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U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (Serologically defined breast cancer antigen NY-BR-99) (U4/U6 snRNP 61 kDa protein) (Protein 61K) (hPrp31)

 PRP31_HUMAN             Reviewed;         499 AA.
Q8WWY3; E7ESA8; F1T0A4; F1T0A5; Q17RB4; Q8N7F9; Q9H271; Q9Y439;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 2.
25-OCT-2017, entry version 143.
RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp31;
AltName: Full=Pre-mRNA-processing factor 31;
AltName: Full=Serologically defined breast cancer antigen NY-BR-99;
AltName: Full=U4/U6 snRNP 61 kDa protein;
Short=Protein 61K;
Short=hPrp31;
Name=PRPF31; Synonyms=PRP31;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION,
FUNCTION, AND INTERACTION WITH C20ORF14.
PubMed=11867543; DOI=10.1093/emboj/21.5.1148;
Makarova O.V., Makarov E.M., Liu S., Vornlocher H.-P., Luehrmann R.;
"Protein 61K, encoded by a gene (PRPF31) linked to autosomal dominant
retinitis pigmentosa, is required for U4/U6.U5 tri-snRNP formation and
pre-mRNA splicing.";
EMBO J. 21:1148-1157(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Mammary gland;
PubMed=12747765;
Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E.,
Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
"Humoral immunity to human breast cancer: antigen definition and
quantitative analysis of mRNA expression.";
Cancer Immun. 1:4-4(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Retinoblastoma;
PubMed=21697133; DOI=10.1167/iovs.11-7479;
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M.,
Toyama S., Usami R., Ohtoko K., Kato S.;
"Full-length transcriptome analysis of human retina-derived cell lines
ARPE-19 and Y79 using the vector-capping method.";
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[10]
SUBUNIT.
PubMed=16723661; DOI=10.1261/rna.55406;
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
"The network of protein-protein interactions within the human U4/U6.U5
tri-snRNP.";
RNA 12:1418-1430(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND THR-455, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND THR-455, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH CTNNBL1.
PubMed=21385873; DOI=10.1074/jbc.M110.208769;
Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.;
"CTNNBL1 is a novel nuclear localization sequence-binding protein that
recognizes RNA-splicing factors CDC5L and Prp31.";
J. Biol. Chem. 286:17091-17102(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-439; THR-440
AND THR-455, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND THR-455, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-478, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-333 IN COMPLEX WITH SNU13
AND STEM-LOOP RNA OF U4 SNRNA, COILED-COIL DOMAIN, INTERACTION WITH
PRPF6, CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216, AND
MUTAGENESIS OF HIS-270.
PubMed=17412961; DOI=10.1126/science.1137924;
Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Luehrmann R.,
Carlomagno T., Wahl M.C.;
"Binding of the human Prp31 Nop domain to a composite RNA-protein
platform in U4 snRNP.";
Science 316:115-120(2007).
[20]
VARIANT RP11 PRO-216.
PubMed=8808602;
Al-Maghtheh M., Vithana E., Tarttelin E., Jay M., Evans K., Moore T.,
Bhattacharya S., Inglehearn C.F.;
"Evidence for a major retinitis pigmentosa locus on 19q13.4 (RP11) and
association with a unique bimodal expressivity phenotype.";
Am. J. Hum. Genet. 59:864-871(1996).
[21]
VARIANTS RP11 GLU-194 AND RP11 PRO-216, AND TISSUE SPECIFICITY.
PubMed=11545739; DOI=10.1016/S1097-2765(01)00305-7;
Vithana E.N., Abu-Safieh L., Allen M.J., Carey A., Papaioannou M.,
Chakarova C., Al-Maghtheh M., Ebenezer N.D., Willis C., Moore A.T.,
Bird A.C., Hunt D.M., Bhattacharya S.S.;
"A human homolog of yeast pre-mRNA splicing gene, PRP31, underlies
autosomal dominant retinitis pigmentosa on chromosome 19q13.4
(RP11).";
Mol. Cell 8:375-381(2001).
[22]
CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216, SUBCELLULAR
LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
351-ARG--GLU-364.
PubMed=12444105; DOI=10.1093/hmg/11.25.3209;
Deery E.C., Vithana E.N., Newbold R.J., Gallon V.A.,
Bhattacharya S.S., Warren M.J., Hunt D.M., Wilkie S.E.;
"Disease mechanism for retinitis pigmentosa (RP11) caused by mutations
in the splicing factor gene PRPF31.";
Hum. Mol. Genet. 11:3209-3219(2002).
[23]
VARIANT RP11 111-HIS--ILE-114 DEL.
PubMed=12923864; DOI=10.1002/ajmg.a.20224;
Wang L., Ribaudo M., Zhao K., Yu N., Chen Q., Sun Q., Wang L.,
Wang Q.;
"Novel deletion in the pre-mRNA splicing gene PRPF31 causes autosomal
dominant retinitis pigmentosa in a large Chinese family.";
Am. J. Med. Genet. A 121:235-239(2003).
-!- FUNCTION: Involved in pre-mRNA splicing. Required for the assembly
of the U4/U5/U6 tri-snRNP complex, one of the building blocks of
the spliceosome. {ECO:0000269|PubMed:11867543}.
-!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of
the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8,
PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13,
EFTUD2, SART1 and USP39. Interacts with a complex formed by SNU13
and U4 snRNA, but not with SNU13 or U4 snRNA alone. Interacts with
PRPF6/U5 snRNP-associated 102 kDa protein. Component of some
MLL1/MLL complex, at least composed of the core components
KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the
facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
and TEX10. Interacts (via its NLS) with CTNNBL1.
{ECO:0000269|PubMed:11867543, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:17412961,
ECO:0000269|PubMed:21385873}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-1567797, EBI-717810;
Q08117-2:AES; NbExp=7; IntAct=EBI-1567797, EBI-11741437;
Q9BXJ1:C1QTNF1; NbExp=3; IntAct=EBI-1567797, EBI-750200;
Q9BXJ1-2:C1QTNF1; NbExp=5; IntAct=EBI-1567797, EBI-11536642;
Q13137:CALCOCO2; NbExp=6; IntAct=EBI-1567797, EBI-739580;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-1567797, EBI-10171416;
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-1567797, EBI-2808286;
Q2TAC2-2:CCDC57; NbExp=5; IntAct=EBI-1567797, EBI-10961624;
O95273:CCNDBP1; NbExp=4; IntAct=EBI-1567797, EBI-748961;
Q96GN5:CDCA7L; NbExp=3; IntAct=EBI-1567797, EBI-5278764;
Q96GN5-2:CDCA7L; NbExp=3; IntAct=EBI-1567797, EBI-9091443;
Q8NHQ1:CEP70; NbExp=8; IntAct=EBI-1567797, EBI-739624;
Q92997:DVL3; NbExp=4; IntAct=EBI-1567797, EBI-739789;
O95967:EFEMP2; NbExp=5; IntAct=EBI-1567797, EBI-743414;
Q14296:FASTK; NbExp=3; IntAct=EBI-1567797, EBI-1754067;
Q08379:GOLGA2; NbExp=10; IntAct=EBI-1567797, EBI-618309;
P61978:HNRNPK; NbExp=6; IntAct=EBI-1567797, EBI-304185;
P61978-2:HNRNPK; NbExp=7; IntAct=EBI-1567797, EBI-7060731;
Q96AA8:JAKMIP2; NbExp=8; IntAct=EBI-1567797, EBI-752007;
Q8NC69:KCTD6; NbExp=8; IntAct=EBI-1567797, EBI-2511344;
Q5VWX1:KHDRBS2; NbExp=8; IntAct=EBI-1567797, EBI-742808;
O75525:KHDRBS3; NbExp=6; IntAct=EBI-1567797, EBI-722504;
P19012:KRT15; NbExp=8; IntAct=EBI-1567797, EBI-739566;
Q6A162:KRT40; NbExp=6; IntAct=EBI-1567797, EBI-10171697;
P60410:KRTAP10-8; NbExp=8; IntAct=EBI-1567797, EBI-10171774;
P60411:KRTAP10-9; NbExp=6; IntAct=EBI-1567797, EBI-10172052;
O95751:LDOC1; NbExp=8; IntAct=EBI-1567797, EBI-740738;
Q96LR2:LURAP1; NbExp=6; IntAct=EBI-1567797, EBI-741355;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-1567797, EBI-741037;
Q99750:MDFI; NbExp=5; IntAct=EBI-1567797, EBI-724076;
Q9UJV3-2:MID2; NbExp=8; IntAct=EBI-1567797, EBI-10172526;
Q8TD10:MIPOL1; NbExp=6; IntAct=EBI-1567797, EBI-2548751;
Q13064:MKRN3; NbExp=10; IntAct=EBI-1567797, EBI-2340269;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-1567797, EBI-742948;
Q5JR59-3:MTUS2; NbExp=5; IntAct=EBI-1567797, EBI-11522433;
Q6IBW4:NCAPH2; NbExp=3; IntAct=EBI-1567797, EBI-2548296;
Q7Z3S9:NOTCH2NL; NbExp=6; IntAct=EBI-1567797, EBI-945833;
Q9P286:PAK5; NbExp=5; IntAct=EBI-1567797, EBI-741896;
A0A0C4DFQ0:PDE4DIP; NbExp=3; IntAct=EBI-1567797, EBI-11953012;
Q5VU43:PDE4DIP; NbExp=3; IntAct=EBI-1567797, EBI-1105124;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-1567797, EBI-713786;
Q8IXK0-5:PHC2; NbExp=3; IntAct=EBI-1567797, EBI-11527347;
Q8ND90:PNMA1; NbExp=10; IntAct=EBI-1567797, EBI-302345;
Q9UL42:PNMA2; NbExp=6; IntAct=EBI-1567797, EBI-302355;
Q96MT3:PRICKLE1; NbExp=6; IntAct=EBI-1567797, EBI-2348662;
O94906:PRPF6; NbExp=2; IntAct=EBI-1567797, EBI-536755;
O43586:PSTPIP1; NbExp=8; IntAct=EBI-1567797, EBI-1050964;
P38159:RBMX; NbExp=7; IntAct=EBI-1567797, EBI-743526;
P0DJD3:RBMY1A1; NbExp=3; IntAct=EBI-1567797, EBI-8638511;
P0DJD3-2:RBMY1A1; NbExp=5; IntAct=EBI-1567797, EBI-11994018;
Q15415:RBMY1J; NbExp=12; IntAct=EBI-1567797, EBI-8642021;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-1567797, EBI-747107;
Q8IUQ4-2:SIAH1; NbExp=3; IntAct=EBI-1567797, EBI-11522811;
Q9Y2D8:SSX2IP; NbExp=6; IntAct=EBI-1567797, EBI-2212028;
O75558:STX11; NbExp=6; IntAct=EBI-1567797, EBI-714135;
O75478:TADA2A; NbExp=3; IntAct=EBI-1567797, EBI-742268;
A0A024R0Y4:TADA2L; NbExp=3; IntAct=EBI-1567797, EBI-11523730;
Q9UBB9:TFIP11; NbExp=10; IntAct=EBI-1567797, EBI-1105213;
O75069-4:TMCC2; NbExp=6; IntAct=EBI-1567797, EBI-10177480;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-1567797, EBI-10175039;
P14373:TRIM27; NbExp=8; IntAct=EBI-1567797, EBI-719493;
Q8WV44:TRIM41; NbExp=3; IntAct=EBI-1567797, EBI-725997;
Q9BZW7:TSGA10; NbExp=6; IntAct=EBI-1567797, EBI-744794;
Q9NTW7:ZFP64; NbExp=3; IntAct=EBI-1567797, EBI-745730;
P17028:ZNF24; NbExp=3; IntAct=EBI-1567797, EBI-707773;
P15622-3:ZNF250; NbExp=6; IntAct=EBI-1567797, EBI-10177272;
Q9H9D4:ZNF408; NbExp=3; IntAct=EBI-1567797, EBI-347633;
Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-1567797, EBI-740727;
Q8WTR7:ZNF473; NbExp=3; IntAct=EBI-1567797, EBI-751409;
Q96SQ5:ZNF587; NbExp=6; IntAct=EBI-1567797, EBI-6427977;
Q9UGI0:ZRANB1; NbExp=4; IntAct=EBI-1567797, EBI-527853;
-!- SUBCELLULAR LOCATION: Nucleus speckle. Nucleus, Cajal body.
Note=Predominantly found in speckles and in Cajal bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8WWY3-1; Sequence=Displayed;
Name=2;
IsoId=Q8WWY3-2; Sequence=VSP_017582, VSP_017584;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8WWY3-3; Sequence=VSP_017581, VSP_017583;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8WWY3-4; Sequence=VSP_057390;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11545739}.
-!- DOMAIN: Interacts with the snRNP via the Nop domain.
-!- DOMAIN: The coiled coil domain is formed by two non-contiguous
helices.
-!- DISEASE: Retinitis pigmentosa 11 (RP11) [MIM:600138]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. Patients typically have night vision blindness and
loss of midperipheral visual field. As their condition progresses,
they lose their far peripheral visual field and eventually central
vision as well. {ECO:0000269|PubMed:11545739,
ECO:0000269|PubMed:12444105, ECO:0000269|PubMed:12923864,
ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:8808602}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the PRP31 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY040822; AAK77986.1; -; mRNA.
EMBL; AF308303; AAG48270.1; -; mRNA.
EMBL; AL050369; CAB43677.1; -; mRNA.
EMBL; AK098547; BAC05329.1; -; mRNA.
EMBL; AB593024; BAJ83978.1; -; mRNA.
EMBL; AB593025; BAJ83979.1; -; mRNA.
EMBL; AC012314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC245052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW72190.1; -; Genomic_DNA.
EMBL; BC117389; AAI17390.1; -; mRNA.
CCDS; CCDS12879.1; -. [Q8WWY3-1]
RefSeq; NP_056444.3; NM_015629.3. [Q8WWY3-1]
RefSeq; XP_006723200.1; XM_006723137.3. [Q8WWY3-1]
UniGene; Hs.515598; -.
PDB; 2OZB; X-ray; 2.60 A; B/E=78-333.
PDB; 3JCR; EM; 7.00 A; J=1-499.
PDB; 3SIU; X-ray; 2.63 A; B/E=85-333.
PDB; 3SIV; X-ray; 3.30 A; B/E/H/K=85-333.
PDB; 5O9Z; EM; 4.50 A; H=1-499.
PDBsum; 2OZB; -.
PDBsum; 3JCR; -.
PDBsum; 3SIU; -.
PDBsum; 3SIV; -.
PDBsum; 5O9Z; -.
ProteinModelPortal; Q8WWY3; -.
SMR; Q8WWY3; -.
BioGrid; 117563; 152.
CORUM; Q8WWY3; -.
IntAct; Q8WWY3; 164.
MINT; MINT-3047742; -.
STRING; 9606.ENSP00000324122; -.
iPTMnet; Q8WWY3; -.
PhosphoSitePlus; Q8WWY3; -.
BioMuta; PRPF31; -.
DMDM; 90101442; -.
EPD; Q8WWY3; -.
MaxQB; Q8WWY3; -.
PaxDb; Q8WWY3; -.
PeptideAtlas; Q8WWY3; -.
PRIDE; Q8WWY3; -.
DNASU; 26121; -.
Ensembl; ENST00000321030; ENSP00000324122; ENSG00000105618. [Q8WWY3-1]
Ensembl; ENST00000419967; ENSP00000405166; ENSG00000105618. [Q8WWY3-4]
Ensembl; ENST00000610903; ENSP00000484896; ENSG00000277154. [Q8WWY3-1]
Ensembl; ENST00000612749; ENSP00000478804; ENSG00000276421. [Q8WWY3-4]
Ensembl; ENST00000613693; ENSP00000483929; ENSG00000275885. [Q8WWY3-1]
Ensembl; ENST00000614518; ENSP00000484151; ENSG00000274651. [Q8WWY3-4]
Ensembl; ENST00000615175; ENSP00000479700; ENSG00000274144. [Q8WWY3-4]
Ensembl; ENST00000616732; ENSP00000485017; ENSG00000276421. [Q8WWY3-1]
Ensembl; ENST00000618595; ENSP00000483382; ENSG00000274894. [Q8WWY3-4]
Ensembl; ENST00000618937; ENSP00000480434; ENSG00000274651. [Q8WWY3-1]
Ensembl; ENST00000619220; ENSP00000484834; ENSG00000277953. [Q8WWY3-4]
Ensembl; ENST00000619391; ENSP00000480636; ENSG00000275885. [Q8WWY3-4]
Ensembl; ENST00000619439; ENSP00000480725; ENSG00000274894. [Q8WWY3-1]
Ensembl; ENST00000619956; ENSP00000481201; ENSG00000275117. [Q8WWY3-1]
Ensembl; ENST00000620142; ENSP00000482626; ENSG00000274144. [Q8WWY3-1]
Ensembl; ENST00000620861; ENSP00000480726; ENSG00000277707. [Q8WWY3-1]
Ensembl; ENST00000621588; ENSP00000481708; ENSG00000277154. [Q8WWY3-4]
Ensembl; ENST00000622300; ENSP00000481654; ENSG00000277953. [Q8WWY3-1]
Ensembl; ENST00000622387; ENSP00000483982; ENSG00000275117. [Q8WWY3-4]
Ensembl; ENST00000622636; ENSP00000477787; ENSG00000277707. [Q8WWY3-4]
GeneID; 26121; -.
KEGG; hsa:26121; -.
UCSC; uc002qdh.3; human. [Q8WWY3-1]
UCSC; uc061cmv.1; human.
CTD; 26121; -.
DisGeNET; 26121; -.
EuPathDB; HostDB:ENSG00000105618.13; -.
GeneCards; PRPF31; -.
GeneReviews; PRPF31; -.
H-InvDB; HIX0027609; -.
H-InvDB; HIX0137464; -.
HGNC; HGNC:15446; PRPF31.
HPA; HPA041939; -.
HPA; HPA061873; -.
MalaCards; PRPF31; -.
MIM; 600138; phenotype.
MIM; 606419; gene.
neXtProt; NX_Q8WWY3; -.
OpenTargets; ENSG00000105618; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA33814; -.
eggNOG; KOG2574; Eukaryota.
eggNOG; COG1498; LUCA.
GeneTree; ENSGT00550000075069; -.
HOGENOM; HOG000207983; -.
HOVERGEN; HBG082193; -.
InParanoid; Q8WWY3; -.
KO; K12844; -.
OMA; KVGYDLK; -.
OrthoDB; EOG091G09U7; -.
PhylomeDB; Q8WWY3; -.
TreeFam; TF300677; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
EvolutionaryTrace; Q8WWY3; -.
GeneWiki; PRPF31; -.
GenomeRNAi; 26121; -.
PRO; PR:Q8WWY3; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105618; -.
CleanEx; HS_PRPF31; -.
ExpressionAtlas; Q8WWY3; baseline and differential.
Genevisible; Q8WWY3; HS.
GO; GO:0015030; C:Cajal body; IDA:MGI.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
GO; GO:0005684; C:U2-type spliceosomal complex; IC:BHF-UCL.
GO; GO:0005687; C:U4 snRNP; IDA:BHF-UCL.
GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:CAFA.
GO; GO:0005690; C:U4atac snRNP; TAS:BHF-UCL.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0070990; F:snRNP binding; IPI:BHF-UCL.
GO; GO:0030621; F:U4 snRNA binding; IDA:GO_Central.
GO; GO:0030622; F:U4atac snRNA binding; IDA:GO_Central.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:MGI.
GO; GO:0071166; P:ribonucleoprotein complex localization; IMP:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:MGI.
InterPro; IPR002687; Nop_dom.
InterPro; IPR036070; Nop_dom_sf.
InterPro; IPR012976; NOSIC.
InterPro; IPR027105; Prp31.
InterPro; IPR019175; Prp31_C.
PANTHER; PTHR13904; PTHR13904; 1.
Pfam; PF01798; Nop; 1.
Pfam; PF09785; Prp31_C; 1.
SMART; SM00931; NOSIC; 1.
SUPFAM; SSF89124; SSF89124; 1.
PROSITE; PS51358; NOP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Disease mutation; Isopeptide bond; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome;
Retinitis pigmentosa; Ribonucleoprotein; RNA-binding; Spliceosome;
Ubl conjugation.
CHAIN 1 499 U4/U6 small nuclear ribonucleoprotein
Prp31.
/FTId=PRO_0000227799.
DOMAIN 215 333 Nop. {ECO:0000255|PROSITE-
ProRule:PRU00690}.
COILED 85 120 {ECO:0000269|PubMed:17412961}.
COILED 181 215 {ECO:0000269|PubMed:17412961}.
MOTIF 351 364 Nuclear localization signal (NLS).
COMPBIAS 16 19 Poly-Glu.
COMPBIAS 25 29 Poly-Glu.
SITE 247 247 Interaction with U4 snRNA.
SITE 270 270 Interaction with U4 snRNA.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 438 438 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CCF0}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 440 440 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 455 455 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 471 471 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 478 478 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 80 Missing (in isoform 3).
{ECO:0000303|PubMed:12747765}.
/FTId=VSP_017581.
VAR_SEQ 333 364 EPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKE -> RRRWL
RPTRSISPAWLSSSRSRARRVALCPPE (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_017582.
VAR_SEQ 359 499 Missing (in isoform 3).
{ECO:0000303|PubMed:12747765}.
/FTId=VSP_017583.
VAR_SEQ 365 499 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_017584.
VAR_SEQ 426 499 RTLQKQSVVYGGKSTIRDRSSGTASSVAFTPLQGLEIVNPQ
AAEKKVAEANQKYFSSMAEFLKVKGEKSGLMST -> VWAR
PRWGWGPRDTRWGEPRSQPPCPPHSGPCRSRASYMAGSPPS
ATAPRARPPAWPSPHSRAWRL (in isoform 4).
{ECO:0000303|PubMed:21697133}.
/FTId=VSP_057390.
VARIANT 111 114 Missing (in RP11; high penetrance).
{ECO:0000269|PubMed:12923864}.
/FTId=VAR_025629.
VARIANT 194 194 A -> E (in RP11; mislocation of the
protein in the cytoplasm and reduced
interaction with PRPF6; the result may be
a deficiency in splicing function in the
retina; dbSNP:rs119475043).
{ECO:0000269|PubMed:11545739,
ECO:0000269|PubMed:12444105,
ECO:0000269|PubMed:17412961}.
/FTId=VAR_025630.
VARIANT 216 216 A -> P (in RP11; mislocation of the
protein in the cytoplasm, but no effect
on interaction with PRPF6; the result may
be a deficiency in splicing function in
the retina; dbSNP:rs119475042).
{ECO:0000269|PubMed:11545739,
ECO:0000269|PubMed:12444105,
ECO:0000269|PubMed:17412961,
ECO:0000269|PubMed:8808602}.
/FTId=VAR_025631.
MUTAGEN 270 270 H->A,K: Reduces binding to the complex
formed by U4 snRNA and SNU13.
{ECO:0000269|PubMed:17412961}.
MUTAGEN 351 364 Missing: Abolishes nuclear localization.
{ECO:0000269|PubMed:12444105}.
CONFLICT 188 188 E -> D (in Ref. 1; AAK77986).
{ECO:0000305}.
CONFLICT 235 235 A -> G (in Ref. 2; AAG48270).
{ECO:0000305}.
CONFLICT 244 244 M -> V (in Ref. 3; CAB43677).
{ECO:0000305}.
HELIX 89 118 {ECO:0000244|PDB:2OZB}.
TURN 119 121 {ECO:0000244|PDB:2OZB}.
HELIX 125 128 {ECO:0000244|PDB:2OZB}.
HELIX 132 142 {ECO:0000244|PDB:2OZB}.
HELIX 146 148 {ECO:0000244|PDB:2OZB}.
HELIX 149 151 {ECO:0000244|PDB:3SIU}.
HELIX 155 157 {ECO:0000244|PDB:2OZB}.
HELIX 161 172 {ECO:0000244|PDB:2OZB}.
HELIX 181 215 {ECO:0000244|PDB:2OZB}.
HELIX 217 235 {ECO:0000244|PDB:2OZB}.
HELIX 238 242 {ECO:0000244|PDB:2OZB}.
HELIX 246 249 {ECO:0000244|PDB:2OZB}.
TURN 250 253 {ECO:0000244|PDB:2OZB}.
TURN 273 276 {ECO:0000244|PDB:2OZB}.
HELIX 278 281 {ECO:0000244|PDB:2OZB}.
HELIX 285 287 {ECO:0000244|PDB:2OZB}.
HELIX 288 307 {ECO:0000244|PDB:2OZB}.
HELIX 315 331 {ECO:0000244|PDB:2OZB}.
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


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