ID PRP8_HUMAN Reviewed; 2335 AA. AC Q6P2Q9; O14547; O75965; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 27-MAR-2024, entry version 198. DE RecName: Full=Pre-mRNA-processing-splicing factor 8; DE AltName: Full=220 kDa U5 snRNP-specific protein; DE AltName: Full=PRP8 homolog; DE AltName: Full=Splicing factor Prp8; DE AltName: Full=p220; GN Name=PRPF8; Synonyms=PRPC8; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, SUBUNIT, AND RP IDENTIFICATION IN U2- AND U12-DEPENDENT SPLICEOSOME COMPLEXES. RX PubMed=10411133; DOI=10.1017/s1355838299990520; RA Luo H.R., Moreau G.A., Levin N., Moore M.J.; RT "The human Prp8 protein is a component of both U2- and U12-dependent RT spliceosomes."; RL RNA 5:893-908(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-68; LEU-874 AND HIS-1293. RA Shimada Y., Fujiwara T., Kawai A., Shimizu F., Okuno S., Ozaki K., RA Takeda S., Watanabe T., Nagata M., Takahashi E.; RT "Human homologue of Saccharomyces cerevisiae PRP8, pre-mRNA splicing RT factor."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-227. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-8; 51-58; 218-227; 268-278; 421-428; 453-460; RP 556-565; 610-623; 643-650; 677-702; 747-758; 822-833; 838-845; 988-995; RP 999-1032; 1113-1131; 1142-1158; 1225-1231; 1246-1258; 1311-1320; 1345-1354; RP 1371-1392; 1450-1459; 1464-1491; 1524-1532; 1571-1578; 1642-1649; RP 1668-1678; 1724-1732; 1736-1744; 1814-1831; 1841-1859; 1902-1908; RP 1926-1935; 1995-2031; 2035-2045; 2050-2070; 2087-2108; 2114-2121; RP 2199-2210; 2230-2239; 2250-2266 AND 2288-2302, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [5] RP IDENTIFICATION IN U5 SNRNP COMPLEX. RX PubMed=2532307; DOI=10.1038/342819a0; RA Anderson G.J., Bach M., Luehrmann R., Beggs J.D.; RT "Conservation between yeast and man of a protein associated with U5 small RT nuclear ribonucleoprotein."; RL Nature 342:819-821(1989). RN [6] RP IDENTIFICATION IN U5 SNRNP COMPLEX. RX PubMed=2527369; DOI=10.1073/pnas.86.16.6038; RA Bach M., Winkelmann G., Luehrmann R.; RT "20S small nuclear ribonucleoprotein U5 shows a surprisingly complex RT protein composition."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6038-6042(1989). RN [7] RP IDENTIFICATION IN U5 SNRNP; U5/4/6 SNRNP AND SPLICEOSOME COMPLEXES. RX PubMed=2479028; DOI=10.1073/pnas.86.22.8742; RA Pinto A.L., Steitz J.A.; RT "The mammalian analogue of the yeast PRP8 splicing protein is present in RT the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8742-8746(1989). RN [8] RP IDENTIFICATION IN SPLICEOSOME COMPLEX, AND INTERACTION WITH PRE-MRNA. RX PubMed=2139226; DOI=10.1073/pnas.87.8.3082; RA Garcia-Blanco M.A., Anderson G.J., Beggs J., Sharp P.A.; RT "A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a RT potential homologue of the yeast PRP8 protein."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3082-3086(1990). RN [9] RP IDENTIFICATION IN U5 SNRNP COMPLEX, AND INTERACTION WITH U5 SNRNA. RX PubMed=8702566; DOI=10.1074/jbc.271.31.19001; RA Hinz M., Moore M.J., Bindereif A.; RT "Domain analysis of human U5 RNA. Cap trimethylation, protein binding, and RT spliceosome assembly."; RL J. Biol. Chem. 271:19001-19007(1996). RN [10] RP INTERACTION WITH PRE-MRNA. RX PubMed=8608445; RA Reyes J.L., Kois P., Konforti B.B., Konarska M.M.; RT "The canonical GU dinucleotide at the 5' splice site is recognized by p220 RT of the U5 snRNP within the spliceosome."; RL RNA 2:213-225(1996). RN [11] RP IDENTIFICATION IN SPLICEOSOME COMPLEX, AND INTERACTION WITH PRE-MRNA. RX PubMed=9303319; DOI=10.1093/emboj/16.15.4746; RA Chiara M.D., Palandjian L., Feld Kramer R., Reed R.; RT "Evidence that U5 snRNP recognizes the 3' splice site for catalytic step II RT in mammals."; RL EMBO J. 16:4746-4759(1997). RN [12] RP IDENTIFICATION IN U5 SNRP COMPLEX, AND INTERACTION WITH SNRP116 AND RP SNRNP40. RX PubMed=9774689; DOI=10.1128/mcb.18.11.6756; RA Achsel T., Ahrens K., Brahms H., Teigelkamp S., Luehrmann R.; RT "The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with RT several U5-specific proteins, including an RNA unwindase, a homologue of RT ribosomal elongation factor EF-2, and a novel WD-40 protein."; RL Mol. Cell. Biol. 18:6756-6766(1998). RN [13] RP INTERACTION WITH PRE-MRNA. RX PubMed=10024169; DOI=10.1017/s1355838299981785; RA Reyes J.L., Gustafson E.H., Luo H.R., Moore M.J., Konarska M.M.; RT "The C-terminal region of hPrp8 interacts with the conserved GU RT dinucleotide at the 5' splice site."; RL RNA 5:167-179(1999). RN [14] RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) RP WITH SRRM1. RX PubMed=10809668; RA Le Hir H., Moore M.J., Maquat L.E.; RT "Pre-mRNA splicing alters mRNP composition: evidence for stable association RT of proteins at exon-exon junctions."; RL Genes Dev. 14:1098-1108(2000). RN [15] RP INTERACTION WITH U5 SNRNA. RX PubMed=11006293; DOI=10.1074/jbc.m007434200; RA Urlaub H., Hartmuth K., Kostka S., Grelle G., Luehrmann R.; RT "A general approach for identification of RNA-protein cross-linking sites RT within native human spliceosomal small nuclear ribonucleoproteins (snRNPs). RT Analysis of RNA-protein contacts in native U1 and U4/U6.U5 snRNPs."; RL J. Biol. Chem. 275:41458-41468(2000). RN [16] RP INTERACTION WITH PRE-MRNA, AND IDENTIFICATION IN U5/4/6 SNRNP COMPLEX. RX PubMed=10983979; DOI=10.1016/s1097-2765(00)00032-0; RA Maroney P.A., Romfo C.M., Nilsen T.W.; RT "Functional recognition of 5' splice site by U4/U6.U5 tri-snRNP defines a RT novel ATP-dependent step in early spliceosome assembly."; RL Mol. Cell 6:317-328(2000). RN [17] RP IDENTIFICATION IN U12-DEPENDENT SPLICEOSOME. RX PubMed=11971955; DOI=10.1128/mcb.22.10.3219-3229.2002; RA Schneider C., Will C.L., Makarova O.V., Makarov E.M., Luehrmann R.; RT "Human U4/U6.U5 and U4atac/U6atac.U5 tri-snRNPs exhibit similar protein RT compositions."; RL Mol. Cell. Biol. 22:3219-3229(2002). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [19] RP REVIEW. RX PubMed=15840809; DOI=10.1261/rna.2220705; RA Grainger R.J., Beggs J.D.; RT "Prp8 protein: at the heart of the spliceosome."; RL RNA 11:533-557(2005). RN [20] RP SUBUNIT. RX PubMed=16723661; DOI=10.1261/rna.55406; RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.; RT "The network of protein-protein interactions within the human U4/U6.U5 tri- RT snRNP."; RL RNA 12:1418-1430(2006). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1463, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [26] RP FUNCTION, AND INTERACTION WITH PRPF3. RX PubMed=20595234; DOI=10.1101/gad.1925010; RA Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D., RA Harper J.W., Elledge S.J., Kirschner M.W., Rape M.; RT "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control RT reversible ubiquitination at the spliceosome."; RL Genes Dev. 24:1434-1447(2010). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [32] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1425, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [33] RP CRYSTALLIZATION, AND INTERACTION WITH AAR2. RX PubMed=26527271; DOI=10.1107/s2053230x15019202; RA Santos K., Preussner M., Heroven A.C., Weber G.; RT "Crystallization and biochemical characterization of the human spliceosomal RT Aar2-Prp8(RNaseH) complex."; RL Acta Crystallogr. F 71:1421-1428(2015). RN [34] RP INTERACTION WITH RPAP3 AND URI1. RX PubMed=28561026; DOI=10.1038/ncomms15615; RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E., RA Bouchard A., Faubert D., Chabot B., Coulombe B.; RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 RT to regulate assembly of U5 small nuclear ribonucleoprotein."; RL Nat. Commun. 8:15615-15615(2017). RN [35] RP INTERACTION WITH C9ORF78. RX PubMed=35167828; DOI=10.1016/j.yexcr.2022.113063; RA Koranne R., Brown K., Vandenbroek H., Taylor W.R.; RT "C9ORF78 partially localizes to centromeres and plays a role in chromosome RT segregation."; RL Exp. Cell Res. 413:113063-113063(2022). RN [36] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1760-2016, DOMAIN, AND LACK OF RP METAL-BINDING. RX PubMed=18843295; DOI=10.1038/emboj.2008.209; RA Pena V., Rozov A., Fabrizio P., Luehrmann R., Wahl M.C.; RT "Structure and function of an RNase H domain at the heart of the RT spliceosome."; RL EMBO J. 27:2929-2940(2008). RN [37] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1769-1990, IDENTIFICATION BY MASS RP SPECTROMETRY, RNA-BINDING, MUTAGENESIS OF VAL-1788 AND THR-1789, AND LACK RP OF METAL-BINDING SITE. RX PubMed=18836455; DOI=10.1038/nsmb.1505; RA Ritchie D.B., Schellenberg M.J., Gesner E.M., Raithatha S.A., Stuart D.T., RA Macmillan A.M.; RT "Structural elucidation of a PRP8 core domain from the heart of the RT spliceosome."; RL Nat. Struct. Mol. Biol. 15:1199-1205(2008). RN [38] {ECO:0007744|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION, RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=26912367; DOI=10.1126/science.aad2085; RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H., RA Luhrmann R., Stark H.; RT "Molecular architecture of the human U4/U6.U5 tri-snRNP."; RL Science 351:1416-1420(2016). RN [39] {ECO:0007744|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033; RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.; RT "An Atomic Structure of the Human Spliceosome."; RL Cell 169:918-929(2017). RN [40] {ECO:0007744|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011; RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N., RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for RT Activation."; RL Cell 170:701-713(2017). RN [41] {ECO:0007744|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=28076346; DOI=10.1038/nature21079; RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K., RA Urlaub H., Kastner B., Stark H., Luhrmann R.; RT "Cryo-EM structure of a human spliceosome activated for step 2 of RT splicing."; RL Nature 542:318-323(2017). RN [42] {ECO:0007744|PDB:6FF4, ECO:0007744|PDB:6FF7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010; RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O., RA Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact RT Complex."; RL Cell 172:454-464(2018). RN [43] {ECO:0007744|PDB:6AH0, ECO:0007744|PDB:6AHD} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30315277; DOI=10.1038/s41422-018-0094-7; RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.; RT "Structures of the human pre-catalytic spliceosome and its precursor RT spliceosome."; RL Cell Res. 28:1129-1140(2018). RN [44] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58} RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29360106; DOI=10.1038/cr.2018.14; RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.; RT "Structure of the human activated spliceosome in three conformational RT states."; RL Cell Res. 28:307-322(2018). RN [45] {ECO:0007744|PDB:5YZG} RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29301961; DOI=10.1126/science.aar6401; RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.; RT "Structure of a human catalytic step I spliceosome."; RL Science 359:537-545(2018). RN [46] {ECO:0007744|PDB:6ICZ, ECO:0007744|PDB:6ID0, ECO:0007744|PDB:6ID1} RP STRUCTURE BY ELECTRON MICROSCOPY (2.86 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=30728453; DOI=10.1038/s41422-019-0143-x; RA Zhang X., Zhan X., Yan C., Zhang W., Liu D., Lei J., Shi Y.; RT "Structures of the human spliceosomes before and after release of the RT ligated exon."; RL Cell Res. 29:274-285(2019). RN [47] {ECO:0007744|PDB:6QDV} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30705154; DOI=10.1126/science.aaw5569; RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.; RT "A human postcatalytic spliceosome structure reveals essential roles of RT metazoan factors for exon ligation."; RL Science 363:710-714(2019). RN [48] {ECO:0007744|PDB:7OS2} RP STRUCTURE BY ELECTRON MICROSCOPY (2.76 ANGSTROMS) OF 2064-2335 IN COMPLEX RP WITH C9ORF78 AND SNRNP200, AND INTERACTION WITH C9ORF78 AND SNRNP200. RX PubMed=35241646; DOI=10.1038/s41467-022-28754-2; RA Bergfort A., Preussner M., Kuropka B., Ilik I.A., Hilal T., Weber G., RA Freund C., Aktas T., Heyd F., Wahl M.C.; RT "A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 RT recruits C9ORF78 to regulate alternative splicing."; RL Nat. Commun. 13:1132-1132(2022). RN [49] {ECO:0007744|PDB:7PX3} RP STRUCTURE BY ELECTRON MICROSCOPY (3.05 ANGSTROMS) OF 2064-2320 IN COMPLEX RP WITH TSSC4 AND SNRNP200, INTERACTION WITH TSSC4 AND SNRNP200, AND DOMAIN. RX PubMed=35188580; DOI=10.1093/nar/gkac087; RA Bergfort A., Hilal T., Kuropka B., Ilik I.A., Weber G., Aktas T., RA Freund C., Wahl M.C.; RT "The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, RT placeholder and multi-interaction coordinator during snRNP assembly and RT recycling."; RL Nucleic Acids Res. 50:2938-2958(2022). RN [50] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). RN [51] RP VARIANTS RP13 THR-2301; LEU-2304; ARG-2309; PRO-2309; GLY-2310; LYS-2310 RP AND LEU-2314. RX PubMed=11468273; DOI=10.1093/hmg/10.15.1555; RA McKie A.B., McHale J.C., Keen T.J., Tarttelin E.E., Goliath R., RA van Lith-Verhoeven J.J., Greenberg J., Ramesar R.S., Hoyng C.B., RA Cremers F.P., Mackey D.A., Bhattacharya S.S., Bird A.C., Markham A.F., RA Inglehearn C.F.; RT "Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal dominant RT retinitis pigmentosa (RP13)."; RL Hum. Mol. Genet. 10:1555-1562(2001). RN [52] RP VARIANTS RP13 GLY-2310 AND ASN-2334. RA De Erkenez A.C., Berson E.L., Dryja T.P.; RT "Novel mutations in the PRPC8 gene, encoding a pre-mRNA splicing factor in RT patients with autosomal dominant retinitis pigmentosa."; RL (er) Invest. Ophthalmol. Vis. Sci. 43:ARVO E-Abstract 791(2002). RN [53] RP VARIANT RP13 LYS-2310. RX PubMed=11910553; DOI=10.1076/opge.23.1.1.2206; RA van Lith-Verhoeven J.J., van der Velde-Visser S.D., Sohocki M.M., RA Deutman A.F., Brink H.M., Cremers F.P., Hoyng C.B.; RT "Clinical characterization, linkage analysis, and PRPC8 mutation analysis RT of a family with autosomal dominant retinitis pigmentosa type 13 (RP13)."; RL Ophthalmic Genet. 23:1-12(2002). RN [54] RP VARIANT RP13 GLY-2310. RX PubMed=12714658; DOI=10.1167/iovs.02-0871; RA Martinez-Gimeno M., Gamundi M.J., Hernan I., Maseras M., Milla E., RA Ayuso C., Garcia-Sandoval B., Beneyto M., Vilela C., Baiget M., RA Antinolo G., Carballo M.; RT "Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31 RT in Spanish families with autosomal dominant retinitis pigmentosa."; RL Invest. Ophthalmol. Vis. Sci. 44:2171-2177(2003). RN [55] RP CHARACTERIZATION OF VARIANTS RP13 LEU-2304; PRO-2309; ARG-2309; GLY-2310; RP LYS-2310 AND LEU-2314, AND INTERACTION WITH EFTUD2 AND SNRNP200. RX PubMed=17317632; DOI=10.1016/j.molcel.2007.01.023; RA Pena V., Liu S., Bujnicki J.M., Luehrmann R., Wahl M.C.; RT "Structure of a multipartite protein-protein interaction domain in splicing RT factor Prp8 and its link to retinitis pigmentosa."; RL Mol. Cell 25:615-624(2007). CC -!- FUNCTION: Plays a role in pre-mRNA splicing as core component of CC precatalytic, catalytic and postcatalytic spliceosomal complexes, both CC of the predominant U2-type spliceosome and the minor U12-type CC spliceosome (PubMed:10411133, PubMed:11971955, PubMed:28502770, CC PubMed:28781166, PubMed:28076346, PubMed:29361316, PubMed:30315277, CC PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154). CC Functions as a scaffold that mediates the ordered assembly of CC spliceosomal proteins and snRNAs. Required for the assembly of the CC U4/U6-U5 tri-snRNP complex, a building block of the spliceosome. CC Functions as a scaffold that positions spliceosomal U2, U5 and U6 CC snRNAs at splice sites on pre-mRNA substrates, so that splicing can CC occur. Interacts with both the 5' and the 3' splice site. CC {ECO:0000269|PubMed:10411133, ECO:0000269|PubMed:11971955, CC ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, CC ECO:0000303|PubMed:15840809}. CC -!- SUBUNIT: Part of the U5 snRNP complex (PubMed:2532307, PubMed:2527369). CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, CC TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 CC (PubMed:2479028, PubMed:16723661, PubMed:26912367). Component of the CC U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes CC (PubMed:11971955). Within the minor spliceosome, which acts on U12-type CC introns, interacts with PPIL2 and RBM48 (PubMed:33509932). Core CC component of U2-type precatalytic, catalytic and postcatalytic CC spliceosomal complexes (PubMed:10411133, PubMed:28502770, CC PubMed:28781166, PubMed:28076346, PubMed:29361316, PubMed:30315277, CC PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154). CC Found in a mRNA splicing-dependent exon junction complex (EJC) with CC SRRM1. Interacts with U5 snRNP proteins SNRP116 and SNRNP40. Interacts CC with EFTUD2. Interacts (via the MPN (JAB/Mov34) domain) with PRPF3 CC ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri- CC snRNP complex. Interacts (via RNase H homology domain) with AAR2 CC (PubMed:26527271). Interacts with RPAP3 and URI1 in a ZNHIT2-dependent CC manner (PubMed:28561026). Interacts with C9orf78 (PubMed:35167828, CC PubMed:35241646). Interacts with SNRNP200; the interaction is direct CC (PubMed:35241646, PubMed:35188580). Interacts with TSSC4; the CC interaction is direct (PubMed:35188580). {ECO:0000269|PubMed:10024169, CC ECO:0000269|PubMed:10411133, ECO:0000269|PubMed:10809668, CC ECO:0000269|PubMed:10983979, ECO:0000269|PubMed:11006293, CC ECO:0000269|PubMed:11971955, ECO:0000269|PubMed:16723661, CC ECO:0000269|PubMed:17317632, ECO:0000269|PubMed:20595234, CC ECO:0000269|PubMed:2139226, ECO:0000269|PubMed:2479028, CC ECO:0000269|PubMed:2527369, ECO:0000269|PubMed:2532307, CC ECO:0000269|PubMed:26527271, ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28561026, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:35167828, CC ECO:0000269|PubMed:35188580, ECO:0000269|PubMed:35241646, CC ECO:0000269|PubMed:8608445, ECO:0000269|PubMed:8702566, CC ECO:0000269|PubMed:9303319, ECO:0000269|PubMed:9774689}. CC -!- INTERACTION: CC Q6P2Q9; P54253: ATXN1; NbExp=6; IntAct=EBI-538479, EBI-930964; CC Q6P2Q9; O75934: BCAS2; NbExp=2; IntAct=EBI-538479, EBI-1050106; CC Q6P2Q9; O95905: ECD; NbExp=3; IntAct=EBI-538479, EBI-2557598; CC Q6P2Q9; Q15029: EFTUD2; NbExp=6; IntAct=EBI-538479, EBI-357897; CC Q6P2Q9; Q92917: GPKOW; NbExp=2; IntAct=EBI-538479, EBI-746309; CC Q6P2Q9; Q15365: PCBP1; NbExp=2; IntAct=EBI-538479, EBI-946095; CC Q6P2Q9; Q9UMS4: PRPF19; NbExp=2; IntAct=EBI-538479, EBI-395746; CC Q6P2Q9; O94906: PRPF6; NbExp=4; IntAct=EBI-538479, EBI-536755; CC Q6P2Q9; Q13435: SF3B2; NbExp=3; IntAct=EBI-538479, EBI-749111; CC Q6P2Q9; Q15427: SF3B4; NbExp=2; IntAct=EBI-538479, EBI-348469; CC Q6P2Q9; O95391: SLU7; NbExp=2; IntAct=EBI-538479, EBI-750559; CC Q6P2Q9; O75643: SNRNP200; NbExp=3; IntAct=EBI-538479, EBI-1045395; CC Q6P2Q9; O75643-1: SNRNP200; NbExp=2; IntAct=EBI-538479, EBI-5456052; CC Q6P2Q9; Q96DI7: SNRNP40; NbExp=4; IntAct=EBI-538479, EBI-538492; CC Q6P2Q9; Q13148: TARDBP; NbExp=3; IntAct=EBI-538479, EBI-372899; CC Q6P2Q9; Q9BRX9: WDR83; NbExp=2; IntAct=EBI-538479, EBI-7705033; CC Q6P2Q9; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-538479, EBI-3920997; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, CC ECO:0000269|PubMed:30728453}. Nucleus speckle {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10411133}. CC -!- DOMAIN: The MPN (JAB/Mov34) domain mediates interaction with TSSC4 and CC SNRNP200 (PubMed:35188580). Has structural similarity with CC deubiquitinating enzymes, but lacks the residues that would bind the CC catalytic metal ion. {ECO:0000250, ECO:0000269|PubMed:35188580}. CC -!- DOMAIN: Contains a region with structural similarity to reverse CC transcripase, presenting the classical thumb, fingers and palm CC architecture, but lacks enzyme activity, since the essential metal- CC binding residues are not conserved. {ECO:0000250}. CC -!- DOMAIN: Contains a region with structural similarity to type-2 CC restriction endonucleases, but the residues that would bind catalytic CC metal ions in endonucleases are instead involved in hydrogen bonds that CC stabilize the protein structure. {ECO:0000250}. CC -!- DOMAIN: Contains a region with structural similarity to RNase H, but CC lacks RNase H activity. {ECO:0000250}. CC -!- DISEASE: Retinitis pigmentosa 13 (RP13) [MIM:600059]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:11468273, CC ECO:0000269|PubMed:11910553, ECO:0000269|PubMed:12714658, CC ECO:0000269|PubMed:17317632, ECO:0000269|Ref.52}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF092565; AAC61776.1; -; mRNA. DR EMBL; AB007510; BAA22563.1; -; mRNA. DR EMBL; BC064370; AAH64370.1; -; mRNA. DR CCDS; CCDS11010.1; -. DR RefSeq; NP_006436.3; NM_006445.3. DR PDB; 3E9L; X-ray; 1.95 A; A=1760-2016. DR PDB; 3ENB; X-ray; 1.85 A; A/B=1769-1990. DR PDB; 3JCR; EM; 7.00 A; A=1-2335. DR PDB; 3LRU; X-ray; 1.85 A; A/B=1831-1990. DR PDB; 4JK7; X-ray; 1.40 A; A/B=1769-1990. DR PDB; 4JK8; X-ray; 1.15 A; A/B=1769-1990. DR PDB; 4JK9; X-ray; 1.50 A; A/B=1769-1990. DR PDB; 4JKA; X-ray; 1.32 A; A/B=1769-1990. DR PDB; 4JKB; X-ray; 1.30 A; A/B=1769-1990. DR PDB; 4JKC; X-ray; 1.50 A; A/B=1769-1990. DR PDB; 4JKD; X-ray; 1.55 A; A/B=1769-1990. DR PDB; 4JKE; X-ray; 1.65 A; A/B=1769-1990. DR PDB; 4JKF; X-ray; 1.95 A; A/B=1769-1990. DR PDB; 4JKG; X-ray; 1.80 A; A/B=1769-1990. DR PDB; 4JKH; X-ray; 1.80 A; A/B=1769-1990. DR PDB; 4KIT; X-ray; 3.60 A; C=2064-2335. DR PDB; 5MQF; EM; 5.90 A; A=1-2335. DR PDB; 5O9Z; EM; 4.50 A; A=1-2335. DR PDB; 5XJC; EM; 3.60 A; A=1-2335. DR PDB; 5YZG; EM; 4.10 A; A=1-2335. DR PDB; 5Z56; EM; 5.10 A; A=1-2335. DR PDB; 5Z57; EM; 6.50 A; A=1-2335. DR PDB; 5Z58; EM; 4.90 A; A=1-2335. DR PDB; 6AH0; EM; 5.70 A; A=1-2335. DR PDB; 6AHD; EM; 3.80 A; A=1-2335. DR PDB; 6FF4; EM; 16.00 A; A=1-2335. DR PDB; 6FF7; EM; 4.50 A; A=1-2335. DR PDB; 6ICZ; EM; 3.00 A; A=1-2335. DR PDB; 6ID0; EM; 2.90 A; A=1-2335. DR PDB; 6ID1; EM; 2.86 A; A=1-2335. DR PDB; 6QDV; EM; 3.30 A; A=1-2335. DR PDB; 6QW6; EM; 2.92 A; 5A=25-2335. DR PDB; 6QX9; EM; 3.28 A; 5A=25-2335. DR PDB; 6S8Q; X-ray; 2.39 A; J=2064-2320. DR PDB; 6S9I; X-ray; 2.60 A; J=2064-2320. DR PDB; 6ZYM; EM; 3.40 A; A=1-1755. DR PDB; 7A5P; EM; 5.00 A; A=1-2335. DR PDB; 7AAV; EM; 4.20 A; A=1-2335. DR PDB; 7ABF; EM; 3.90 A; A=1-2335. DR PDB; 7ABG; EM; 7.80 A; A=1-2335. DR PDB; 7ABI; EM; 8.00 A; A=1-2335. DR PDB; 7BDI; X-ray; 2.80 A; J=2064-2320. DR PDB; 7BDJ; X-ray; 2.59 A; J=2064-2320. DR PDB; 7BDK; X-ray; 2.52 A; J=2064-2320. DR PDB; 7BDL; X-ray; 2.69 A; J=2064-2320. DR PDB; 7DVQ; EM; 2.89 A; A=1-2335. DR PDB; 7OS2; EM; 2.76 A; J=2064-2335. DR PDB; 7PJH; X-ray; 2.35 A; B=1758-2016. DR PDB; 7PX3; EM; 3.05 A; J=2064-2320. DR PDB; 7QTT; EM; 3.10 A; a=1-2335. DR PDB; 7W59; EM; 3.60 A; A=1-2335. DR PDB; 7W5A; EM; 3.60 A; A=1-2335. DR PDB; 7W5B; EM; 4.30 A; A=1-2335. DR PDB; 8BC8; X-ray; 2.39 A; J=2064-2320. DR PDB; 8BC9; X-ray; 2.30 A; J=2064-2320. DR PDB; 8BCA; X-ray; 2.80 A; J=2064-2320. DR PDB; 8BCB; X-ray; 2.38 A; J=2064-2320. DR PDB; 8BCC; X-ray; 2.35 A; J=2064-2320. DR PDB; 8BCD; X-ray; 3.50 A; J=2064-2320. DR PDB; 8BCE; X-ray; 2.05 A; J=2064-2320. DR PDB; 8BCF; X-ray; 2.42 A; J=2064-2320. DR PDB; 8BCG; X-ray; 2.39 A; J=2064-2320. DR PDB; 8C6J; EM; 2.80 A; A=1-2335. DR PDB; 8CH6; EM; 5.90 A; a=1-2335. DR PDBsum; 3E9L; -. DR PDBsum; 3ENB; -. DR PDBsum; 3JCR; -. DR PDBsum; 3LRU; -. DR PDBsum; 4JK7; -. DR PDBsum; 4JK8; -. DR PDBsum; 4JK9; -. DR PDBsum; 4JKA; -. DR PDBsum; 4JKB; -. DR PDBsum; 4JKC; -. DR PDBsum; 4JKD; -. DR PDBsum; 4JKE; -. DR PDBsum; 4JKF; -. DR PDBsum; 4JKG; -. DR PDBsum; 4JKH; -. DR PDBsum; 4KIT; -. DR PDBsum; 5MQF; -. DR PDBsum; 5O9Z; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6QW6; -. DR PDBsum; 6QX9; -. DR PDBsum; 6S8Q; -. DR PDBsum; 6S9I; -. DR PDBsum; 6ZYM; -. DR PDBsum; 7A5P; -. DR PDBsum; 7AAV; -. DR PDBsum; 7ABF; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR PDBsum; 7BDI; -. DR PDBsum; 7BDJ; -. DR PDBsum; 7BDK; -. DR PDBsum; 7BDL; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7OS2; -. DR PDBsum; 7PJH; -. DR PDBsum; 7PX3; -. DR PDBsum; 7QTT; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 8BC8; -. DR PDBsum; 8BC9; -. DR PDBsum; 8BCA; -. DR PDBsum; 8BCB; -. DR PDBsum; 8BCC; -. DR PDBsum; 8BCD; -. DR PDBsum; 8BCE; -. DR PDBsum; 8BCF; -. DR PDBsum; 8BCG; -. DR PDBsum; 8C6J; -. DR PDBsum; 8CH6; -. DR AlphaFoldDB; Q6P2Q9; -. DR EMDB; EMD-11569; -. DR EMDB; EMD-11693; -. DR EMDB; EMD-11694; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-13046; -. DR EMDB; EMD-13690; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-4255; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; Q6P2Q9; -. DR BioGRID; 115842; 770. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR CORUM; Q6P2Q9; -. DR DIP; DIP-29614N; -. DR IntAct; Q6P2Q9; 125. DR MINT; Q6P2Q9; -. DR STRING; 9606.ENSP00000460348; -. DR CarbonylDB; Q6P2Q9; -. DR GlyGen; Q6P2Q9; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q6P2Q9; -. DR MetOSite; Q6P2Q9; -. DR PhosphoSitePlus; Q6P2Q9; -. DR SwissPalm; Q6P2Q9; -. DR BioMuta; PRPF8; -. DR DMDM; 67460824; -. DR EPD; Q6P2Q9; -. DR jPOST; Q6P2Q9; -. DR MassIVE; Q6P2Q9; -. DR MaxQB; Q6P2Q9; -. DR PaxDb; 9606-ENSP00000460348; -. DR PeptideAtlas; Q6P2Q9; -. DR ProteomicsDB; 66917; -. DR Pumba; Q6P2Q9; -. DR Antibodypedia; 4094; 211 antibodies from 31 providers. DR DNASU; 10594; -. DR Ensembl; ENST00000304992.11; ENSP00000304350.6; ENSG00000174231.18. DR Ensembl; ENST00000572621.5; ENSP00000460348.1; ENSG00000174231.18. DR Ensembl; ENST00000614672.2; ENSP00000479194.1; ENSG00000274442.2. DR Ensembl; ENST00000634039.1; ENSP00000488611.1; ENSG00000274442.2. DR GeneID; 10594; -. DR KEGG; hsa:10594; -. DR MANE-Select; ENST00000304992.11; ENSP00000304350.6; NM_006445.4; NP_006436.3. DR UCSC; uc002fte.3; human. DR AGR; HGNC:17340; -. DR CTD; 10594; -. DR DisGeNET; 10594; -. DR GeneCards; PRPF8; -. DR GeneReviews; PRPF8; -. DR HGNC; HGNC:17340; PRPF8. DR HPA; ENSG00000174231; Low tissue specificity. DR MalaCards; PRPF8; -. DR MIM; 600059; phenotype. DR MIM; 607300; gene. DR neXtProt; NX_Q6P2Q9; -. DR OpenTargets; ENSG00000174231; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA33815; -. DR VEuPathDB; HostDB:ENSG00000174231; -. DR eggNOG; KOG1795; Eukaryota. DR GeneTree; ENSGT00390000015210; -. DR HOGENOM; CLU_000380_3_0_1; -. DR InParanoid; Q6P2Q9; -. DR OMA; ANKWNTS; -. DR OrthoDB; 246127at2759; -. DR PhylomeDB; Q6P2Q9; -. DR TreeFam; TF105613; -. DR PathwayCommons; Q6P2Q9; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR SignaLink; Q6P2Q9; -. DR SIGNOR; Q6P2Q9; -. DR BioGRID-ORCS; 10594; 833 hits in 1166 CRISPR screens. DR ChiTaRS; PRPF8; human. DR EvolutionaryTrace; Q6P2Q9; -. DR GeneWiki; PRPF8; -. DR GenomeRNAi; 10594; -. DR Pharos; Q6P2Q9; Tbio. DR PRO; PR:Q6P2Q9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6P2Q9; Protein. DR Bgee; ENSG00000174231; Expressed in adenohypophysis and 94 other cell types or tissues. DR ExpressionAtlas; Q6P2Q9; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:CAFA. DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central. DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central. DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central. DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central. DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB. DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB. DR CDD; cd08056; MPN_PRP8; 1. DR CDD; cd13838; RNase_H_like_Prp8_IV; 1. DR Gene3D; 1.20.80.40; -; 1. DR Gene3D; 3.30.420.230; -; 1. DR Gene3D; 3.90.1570.40; -; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1. DR Gene3D; 3.30.43.40; Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain; 1. DR InterPro; IPR000555; JAMM/MPN+_dom. DR InterPro; IPR037518; MPN. DR InterPro; IPR012591; PRO8NT. DR InterPro; IPR012592; PROCN. DR InterPro; IPR012984; PROCT. DR InterPro; IPR027652; PRP8. DR InterPro; IPR021983; PRP8_domainIV. DR InterPro; IPR043173; Prp8_domainIV_fingers. DR InterPro; IPR043172; Prp8_domainIV_palm. DR InterPro; IPR019581; Prp8_U5-snRNA-bd. DR InterPro; IPR042516; Prp8_U5-snRNA-bd_sf. DR InterPro; IPR019580; Prp8_U6-snRNA-bd. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR019582; RRM_spliceosomal_PrP8. DR PANTHER; PTHR11140; PRE-MRNA SPLICING FACTOR PRP8; 1. DR PANTHER; PTHR11140:SF0; PRE-MRNA-PROCESSING-SPLICING FACTOR 8; 1. DR Pfam; PF01398; JAB; 1. DR Pfam; PF08082; PRO8NT; 1. DR Pfam; PF08083; PROCN; 1. DR Pfam; PF08084; PROCT; 1. DR Pfam; PF12134; PRP8_domainIV; 1. DR Pfam; PF10598; RRM_4; 1. DR Pfam; PF10597; U5_2-snRNA_bdg; 1. DR Pfam; PF10596; U6-snRNA_bdg; 1. DR SMART; SM00232; JAB_MPN; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 2. DR PROSITE; PS50249; MPN; 1. DR Genevisible; Q6P2Q9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Retinitis pigmentosa; Ribonucleoprotein; RNA-binding; KW Spliceosome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..2335 FT /note="Pre-mRNA-processing-splicing factor 8" FT /id="PRO_0000097040" FT DOMAIN 2103..2234 FT /note="MPN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182" FT REGION 812..1303 FT /note="Reverse transcriptase homology domain" FT REGION 1304..1577 FT /note="Linker" FT REGION 1513..1526 FT /note="Important for branch point selection" FT /evidence="ECO:0000250" FT REGION 1581..1752 FT /note="Restriction endonuclease homology domain" FT REGION 1669..2034 FT /note="Involved in interaction with pre-mRNA 5' splice FT site" FT REGION 1767..2020 FT /note="RNase H homology domain" FT REGION 2301..2335 FT /note="Required for interaction with EFTUD2 and SNRNP200" FT /evidence="ECO:0000269|PubMed:17317632" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 859 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1358 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1425 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1463 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 68 FT /note="K -> E (in dbSNP:rs1043391)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_022622" FT VARIANT 227 FT /note="R -> H (in dbSNP:rs11559304)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_022623" FT VARIANT 874 FT /note="P -> L (in dbSNP:rs1043396)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_022624" FT VARIANT 1293 FT /note="N -> H (in dbSNP:rs1043399)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_022625" FT VARIANT 2301 FT /note="P -> T (in RP13; no effect on interaction with FT SNRNP200 and EFTUD2; dbSNP:rs121434239)" FT /evidence="ECO:0000269|PubMed:11468273" FT /id="VAR_022626" FT VARIANT 2304 FT /note="F -> L (in RP13; dbSNP:rs121434240)" FT /evidence="ECO:0000269|PubMed:11468273, FT ECO:0000269|PubMed:17317632" FT /id="VAR_022627" FT VARIANT 2309 FT /note="H -> P (in RP13; no effect on interaction with FT SNRNP200 and EFTUD2; dbSNP:rs121434236)" FT /evidence="ECO:0000269|PubMed:11468273, FT ECO:0000269|PubMed:17317632" FT /id="VAR_022628" FT VARIANT 2309 FT /note="H -> R (in RP13; no effect on interaction with FT SNRNP200 and EFTUD2; dbSNP:rs121434236)" FT /evidence="ECO:0000269|PubMed:11468273, FT ECO:0000269|PubMed:17317632" FT /id="VAR_022629" FT VARIANT 2310 FT /note="R -> G (in RP13; reduces interaction with SNRNP200 FT and EFTUD2)" FT /evidence="ECO:0000269|PubMed:11468273, FT ECO:0000269|PubMed:12714658, ECO:0000269|PubMed:17317632, FT ECO:0000269|Ref.52" FT /id="VAR_022630" FT VARIANT 2310 FT /note="R -> K (in RP13; reduces interaction with SNRNP200 FT and EFTUD2; dbSNP:rs121434238)" FT /evidence="ECO:0000269|PubMed:11468273, FT ECO:0000269|PubMed:11910553, ECO:0000269|PubMed:17317632" FT /id="VAR_022631" FT VARIANT 2314 FT /note="F -> L (in RP13; reduces interaction with EFTUD2, FT but not with SNRNP200)" FT /evidence="ECO:0000269|PubMed:11468273, FT ECO:0000269|PubMed:17317632" FT /id="VAR_022632" FT VARIANT 2334 FT /note="Y -> N (in RP13)" FT /evidence="ECO:0000269|Ref.52" FT /id="VAR_022633" FT MUTAGEN 1788 FT /note="V->D: Strongly reduced interaction with RNA." FT /evidence="ECO:0000269|PubMed:18836455" FT MUTAGEN 1789 FT /note="T->P: Strongly reduced interaction with RNA." FT /evidence="ECO:0000269|PubMed:18836455" FT CONFLICT 184 FT /note="D -> N (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT CONFLICT 492..493 FT /note="VG -> GW (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT CONFLICT 604 FT /note="M -> V (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT CONFLICT 806 FT /note="A -> T (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT CONFLICT 997 FT /note="L -> V (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT CONFLICT 1390 FT /note="A -> S (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT CONFLICT 1867 FT /note="G -> D (in Ref. 2; BAA22563)" FT /evidence="ECO:0000305" FT HELIX 27..44 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 64..72 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 85..91 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 95..104 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 137..156 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 166..169 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 182..184 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 197..208 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:6ICZ" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 232..241 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:6ICZ" FT TURN 286..289 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 312..315 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 317..320 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 374..377 FT /evidence="ECO:0007829|PDB:6ICZ" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:6ZYM" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:6ID0" FT HELIX 398..405 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 409..412 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 414..417 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 428..432 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:6ICZ" FT HELIX 441..459 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 472..476 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 479..488 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 489..510 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:6FF4" FT STRAND 524..528 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 532..537 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 542..565 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 572..583 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 585..588 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 591..593 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 596..598 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 599..616 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 619..621 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 623..625 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 631..661 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 677..696 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 706..721 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 729..731 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 733..763 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 769..796 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 800..803 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 804..819 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 835..847 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 849..851 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 858..872 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 874..886 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 894..900 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 902..910 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 913..932 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 940..942 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 944..946 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 948..960 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 963..966 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 969..971 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 972..980 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 982..987 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 990..1000 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1003..1013 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1016..1019 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1022..1025 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1027..1029 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1037..1053 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1055..1062 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1065..1067 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1077..1080 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1083..1091 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1094..1102 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1103..1116 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1123..1125 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1132..1134 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1136..1138 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1144..1158 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1159..1161 FT /evidence="ECO:0007829|PDB:6FF4" FT TURN 1163..1165 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1170..1172 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1174..1178 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1185..1188 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1190..1202 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1203..1205 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 1209..1212 FT /evidence="ECO:0007829|PDB:6FF4" FT STRAND 1213..1217 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1219..1221 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1223..1232 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1234..1248 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1249..1251 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1254..1257 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1258..1273 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1275..1280 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1282..1303 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1308..1310 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 1314..1317 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1320..1322 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1331..1333 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 1337..1339 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1340..1345 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1350..1356 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1360..1362 FT /evidence="ECO:0007829|PDB:6ICZ" FT TURN 1368..1371 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1375..1398 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1405..1410 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1411..1413 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1415..1418 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1419..1423 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1425..1428 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 1430..1432 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1436..1441 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1442..1446 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1447..1449 FT /evidence="ECO:0007829|PDB:7DVQ" FT TURN 1452..1455 FT /evidence="ECO:0007829|PDB:7DVQ" FT TURN 1458..1460 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1469..1478 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1480..1485 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1486..1489 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1490..1493 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1498..1500 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 1501..1503 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1507..1509 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1512..1515 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1520..1522 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1523..1527 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1529..1531 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1532..1537 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1539..1542 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1545..1547 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1550..1555 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 1556..1558 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 1561..1564 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 1569..1576 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1578..1580 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1581..1597 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1601..1603 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1606..1611 FT /evidence="ECO:0007829|PDB:7DVQ" FT TURN 1617..1620 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1628..1631 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1632..1635 FT /evidence="ECO:0007829|PDB:6ZYM" FT STRAND 1637..1639 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 1642..1644 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1654..1658 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 1660..1667 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1671..1673 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1676..1687 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1688..1693 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1696..1698 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 1701..1706 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1707..1710 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1711..1717 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1720..1722 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1723..1733 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 1734..1736 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1738..1751 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1753..1757 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 1761..1763 FT /evidence="ECO:0007829|PDB:3E9L" FT TURN 1765..1767 FT /evidence="ECO:0007829|PDB:3E9L" FT HELIX 1768..1772 FT /evidence="ECO:0007829|PDB:3E9L" FT STRAND 1773..1775 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1777..1781 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1785..1792 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1794..1796 FT /evidence="ECO:0007829|PDB:3E9L" FT STRAND 1798..1803 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1805..1810 FT /evidence="ECO:0007829|PDB:4JK8" FT TURN 1812..1814 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1816..1822 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1824..1827 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1833..1851 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1854..1856 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1859..1865 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1866..1868 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1869..1875 FT /evidence="ECO:0007829|PDB:4JK8" FT TURN 1876..1878 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1883..1886 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1893..1898 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1900..1908 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1913..1918 FT /evidence="ECO:0007829|PDB:4JK8" FT TURN 1919..1922 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1923..1925 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1929..1945 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1947..1953 FT /evidence="ECO:0007829|PDB:4JK8" FT STRAND 1957..1959 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 1966..1968 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 1973..1989 FT /evidence="ECO:0007829|PDB:4JK8" FT HELIX 1999..2001 FT /evidence="ECO:0007829|PDB:3E9L" FT HELIX 2004..2012 FT /evidence="ECO:0007829|PDB:3E9L" FT HELIX 2072..2080 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2081..2088 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2089..2092 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2095..2097 FT /evidence="ECO:0007829|PDB:7PX3" FT STRAND 2099..2101 FT /evidence="ECO:0007829|PDB:8BCA" FT STRAND 2103..2107 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2108..2116 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2120..2122 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2125..2131 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2139..2146 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2149..2152 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2167..2169 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2172..2183 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2190..2202 FT /evidence="ECO:0007829|PDB:8BCE" FT TURN 2208..2210 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2212..2217 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2222..2230 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2232..2239 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2245..2247 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2253..2255 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2256..2258 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2260..2267 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2270..2277 FT /evidence="ECO:0007829|PDB:8BCE" FT TURN 2282..2284 FT /evidence="ECO:0007829|PDB:8BCG" FT HELIX 2285..2287 FT /evidence="ECO:0007829|PDB:8BCE" FT STRAND 2296..2298 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2307..2309 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2311..2316 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2317..2319 FT /evidence="ECO:0007829|PDB:8BCE" FT HELIX 2323..2326 FT /evidence="ECO:0007829|PDB:7OS2" SQ SEQUENCE 2335 AA; 273600 MW; E823A15C60EA61C9 CRC64; MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVPVLY HITGAISFVN EIPWVIEPVY ISQWGSMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD NILDVEPLEA IQLELDPEED APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR LANQLLTDLV DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF YFDPLINPIS HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN GIALLWAPRP FNLRSGRTRR ALDIPLVKNW YREHCPAGQP VKVRVSYQKL LKYYVLNALK HRPPKAQKKR YLFRSFKATK FFQSTKLDWV EVGLQVCRQG YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF GNAFHLCREV LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER WLGNLLARQF EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG IKQNKARTIL QHLSEAWRCW KANIPWKVPG LPTPIENMIL RYVKAKADWW TNTAHYNRER IRRGATVDKT VCKKNLGRLT RLYLKAEQER QHNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL LVYKWCQGIN NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI VDHNIADYMT AKNNVVINYK DMNHTNSYGI IRGLQFASFI VQYYGLVMDL LVLGLHRASE MAGPPQMPND FLSFQDIATE AAHPIRLFCR YIDRIHIFFR FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM RLMKHDVNLG RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA SGSTTFTKIV NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK IGLNSKMPSR FPPVVFYTPK ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI THFRSGMSHE EDQLIPNLYR YIQPWESEFI DSQRVWAEYA LKRQEAIAQN RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT DFKQYQVLKQ NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG FQVQLDLTGI FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE LDALEIETVQ KETIHPRKSY KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA RAKFLDYTTD NMSIYPSPTG VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL YVLRERIRKG LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR SLPVEEQPKQ IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE KFGDLILKAT EPQMVLFNLY DDWLKTISSY TAFSRLILIL RALHVNNDRA KVILKPDKTT ITEPHHIWPT LTDEEWIKVE VQLKDLILAD YGKKNNVNVA SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT ATQTRTVNKH GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ WGTHQTVHLP GQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM ADNPSWDGEK TIIITCSFTP GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN YNFMGVRHDP NMKYELQLAN PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA //