PRPF3_HUMAN
ID PRPF3_HUMAN Reviewed; 683 AA.
AC O43395; B4DSY9; O43446; Q5VT54;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp3;
DE AltName: Full=Pre-mRNA-splicing factor 3;
DE Short=hPrp3;
DE AltName: Full=U4/U6 snRNP 90 kDa protein;
GN Name=PRPF3; Synonyms=HPRP3 {ECO:0000303|PubMed:11773002}, PRP3;
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), INTERACTION WITH PRPF4 AND U4/U5/U6
RP SNRNPS, AND SUBCELLULAR LOCATION.
RX PubMed=9328476; DOI=10.1093/hmg/6.12.2117;
RA Wang A., Forman-Kay J., Luo Y., Luo M., Chow Y.-H., Plumb J., Friesen J.D.,
RA Tsui L.-C., Heng H.H.Q., Woolford J.L. Jr., Hu J.;
RT "Identification and characterization of human genes encoding Hprp3p and
RT Hprp4p, interacting components of the spliceosome.";
RL Hum. Mol. Genet. 6:2117-2126(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 93-101;
RP 253-267; 351-361; 409-428 AND 560-576, INTERACTION WITH PPIH; PRPF4 AND
RP U4/U6 SNRNPS, AND SUBCELLULAR LOCATION.
RC TISSUE=Neuroepithelium;
RX PubMed=9404889;
RA Horowitz D.S., Kobayashi R., Krainer A.R.;
RT "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a
RT complex associated with U4/U6 snRNPs.";
RL RNA 3:1374-1387(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Skin;
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 [7]
RP INTERACTION WITH SART3, AND REGION.
RX PubMed=15314151; DOI=10.1128/mcb.24.17.7392-7401.2004;
RA Medenbach J., Schreiner S., Liu S., Luhrmann R., Bindereif A.;
RT "Human U4/U6 snRNP recycling factor p110: mutational analysis reveals the
RT function of the tetratricopeptide repeat domain in recycling.";
RL Mol. Cell. Biol. 24:7392-7401(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-167, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP 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 [14]
RP FUNCTION, INTERACTION WITH PRPF8; PRPF19 AND SART3, UBIQUITINATION BY
RP PRPF19, AND DEUBIQUITINATION BY USP4.
RX PubMed=20595234; DOI=10.1101/gad.1925010;
RA Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
RA Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
RT "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
RT reversible ubiquitination at the spliceosome.";
RL Genes Dev. 24:1434-1447(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; THR-167 AND SER-619, AND
RP IDENTIFICATION BY 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-619, AND
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP 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 [20]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-244 AND LYS-252, 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 [22]
RP STRUCTURE BY NMR OF 1-79.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PWI domain in U4/U6 small nuclear ribonucleoprotein
RT PRP3(HPRP3).";
RL Submitted (NOV-2005) to the PDB data bank.
RN [23] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
RN [24] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [25]
RP VARIANTS RP18 SER-493 AND MET-494, AND TISSUE SPECIFICITY.
RX PubMed=11773002; DOI=10.1093/hmg/11.1.87;
RA Chakarova C.F., Hims M.M., Bolz H., Abu-Safieh L., Patel R.J.,
RA Papaioannou M.G., Inglehearn C.F., Keen T.J., Willis C., Moore A.T.,
RA Rosenberg T., Webster A.R., Bird A.C., Gal A., Hunt D., Vithana E.N.,
RA Bhattacharya S.S.;
RT "Mutations in HPRP3, a third member of pre-mRNA splicing factor genes,
RT implicated in autosomal dominant retinitis pigmentosa.";
RL Hum. Mol. Genet. 11:87-92(2002).
RN [26]
RP VARIANT RP18 MET-494.
RX PubMed=12714658; DOI=10.1167/iovs.02-0871;
RA Martinez-Gimeno M., Gamundi M.J., Hernan I., Maseras M., Milla E.,
RA Ayuso C., Garcia-Sandoval B., Beneyto M., Vilela C., Baiget M.,
RA Antinolo G., Carballo M.;
RT "Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31
RT in Spanish families with autosomal dominant retinitis pigmentosa.";
RL Invest. Ophthalmol. Vis. Sci. 44:2171-2177(2003).
RN [27]
RP CHARACTERIZATION OF VARIANT RP18 MET-494, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17932117; DOI=10.1093/hmg/ddm300;
RA Gonzalez-Santos J.M., Cao H., Duan R.C., Hu J.;
RT "Mutation in the splicing factor Hprp3p linked to retinitis pigmentosa
RT impairs interactions within the U4/U6 snRNP complex.";
RL Hum. Mol. Genet. 17:225-239(2008).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex that is involved in spliceosome assembly, and as
CC component of the precatalytic spliceosome (spliceosome B complex).
CC {ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166,
CC ECO:0000305|PubMed:20595234}.
CC -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC complex) (PubMed:28781166). Component of the U4/U6-U5 tri-snRNP
CC complex, a building block of the precatalytic spliceosome (spliceosome
CC B complex) (PubMed:9328476, PubMed:9404889, PubMed:28781166,
CC PubMed:26912367, PubMed:17932117). The U4/U6-U5 tri-snRNP complex is
CC composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6,
CC PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1
CC and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8
CC (PubMed:16723661, PubMed:26912367). Interacts directly with PRPF4
CC (PubMed:9328476, PubMed:9404889, PubMed:17932117). Part of a
CC heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in
CC the absence of RNA (PubMed:9404889). Interacts with SART3; the
CC interaction is direct and recruits the deubiquitinase USP4 to PRPF3
CC (PubMed:15314151, PubMed:20595234). Interacts with PRPF19. Interacts
CC ('Lys-63'-linked polyubiquitinated) with PRPF8 (via the MPN (JAB/Mov34)
CC domain); may stabilize the U4/U6-U5 tri-snRNP complex
CC (PubMed:20595234). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000269|PubMed:15314151, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:17932117, ECO:0000269|PubMed:20595234,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9328476,
CC ECO:0000269|PubMed:9404889}.
CC -!- INTERACTION:
CC O43395; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-744322, EBI-3866279;
CC O43395; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-744322, EBI-11977221;
CC O43395; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-744322, EBI-739624;
CC O43395; Q92997: DVL3; NbExp=2; IntAct=EBI-744322, EBI-739789;
CC O43395; Q8IZU0: FAM9B; NbExp=9; IntAct=EBI-744322, EBI-10175124;
CC O43395; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-744322, EBI-11977403;
CC O43395; Q08379: GOLGA2; NbExp=3; IntAct=EBI-744322, EBI-618309;
CC O43395; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-744322, EBI-473189;
CC O43395; O75031: HSF2BP; NbExp=3; IntAct=EBI-744322, EBI-7116203;
CC O43395; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-744322, EBI-1216080;
CC O43395; P55081: MFAP1; NbExp=2; IntAct=EBI-744322, EBI-1048159;
CC O43395; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-744322, EBI-10172526;
CC O43395; Q96RE7: NACC1; NbExp=3; IntAct=EBI-744322, EBI-7950997;
CC O43395; Q8N5F7: NKAP; NbExp=2; IntAct=EBI-744322, EBI-721539;
CC O43395; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-744322, EBI-3920396;
CC O43395; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-744322, EBI-1051317;
CC O43395; Q8IXK0-5: PHC2; NbExp=3; IntAct=EBI-744322, EBI-11527347;
CC O43395; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-744322, EBI-11532361;
CC O43395; O43395: PRPF3; NbExp=2; IntAct=EBI-744322, EBI-744322;
CC O43395; O94906: PRPF6; NbExp=3; IntAct=EBI-744322, EBI-536755;
CC O43395; O43242: PSMD3; NbExp=3; IntAct=EBI-744322, EBI-357622;
CC O43395; Q15276: RABEP1; NbExp=3; IntAct=EBI-744322, EBI-447043;
CC O43395; Q2KHN1: RNF151; NbExp=3; IntAct=EBI-744322, EBI-12002474;
CC O43395; O43290: SART1; NbExp=4; IntAct=EBI-744322, EBI-607761;
CC O43395; Q13435: SF3B2; NbExp=2; IntAct=EBI-744322, EBI-749111;
CC O43395; Q8TBC3: SHKBP1; NbExp=3; IntAct=EBI-744322, EBI-724292;
CC O43395; O95391: SLU7; NbExp=2; IntAct=EBI-744322, EBI-750559;
CC O43395; O75940: SMNDC1; NbExp=2; IntAct=EBI-744322, EBI-1052641;
CC O43395; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-744322, EBI-2212028;
CC O43395; Q9HCM9: TRIM39; NbExp=4; IntAct=EBI-744322, EBI-739510;
CC O43395; Q9HCM9-2: TRIM39; NbExp=8; IntAct=EBI-744322, EBI-11523450;
CC O43395; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-744322, EBI-723389;
CC O43395; P40222: TXLNA; NbExp=3; IntAct=EBI-744322, EBI-359793;
CC O43395; P26368: U2AF2; NbExp=2; IntAct=EBI-744322, EBI-742339;
CC O43395; P26368-2: U2AF2; NbExp=3; IntAct=EBI-744322, EBI-11097439;
CC O43395; Q8WW38: ZFPM2; NbExp=3; IntAct=EBI-744322, EBI-947213;
CC O43395; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-744322, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17932117,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889}. Nucleus
CC speckle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43395-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43395-3; Sequence=VSP_056265, VSP_056266, VSP_056267;
CC -!- TISSUE SPECIFICITY: Highly expressed in retina, liver, kidney and
CC blood. Detected at lower levels in heart and brain.
CC {ECO:0000269|PubMed:11773002}.
CC -!- PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination by
CC PRPF19 and deubiquitination by USP4. 'Lys-63'-linked ubiquitination
CC increases the affinity for PRPF8 and may regulate the assembly of the
CC U4/U6-U5 tri-snRNP complex. {ECO:0000269|PubMed:20595234}.
CC -!- DISEASE: Retinitis pigmentosa 18 (RP18) [MIM:601414]: 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:11773002,
CC ECO:0000269|PubMed:12714658, ECO:0000269|PubMed:17932117}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AF001947; AAC09069.1; -; mRNA.
DR EMBL; AF016370; AAC51926.1; -; mRNA.
DR EMBL; AK299980; BAG61801.1; -; mRNA.
DR EMBL; AL611942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53556.1; -; Genomic_DNA.
DR EMBL; BC000184; AAH00184.1; -; mRNA.
DR EMBL; BC001954; AAH01954.1; -; mRNA.
DR CCDS; CCDS951.1; -. [O43395-1]
DR PIR; T50839; T50839.
DR PIR; T50840; T50840.
DR RefSeq; NP_004689.1; NM_004698.2. [O43395-1]
DR PDB; 1X4Q; NMR; -; A=1-79.
DR PDB; 3JCR; EM; 7.00 A; K=1-683.
DR PDB; 5O9Z; EM; 4.50 A; E=1-683.
DR PDB; 6AH0; EM; 5.70 A; J=1-683.
DR PDB; 6AHD; EM; 3.80 A; J=1-683.
DR PDB; 6QW6; EM; 2.92 A; 4A=1-683.
DR PDB; 6QX9; EM; 3.28 A; 4A=1-683.
DR PDBsum; 1X4Q; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; O43395; -.
DR SMR; O43395; -.
DR BioGRID; 114577; 226.
DR CORUM; O43395; -.
DR DIP; DIP-34508N; -.
DR IntAct; O43395; 104.
DR MINT; O43395; -.
DR STRING; 9606.ENSP00000315379; -.
DR GlyGen; O43395; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O43395; -.
DR MetOSite; O43395; -.
DR PhosphoSitePlus; O43395; -.
DR SwissPalm; O43395; -.
DR BioMuta; PRPF3; -.
DR EPD; O43395; -.
DR jPOST; O43395; -.
DR MassIVE; O43395; -.
DR MaxQB; O43395; -.
DR PaxDb; O43395; -.
DR PeptideAtlas; O43395; -.
DR PRIDE; O43395; -.
DR ProteomicsDB; 48921; -. [O43395-1]
DR ProteomicsDB; 5058; -.
DR Antibodypedia; 20281; 190 antibodies from 31 providers.
DR DNASU; 9129; -.
DR Ensembl; ENST00000324862.7; ENSP00000315379.6; ENSG00000117360.13. [O43395-1]
DR GeneID; 9129; -.
DR KEGG; hsa:9129; -.
DR MANE-Select; ENST00000324862.7; ENSP00000315379.6; NM_004698.4; NP_004689.1.
DR UCSC; uc001eum.5; human. [O43395-1]
DR CTD; 9129; -.
DR DisGeNET; 9129; -.
DR GeneCards; PRPF3; -.
DR GeneReviews; PRPF3; -.
DR HGNC; HGNC:17348; PRPF3.
DR HPA; ENSG00000117360; Low tissue specificity.
DR MalaCards; PRPF3; -.
DR MIM; 601414; phenotype.
DR MIM; 607301; gene.
DR neXtProt; NX_O43395; -.
DR OpenTargets; ENSG00000117360; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA134892509; -.
DR VEuPathDB; HostDB:ENSG00000117360; -.
DR eggNOG; KOG2769; Eukaryota.
DR GeneTree; ENSGT00390000011497; -.
DR HOGENOM; CLU_015750_3_0_1; -.
DR InParanoid; O43395; -.
DR OMA; AQKPTVR; -.
DR OrthoDB; 1322299at2759; -.
DR PhylomeDB; O43395; -.
DR TreeFam; TF313082; -.
DR PathwayCommons; O43395; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O43395; -.
DR SIGNOR; O43395; -.
DR BioGRID-ORCS; 9129; 644 hits in 1081 CRISPR screens.
DR ChiTaRS; PRPF3; human.
DR EvolutionaryTrace; O43395; -.
DR GeneWiki; PRPF3; -.
DR GenomeRNAi; 9129; -.
DR Pharos; O43395; Tbio.
DR PRO; PR:O43395; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43395; protein.
DR Bgee; ENSG00000117360; Expressed in sural nerve and 200 other tissues.
DR Genevisible; O43395; HS.
DR GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
DR InterPro; IPR013881; Pre-mRNA_splic_Prp3.
DR InterPro; IPR027104; Prp3.
DR InterPro; IPR010541; Prp3_C.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR PANTHER; PTHR14212; PTHR14212; 1.
DR Pfam; PF06544; DUF1115; 1.
DR Pfam; PF08572; PRP3; 1.
DR Pfam; PF01480; PWI; 1.
DR SMART; SM00311; PWI; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR PROSITE; PS51025; PWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Retinitis pigmentosa; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..683
FT /note="U4/U6 small nuclear ribonucleoprotein Prp3"
FT /id="PRO_0000097044"
FT DOMAIN 1..87
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 73..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..550
FT /note="Mediates interaction with SART3"
FT /evidence="ECO:0000269|PubMed:15314151"
FT COMPBIAS 73..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056265"
FT VAR_SEQ 402..416
FT /note="TEENPKREDYFGITN -> GKSQERRLFWNHKSC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056266"
FT VAR_SEQ 417..683
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056267"
FT VARIANT 12
FT /note="K -> N (in dbSNP:rs12736964)"
FT /id="VAR_051286"
FT VARIANT 493
FT /note="P -> S (in RP18; dbSNP:rs121434242)"
FT /evidence="ECO:0000269|PubMed:11773002"
FT /id="VAR_046735"
FT VARIANT 494
FT /note="T -> M (in RP18; reduces phosphorylation; impairs
FT binding to PRPF4; impairs self-association; affects
FT interaction with the U4/U5/U6 tri-snRNP complex; does not
FT affect global pre-mRNA splicing; dbSNP:rs121434241)"
FT /evidence="ECO:0000269|PubMed:11773002,
FT ECO:0000269|PubMed:12714658, ECO:0000269|PubMed:17932117"
FT /id="VAR_016877"
FT CONFLICT 142
FT /note="I -> T (in Ref. 1; AAC09069)"
FT /evidence="ECO:0000305"
FT CONFLICT 273..274
FT /note="EL -> SV (in Ref. 1; AAC09069)"
FT /evidence="ECO:0000305"
FT HELIX 5..23
FT /evidence="ECO:0007829|PDB:1X4Q"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:1X4Q"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:1X4Q"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1X4Q"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1X4Q"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1X4Q"
SQ SEQUENCE 683 AA; 77529 MW; 4AA6AA4C99110284 CRC64;
MALSKRELDE LKPWIEKTVK RVLGFSEPTV VTAALNCVGK GMDKKKAADH LKPFLDDSTL
RFVDKLFEAV EEGRSSRHSK SSSDRSRKRE LKEVFGDDSE ISKESSGVKK RRIPRFEEVE
EEPEVIPGPP SESPGMLTKL QIKQMMEAAT RQIEERKKQL SFISPPTPQP KTPSSSQPER
LPIGNTIQPS QAATFMNDAI EKARKAAELQ ARIQAQLALK PGLIGNANMV GLANLHAMGI
APPKVELKDQ TKPTPLILDE QGRTVDATGK EIELTHRMPT LKANIRAVKR EQFKQQLKEK
PSEDMESNTF FDPRVSIAPS QRQRRTFKFH DKGKFEKIAQ RLRTKAQLEK LQAEISQAAR
KTGIHTSTRL ALIAPKKELK EGDIPEIEWW DSYIIPNGFD LTEENPKRED YFGITNLVEH
PAQLNPPVDN DTPVTLGVYL TKKEQKKLRR QTRREAQKEL QEKVRLGLMP PPEPKVRISN
LMRVLGTEAV QDPTKVEAHV RAQMAKRQKA HEEANAARKL TAEQRKVKKI KKLKEDISQG
VHISVYRVRN LSNPAKKFKI EANAGQLYLT GVVVLHKDVN VVVVEGGPKA QKKFKRLMLH
RIKWDEQTSN TKGDDDEESD EEAVKKTNKC VLVWEGTAKD RSFGEMKFKQ CPTENMAREH
FKKHGAEHYW DLALSESVLE STD
