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Database: UniProt
Entry: Q6P2Q9
LinkDB: Q6P2Q9
Original site: Q6P2Q9 
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   29-SEP-2021, entry version 186.
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 68-GLU; 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   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   [36]
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   [37] {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   [38] {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   [39] {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   [40] {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   [41] {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   [42] {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   [43] {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   [44] {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   [45] {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   [46] {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   [47]
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   [48]
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   [49]
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   [50]
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   [51]
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 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 scaffold that positions spliceosomal U2, U5 and U6 snRNAs
CC       at splice sites on pre-mRNA substrates, so that splicing can occur.
CC       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). Core component of U2-type precatalytic, catalytic
CC       and postcatalytic spliceosomal complexes (PubMed:10411133,
CC       PubMed:28502770, PubMed:28781166, PubMed:28076346, PubMed:29361316,
CC       PubMed:30315277, PubMed:29360106, PubMed:29301961, PubMed:30728453,
CC       PubMed:30705154). Found in a mRNA splicing-dependent exon junction
CC       complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and
CC       SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN
CC       (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may
CC       stabilize the U4/U6-U5 tri-snRNP complex. Interacts (via RNase H
CC       homology domain) with AAR2 (PubMed:26527271). Interacts with RPAP3 and
CC       URI1 in a ZNHIT2-dependent manner (PubMed:28561026).
CC       {ECO:0000269|PubMed:10024169, ECO:0000269|PubMed:10411133,
CC       ECO:0000269|PubMed:10809668, ECO:0000269|PubMed:10983979,
CC       ECO:0000269|PubMed:11006293, ECO:0000269|PubMed:11971955,
CC       ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:17317632,
CC       ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:2139226,
CC       ECO:0000269|PubMed:2479028, ECO:0000269|PubMed:2527369,
CC       ECO:0000269|PubMed:2532307, ECO:0000269|PubMed:26527271,
CC       ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28561026,
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, ECO:0000269|PubMed:8608445,
CC       ECO:0000269|PubMed:8702566, ECO:0000269|PubMed:9303319,
CC       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 has structural similarity with
CC       deubiquitinating enzymes, but lacks the residues that would bind the
CC       catalytic metal ion. {ECO:0000250}.
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.48}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
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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   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   SMR; Q6P2Q9; -.
DR   BioGRID; 115842; 650.
DR   CORUM; Q6P2Q9; -.
DR   DIP; DIP-29614N; -.
DR   IntAct; Q6P2Q9; 114.
DR   MINT; Q6P2Q9; -.
DR   STRING; 9606.ENSP00000460348; -.
DR   CarbonylDB; Q6P2Q9; -.
DR   GlyGen; Q6P2Q9; 1 site, 1 O-linked glycan (1 site).
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; Q6P2Q9; -.
DR   PeptideAtlas; Q6P2Q9; -.
DR   PRIDE; Q6P2Q9; -.
DR   ProteomicsDB; 66917; -.
DR   Antibodypedia; 4094; 159 antibodies.
DR   DNASU; 10594; -.
DR   Ensembl; ENST00000304992; ENSP00000304350; ENSG00000174231.
DR   Ensembl; ENST00000572621; ENSP00000460348; ENSG00000174231.
DR   Ensembl; ENST00000614672; ENSP00000479194; ENSG00000274442.
DR   Ensembl; ENST00000634039; ENSP00000488611; ENSG00000274442.
DR   GeneID; 10594; -.
DR   KEGG; hsa:10594; -.
DR   UCSC; uc002fte.3; human.
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; 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; WVDRSDN; -.
DR   OrthoDB; 156083at2759; -.
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   BioGRID-ORCS; 10594; 791 hits in 1025 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 242 other tissues.
DR   ExpressionAtlas; Q6P2Q9; baseline and differential.
DR   Genevisible; Q6P2Q9; HS.
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:0070122; F:isopeptidase activity; IEA:InterPro.
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; cd13838; RNase_H_like_Prp8_IV; 1.
DR   Gene3D; 1.20.80.40; -; 1.
DR   Gene3D; 3.30.420.230; -; 1.
DR   Gene3D; 3.30.43.40; -; 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; PTHR11140; 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; SSF53098; 2.
DR   PROSITE; PS50249; MPN; 1.
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                   /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.48"
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.48"
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   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:6ID0"
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:6ICZ"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:6ICZ"
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           291..297
FT                   /evidence="ECO:0007829|PDB:6FF4"
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:6ICZ"
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   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:6FF4"
FT   HELIX           948..960
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          962..964
FT                   /evidence="ECO:0007829|PDB:6ZYM"
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   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:6ICZ"
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:6ICZ"
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   TURN            1452..1455
FT                   /evidence="ECO:0007829|PDB:6ICZ"
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   STRAND          1498..1500
FT                   /evidence="ECO:0007829|PDB:6FF4"
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          1552..1554
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   STRAND          1556..1558
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   STRAND          1561..1564
FT                   /evidence="ECO:0007829|PDB:6ICZ"
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:6ICZ"
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          1642..1644
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          1656..1658
FT                   /evidence="ECO:0007829|PDB:6FF4"
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:6ICZ"
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..1960
FT                   /evidence="ECO:0007829|PDB:6ICZ"
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:6S8Q"
FT   HELIX           2081..2088
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2089..2092
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2099..2101
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   STRAND          2103..2107
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2108..2116
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2120..2122
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2125..2131
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2139..2146
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2149..2152
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2167..2169
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2172..2183
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2190..2202
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   TURN            2208..2210
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2212..2217
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2222..2230
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2232..2240
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2245..2247
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2253..2255
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2256..2259
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2261..2267
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2270..2277
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2285..2287
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   STRAND          2296..2298
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2307..2309
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2311..2315
FT                   /evidence="ECO:0007829|PDB:6S8Q"
FT   HELIX           2321..2325
FT                   /evidence="ECO:0007829|PDB:6ICZ"
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
//
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