6qw6

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[[http://www.uniprot.org/uniprot/U5S1_HUMAN U5S1_HUMAN]] Mandibulofacial dysostosis-microcephaly syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN]] Retinitis pigmentosa. Retinitis pigmentosa 33 (RP33) [MIM:[http://omim.org/entry/610359 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.<ref>PMID:16723661</ref> <ref>PMID:23045696</ref> <ref>PMID:19878916</ref> <ref>PMID:19710410</ref> <ref>PMID:21618346</ref> [[http://www.uniprot.org/uniprot/PRPF3_HUMAN PRPF3_HUMAN]] Defects in PRPF3 are the cause of retinitis pigmentosa type 18 (RP18) [MIM:[http://omim.org/entry/601414 601414]]. 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. RP18 inheritance is autosomal dominant.<ref>PMID:11773002</ref> <ref>PMID:12714658</ref> <ref>PMID:17932117</ref> [[http://www.uniprot.org/uniprot/PRP8_HUMAN PRP8_HUMAN]] Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM:[http://omim.org/entry/600059 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.<ref>PMID:17317632</ref> <ref>PMID:11468273</ref> [:]<ref>PMID:11910553</ref> <ref>PMID:12714658</ref> [[http://www.uniprot.org/uniprot/PRP31_HUMAN PRP31_HUMAN]] Defects in PRPF31 are the cause of retinitis pigmentosa type 11 (RP11) [MIM:[http://omim.org/entry/600138 600138]]. 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. RP11 inheritance is autosomal dominant.<ref>PMID:17412961</ref> <ref>PMID:12444105</ref> <ref>PMID:11545739</ref> <ref>PMID:8808602</ref> <ref>PMID:12923864</ref> [[http://www.uniprot.org/uniprot/PRP6_HUMAN PRP6_HUMAN]] Retinitis pigmentosa. The disease may be caused by mutations affecting the gene represented in this entry. Cells from RP60 patients show intron retention for pre-mRNA bearing specific splicing signals.
[[http://www.uniprot.org/uniprot/U5S1_HUMAN U5S1_HUMAN]] Mandibulofacial dysostosis-microcephaly syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN]] Retinitis pigmentosa. Retinitis pigmentosa 33 (RP33) [MIM:[http://omim.org/entry/610359 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.<ref>PMID:16723661</ref> <ref>PMID:23045696</ref> <ref>PMID:19878916</ref> <ref>PMID:19710410</ref> <ref>PMID:21618346</ref> [[http://www.uniprot.org/uniprot/PRPF3_HUMAN PRPF3_HUMAN]] Defects in PRPF3 are the cause of retinitis pigmentosa type 18 (RP18) [MIM:[http://omim.org/entry/601414 601414]]. 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. RP18 inheritance is autosomal dominant.<ref>PMID:11773002</ref> <ref>PMID:12714658</ref> <ref>PMID:17932117</ref> [[http://www.uniprot.org/uniprot/PRP8_HUMAN PRP8_HUMAN]] Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM:[http://omim.org/entry/600059 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.<ref>PMID:17317632</ref> <ref>PMID:11468273</ref> [:]<ref>PMID:11910553</ref> <ref>PMID:12714658</ref> [[http://www.uniprot.org/uniprot/PRP31_HUMAN PRP31_HUMAN]] Defects in PRPF31 are the cause of retinitis pigmentosa type 11 (RP11) [MIM:[http://omim.org/entry/600138 600138]]. 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. RP11 inheritance is autosomal dominant.<ref>PMID:17412961</ref> <ref>PMID:12444105</ref> <ref>PMID:11545739</ref> <ref>PMID:8808602</ref> <ref>PMID:12923864</ref> [[http://www.uniprot.org/uniprot/PRP6_HUMAN PRP6_HUMAN]] Retinitis pigmentosa. The disease may be caused by mutations affecting the gene represented in this entry. Cells from RP60 patients show intron retention for pre-mRNA bearing specific splicing signals.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SNUT2_HUMAN SNUT2_HUMAN]] Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity, but could be a competitor of ubiquitin C-terminal hydrolases (UCHs).<ref>PMID:11350945</ref> <ref>PMID:18728397</ref> [[http://www.uniprot.org/uniprot/RUXE_HUMAN 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. [[http://www.uniprot.org/uniprot/DDX23_HUMAN DDX23_HUMAN]] Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation.<ref>PMID:18425142</ref> [[http://www.uniprot.org/uniprot/PRP4_HUMAN PRP4_HUMAN]] Involved in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/LSM5_HUMAN LSM5_HUMAN]] Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex formation in vitro. [[http://www.uniprot.org/uniprot/U5S1_HUMAN U5S1_HUMAN]] Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP. [[http://www.uniprot.org/uniprot/SNR27_HUMAN SNR27_HUMAN]] May play a role in mRNA splicing. [[http://www.uniprot.org/uniprot/TXN4A_HUMAN TXN4A_HUMAN]] Essential role in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/RBM42_HUMAN RBM42_HUMAN]] Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA. [[http://www.uniprot.org/uniprot/LSM2_HUMAN LSM2_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/RUXG_HUMAN 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. [[http://www.uniprot.org/uniprot/U520_HUMAN 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.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref> [[http://www.uniprot.org/uniprot/LSM8_HUMAN LSM8_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome. [[http://www.uniprot.org/uniprot/PRPF3_HUMAN PRPF3_HUMAN]] Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex. [[http://www.uniprot.org/uniprot/LSM6_HUMAN LSM6_HUMAN]] Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). [[http://www.uniprot.org/uniprot/LSM4_HUMAN LSM4_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/LSM7_HUMAN LSM7_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome. [[http://www.uniprot.org/uniprot/SMD1_HUMAN SMD1_HUMAN]] May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. [[http://www.uniprot.org/uniprot/NH2L1_HUMAN NH2L1_HUMAN]] Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.<ref>PMID:10545122</ref> <ref>PMID:17412961</ref> [[http://www.uniprot.org/uniprot/RUXF_HUMAN 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. [[http://www.uniprot.org/uniprot/PRP8_HUMAN 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. [[http://www.uniprot.org/uniprot/SNR40_HUMAN 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.<ref>PMID:9774689</ref> [[http://www.uniprot.org/uniprot/PRP31_HUMAN PRP31_HUMAN]] Involved in pre-mRNA splicing. Required for U4/U6.U5 tri-snRNP formation.<ref>PMID:11867543</ref> [[http://www.uniprot.org/uniprot/SMD2_HUMAN SMD2_HUMAN]] Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity). [[http://www.uniprot.org/uniprot/LSM3_HUMAN LSM3_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/RSMB_HUMAN 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). [[http://www.uniprot.org/uniprot/PRP6_HUMAN PRP6_HUMAN]] Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation.<ref>PMID:12039962</ref> [[http://www.uniprot.org/uniprot/SNUT1_HUMAN SNUT1_HUMAN]] Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA.<ref>PMID:11350945</ref> [[http://www.uniprot.org/uniprot/SMD3_HUMAN 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.<ref>PMID:11574479</ref>
+
[[http://www.uniprot.org/uniprot/SNUT2_HUMAN SNUT2_HUMAN]] Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity, but could be a competitor of ubiquitin C-terminal hydrolases (UCHs).<ref>PMID:11350945</ref> <ref>PMID:18728397</ref> [[http://www.uniprot.org/uniprot/DDX23_HUMAN DDX23_HUMAN]] Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation.<ref>PMID:18425142</ref> [[http://www.uniprot.org/uniprot/PRP4_HUMAN PRP4_HUMAN]] Involved in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/LSM5_HUMAN LSM5_HUMAN]] Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex formation in vitro. [[http://www.uniprot.org/uniprot/U5S1_HUMAN U5S1_HUMAN]] Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP. [[http://www.uniprot.org/uniprot/SNR27_HUMAN SNR27_HUMAN]] May play a role in mRNA splicing. [[http://www.uniprot.org/uniprot/TXN4A_HUMAN TXN4A_HUMAN]] Essential role in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/RBM42_HUMAN RBM42_HUMAN]] Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA. [[http://www.uniprot.org/uniprot/U520_HUMAN 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.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref> [[http://www.uniprot.org/uniprot/LSM6_HUMAN LSM6_HUMAN]] Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). [[http://www.uniprot.org/uniprot/LSM4_HUMAN LSM4_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/LSM7_HUMAN LSM7_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome. [[http://www.uniprot.org/uniprot/SNR40_HUMAN 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.<ref>PMID:9774689</ref> [[http://www.uniprot.org/uniprot/LSM3_HUMAN LSM3_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. [[http://www.uniprot.org/uniprot/RSMB_HUMAN 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). [[http://www.uniprot.org/uniprot/SNUT1_HUMAN SNUT1_HUMAN]] Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA.<ref>PMID:11350945</ref> [[http://www.uniprot.org/uniprot/RUXE_HUMAN 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. [[http://www.uniprot.org/uniprot/RUXG_HUMAN 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. [[http://www.uniprot.org/uniprot/LSM2_HUMAN LSM2_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/LSM8_HUMAN LSM8_HUMAN]] Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome. [[http://www.uniprot.org/uniprot/PRPF3_HUMAN PRPF3_HUMAN]] Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex. [[http://www.uniprot.org/uniprot/SMD1_HUMAN SMD1_HUMAN]] May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. [[http://www.uniprot.org/uniprot/NH2L1_HUMAN NH2L1_HUMAN]] Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.<ref>PMID:10545122</ref> <ref>PMID:17412961</ref> [[http://www.uniprot.org/uniprot/RUXF_HUMAN 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. [[http://www.uniprot.org/uniprot/PRP8_HUMAN 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. [[http://www.uniprot.org/uniprot/PRP31_HUMAN PRP31_HUMAN]] Involved in pre-mRNA splicing. Required for U4/U6.U5 tri-snRNP formation.<ref>PMID:11867543</ref> [[http://www.uniprot.org/uniprot/SMD2_HUMAN SMD2_HUMAN]] Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity). [[http://www.uniprot.org/uniprot/PRP6_HUMAN PRP6_HUMAN]] Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation.<ref>PMID:12039962</ref> [[http://www.uniprot.org/uniprot/SMD3_HUMAN 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.<ref>PMID:11574479</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Current revision

Structure of the human U5.U4/U6 tri-snRNP at 2.9A resolution.

6qw6, resolution 2.92Å

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