PRP6_HUMAN
ID PRP6_HUMAN Reviewed; 941 AA.
AC O94906; B2RAR5; B3KMC6; O95109; Q5VXS5; Q9H3Z1; Q9H4T9; Q9H4U8; Q9NTE6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Pre-mRNA-processing factor 6;
DE AltName: Full=Androgen receptor N-terminal domain-transactivating protein 1;
DE Short=ANT-1;
DE AltName: Full=PRP6 homolog;
DE AltName: Full=U5 snRNP-associated 102 kDa protein;
DE Short=U5-102 kDa protein;
GN Name=PRPF6; Synonyms=C20orf14;
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), PROTEIN SEQUENCE OF 138-147;
RP 300-309; 352-359; 776-784 AND 891-898, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=10561546; DOI=10.1016/s0167-4838(99)00203-4;
RA Nishikimi A., Mukai J., Kioka N., Yamada M.;
RT "A novel mammalian nuclear protein similar to Schizosaccharomyces pombe
RT Prp1p/Zer1p and Saccharomyces cerevisiae Prp6p pre-mRNA splicing factors.";
RL Biochim. Biophys. Acta 1435:147-152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 324-334;
RP 395-408; 755-768; 871-883 AND 917-924, AND INTERACTION WITH U5 AND U4/U6
RP SNRNPS.
RC TISSUE=Cervix carcinoma;
RX PubMed=10788320; DOI=10.1006/jmbi.2000.3685;
RA Makarov E.M., Makarova O.V., Achsel T., Luehrmann R.;
RT "The human homologue of the yeast splicing factor Prp6p contains multiple
RT TPR elements and is stably associated with the U5 snRNP via protein-protein
RT interactions.";
RL J. Mol. Biol. 298:567-575(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH ARAF.
RC TISSUE=Cervix carcinoma;
RX PubMed=10848612; DOI=10.1128/mcb.20.13.4870-4878.2000;
RA Yuryev A., Ono M., Goff S.A., Macaluso F., Wennogle L.P.;
RT "Isoform-specific localization of A-RAF in mitochondria.";
RL Mol. Cell. Biol. 20:4870-4878(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, and 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 GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 402-941.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP FUNCTION, INTERACTION WITH AR AND NR3C1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12039962; DOI=10.1074/jbc.m203811200;
RA Zhao Y., Goto K., Saitoh M., Yanase T., Nomura M., Okabe T., Takayanagi R.,
RA Nawata H.;
RT "Activation function-1 domain of androgen receptor contributes to the
RT interaction between subnuclear splicing factor compartment and nuclear
RT receptor compartment. Identification of the p102 U5 small nuclear
RT ribonucleoprotein particle-binding protein as a coactivator for the
RT receptor.";
RL J. Biol. Chem. 277:30031-30039(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
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 THR-266; THR-275 AND SER-279, 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 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-266; THR-275 AND SER-279, 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND THR-266, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-266, 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 [17]
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 [18] {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 [19] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, 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 [20]
RP VARIANT RP60 TRP-729, CHARACTERIZATION OF VARIANT RP60 TRP-729, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=21549338; DOI=10.1016/j.ajhg.2011.04.008;
RA Tanackovic G., Ransijn A., Ayuso C., Harper S., Berson E.L., Rivolta C.;
RT "A missense mutation in PRPF6 causes impairment of pre-mRNA splicing and
RT autosomal-dominant retinitis pigmentosa.";
RL Am. J. Hum. Genet. 88:643-649(2011).
RN [21]
RP VARIANT SER-477.
RX PubMed=22235333; DOI=10.1371/journal.pone.0029729;
RA Velinov M., Dolzhanskaya N., Gonzalez M., Powell E., Konidari I., Hulme W.,
RA Staropoli J.F., Xin W., Wen G.Y., Barone R., Coppel S.H., Sims K.,
RA Brown W.T., Zuchner S.;
RT "Mutations in the gene DNAJC5 cause autosomal dominant Kufs disease in a
RT proportion of cases: study of the Parry family and 8 other families.";
RL PLoS ONE 7:E29729-E29729(2012).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex, one of the building blocks of the spliceosome
CC (PubMed:28781166, PubMed:21549338). Enhances dihydrotestosterone-
CC induced transactivation activity of AR, as well as dexamethasone-
CC induced transactivation activity of NR3C1, but does not affect
CC estrogen-induced transactivation. {ECO:0000269|PubMed:12039962,
CC ECO:0000269|PubMed:21549338, ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Identified in the spliceosome B complex (PubMed:28781166).
CC Identified in the spliceosome C complex (PubMed:11991638). Associates
CC with the U5 snRNP particle (PubMed:10788320). Component of the U4/U6-U5
CC tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least
CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23,
CC CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, LSm proteins LSm2-8 and
CC Sm proteins (PubMed:16723661, PubMed:26912367, PubMed:28781166).
CC Interacts with ARAF (PubMed:10848612). Interacts with AR and NR3C1, but
CC not ESR1, independently of the presence of hormones (PubMed:12039962).
CC Interacts with USH1G (PubMed:34023904). {ECO:0000269|PubMed:10788320,
CC ECO:0000269|PubMed:10848612, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:34023904}.
CC -!- INTERACTION:
CC O94906; P10398: ARAF; NbExp=4; IntAct=EBI-536755, EBI-365961;
CC O94906; P35226: BMI1; NbExp=8; IntAct=EBI-536755, EBI-2341576;
CC O94906; O95400: CD2BP2; NbExp=6; IntAct=EBI-536755, EBI-768015;
CC O94906; Q13123: IK; NbExp=2; IntAct=EBI-536755, EBI-713456;
CC O94906; O43395: PRPF3; NbExp=3; IntAct=EBI-536755, EBI-744322;
CC O94906; Q8WWY3: PRPF31; NbExp=5; IntAct=EBI-536755, EBI-1567797;
CC O94906; O94906: PRPF6; NbExp=2; IntAct=EBI-536755, EBI-536755;
CC O94906; Q6P2Q9: PRPF8; NbExp=4; IntAct=EBI-536755, EBI-538479;
CC O94906; O43290: SART1; NbExp=4; IntAct=EBI-536755, EBI-607761;
CC O94906; O75643: SNRNP200; NbExp=5; IntAct=EBI-536755, EBI-1045395;
CC O94906; P83876: TXNL4A; NbExp=4; IntAct=EBI-536755, EBI-746539;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10561546, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:34023904}. Nucleus
CC speckle {ECO:0000269|PubMed:21549338}. Note=Localized in splicing
CC speckles. {ECO:0000269|PubMed:21549338}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94906-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94906-2; Sequence=VSP_041857;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12039962}.
CC -!- DISEASE: Retinitis pigmentosa 60 (RP60) [MIM:613983]: 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:21549338}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry. Cells from RP60 patients show intron
CC retention for pre-mRNA bearing specific splicing signals.
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DR EMBL; AB019219; BAA37140.1; -; mRNA.
DR EMBL; AF221842; AAF66128.1; -; mRNA.
DR EMBL; AF026031; AAD01798.1; -; mRNA.
DR EMBL; AK001554; BAG50938.1; -; mRNA.
DR EMBL; AK314310; BAG36962.1; -; mRNA.
DR EMBL; AL118506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001666; AAH01666.1; -; mRNA.
DR EMBL; AL137320; CAB70695.1; -; mRNA.
DR CCDS; CCDS13550.1; -. [O94906-1]
DR PIR; T46386; T46386.
DR RefSeq; NP_036601.2; NM_012469.3. [O94906-1]
DR PDB; 3JCR; EM; 7.00 A; G=1-941.
DR PDB; 5O9Z; EM; 4.50 A; G=1-941.
DR PDB; 6AH0; EM; 5.70 A; N=1-941.
DR PDB; 6AHD; EM; 3.80 A; N=1-941.
DR PDB; 6QW6; EM; 2.92 A; 5J=1-941.
DR PDB; 6QX9; EM; 3.28 A; 5J=656-937.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; O94906; -.
DR SMR; O94906; -.
DR BioGRID; 117298; 301.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; O94906; -.
DR DIP; DIP-29006N; -.
DR IntAct; O94906; 86.
DR MINT; O94906; -.
DR STRING; 9606.ENSP00000266079; -.
DR MoonDB; O94906; Predicted.
DR GlyGen; O94906; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94906; -.
DR MetOSite; O94906; -.
DR PhosphoSitePlus; O94906; -.
DR SwissPalm; O94906; -.
DR BioMuta; PRPF6; -.
DR EPD; O94906; -.
DR jPOST; O94906; -.
DR MassIVE; O94906; -.
DR MaxQB; O94906; -.
DR PaxDb; O94906; -.
DR PeptideAtlas; O94906; -.
DR PRIDE; O94906; -.
DR ProteomicsDB; 50541; -. [O94906-1]
DR ProteomicsDB; 50542; -. [O94906-2]
DR Antibodypedia; 15475; 220 antibodies from 30 providers.
DR DNASU; 24148; -.
DR Ensembl; ENST00000266079.5; ENSP00000266079.4; ENSG00000101161.8. [O94906-1]
DR GeneID; 24148; -.
DR KEGG; hsa:24148; -.
DR MANE-Select; ENST00000266079.5; ENSP00000266079.4; NM_012469.4; NP_036601.2.
DR UCSC; uc002yho.4; human. [O94906-1]
DR CTD; 24148; -.
DR DisGeNET; 24148; -.
DR GeneCards; PRPF6; -.
DR GeneReviews; PRPF6; -.
DR HGNC; HGNC:15860; PRPF6.
DR HPA; ENSG00000101161; Low tissue specificity.
DR MalaCards; PRPF6; -.
DR MIM; 613979; gene.
DR MIM; 613983; phenotype.
DR neXtProt; NX_O94906; -.
DR OpenTargets; ENSG00000101161; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA25682; -.
DR VEuPathDB; HostDB:ENSG00000101161; -.
DR eggNOG; KOG0495; Eukaryota.
DR GeneTree; ENSGT00550000075016; -.
DR HOGENOM; CLU_007010_0_0_1; -.
DR InParanoid; O94906; -.
DR OMA; DGWAWYY; -.
DR OrthoDB; 335779at2759; -.
DR PhylomeDB; O94906; -.
DR TreeFam; TF105743; -.
DR PathwayCommons; O94906; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; O94906; -.
DR BioGRID-ORCS; 24148; 758 hits in 1044 CRISPR screens.
DR ChiTaRS; PRPF6; human.
DR GeneWiki; PRPF6; -.
DR GenomeRNAi; 24148; -.
DR Pharos; O94906; Tbio.
DR PRO; PR:O94906; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O94906; protein.
DR Bgee; ENSG00000101161; Expressed in tendon of biceps brachii and 203 other tissues.
DR Genevisible; O94906; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:BHF-UCL.
DR GO; GO:0005682; C:U5 snRNP; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IGI:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006403; P:RNA localization; IMP:MGI.
DR GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; NAS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IMP:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR010491; PRP1_N.
DR InterPro; IPR027108; Prp6/Prp1/STA1.
DR InterPro; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11246; PTHR11246; 1.
DR PANTHER; PTHR11246:SF1; PTHR11246:SF1; 1.
DR Pfam; PF06424; PRP1_N; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00386; HAT; 13.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Retinitis pigmentosa; Spliceosome.
FT CHAIN 1..941
FT /note="Pre-mRNA-processing factor 6"
FT /id="PRO_0000205759"
FT REPEAT 384..416
FT /note="HAT 1"
FT REPEAT 418..444
FT /note="HAT 2"
FT REPEAT 445..476
FT /note="HAT 3"
FT REPEAT 554..586
FT /note="HAT 4"
FT REPEAT 588..620
FT /note="HAT 5"
FT REPEAT 622..654
FT /note="HAT 6"
FT REPEAT 689..721
FT /note="HAT 7"
FT REPEAT 723..755
FT /note="HAT 8"
FT REPEAT 855..887
FT /note="HAT 9"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 637..676
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041857"
FT VARIANT 477
FT /note="N -> S (very rare variant found in a family with
FT neuronal ceroid lipofuscinosis carrying a causative
FT mutation in DNAJC5; uncertain role as a disease phenotype
FT modifier; dbSNP:rs1433048453)"
FT /evidence="ECO:0000269|PubMed:22235333"
FT /id="VAR_069766"
FT VARIANT 729
FT /note="R -> W (in RP60; impaired function in pre-mRNA
FT splicing; mislocalized in Cajal bodies; partial loss of
FT localization in splicing speckles; dbSNP:rs387907100)"
FT /evidence="ECO:0000269|PubMed:21549338"
FT /id="VAR_065768"
FT CONFLICT 20
FT /note="G -> W (in Ref. 3; AAD01798)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="P -> R (in Ref. 3; AAD01798)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="H -> R (in Ref. 4; BAG50938)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="I -> T (in Ref. 4; BAG36962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 941 AA; 106925 MW; 91C2F1ADCA439BE9 CRC64;
MNKKKKPFLG MPAPLGYVPG LGRGATGFTT RSDIGPARDA NDPVDDRHAP PGKRTVGDQM
KKNQAADDDD EDLNDTNYDE FNGYAGSLFS SGPYEKDDEE ADAIYAALDK RMDERRKERR
EQREKEEIEK YRMERPKIQQ QFSDLKRKLA EVTEEEWLSI PEVGDARNKR QRNPRYEKLT
PVPDSFFAKH LQTGENHTSV DPRQTQFGGL NTPYPGGLNT PYPGGMTPGL MTPGTGELDM
RKIGQARNTL MDMRLSQVSD SVSGQTVVDP KGYLTDLNSM IPTHGGDIND IKKARLLLKS
VRETNPHHPP AWIASARLEE VTGKLQVARN LIMKGTEMCP KSEDVWLEAA RLQPGDTAKA
VVAQAVRHLP QSVRIYIRAA ELETDIRAKK RVLRKALEHV PNSVRLWKAA VELEEPEDAR
IMLSRAVECC PTSVELWLAL ARLETYENAR KVLNKARENI PTDRHIWITA AKLEEANGNT
QMVEKIIDRA ITSLRANGVE INREQWIQDA EECDRAGSVA TCQAVMRAVI GIGIEEEDRK
HTWMEDADSC VAHNALECAR AIYAYALQVF PSKKSVWLRA AYFEKNHGTR ESLEALLQRA
VAHCPKAEVL WLMGAKSKWL AGDVPAARSI LALAFQANPN SEEIWLAAVK LESENDEYER
ARRLLAKARS SAPTARVFMK SVKLEWVQDN IRAAQDLCEE ALRHYEDFPK LWMMKGQIEE
QKEMMEKARE AYNQGLKKCP HSTPLWLLLS RLEEKIGQLT RARAILEKSR LKNPKNPGLW
LESVRLEYRA GLKNIANTLM AKALQECPNS GILWSEAIFL EARPQRRTKS VDALKKCEHD
PHVLLAVAKL FWSQRKITKA REWFHRTVKI DSDLGDAWAF FYKFELQHGT EEQQEEVRKR
CESAEPRHGE LWCAVSKDIA NWQKKIGDIL RLVAGRIKNT F
