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 27-MAR-2024, entry version 218. 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 O94906; Q69YN4: VIRMA; NbExp=2; IntAct=EBI-536755, EBI-2819293; 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-3766; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR SMR; O94906; -. DR BioGRID; 117298; 346. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR CORUM; O94906; -. DR DIP; DIP-29006N; -. DR IntAct; O94906; 93. DR MINT; O94906; -. DR STRING; 9606.ENSP00000266079; -. DR MoonDB; O94906; Predicted. DR GlyCosmos; O94906; 1 site, 1 glycan. DR GlyGen; O94906; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000266079; -. DR PeptideAtlas; O94906; -. DR ProteomicsDB; 50541; -. [O94906-1] DR ProteomicsDB; 50542; -. [O94906-2] DR Pumba; O94906; -. DR Antibodypedia; 15475; 238 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 AGR; HGNC:15860; -. 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; 655233at2759; -. 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 SIGNOR; O94906; -. DR BioGRID-ORCS; 24148; 770 hits in 1112 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 205 other cell types or tissues. 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:HPA. 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:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IDA: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; Tetratricopeptide repeat domain; 4. DR InterPro; IPR003107; HAT. DR InterPro; IPR010491; PRP1_N. DR InterPro; IPR045075; Syf1-like. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR11246; PRE-MRNA SPLICING FACTOR; 1. DR PANTHER; PTHR11246:SF1; PRE-MRNA-PROCESSING FACTOR 6; 1. DR Pfam; PF06424; PRP1_N; 1. DR Pfam; PF13432; TPR_16; 1. DR Pfam; PF14559; TPR_19; 1. DR SMART; SM00386; HAT; 13. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; TPR-like; 4. DR Genevisible; O94906; HS. 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 (found in a family with neuronal ceroid FT lipofuscinosis carrying a causative mutation in DNAJC5; FT uncertain significance; might act as modifier of disease FT phenotype; 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 //