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Pre-mRNA-processing-splicing factor 8 (220 kDa U5 snRNP-specific protein) (PRP8 homolog) (Splicing factor Prp8) (p220)

 PRP8_HUMAN              Reviewed;        2335 AA.
Q6P2Q9; O14547; O75965;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=Pre-mRNA-processing-splicing factor 8;
AltName: Full=220 kDa U5 snRNP-specific protein;
AltName: Full=PRP8 homolog;
AltName: Full=Splicing factor Prp8;
AltName: Full=p220;
Name=PRPF8; Synonyms=PRPC8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION IN
U2- AND U12-DEPENDENT SPLICEOSOME COMPLEXES.
PubMed=10411133; DOI=10.1017/S1355838299990520;
Luo H.R., Moreau G.A., Levin N., Moore M.J.;
"The human Prp8 protein is a component of both U2- and U12-dependent
spliceosomes.";
RNA 5:893-908(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS 68-GLU; LEU-874 AND HIS-1293.
Shimada Y., Fujiwara T., Kawai A., Shimizu F., Okuno S., Ozaki K.,
Takeda S., Watanabe T., Nagata M., Takahashi E.;
"Human homologue of Saccharomyces cerevisiae PRP8, pre-mRNA splicing
factor.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-227.
TISSUE=Testis;
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).
[4]
PROTEIN SEQUENCE OF 2-8; 51-58; 218-227; 268-278; 421-428; 453-460;
556-565; 610-623; 643-650; 677-702; 747-758; 822-833; 838-845;
988-995; 999-1032; 1113-1131; 1142-1158; 1225-1231; 1246-1258;
1311-1320; 1345-1354; 1371-1392; 1450-1459; 1464-1491; 1524-1532;
1571-1578; 1642-1649; 1668-1678; 1724-1732; 1736-1744; 1814-1831;
1841-1859; 1902-1908; 1926-1935; 1995-2031; 2035-2045; 2050-2070;
2087-2108; 2114-2121; 2199-2210; 2230-2239; 2250-2266 AND 2288-2302,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[5]
IDENTIFICATION IN U5 SNRNP COMPLEX.
PubMed=2532307; DOI=10.1038/342819a0;
Anderson G.J., Bach M., Luehrmann R., Beggs J.D.;
"Conservation between yeast and man of a protein associated with U5
small nuclear ribonucleoprotein.";
Nature 342:819-821(1989).
[6]
IDENTIFICATION IN U5 SNRNP COMPLEX.
PubMed=2527369; DOI=10.1073/pnas.86.16.6038;
Bach M., Winkelmann G., Luehrmann R.;
"20S small nuclear ribonucleoprotein U5 shows a surprisingly complex
protein composition.";
Proc. Natl. Acad. Sci. U.S.A. 86:6038-6042(1989).
[7]
IDENTIFICATION IN U5 SNRNP; U5/4/6 SNRNP AND SPLICEOSOME COMPLEXES.
PubMed=2479028; DOI=10.1073/pnas.86.22.8742;
Pinto A.L., Steitz J.A.;
"The mammalian analogue of the yeast PRP8 splicing protein is present
in the U4/5/6 small nuclear ribonucleoprotein particle and the
spliceosome.";
Proc. Natl. Acad. Sci. U.S.A. 86:8742-8746(1989).
[8]
IDENTIFICATION IN SPLICEOSOME COMPLEX, AND INTERACTION WITH PRE-MRNA.
PubMed=2139226; DOI=10.1073/pnas.87.8.3082;
Garcia-Blanco M.A., Anderson G.J., Beggs J., Sharp P.A.;
"A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a
potential homologue of the yeast PRP8 protein.";
Proc. Natl. Acad. Sci. U.S.A. 87:3082-3086(1990).
[9]
IDENTIFICATION IN U5 SNRNP COMPLEX, AND INTERACTION WITH U5 SNRNA.
PubMed=8702566; DOI=10.1074/jbc.271.31.19001;
Hinz M., Moore M.J., Bindereif A.;
"Domain analysis of human U5 RNA. Cap trimethylation, protein binding,
and spliceosome assembly.";
J. Biol. Chem. 271:19001-19007(1996).
[10]
INTERACTION WITH PRE-MRNA.
PubMed=8608445;
Reyes J.L., Kois P., Konforti B.B., Konarska M.M.;
"The canonical GU dinucleotide at the 5' splice site is recognized by
p220 of the U5 snRNP within the spliceosome.";
RNA 2:213-225(1996).
[11]
IDENTIFICATION IN SPLICEOSOME COMPLEX, AND INTERACTION WITH PRE-MRNA.
PubMed=9303319; DOI=10.1093/emboj/16.15.4746;
Chiara M.D., Palandjian L., Feld Kramer R., Reed R.;
"Evidence that U5 snRNP recognizes the 3' splice site for catalytic
step II in mammals.";
EMBO J. 16:4746-4759(1997).
[12]
IDENTIFICATION IN U5 SNRP COMPLEX, AND INTERACTION WITH SNRP116 AND
SNRNP40.
PubMed=9774689; DOI=10.1128/MCB.18.11.6756;
Achsel T., Ahrens K., Brahms H., Teigelkamp S., Luehrmann R.;
"The human U5-220kD protein (hPrp8) forms a stable RNA-free complex
with several U5-specific proteins, including an RNA unwindase, a
homologue of ribosomal elongation factor EF-2, and a novel WD-40
protein.";
Mol. Cell. Biol. 18:6756-6766(1998).
[13]
INTERACTION WITH PRE-MRNA.
PubMed=10024169; DOI=10.1017/S1355838299981785;
Reyes J.L., Gustafson E.H., Luo H.R., Moore M.J., Konarska M.M.;
"The C-terminal region of hPrp8 interacts with the conserved GU
dinucleotide at the 5' splice site.";
RNA 5:167-179(1999).
[14]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX
(EJC) WITH SRRM1.
PubMed=10809668;
Le Hir H., Moore M.J., Maquat L.E.;
"Pre-mRNA splicing alters mRNP composition: evidence for stable
association of proteins at exon-exon junctions.";
Genes Dev. 14:1098-1108(2000).
[15]
INTERACTION WITH U5 SNRNA.
PubMed=11006293; DOI=10.1074/jbc.M007434200;
Urlaub H., Hartmuth K., Kostka S., Grelle G., Luehrmann R.;
"A general approach for identification of RNA-protein cross-linking
sites within native human spliceosomal small nuclear
ribonucleoproteins (snRNPs). Analysis of RNA-protein contacts in
native U1 and U4/U6.U5 snRNPs.";
J. Biol. Chem. 275:41458-41468(2000).
[16]
INTERACTION WITH PRE-MRNA, AND IDENTIFICATION IN U5/4/6 SNRNP COMPLEX.
PubMed=10983979; DOI=10.1016/S1097-2765(00)00032-0;
Maroney P.A., Romfo C.M., Nilsen T.W.;
"Functional recognition of 5' splice site by U4/U6.U5 tri-snRNP
defines a novel ATP-dependent step in early spliceosome assembly.";
Mol. Cell 6:317-328(2000).
[17]
IDENTIFICATION IN U12-DEPENDENT SPLICEOSOME.
PubMed=11971955; DOI=10.1128/MCB.22.10.3219-3229.2002;
Schneider C., Will C.L., Makarova O.V., Makarov E.M., Luehrmann R.;
"Human U4/U6.U5 and U4atac/U6atac.U5 tri-snRNPs exhibit similar
protein compositions.";
Mol. Cell. Biol. 22:3219-3229(2002).
[18]
REVIEW.
PubMed=15840809; DOI=10.1261/rna.2220705;
Grainger R.J., Beggs J.D.;
"Prp8 protein: at the heart of the spliceosome.";
RNA 11:533-557(2005).
[19]
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).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
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).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1463, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
FUNCTION, AND INTERACTION WITH PRPF3.
PubMed=20595234; DOI=10.1101/gad.1925010;
Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
"The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
reversible ubiquitination at the spliceosome.";
Genes Dev. 24:1434-1447(2010).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, 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).
[27]
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).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[30]
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).
[31]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1425, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[32]
CRYSTALLIZATION, AND INTERACTION WITH AAR2.
PubMed=26527271; DOI=10.1107/S2053230X15019202;
Santos K., Preussner M., Heroven A.C., Weber G.;
"Crystallization and biochemical characterization of the human
spliceosomal Aar2-Prp8(RNaseH) complex.";
Acta Crystallogr. F 71:1421-1428(2015).
[33]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1760-2016, DOMAIN, AND LACK
OF METAL-BINDING.
PubMed=18843295; DOI=10.1038/emboj.2008.209;
Pena V., Rozov A., Fabrizio P., Luehrmann R., Wahl M.C.;
"Structure and function of an RNase H domain at the heart of the
spliceosome.";
EMBO J. 27:2929-2940(2008).
[34]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1769-1990, IDENTIFICATION BY
MASS SPECTROMETRY, RNA-BINDING, MUTAGENESIS OF VAL-1788 AND THR-1789,
AND LACK OF METAL-BINDING SITE.
PubMed=18836455; DOI=10.1038/nsmb.1505;
Ritchie D.B., Schellenberg M.J., Gesner E.M., Raithatha S.A.,
Stuart D.T., Macmillan A.M.;
"Structural elucidation of a PRP8 core domain from the heart of the
spliceosome.";
Nat. Struct. Mol. Biol. 15:1199-1205(2008).
[35]
VARIANTS RP13 THR-2301; LEU-2304; ARG-2309; PRO-2309; GLY-2310;
LYS-2310 AND LEU-2314.
PubMed=11468273; DOI=10.1093/hmg/10.15.1555;
McKie A.B., McHale J.C., Keen T.J., Tarttelin E.E., Goliath R.,
van Lith-Verhoeven J.J., Greenberg J., Ramesar R.S., Hoyng C.B.,
Cremers F.P., Mackey D.A., Bhattacharya S.S., Bird A.C., Markham A.F.,
Inglehearn C.F.;
"Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal
dominant retinitis pigmentosa (RP13).";
Hum. Mol. Genet. 10:1555-1562(2001).
[36]
VARIANTS RP13 GLY-2310 AND ASN-2334.
De Erkenez A.C., Berson E.L., Dryja T.P.;
"Novel mutations in the PRPC8 gene, encoding a pre-mRNA splicing
factor in patients with autosomal dominant retinitis pigmentosa.";
(er) Invest. Ophthalmol. Vis. Sci. 43:ARVO E-Abstract 791(2002).
[37]
VARIANT RP13 LYS-2310.
PubMed=11910553; DOI=10.1076/opge.23.1.1.2206;
van Lith-Verhoeven J.J., van der Velde-Visser S.D., Sohocki M.M.,
Deutman A.F., Brink H.M., Cremers F.P., Hoyng C.B.;
"Clinical characterization, linkage analysis, and PRPC8 mutation
analysis of a family with autosomal dominant retinitis pigmentosa type
13 (RP13).";
Ophthalmic Genet. 23:1-12(2002).
[38]
VARIANT RP13 GLY-2310.
PubMed=12714658; DOI=10.1167/iovs.02-0871;
Martinez-Gimeno M., Gamundi M.J., Hernan I., Maseras M., Milla E.,
Ayuso C., Garcia-Sandoval B., Beneyto M., Vilela C., Baiget M.,
Antinolo G., Carballo M.;
"Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and
PRPF31 in Spanish families with autosomal dominant retinitis
pigmentosa.";
Invest. Ophthalmol. Vis. Sci. 44:2171-2177(2003).
[39]
CHARACTERIZATION OF VARIANTS RP13 LEU-2304; PRO-2309; ARG-2309;
GLY-2310; LYS-2310 AND LEU-2314, AND INTERACTION WITH EFTUD2 AND
SNRNP200.
PubMed=17317632; DOI=10.1016/j.molcel.2007.01.023;
Pena V., Liu S., Bujnicki J.M., Luehrmann R., Wahl M.C.;
"Structure of a multipartite protein-protein interaction domain in
splicing factor Prp8 and its link to retinitis pigmentosa.";
Mol. Cell 25:615-624(2007).
-!- FUNCTION: Functions as a scaffold that mediates the ordered
assembly of spliceosomal proteins and snRNAs. Required for the
assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold
that positions spliceosomal U2, U5 and U6 snRNAs at splice sites
on pre-mRNA substrates, so that splicing can occur. Interacts with
both the 5' and the 3' splice site. {ECO:0000269|PubMed:20595234,
ECO:0000303|PubMed:15840809}.
-!- SUBUNIT: Part of the U5 snRNP complex. 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.
Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent
spliceosomes. Found in a mRNA splicing-dependent exon junction
complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116
and SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via
the MPN (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked
polyubiquitinated); may stabilize the U4/U6-U5 tri-snRNP complex.
Interacts (via RNase H homology domain) with AAR2
(PubMed:26527271). {ECO:0000269|PubMed:10024169,
ECO:0000269|PubMed:10411133, ECO:0000269|PubMed:10809668,
ECO:0000269|PubMed:10983979, ECO:0000269|PubMed:11006293,
ECO:0000269|PubMed:11971955, ECO:0000269|PubMed:16723661,
ECO:0000269|PubMed:17317632, ECO:0000269|PubMed:20595234,
ECO:0000269|PubMed:2139226, ECO:0000269|PubMed:2479028,
ECO:0000269|PubMed:2527369, ECO:0000269|PubMed:2532307,
ECO:0000269|PubMed:26527271, ECO:0000269|PubMed:8608445,
ECO:0000269|PubMed:8702566, ECO:0000269|PubMed:9303319,
ECO:0000269|PubMed:9774689}.
-!- INTERACTION:
O75934:BCAS2; NbExp=2; IntAct=EBI-538479, EBI-1050106;
O95905:ECD; NbExp=2; IntAct=EBI-538479, EBI-2557598;
Q15029:EFTUD2; NbExp=2; IntAct=EBI-538479, EBI-357897;
Q92917:GPKOW; NbExp=2; IntAct=EBI-538479, EBI-746309;
Q15365:PCBP1; NbExp=2; IntAct=EBI-538479, EBI-946095;
Q9UMS4:PRPF19; NbExp=2; IntAct=EBI-538479, EBI-395746;
Q13435:SF3B2; NbExp=3; IntAct=EBI-538479, EBI-749111;
Q15427:SF3B4; NbExp=2; IntAct=EBI-538479, EBI-348469;
O95391:SLU7; NbExp=2; IntAct=EBI-538479, EBI-750559;
O75643-1:SNRNP200; NbExp=2; IntAct=EBI-538479, EBI-5456052;
Q96DI7:SNRNP40; NbExp=3; IntAct=EBI-538479, EBI-538492;
Q9BRX9:WDR83; NbExp=2; IntAct=EBI-538479, EBI-7705033;
Q96NB3:ZNF830; NbExp=2; IntAct=EBI-538479, EBI-3920997;
-!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10411133}.
-!- DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with
deubiquitinating enzymes, but lacks the residues that would bind
the catalytic metal ion. {ECO:0000250}.
-!- DOMAIN: Contains a region with structural similarity to reverse
transcripase, presenting the classical thumb, fingers and palm
architecture, but lacks enzyme activity, since the essential
metal-binding residues are not conserved. {ECO:0000250}.
-!- DOMAIN: Contains a region with structural similarity to type-2
restriction endonucleases, but the residues that would bind
catalytic metal ions in endonucleases are instead involved in
hydrogen bonds that stabilize the protein structure.
{ECO:0000250}.
-!- DOMAIN: Contains a region with structural similarity to RNase H,
but lacks RNase H activity. {ECO:0000250}.
-!- DISEASE: Retinitis pigmentosa 13 (RP13) [MIM:600059]: 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:11468273,
ECO:0000269|PubMed:11910553, ECO:0000269|PubMed:12714658,
ECO:0000269|PubMed:17317632, ECO:0000269|Ref.36}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
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EMBL; AF092565; AAC61776.1; -; mRNA.
EMBL; AB007510; BAA22563.1; -; mRNA.
EMBL; BC064370; AAH64370.1; -; mRNA.
CCDS; CCDS11010.1; -.
RefSeq; NP_006436.3; NM_006445.3.
UniGene; Hs.181368; -.
PDB; 3E9L; X-ray; 1.95 A; A=1760-2016.
PDB; 3ENB; X-ray; 1.85 A; A/B=1769-1990.
PDB; 3JCR; EM; 7.00 A; A=1-2335.
PDB; 3LRU; X-ray; 1.85 A; A/B=1831-1990.
PDB; 4JK7; X-ray; 1.40 A; A/B=1769-1990.
PDB; 4JK8; X-ray; 1.15 A; A/B=1769-1990.
PDB; 4JK9; X-ray; 1.50 A; A/B=1769-1990.
PDB; 4JKA; X-ray; 1.32 A; A/B=1769-1990.
PDB; 4JKB; X-ray; 1.30 A; A/B=1769-1990.
PDB; 4JKC; X-ray; 1.50 A; A/B=1769-1990.
PDB; 4JKD; X-ray; 1.55 A; A/B=1769-1990.
PDB; 4JKE; X-ray; 1.65 A; A/B=1769-1990.
PDB; 4JKF; X-ray; 1.95 A; A/B=1769-1990.
PDB; 4JKG; X-ray; 1.80 A; A/B=1769-1990.
PDB; 4JKH; X-ray; 1.80 A; A/B=1769-1990.
PDB; 4KIT; X-ray; 3.60 A; C=2064-2335.
PDB; 5MQF; EM; 5.90 A; A=1-2335.
PDB; 5O9Z; EM; 4.50 A; A=1-2335.
PDB; 5XJC; EM; 3.60 A; A=1-2335.
PDBsum; 3E9L; -.
PDBsum; 3ENB; -.
PDBsum; 3JCR; -.
PDBsum; 3LRU; -.
PDBsum; 4JK7; -.
PDBsum; 4JK8; -.
PDBsum; 4JK9; -.
PDBsum; 4JKA; -.
PDBsum; 4JKB; -.
PDBsum; 4JKC; -.
PDBsum; 4JKD; -.
PDBsum; 4JKE; -.
PDBsum; 4JKF; -.
PDBsum; 4JKG; -.
PDBsum; 4JKH; -.
PDBsum; 4KIT; -.
PDBsum; 5MQF; -.
PDBsum; 5O9Z; -.
PDBsum; 5XJC; -.
ProteinModelPortal; Q6P2Q9; -.
SMR; Q6P2Q9; -.
BioGrid; 115842; 177.
CORUM; Q6P2Q9; -.
DIP; DIP-29614N; -.
IntAct; Q6P2Q9; 63.
MINT; MINT-1131724; -.
STRING; 9606.ENSP00000304350; -.
iPTMnet; Q6P2Q9; -.
PhosphoSitePlus; Q6P2Q9; -.
SwissPalm; Q6P2Q9; -.
BioMuta; PRPF8; -.
DMDM; 67460824; -.
EPD; Q6P2Q9; -.
MaxQB; Q6P2Q9; -.
PaxDb; Q6P2Q9; -.
PeptideAtlas; Q6P2Q9; -.
PRIDE; Q6P2Q9; -.
DNASU; 10594; -.
Ensembl; ENST00000304992; ENSP00000304350; ENSG00000174231.
Ensembl; ENST00000572621; ENSP00000460348; ENSG00000174231.
Ensembl; ENST00000614672; ENSP00000479194; ENSG00000274442.
Ensembl; ENST00000634039; ENSP00000488611; ENSG00000274442.
GeneID; 10594; -.
KEGG; hsa:10594; -.
UCSC; uc002fte.3; human.
CTD; 10594; -.
DisGeNET; 10594; -.
EuPathDB; HostDB:ENSG00000174231.16; -.
GeneCards; PRPF8; -.
GeneReviews; PRPF8; -.
HGNC; HGNC:17340; PRPF8.
HPA; CAB009941; -.
HPA; CAB015457; -.
MalaCards; PRPF8; -.
MIM; 600059; phenotype.
MIM; 607300; gene.
neXtProt; NX_Q6P2Q9; -.
OpenTargets; ENSG00000174231; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA33815; -.
eggNOG; KOG1795; Eukaryota.
eggNOG; COG5178; LUCA.
GeneTree; ENSGT00390000015210; -.
HOGENOM; HOG000184103; -.
HOVERGEN; HBG052796; -.
InParanoid; Q6P2Q9; -.
KO; K12856; -.
OMA; QNKVNTV; -.
OrthoDB; EOG091G003B; -.
PhylomeDB; Q6P2Q9; -.
TreeFam; TF105613; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
ChiTaRS; PRPF8; human.
EvolutionaryTrace; Q6P2Q9; -.
GeneWiki; PRPF8; -.
GenomeRNAi; 10594; -.
PRO; PR:Q6P2Q9; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000174231; -.
CleanEx; HS_PRPF8; -.
ExpressionAtlas; Q6P2Q9; baseline and differential.
Genevisible; Q6P2Q9; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:CAFA.
GO; GO:0005682; C:U5 snRNP; TAS:ProtInc.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000386; F:second spliceosomal transesterification activity; IBA:GO_Central.
GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
CDD; cd13838; RNase_H_like_Prp8_IV; 1.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR012591; PRO8NT.
InterPro; IPR012592; PROCN.
InterPro; IPR012984; PROCT.
InterPro; IPR027652; PRP8.
InterPro; IPR021983; PRP8_domainIV.
InterPro; IPR019581; Prp8_U5-snRNA-bd.
InterPro; IPR019580; Prp8_U6-snRNA-bd.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR019582; RRM_spliceosomal_PrP8.
PANTHER; PTHR11140; PTHR11140; 1.
Pfam; PF01398; JAB; 1.
Pfam; PF08082; PRO8NT; 1.
Pfam; PF08083; PROCN; 1.
Pfam; PF08084; PROCT; 1.
Pfam; PF12134; PRP8_domainIV; 1.
Pfam; PF10598; RRM_4; 1.
Pfam; PF10597; U5_2-snRNA_bdg; 1.
Pfam; PF10596; U6-snRNA_bdg; 1.
ProDom; PD149576; Pre-mRNA-splicing_factor-8; 1.
SMART; SM00232; JAB_MPN; 1.
SUPFAM; SSF53098; SSF53098; 2.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disease mutation; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Retinitis pigmentosa; Ribonucleoprotein;
RNA-binding; Spliceosome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.4}.
CHAIN 2 2335 Pre-mRNA-processing-splicing factor 8.
/FTId=PRO_0000097040.
DOMAIN 2103 2234 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
REGION 812 1303 Reverse transcriptase homology domain.
REGION 1304 1577 Linker.
REGION 1513 1526 Important for branch point selection.
{ECO:0000250}.
REGION 1581 1752 Restriction endonuclease homology domain.
REGION 1669 2034 Involved in interaction with pre-mRNA 5'
splice site.
REGION 1767 2020 RNase H homology domain.
REGION 2301 2335 Required for interaction with EFTUD2 and
SNRNP200. {ECO:0000269|PubMed:17317632}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.4}.
MOD_RES 859 859 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1358 1358 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1425 1425 N6,N6-dimethyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1463 1463 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 68 68 K -> E (in dbSNP:rs1043391).
/FTId=VAR_022622.
VARIANT 227 227 R -> H (in dbSNP:rs11559304).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_022623.
VARIANT 874 874 P -> L (in dbSNP:rs1043396).
{ECO:0000269|Ref.2}.
/FTId=VAR_022624.
VARIANT 1293 1293 N -> H (in dbSNP:rs1043399).
{ECO:0000269|Ref.2}.
/FTId=VAR_022625.
VARIANT 2301 2301 P -> T (in RP13; no effect on interaction
with SNRNP200 and EFTUD2;
dbSNP:rs121434239).
{ECO:0000269|PubMed:11468273}.
/FTId=VAR_022626.
VARIANT 2304 2304 F -> L (in RP13; dbSNP:rs121434240).
{ECO:0000269|PubMed:11468273,
ECO:0000269|PubMed:17317632}.
/FTId=VAR_022627.
VARIANT 2309 2309 H -> P (in RP13; no effect on interaction
with SNRNP200 and EFTUD2;
dbSNP:rs121434236).
{ECO:0000269|PubMed:11468273,
ECO:0000269|PubMed:17317632}.
/FTId=VAR_022628.
VARIANT 2309 2309 H -> R (in RP13; no effect on interaction
with SNRNP200 and EFTUD2;
dbSNP:rs121434236).
{ECO:0000269|PubMed:11468273,
ECO:0000269|PubMed:17317632}.
/FTId=VAR_022629.
VARIANT 2310 2310 R -> G (in RP13; reduces interaction with
SNRNP200 and EFTUD2).
{ECO:0000269|PubMed:11468273,
ECO:0000269|PubMed:12714658,
ECO:0000269|PubMed:17317632,
ECO:0000269|Ref.36}.
/FTId=VAR_022630.
VARIANT 2310 2310 R -> K (in RP13; reduces interaction with
SNRNP200 and EFTUD2; dbSNP:rs121434238).
{ECO:0000269|PubMed:11468273,
ECO:0000269|PubMed:11910553,
ECO:0000269|PubMed:17317632}.
/FTId=VAR_022631.
VARIANT 2314 2314 F -> L (in RP13; reduces interaction with
EFTUD2, but not with SNRNP200).
{ECO:0000269|PubMed:11468273,
ECO:0000269|PubMed:17317632}.
/FTId=VAR_022632.
VARIANT 2334 2334 Y -> N (in RP13). {ECO:0000269|Ref.36}.
/FTId=VAR_022633.
MUTAGEN 1788 1788 V->D: Strongly reduced interaction with
RNA. {ECO:0000269|PubMed:18836455}.
MUTAGEN 1789 1789 T->P: Strongly reduced interaction with
RNA. {ECO:0000269|PubMed:18836455}.
CONFLICT 184 184 D -> N (in Ref. 2; BAA22563).
{ECO:0000305}.
CONFLICT 492 493 VG -> GW (in Ref. 2; BAA22563).
{ECO:0000305}.
CONFLICT 604 604 M -> V (in Ref. 2; BAA22563).
{ECO:0000305}.
CONFLICT 806 806 A -> T (in Ref. 2; BAA22563).
{ECO:0000305}.
CONFLICT 997 997 L -> V (in Ref. 2; BAA22563).
{ECO:0000305}.
CONFLICT 1390 1390 A -> S (in Ref. 2; BAA22563).
{ECO:0000305}.
CONFLICT 1867 1867 G -> D (in Ref. 2; BAA22563).
{ECO:0000305}.
STRAND 1761 1763 {ECO:0000244|PDB:3E9L}.
TURN 1765 1767 {ECO:0000244|PDB:3E9L}.
HELIX 1768 1772 {ECO:0000244|PDB:3E9L}.
STRAND 1773 1775 {ECO:0000244|PDB:4JK8}.
STRAND 1777 1781 {ECO:0000244|PDB:4JK8}.
STRAND 1785 1792 {ECO:0000244|PDB:4JK8}.
STRAND 1794 1796 {ECO:0000244|PDB:3E9L}.
STRAND 1798 1803 {ECO:0000244|PDB:4JK8}.
STRAND 1805 1810 {ECO:0000244|PDB:4JK8}.
TURN 1812 1814 {ECO:0000244|PDB:4JK8}.
STRAND 1816 1822 {ECO:0000244|PDB:4JK8}.
HELIX 1824 1827 {ECO:0000244|PDB:4JK8}.
HELIX 1833 1851 {ECO:0000244|PDB:4JK8}.
HELIX 1854 1856 {ECO:0000244|PDB:4JK8}.
STRAND 1859 1865 {ECO:0000244|PDB:4JK8}.
HELIX 1866 1868 {ECO:0000244|PDB:4JK8}.
HELIX 1869 1875 {ECO:0000244|PDB:4JK8}.
TURN 1876 1878 {ECO:0000244|PDB:4JK8}.
STRAND 1883 1886 {ECO:0000244|PDB:4JK8}.
HELIX 1893 1898 {ECO:0000244|PDB:4JK8}.
HELIX 1900 1908 {ECO:0000244|PDB:4JK8}.
STRAND 1913 1918 {ECO:0000244|PDB:4JK8}.
TURN 1919 1922 {ECO:0000244|PDB:4JK8}.
HELIX 1923 1925 {ECO:0000244|PDB:4JK8}.
HELIX 1929 1945 {ECO:0000244|PDB:4JK8}.
HELIX 1947 1953 {ECO:0000244|PDB:4JK8}.
HELIX 1973 1989 {ECO:0000244|PDB:4JK8}.
HELIX 1999 2001 {ECO:0000244|PDB:3E9L}.
HELIX 2004 2012 {ECO:0000244|PDB:3E9L}.
SEQUENCE 2335 AA; 273600 MW; E823A15C60EA61C9 CRC64;
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED
MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVPVLY
HITGAISFVN EIPWVIEPVY ISQWGSMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD
NILDVEPLEA IQLELDPEED APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR
LANQLLTDLV DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN
KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF YFDPLINPIS
HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN GIALLWAPRP FNLRSGRTRR
ALDIPLVKNW YREHCPAGQP VKVRVSYQKL LKYYVLNALK HRPPKAQKKR YLFRSFKATK
FFQSTKLDWV EVGLQVCRQG YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF
GNAFHLCREV LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR
QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER WLGNLLARQF
EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG IKQNKARTIL QHLSEAWRCW
KANIPWKVPG LPTPIENMIL RYVKAKADWW TNTAHYNRER IRRGATVDKT VCKKNLGRLT
RLYLKAEQER QHNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI
LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD
LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL LVYKWCQGIN
NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI VDHNIADYMT AKNNVVINYK
DMNHTNSYGI IRGLQFASFI VQYYGLVMDL LVLGLHRASE MAGPPQMPND FLSFQDIATE
AAHPIRLFCR YIDRIHIFFR FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM
RLMKHDVNLG RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC
RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA SGSTTFTKIV
NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK IGLNSKMPSR FPPVVFYTPK
ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI THFRSGMSHE EDQLIPNLYR YIQPWESEFI
DSQRVWAEYA LKRQEAIAQN RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT
DFKQYQVLKQ NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG
LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG FQVQLDLTGI
FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE LDALEIETVQ KETIHPRKSY
KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA
RAKFLDYTTD NMSIYPSPTG VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL
YVLRERIRKG LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT
KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR SLPVEEQPKQ
IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE KFGDLILKAT EPQMVLFNLY
DDWLKTISSY TAFSRLILIL RALHVNNDRA KVILKPDKTT ITEPHHIWPT LTDEEWIKVE
VQLKDLILAD YGKKNNVNVA SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT
ATQTRTVNKH GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET
GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ WGTHQTVHLP
GQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM ADNPSWDGEK TIIITCSFTP
GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN
YNFMGVRHDP NMKYELQLAN PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA


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