PRP31_HUMAN
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 03-AUG-2022, entry version 177.
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 RP11 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; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-1567797, EBI-11519926;
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; 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}.
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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 SMR; Q8WWY3; -.
DR BioGRID; 117563; 326.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q8WWY3; -.
DR IntAct; Q8WWY3; 207.
DR MINT; Q8WWY3; -.
DR STRING; 9606.ENSP00000324122; -.
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; Q8WWY3; -.
DR PeptideAtlas; Q8WWY3; -.
DR PRIDE; Q8WWY3; -.
DR ProteomicsDB; 17949; -.
DR ProteomicsDB; 74955; -. [Q8WWY3-1]
DR ProteomicsDB; 74956; -. [Q8WWY3-2]
DR ProteomicsDB; 74957; -. [Q8WWY3-3]
DR Antibodypedia; 32797; 279 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; ENST00000613693.4; ENSP00000483929.1; ENSG00000275885.4. [Q8WWY3-1]
DR Ensembl; ENST00000619391.1; ENSP00000480636.1; ENSG00000275885.4. [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 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; IIGNGPM; -.
DR OrthoDB; 791296at2759; -.
DR PhylomeDB; Q8WWY3; -.
DR TreeFam; TF300677; -.
DR PathwayCommons; Q8WWY3; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8WWY3; -.
DR BioGRID-ORCS; 26121; 763 hits in 1086 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 98 other tissues.
DR ExpressionAtlas; Q8WWY3; baseline and differential.
DR Genevisible; Q8WWY3; HS.
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; 1.10.246.90; -; 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; PTHR13904; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF09785; Prp31_C; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 1.
DR PROSITE; PS51358; NOP; 1.
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
