ID PRP31_HUMAN Reviewed; 499 AA. AC Q8WWY3; E7ESA8; F1T0A4; F1T0A5; Q17RB4; Q8N7F9; Q9H271; Q9Y439; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp31; DE AltName: Full=Pre-mRNA-processing factor 31; DE AltName: Full=Serologically defined breast cancer antigen NY-BR-99; DE AltName: Full=U4/U6 snRNP 61 kDa protein; DE Short=Protein 61K; DE Short=hPrp31; GN Name=PRPF31; Synonyms=PRP31; 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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBUNIT, RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH PRPF6. RX PubMed=11867543; DOI=10.1093/emboj/21.5.1148; RA Makarova O.V., Makarov E.M., Liu S., Vornlocher H.-P., Luehrmann R.; RT "Protein 61K, encoded by a gene (PRPF31) linked to autosomal dominant RT retinitis pigmentosa, is required for U4/U6.U5 tri-snRNP formation and pre- RT mRNA splicing."; RL EMBO J. 21:1148-1157(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Mammary gland; RX PubMed=12747765; RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.; RT "Humoral immunity to human breast cancer: antigen definition and RT quantitative analysis of mRNA expression."; RL Cancer Immun. 1:4-4(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Retinoblastoma; RX PubMed=21697133; DOI=10.1167/iovs.11-7479; RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., RA Usami R., Ohtoko K., Kato S.; RT "Full-length transcriptome analysis of human retina-derived cell lines RT ARPE-19 and Y79 using the vector-capping method."; RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [9] RP IDENTIFICATION IN THE MLL1/MLL COMPLEX. RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031; RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.; RT "Physical association and coordinate function of the H3 K4 RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."; RL Cell 121:873-885(2005). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND THR-455, AND 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND THR-455, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, 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 [14] 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 [15] RP INTERACTION WITH CTNNBL1. RX PubMed=21385873; DOI=10.1074/jbc.m110.208769; RA Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.; RT "CTNNBL1 is a novel nuclear localization sequence-binding protein that RT recognizes RNA-splicing factors CDC5L and Prp31."; RL J. Biol. Chem. 286:17091-17102(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-439; THR-440 AND RP THR-455, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND THR-455, AND 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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-478, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] RP INTERACTION WITH USH1G, AND SUBCELLULAR LOCATION. RX PubMed=34023904; DOI=10.1093/nar/gkab386; RA Yildirim A., Mozaffari-Jovin S., Wallisch A.K., Schaefer J., Ludwig S.E.J., RA Urlaub H., Luehrmann R., Wolfrum U.; RT "SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear RT transfer of tri-snRNP complexes."; RL Nucleic Acids Res. 49:5845-5866(2021). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-333 IN COMPLEX WITH SNU13 AND RP STEM-LOOP RNA OF U4 SNRNA, COILED-COIL DOMAIN, INTERACTION WITH PRPF6, RP CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216, AND MUTAGENESIS OF RP HIS-270. RX PubMed=17412961; DOI=10.1126/science.1137924; RA Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Luehrmann R., RA Carlomagno T., Wahl M.C.; RT "Binding of the human Prp31 Nop domain to a composite RNA-protein platform RT in U4 snRNP."; RL Science 316:115-120(2007). RN [21] {ECO:0007744|PDB:3SIU, ECO:0007744|PDB:3SIV} RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 85-333 IN COMPLEX WITH SNU13 AND RP STEM-LOOP RNA OF U4ATAC SNRNA, SUBUNIT, DOMAIN, AND COILED COIL. RX PubMed=21784869; DOI=10.1261/rna.2690611; RA Liu S., Ghalei H., Luhrmann R., Wahl M.C.; RT "Structural basis for the dual U4 and U4atac snRNA-binding specificity of RT spliceosomal protein hPrp31."; RL RNA 17:1655-1663(2011). RN [22] {ECO:0007744|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBUNIT, SUBCELLULAR RP LOCATION, 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 [23] {ECO:0007744|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, IDENTIFICATION RP BY MASS SPECTROMETRY, SUBCELLULAR 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 [24] RP VARIANT RP11 PRO-216. RX PubMed=8808602; RA Al-Maghtheh M., Vithana E., Tarttelin E., Jay M., Evans K., Moore T., RA Bhattacharya S., Inglehearn C.F.; RT "Evidence for a major retinitis pigmentosa locus on 19q13.4 (RP11) and RT association with a unique bimodal expressivity phenotype."; RL Am. J. Hum. Genet. 59:864-871(1996). RN [25] RP VARIANTS RP11 GLU-194 AND PRO-216, AND TISSUE SPECIFICITY. RX PubMed=11545739; DOI=10.1016/s1097-2765(01)00305-7; RA Vithana E.N., Abu-Safieh L., Allen M.J., Carey A., Papaioannou M., RA Chakarova C., Al-Maghtheh M., Ebenezer N.D., Willis C., Moore A.T., RA Bird A.C., Hunt D.M., Bhattacharya S.S.; RT "A human homolog of yeast pre-mRNA splicing gene, PRP31, underlies RT autosomal dominant retinitis pigmentosa on chromosome 19q13.4 (RP11)."; RL Mol. Cell 8:375-381(2001). RN [26] RP CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216, SUBCELLULAR RP LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF 351-ARG--GLU-364. RX PubMed=12444105; DOI=10.1093/hmg/11.25.3209; RA Deery E.C., Vithana E.N., Newbold R.J., Gallon V.A., Bhattacharya S.S., RA Warren M.J., Hunt D.M., Wilkie S.E.; RT "Disease mechanism for retinitis pigmentosa (RP11) caused by mutations in RT the splicing factor gene PRPF31."; RL Hum. Mol. Genet. 11:3209-3219(2002). RN [27] RP VARIANT RP11 111-HIS--ILE-114 DEL. RX PubMed=12923864; DOI=10.1002/ajmg.a.20224; RA Wang L., Ribaudo M., Zhao K., Yu N., Chen Q., Sun Q., Wang L., Wang Q.; RT "Novel deletion in the pre-mRNA splicing gene PRPF31 causes autosomal RT dominant retinitis pigmentosa in a large Chinese family."; RL Am. J. Med. Genet. A 121:235-239(2003). CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome CC (PubMed:11867543, PubMed:28781166). Required for the assembly of the CC U4/U5/U6 tri-snRNP complex, one of the building blocks of the CC spliceosome (PubMed:11867543). {ECO:0000269|PubMed:11867543, CC ECO:0000269|PubMed:28781166}. CC -!- SUBUNIT: Identified in the spliceosome B complex (PubMed:28781166). 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:11867543, PubMed:16723661, PubMed:26912367). Interacts with a CC complex formed by SNU13 and U4 snRNA, but not with SNU13 or U4 snRNA CC alone (PubMed:17412961, PubMed:21784869). The complex formed by SNU13 CC and PRPF31 binds also U4atac snRNA, a characteristic component of CC specific, less abundant spliceosomal complexes (PubMed:21784869). CC Interacts with PRPF6/U5 snRNP-associated 102 kDa protein CC (PubMed:11867543, PubMed:17412961, PubMed:26912367). Component of some CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, CC MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). CC Interacts (via its NLS) with CTNNBL1 (PubMed:21385873). Interacts with CC USH1G (PubMed:34023904). {ECO:0000269|PubMed:11867543, CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16723661, CC ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:21385873, CC ECO:0000269|PubMed:21784869, ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:34023904}. CC -!- INTERACTION: CC Q8WWY3; Q8WXK1: ASB15; NbExp=3; IntAct=EBI-1567797, EBI-12809012; CC Q8WWY3; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-1567797, EBI-11975051; CC Q8WWY3; Q9BXJ1: C1QTNF1; NbExp=3; IntAct=EBI-1567797, EBI-750200; CC Q8WWY3; Q9BXJ1-2: C1QTNF1; NbExp=6; IntAct=EBI-1567797, EBI-11536642; CC Q8WWY3; Q13137: CALCOCO2; NbExp=6; IntAct=EBI-1567797, EBI-739580; CC Q8WWY3; Q96L46: CAPNS2; NbExp=3; IntAct=EBI-1567797, EBI-12188723; CC Q8WWY3; Q9BXL6-2: CARD14; NbExp=4; IntAct=EBI-1567797, EBI-12114736; CC Q8WWY3; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-1567797, EBI-711501; CC Q8WWY3; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-1567797, EBI-10171416; CC Q8WWY3; Q8N5R6: CCDC33; NbExp=3; IntAct=EBI-1567797, EBI-740841; CC Q8WWY3; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-1567797, EBI-2808286; CC Q8WWY3; Q2TAC2-2: CCDC57; NbExp=6; IntAct=EBI-1567797, EBI-10961624; CC Q8WWY3; Q6NSX1: CCDC70; NbExp=3; IntAct=EBI-1567797, EBI-6873045; CC Q8WWY3; O95273: CCNDBP1; NbExp=5; IntAct=EBI-1567797, EBI-748961; CC Q8WWY3; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-1567797, EBI-396137; CC Q8WWY3; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-1567797, EBI-5278764; CC Q8WWY3; Q96GN5-2: CDCA7L; NbExp=3; IntAct=EBI-1567797, EBI-9091443; CC Q8WWY3; Q86X02: CDR2L; NbExp=3; IntAct=EBI-1567797, EBI-11063830; CC Q8WWY3; Q8NHQ1: CEP70; NbExp=9; IntAct=EBI-1567797, EBI-739624; CC Q8WWY3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1567797, EBI-3867333; CC Q8WWY3; Q92997: DVL3; NbExp=3; IntAct=EBI-1567797, EBI-739789; CC Q8WWY3; O95967: EFEMP2; NbExp=6; IntAct=EBI-1567797, EBI-743414; CC Q8WWY3; O60447: EVI5; NbExp=3; IntAct=EBI-1567797, EBI-852291; CC Q8WWY3; Q14296: FASTK; NbExp=3; IntAct=EBI-1567797, EBI-1754067; CC Q8WWY3; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-1567797, EBI-11533409; CC Q8WWY3; A1L4K1: FSD2; NbExp=3; IntAct=EBI-1567797, EBI-5661036; CC Q8WWY3; P51114-2: FXR1; NbExp=3; IntAct=EBI-1567797, EBI-11022345; CC Q8WWY3; Q08379: GOLGA2; NbExp=11; IntAct=EBI-1567797, EBI-618309; CC Q8WWY3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1567797, EBI-5916454; CC Q8WWY3; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-1567797, EBI-11519926; CC Q8WWY3; P54257: HAP1; NbExp=3; IntAct=EBI-1567797, EBI-712814; CC Q8WWY3; Q9BYE0: HES7; NbExp=3; IntAct=EBI-1567797, EBI-12163087; CC Q8WWY3; P61978: HNRNPK; NbExp=6; IntAct=EBI-1567797, EBI-304185; CC Q8WWY3; P61978-2: HNRNPK; NbExp=8; IntAct=EBI-1567797, EBI-7060731; CC Q8WWY3; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-1567797, EBI-10961706; CC Q8WWY3; O75031: HSF2BP; NbExp=3; IntAct=EBI-1567797, EBI-7116203; CC Q8WWY3; P42858: HTT; NbExp=3; IntAct=EBI-1567797, EBI-466029; CC Q8WWY3; Q96AA8: JAKMIP2; NbExp=8; IntAct=EBI-1567797, EBI-752007; CC Q8WWY3; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-1567797, EBI-2556193; CC Q8WWY3; Q8NC69: KCTD6; NbExp=10; IntAct=EBI-1567797, EBI-2511344; CC Q8WWY3; Q5VWX1: KHDRBS2; NbExp=8; IntAct=EBI-1567797, EBI-742808; CC Q8WWY3; O75525: KHDRBS3; NbExp=6; IntAct=EBI-1567797, EBI-722504; CC Q8WWY3; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-1567797, EBI-14069005; CC Q8WWY3; P19012: KRT15; NbExp=9; IntAct=EBI-1567797, EBI-739566; CC Q8WWY3; Q15323: KRT31; NbExp=3; IntAct=EBI-1567797, EBI-948001; CC Q8WWY3; O76011: KRT34; NbExp=3; IntAct=EBI-1567797, EBI-1047093; CC Q8WWY3; Q92764: KRT35; NbExp=3; IntAct=EBI-1567797, EBI-1058674; CC Q8WWY3; Q6A162: KRT40; NbExp=6; IntAct=EBI-1567797, EBI-10171697; CC Q8WWY3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1567797, EBI-11959885; CC Q8WWY3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1567797, EBI-11749135; CC Q8WWY3; P60410: KRTAP10-8; NbExp=9; IntAct=EBI-1567797, EBI-10171774; CC Q8WWY3; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-1567797, EBI-10172052; CC Q8WWY3; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-1567797, EBI-1048945; CC Q8WWY3; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-1567797, EBI-10302392; CC Q8WWY3; P52954: LBX1; NbExp=3; IntAct=EBI-1567797, EBI-20141748; CC Q8WWY3; O95751: LDOC1; NbExp=10; IntAct=EBI-1567797, EBI-740738; CC Q8WWY3; Q68G74: LHX8; NbExp=3; IntAct=EBI-1567797, EBI-8474075; CC Q8WWY3; Q96LR2: LURAP1; NbExp=6; IntAct=EBI-1567797, EBI-741355; CC Q8WWY3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1567797, EBI-741037; CC Q8WWY3; Q99750: MDFI; NbExp=5; IntAct=EBI-1567797, EBI-724076; CC Q8WWY3; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-1567797, EBI-18582591; CC Q8WWY3; Q9UJV3-2: MID2; NbExp=11; IntAct=EBI-1567797, EBI-10172526; CC Q8WWY3; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-1567797, EBI-2548751; CC Q8WWY3; Q13064: MKRN3; NbExp=11; IntAct=EBI-1567797, EBI-2340269; CC Q8WWY3; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1567797, EBI-742948; CC Q8WWY3; Q5JR59-3: MTUS2; NbExp=6; IntAct=EBI-1567797, EBI-11522433; CC Q8WWY3; Q6IBW4: NCAPH2; NbExp=3; IntAct=EBI-1567797, EBI-2548296; CC Q8WWY3; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-1567797, EBI-10963850; CC Q8WWY3; Q7Z3S9: NOTCH2NLA; NbExp=6; IntAct=EBI-1567797, EBI-945833; CC Q8WWY3; Q9P286: PAK5; NbExp=6; IntAct=EBI-1567797, EBI-741896; CC Q8WWY3; Q5VU43: PDE4DIP; NbExp=7; IntAct=EBI-1567797, EBI-1105124; CC Q8WWY3; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-1567797, EBI-713786; CC Q8WWY3; Q8IXK0-5: PHC2; NbExp=3; IntAct=EBI-1567797, EBI-11527347; CC Q8WWY3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1567797, EBI-79165; CC Q8WWY3; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-1567797, EBI-949255; CC Q8WWY3; Q8ND90: PNMA1; NbExp=11; IntAct=EBI-1567797, EBI-302345; CC Q8WWY3; Q9UL42: PNMA2; NbExp=6; IntAct=EBI-1567797, EBI-302355; CC Q8WWY3; Q9UL41: PNMA3; NbExp=3; IntAct=EBI-1567797, EBI-11278955; CC Q8WWY3; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-1567797, EBI-710402; CC Q8WWY3; Q969Q6: PPP2R3C; NbExp=3; IntAct=EBI-1567797, EBI-2561661; CC Q8WWY3; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-1567797, EBI-3957793; CC Q8WWY3; Q96MT3: PRICKLE1; NbExp=6; IntAct=EBI-1567797, EBI-2348662; CC Q8WWY3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-1567797, EBI-1567797; CC Q8WWY3; O94906: PRPF6; NbExp=5; IntAct=EBI-1567797, EBI-536755; CC Q8WWY3; O43586: PSTPIP1; NbExp=9; IntAct=EBI-1567797, EBI-1050964; CC Q8WWY3; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-1567797, EBI-1210429; CC Q8WWY3; P38159: RBMX; NbExp=6; IntAct=EBI-1567797, EBI-743526; CC Q8WWY3; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-1567797, EBI-8638511; CC Q8WWY3; P0DJD3-2: RBMY1A1; NbExp=6; IntAct=EBI-1567797, EBI-11994018; CC Q8WWY3; Q15415: RBMY1J; NbExp=9; IntAct=EBI-1567797, EBI-8642021; CC Q8WWY3; Q04864-2: REL; NbExp=3; IntAct=EBI-1567797, EBI-10829018; CC Q8WWY3; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-1567797, EBI-11957366; CC Q8WWY3; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1567797, EBI-747107; CC Q8WWY3; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-1567797, EBI-11522811; CC Q8WWY3; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-1567797, EBI-10269374; CC Q8WWY3; P84103: SRSF3; NbExp=3; IntAct=EBI-1567797, EBI-372557; CC Q8WWY3; Q9Y2D8: SSX2IP; NbExp=6; IntAct=EBI-1567797, EBI-2212028; CC Q8WWY3; O75558: STX11; NbExp=6; IntAct=EBI-1567797, EBI-714135; CC Q8WWY3; A0A024R0Y4: TADA2A; NbExp=3; IntAct=EBI-1567797, EBI-11523730; CC Q8WWY3; O75478: TADA2A; NbExp=3; IntAct=EBI-1567797, EBI-742268; CC Q8WWY3; Q9UBB9: TFIP11; NbExp=12; IntAct=EBI-1567797, EBI-1105213; CC Q8WWY3; Q08117: TLE5; NbExp=3; IntAct=EBI-1567797, EBI-717810; CC Q8WWY3; Q08117-2: TLE5; NbExp=10; IntAct=EBI-1567797, EBI-11741437; CC Q8WWY3; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-1567797, EBI-11952721; CC Q8WWY3; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-1567797, EBI-10175039; CC Q8WWY3; Q14142: TRIM14; NbExp=3; IntAct=EBI-1567797, EBI-2820256; CC Q8WWY3; P36406: TRIM23; NbExp=3; IntAct=EBI-1567797, EBI-740098; CC Q8WWY3; P14373: TRIM27; NbExp=8; IntAct=EBI-1567797, EBI-719493; CC Q8WWY3; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-1567797, EBI-725997; CC Q8WWY3; Q9BZW7: TSGA10; NbExp=6; IntAct=EBI-1567797, EBI-744794; CC Q8WWY3; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-1567797, EBI-11524408; CC Q8WWY3; Q495M9: USH1G; NbExp=3; IntAct=EBI-1567797, EBI-8601749; CC Q8WWY3; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-1567797, EBI-11957238; CC Q8WWY3; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-1567797, EBI-711679; CC Q8WWY3; Q9UJL9: ZFP69B; NbExp=3; IntAct=EBI-1567797, EBI-10322364; CC Q8WWY3; P17028: ZNF24; NbExp=3; IntAct=EBI-1567797, EBI-707773; CC Q8WWY3; P15622-3: ZNF250; NbExp=6; IntAct=EBI-1567797, EBI-10177272; CC Q8WWY3; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-1567797, EBI-347633; CC Q8WWY3; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1567797, EBI-740727; CC Q8WWY3; Q8WTR7: ZNF473; NbExp=3; IntAct=EBI-1567797, EBI-751409; CC Q8WWY3; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-1567797, EBI-12006434; CC Q8WWY3; Q96SQ5: ZNF587; NbExp=6; IntAct=EBI-1567797, EBI-6427977; CC Q8WWY3; Q96K58-2: ZNF668; NbExp=3; IntAct=EBI-1567797, EBI-12817597; CC Q8WWY3; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-1567797, EBI-7138235; CC Q8WWY3; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-1567797, EBI-10251462; CC Q8WWY3; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-1567797, EBI-10240849; CC Q8WWY3; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-1567797, EBI-11962574; CC Q8WWY3; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-1567797, EBI-527853; CC Q8WWY3; P10073: ZSCAN22; NbExp=3; IntAct=EBI-1567797, EBI-10178224; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12444105, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:34023904}. Nucleus speckle CC {ECO:0000269|PubMed:11867543}. Nucleus, Cajal body CC {ECO:0000269|PubMed:11867543}. Note=Predominantly found in speckles and CC in Cajal bodies. {ECO:0000269|PubMed:11867543}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8WWY3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WWY3-2; Sequence=VSP_017582, VSP_017584; CC Name=3; CC IsoId=Q8WWY3-3; Sequence=VSP_017581, VSP_017583; CC Name=4; CC IsoId=Q8WWY3-4; Sequence=VSP_057390; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:11545739}. CC -!- DOMAIN: Interacts with the snRNP via the Nop domain. CC {ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:21784869}. CC -!- DOMAIN: The coiled coil domain is formed by two non-contiguous helices. CC {ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:21784869}. CC -!- DISEASE: Retinitis pigmentosa 11 (RP11) [MIM:600138]: 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:11545739, CC ECO:0000269|PubMed:12444105, ECO:0000269|PubMed:12923864, CC ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:8808602}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the PRP31 family. {ECO:0000305}. 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; AY040822; AAK77986.1; -; mRNA. DR EMBL; AF308303; AAG48270.1; -; mRNA. DR EMBL; AL050369; CAB43677.1; -; mRNA. DR EMBL; AK098547; BAC05329.1; -; mRNA. DR EMBL; AB593024; BAJ83978.1; -; mRNA. DR EMBL; AB593025; BAJ83979.1; -; mRNA. DR EMBL; AC012314; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC245052; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471135; EAW72190.1; -; Genomic_DNA. DR EMBL; BC117389; AAI17390.1; -; mRNA. DR CCDS; CCDS12879.1; -. [Q8WWY3-1] DR RefSeq; NP_056444.3; NM_015629.3. [Q8WWY3-1] DR RefSeq; XP_006723200.1; XM_006723137.3. [Q8WWY3-1] DR PDB; 2OZB; X-ray; 2.60 A; B/E=78-333. DR PDB; 3JCR; EM; 7.00 A; J=1-499. DR PDB; 3SIU; X-ray; 2.63 A; B/E=85-333. DR PDB; 3SIV; X-ray; 3.30 A; B/E/H/K=85-333. DR PDB; 5O9Z; EM; 4.50 A; H=1-499. DR PDB; 6AH0; EM; 5.70 A; L=1-499. DR PDB; 6AHD; EM; 3.80 A; L=1-499. DR PDB; 6QW6; EM; 2.92 A; 4C=1-499. DR PDB; 6QX9; EM; 3.28 A; 4C=1-499. DR PDBsum; 2OZB; -. DR PDBsum; 3JCR; -. DR PDBsum; 3SIU; -. DR PDBsum; 3SIV; -. DR PDBsum; 5O9Z; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6QW6; -. DR PDBsum; 6QX9; -. DR AlphaFoldDB; Q8WWY3; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR SMR; Q8WWY3; -. DR BioGRID; 117563; 373. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR CORUM; Q8WWY3; -. DR IntAct; Q8WWY3; 214. DR MINT; Q8WWY3; -. DR STRING; 9606.ENSP00000324122; -. DR MoonProt; Q8WWY3; -. DR GlyGen; Q8WWY3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8WWY3; -. DR MetOSite; Q8WWY3; -. DR PhosphoSitePlus; Q8WWY3; -. DR BioMuta; PRPF31; -. DR DMDM; 90101442; -. DR EPD; Q8WWY3; -. DR jPOST; Q8WWY3; -. DR MassIVE; Q8WWY3; -. DR MaxQB; Q8WWY3; -. DR PaxDb; 9606-ENSP00000324122; -. DR PeptideAtlas; Q8WWY3; -. DR ProteomicsDB; 17949; -. DR ProteomicsDB; 74955; -. [Q8WWY3-1] DR ProteomicsDB; 74956; -. [Q8WWY3-2] DR ProteomicsDB; 74957; -. [Q8WWY3-3] DR Pumba; Q8WWY3; -. DR Antibodypedia; 32797; 299 antibodies from 31 providers. DR DNASU; 26121; -. DR Ensembl; ENST00000321030.9; ENSP00000324122.4; ENSG00000105618.14. [Q8WWY3-1] DR Ensembl; ENST00000419967.5; ENSP00000405166.2; ENSG00000105618.14. [Q8WWY3-4] DR Ensembl; ENST00000610903.1; ENSP00000484896.1; ENSG00000277154.4. [Q8WWY3-1] DR Ensembl; ENST00000612749.4; ENSP00000478804.1; ENSG00000276421.4. [Q8WWY3-4] DR Ensembl; ENST00000613693.4; ENSP00000483929.1; ENSG00000275885.4. [Q8WWY3-1] DR Ensembl; ENST00000614518.4; ENSP00000484151.1; ENSG00000274651.4. [Q8WWY3-4] DR Ensembl; ENST00000615175.4; ENSP00000479700.1; ENSG00000274144.4. [Q8WWY3-4] DR Ensembl; ENST00000616732.1; ENSP00000485017.1; ENSG00000276421.4. [Q8WWY3-1] DR Ensembl; ENST00000618595.4; ENSP00000483382.1; ENSG00000274894.4. [Q8WWY3-4] DR Ensembl; ENST00000618937.1; ENSP00000480434.1; ENSG00000274651.4. [Q8WWY3-1] DR Ensembl; ENST00000619220.4; ENSP00000484834.1; ENSG00000277953.4. [Q8WWY3-4] DR Ensembl; ENST00000619391.1; ENSP00000480636.1; ENSG00000275885.4. [Q8WWY3-4] DR Ensembl; ENST00000619439.1; ENSP00000480725.1; ENSG00000274894.4. [Q8WWY3-1] DR Ensembl; ENST00000619956.1; ENSP00000481201.1; ENSG00000275117.4. [Q8WWY3-1] DR Ensembl; ENST00000620142.1; ENSP00000482626.1; ENSG00000274144.4. [Q8WWY3-1] DR Ensembl; ENST00000620861.1; ENSP00000480726.1; ENSG00000277707.4. [Q8WWY3-1] DR Ensembl; ENST00000621588.4; ENSP00000481708.1; ENSG00000277154.4. [Q8WWY3-4] DR Ensembl; ENST00000622300.1; ENSP00000481654.1; ENSG00000277953.4. [Q8WWY3-1] DR Ensembl; ENST00000622387.4; ENSP00000483982.1; ENSG00000275117.4. [Q8WWY3-4] DR Ensembl; ENST00000622636.4; ENSP00000477787.1; ENSG00000277707.4. [Q8WWY3-4] DR GeneID; 26121; -. DR KEGG; hsa:26121; -. DR MANE-Select; ENST00000321030.9; ENSP00000324122.4; NM_015629.4; NP_056444.3. DR UCSC; uc002qdh.3; human. [Q8WWY3-1] DR UCSC; uc061cmv.1; human. DR AGR; HGNC:15446; -. DR CTD; 26121; -. DR DisGeNET; 26121; -. DR GeneCards; PRPF31; -. DR GeneReviews; PRPF31; -. DR HGNC; HGNC:15446; PRPF31. DR HPA; ENSG00000105618; Low tissue specificity. DR MalaCards; PRPF31; -. DR MIM; 600138; phenotype. DR MIM; 606419; gene. DR neXtProt; NX_Q8WWY3; -. DR OpenTargets; ENSG00000105618; -. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA33814; -. DR VEuPathDB; HostDB:ENSG00000105618; -. DR eggNOG; KOG2574; Eukaryota. DR GeneTree; ENSGT00550000075069; -. DR InParanoid; Q8WWY3; -. DR OMA; IGNGPMD; -. DR OrthoDB; 4493115at2759; -. DR PhylomeDB; Q8WWY3; -. DR TreeFam; TF300677; -. DR PathwayCommons; Q8WWY3; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q8WWY3; -. DR SIGNOR; Q8WWY3; -. DR BioGRID-ORCS; 26121; 792 hits in 1165 CRISPR screens. DR ChiTaRS; PRPF31; human. DR EvolutionaryTrace; Q8WWY3; -. DR GeneWiki; PRPF31; -. DR GenomeRNAi; 26121; -. DR Pharos; Q8WWY3; Tbio. DR PRO; PR:Q8WWY3; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8WWY3; Protein. DR Bgee; ENSG00000105618; Expressed in stromal cell of endometrium and 100 other cell types or tissues. DR ExpressionAtlas; Q8WWY3; baseline and differential. DR GO; GO:0015030; C:Cajal body; IDA:MGI. DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central. DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0005684; C:U2-type spliceosomal complex; IC:BHF-UCL. DR GO; GO:0005687; C:U4 snRNP; IDA:BHF-UCL. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB. DR GO; GO:0005690; C:U4atac snRNP; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0070990; F:snRNP binding; IPI:BHF-UCL. DR GO; GO:0030621; F:U4 snRNA binding; IDA:GO_Central. DR GO; GO:0030622; F:U4atac snRNA binding; IDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0071166; P:ribonucleoprotein complex localization; IMP:UniProtKB. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:MGI. DR Gene3D; 1.10.287.4070; -; 1. DR Gene3D; 1.10.246.90; Nop domain; 1. DR InterPro; IPR042239; Nop_C. DR InterPro; IPR002687; Nop_dom. DR InterPro; IPR036070; Nop_dom_sf. DR InterPro; IPR012976; NOSIC. DR InterPro; IPR027105; Prp31. DR InterPro; IPR019175; Prp31_C. DR PANTHER; PTHR13904; PRE-MRNA SPLICING FACTOR PRP31; 1. DR PANTHER; PTHR13904:SF0; U4_U6 SMALL NUCLEAR RIBONUCLEOPROTEIN PRP31; 1. DR Pfam; PF01798; Nop; 1. DR Pfam; PF09785; Prp31_C; 1. DR SMART; SM00931; NOSIC; 1. DR SUPFAM; SSF89124; Nop domain; 1. DR PROSITE; PS51358; NOP; 1. DR Genevisible; Q8WWY3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; KW Direct protein sequencing; Disease variant; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Retinitis pigmentosa; Ribonucleoprotein; RNA-binding; KW Spliceosome; Ubl conjugation. FT CHAIN 1..499 FT /note="U4/U6 small nuclear ribonucleoprotein Prp31" FT /id="PRO_0000227799" FT DOMAIN 215..333 FT /note="Nop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 334..357 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 85..120 FT /evidence="ECO:0000269|PubMed:17412961" FT COILED 181..215 FT /evidence="ECO:0000269|PubMed:17412961" FT MOTIF 351..364 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000269|PubMed:12444105" FT COMPBIAS 9..37 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 247 FT /note="Interaction with U4 snRNA" FT /evidence="ECO:0000269|PubMed:17412961" FT SITE 270 FT /note="Interaction with U4 snRNA and U4atac snRNA" FT /evidence="ECO:0000269|PubMed:17412961" FT SITE 289 FT /note="Interaction with U4atac snRNA" FT /evidence="ECO:0000269|PubMed:17412961" FT SITE 293 FT /note="Interaction with U4 snRNA and U4atac snRNA" FT /evidence="ECO:0000269|PubMed:17412961" FT SITE 298 FT /note="Interaction with U4 snRNA and U4atac snRNA" FT /evidence="ECO:0000269|PubMed:17412961" FT MOD_RES 379 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 438 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CCF0" FT MOD_RES 439 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 440 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 455 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT CROSSLNK 471 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 478 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..80 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12747765" FT /id="VSP_017581" FT VAR_SEQ 333..364 FT /note="EPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKE -> RRRWLRPTRSISPAWL FT SSSRSRARRVALCPPE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017582" FT VAR_SEQ 359..499 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12747765" FT /id="VSP_017583" FT VAR_SEQ 365..499 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017584" FT VAR_SEQ 426..499 FT /note="RTLQKQSVVYGGKSTIRDRSSGTASSVAFTPLQGLEIVNPQAAEKKVAEANQ FT KYFSSMAEFLKVKGEKSGLMST -> VWARPRWGWGPRDTRWGEPRSQPPCPPHSGPCR FT SRASYMAGSPPSATAPRARPPAWPSPHSRAWRL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:21697133" FT /id="VSP_057390" FT VARIANT 111..114 FT /note="Missing (in RP11; high penetrance)" FT /evidence="ECO:0000269|PubMed:12923864" FT /id="VAR_025629" FT VARIANT 194 FT /note="A -> E (in RP11; mislocation of the protein in the FT cytoplasm and reduced interaction with PRPF6; the result FT may be a deficiency in splicing function in the retina; FT dbSNP:rs119475043)" FT /evidence="ECO:0000269|PubMed:11545739, FT ECO:0000269|PubMed:12444105, ECO:0000269|PubMed:17412961" FT /id="VAR_025630" FT VARIANT 216 FT /note="A -> P (in RP11; mislocation of the protein in the FT cytoplasm, but no effect on interaction with PRPF6; the FT result may be a deficiency in splicing function in the FT retina; dbSNP:rs119475042)" FT /evidence="ECO:0000269|PubMed:11545739, FT ECO:0000269|PubMed:12444105, ECO:0000269|PubMed:17412961, FT ECO:0000269|PubMed:8808602" FT /id="VAR_025631" FT MUTAGEN 270 FT /note="H->A,K: Reduces binding to the complex formed by U4 FT snRNA and SNU13." FT /evidence="ECO:0000269|PubMed:17412961" FT MUTAGEN 351..364 FT /note="Missing: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:12444105" FT CONFLICT 188 FT /note="E -> D (in Ref. 1; AAK77986)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="A -> G (in Ref. 2; AAG48270)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="M -> V (in Ref. 3; CAB43677)" FT /evidence="ECO:0000305" FT HELIX 89..118 FT /evidence="ECO:0007829|PDB:2OZB" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 132..142 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:3SIU" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 161..172 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 181..215 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 217..235 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 238..242 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:2OZB" FT TURN 250..253 FT /evidence="ECO:0007829|PDB:2OZB" FT TURN 273..276 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 278..281 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 288..307 FT /evidence="ECO:0007829|PDB:2OZB" FT HELIX 315..331 FT /evidence="ECO:0007829|PDB:2OZB" SQ SEQUENCE 499 AA; 55456 MW; 7B50EC4C3393795C CRC64; MSLADELLAD LEEAAEEEEG GSYGEEEEEP AIEDVQEETQ LDLSGDSVKT IAKLWDSKMF AEIMMKIEEY ISKQAKASEV MGPVEAAPEY RVIVDANNLT VEIENELNII HKFIRDKYSK RFPELESLVP NALDYIRTVK ELGNSLDKCK NNENLQQILT NATIMVVSVT ASTTQGQQLS EEELERLEEA CDMALELNAS KHRIYEYVES RMSFIAPNLS IIIGASTAAK IMGVAGGLTN LSKMPACNIM LLGAQRKTLS GFSSTSVLPH TGYIYHSDIV QSLPPDLRRK AARLVAAKCT LAARVDSFHE STEGKVGYEL KDEIERKFDK WQEPPPVKQV KPLPAPLDGQ RKKRGGRRYR KMKERLGLTE IRKQANRMSF GEIEEDAYQE DLGFSLGHLG KSGSGRVRQT QVNEATKARI SKTLQRTLQK QSVVYGGKST IRDRSSGTAS SVAFTPLQGL EIVNPQAAEK KVAEANQKYF SSMAEFLKVK GEKSGLMST //