuh P, Lamond AI, Katinger H, Grillari J. Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome. Biochem J. 2005 Jun 1;388(Pt 2):593-603. PMID:15660529 doi:10.1042/BJ20041517
15. ↑ Zhang N, Kaur R, Lu X, Shen X, Li L, Legerski RJ. The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links. J Biol Chem. 2005 Dec 9;280(49):40559-67. Epub 2005 Oct 12. PMID:16223718 doi:M508453200
16. ↑ Voglauer R, Chang MW, Dampier B, Wieser M, Baumann K, Sterovsky T, Schreiber M, Katinger H, Grillari J. SNEV overexpression extends the life span of human endothelial cells. Exp Cell Res. 2006 Apr 1;312(6):746-59. Epub 2006 Jan 4. PMID:16388800 doi:S0014-4827(05)00560-4
17. ↑ Grote M, Wolf E, Will CL, Lemm I, Agafonov DE, Schomburg A, Fischle W, Urlaub H, Luhrmann R. Molecular architecture of the human Prp19/CDC5L complex. Mol Cell Biol. 2010 May;30(9):2105-19. doi: 10.1128/MCB.01505-09. Epub 2010 Feb, 22. PMID:20176811 doi:http://dx.doi.org/10.1128/MCB.01505-09
18. ↑ Blencowe BJ, Bauren G, Eldridge AG, Issner R, Nickerson JA, Rosonina E, Sharp PA. The SRm160/300 splicing coactivator subunits. RNA. 2000 Jan;6(1):111-20. PMID:10668804
19. ↑ Will CL, Urlaub H, Achsel T, Gentzel M, Wilm M, Luhrmann R. Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J. 2002 Sep 16;21(18):4978-88. PMID:12234937
20. ↑ Will CL, Urlaub H, Achsel T, Gentzel M, Wilm M, Luhrmann R. Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J. 2002 Sep 16;21(18):4978-88. PMID:12234937
21. ↑ Schellenberg MJ, Edwards RA, Ritchie DB, Kent OA, Golas MM, Stark H, Luhrmann R, Glover JN, MacMillan AM. Crystal structure of a core spliceosomal protein interface. Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1266-71. Epub 2006 Jan 23. PMID:16432215
22. ↑ Cretu C, Schmitzova J, Ponce-Salvatierra A, Dybkov O, De Laurentiis EI, Sharma K, Will CL, Urlaub H, Luhrmann R, Pena V. Molecular Architecture of SF3b and Structural Consequences of Its Cancer-Related Mutations. Mol Cell. 2016 Oct 20;64(2):307-319. doi: 10.1016/j.molcel.2016.08.036. Epub 2016, Oct 6. PMID:27720643 doi:http://dx.doi.org/10.1016/j.molcel.2016.08.036
23. ↑ Blencowe BJ, Issner R, Nickerson JA, Sharp PA. A coactivator of pre-mRNA splicing. Genes Dev. 1998 Apr 1;12(7):996-1009. PMID:9531537
24. ↑ Eldridge AG, Li Y, Sharp PA, Blencowe BJ. The SRm160/300 splicing coactivator is required for exon-enhancer function. Proc Natl Acad Sci U S A. 1999 May 25;96(11):6125-30. PMID:10339552
25. ↑ Blencowe BJ, Bauren G, Eldridge AG, Issner R, Nickerson JA, Rosonina E, Sharp PA. The SRm160/300 splicing coactivator subunits. RNA. 2000 Jan;6(1):111-20. PMID:10668804
26. ↑ McCracken S, Lambermon M, Blencowe BJ. SRm160 splicing coactivator promotes transcript 3'-end cleavage. Mol Cell Biol. 2002 Jan;22(1):148-60. PMID:11739730
27. ↑ McCracken S, Longman D, Johnstone IL, Caceres JF, Blencowe BJ. An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation. J Biol Chem. 2003 Nov 7;278(45):44153-60. Epub 2003 Aug 27. PMID:12944400 doi:http://dx.doi.org/10.1074/jbc.M306856200
28. ↑ Szymczyna BR, Bowman J, McCracken S, Pineda-Lucena A, Lu Y, Cox B, Lambermon M, Graveley BR, Arrowsmith CH, Blencowe BJ. Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing. Genes Dev. 2003 Feb 15;17(4):461-75. PMID:12600940 doi:10.1101/gad.1060403
29. ↑ Liu S, Rauhut R, Vornlocher HP, Luhrmann R. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. RNA. 2006 Jul;12(7):1418-30. Epub 2006 May 24. PMID:16723661 doi:rna.55406
30. ↑ Lauber J, Fabrizio P, Teigelkamp S, Lane WS, Hartmann E, Luhrmann R. The HeLa 200 kDa U5 snRNP-specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH-box protein family of putative RNA helicases. EMBO J. 1996 Aug 1;15(15):4001-15. PMID:8670905
31. ↑ Laggerbauer B, Achsel T, Luhrmann R. The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro. Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4188-92. PMID:9539711
32. ↑ Santos KF, Jovin SM, Weber G, Pena V, Luhrmann R, Wahl MC. Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045696 doi:10.1073/pnas.1208098109
33. ↑ Zhou S, Fujimuro M, Hsieh JJ, Chen L, Hayward SD. A role for SKIP in EBNA2 activation of CBF1-repressed promoters. J Virol. 2000 Feb;74(4):1939-47. PMID:10644367
34. ↑ Leong GM, Subramaniam N, Figueroa J, Flanagan JL, Hayman MJ, Eisman JA, Kouzmenko AP. Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription. J Biol Chem. 2001 May 25;276(21):18243-8. Epub 2001 Mar 6. PMID:11278756 doi:http://dx.doi.org/10.1074/jbc.M010815200
35. ↑ Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K. The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression. Hum Mol Genet. 2001 May 15;10(11):1129-39. PMID:11371506
36. ↑ Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN. Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription. J Biol Chem. 2001 Nov 2;276(44):40614-20. Epub 2001 Aug 20. PMID:11514567 doi:http://dx.doi.org/10.1074/jbc.M106263200
37. ↑ Zhang C, Dowd DR, Staal A, Gu C, Lian JB, van Wijnen AJ, Stein GS, MacDonald PN. Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing. J Biol Chem. 2003 Sep 12;278(37):35325-36. Epub 2003 Jul 2. PMID:12840015 doi:http://dx.doi.org/10.1074/jbc.M305191200
38. ↑ Leong GM, Subramaniam N, Issa LL, Barry JB, Kino T, Driggers PH, Hayman MJ, Eisman JA, Gardiner EM. Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300. Biochem Biophys Res Commun. 2004 Mar 19;315(4):1070-6. PMID:14985122 doi:http://dx.doi.org/10.1016/j.bbrc.2004.02.004
39. ↑ Figueroa JD, Hayman MJ. The human Ski-interacting protein functionally substitutes for the yeast PRP45 gene. Biochem Biophys Res Commun. 2004 Jul 9;319(4):1105-9. PMID:15194481 doi:http://dx.doi.org/10.1016/j.bbrc.2004.05.096
40. ↑ Bres V, Gomes N, Pickle L, Jones KA. A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat. Genes Dev. 2005 May 15;19(10):1211-26. PMID:15905409 doi:http://dx.doi.org/10.1101/gad.1291705
41. ↑ Bracken CP, Wall SJ, Barre B, Panov KI, Ajuh PM, Perkins ND. Regulation of cyclin D1 RNA stability by SNIP1. Cancer Res. 2008 Sep 15;68(18):7621-8. doi: 10.1158/0008-5472.CAN-08-1217. PMID:18794151 doi:http://dx.doi.org/10.1158/0008-5472.CAN-08-1217
42. ↑ Bres V, Yoshida T, Pickle L, Jones KA. SKIP interacts with c-Myc and Menin to promote HIV-1 Tat transactivation. Mol Cell. 2009 Oct 9;36(1):75-87. doi: 10.1016/j.molcel.2009.08.015. PMID:19818711 doi:http://dx.doi.org/10.1016/j.molcel.2009.08.015
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49. ↑ Alexandrov A, Colognori D, Shu MD, Steitz JA. Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay. Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):21313-8. doi:, 10.1073/pnas.1219725110. Epub 2012 Dec 10. PMID:23236153 doi:http://dx.doi.org/10.1073/pnas.1219725110
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52. ↑ Zang S, Lin TY, Chen X, Gencheva M, Newo AN, Yang L, Rossi D, Hu J, Lin SB, Huang A, Lin RJ. GPKOW is essential for pre-mRNA splicing in vitro and suppresses splicing defect caused by dominant-negative DHX16 mutation in vivo. Biosci Rep. 2014 Dec 12;34(6):e00163. doi: 10.1042/BSR20140142. PMID:25296192 doi:http://dx.doi.org/10.1042/BSR20140142
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63. ↑ Roche KC, Wiechens N, Owen-Hughes T, Perkins ND. The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression. Oncogene. 2004 Oct 28;23(50):8185-95. doi: 10.1038/sj.onc.1208025. PMID:15378006 doi:http://dx.doi.org/10.1038/sj.onc.1208025
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65. ↑ Bracken CP, Wall SJ, Barre B, Panov KI, Ajuh PM, Perkins ND. Regulation of cyclin D1 RNA stability by SNIP1. Cancer Res. 2008 Sep 15;68(18):7621-8. doi: 10.1158/0008-5472.CAN-08-1217. PMID:18794151 doi:http://dx.doi.org/10.1158/0008-5472.CAN-08-1217
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75. ↑ Pillai RS, Will CL, Luhrmann R, Schumperli D, Muller B. Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein. EMBO J. 2001 Oct 1;20(19):5470-9. PMID:11574479 doi:10.1093/emboj/20.19.5470
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