Details for: PRPF8
Associated with
Other Information
Genular Protein ID: 1912533602
Symbol: PRP8_HUMAN
Name: Pre-mRNA-processing-splicing factor 8
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 10411133
Title: The human Prp8 protein is a component of both U2- and U12-dependent spliceosomes.
PubMed ID: 10411133
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 2532307
Title: Conservation between yeast and man of a protein associated with U5 small nuclear ribonucleoprotein.
PubMed ID: 2532307
DOI: 10.1038/342819a0
PubMed ID: 2527369
Title: 20S small nuclear ribonucleoprotein U5 shows a surprisingly complex protein composition.
PubMed ID: 2527369
PubMed ID: 2479028
Title: The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.
PubMed ID: 2479028
PubMed ID: 2139226
Title: A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a potential homologue of the yeast PRP8 protein.
PubMed ID: 2139226
PubMed ID: 8702566
Title: Domain analysis of human U5 RNA. Cap trimethylation, protein binding, and spliceosome assembly.
PubMed ID: 8702566
PubMed ID: 8608445
Title: The canonical GU dinucleotide at the 5' splice site is recognized by p220 of the U5 snRNP within the spliceosome.
PubMed ID: 8608445
PubMed ID: 9303319
Title: Evidence that U5 snRNP recognizes the 3' splice site for catalytic step II in mammals.
PubMed ID: 9303319
PubMed ID: 9774689
Title: 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.
PubMed ID: 9774689
PubMed ID: 10024169
Title: The C-terminal region of hPrp8 interacts with the conserved GU dinucleotide at the 5' splice site.
PubMed ID: 10024169
PubMed ID: 10809668
Title: Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions.
PubMed ID: 10809668
PubMed ID: 11006293
Title: 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.
PubMed ID: 11006293
PubMed ID: 10983979
Title: Functional recognition of 5' splice site by U4/U6.U5 tri-snRNP defines a novel ATP-dependent step in early spliceosome assembly.
PubMed ID: 10983979
PubMed ID: 11971955
Title: Human U4/U6.U5 and U4atac/U6atac.U5 tri-snRNPs exhibit similar protein compositions.
PubMed ID: 11971955
PubMed ID: 14654843
Title: Proteomic characterization of the human centrosome by protein correlation profiling.
PubMed ID: 14654843
DOI: 10.1038/nature02166
PubMed ID: 15840809
PubMed ID: 16723661
Title: The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP.
PubMed ID: 16723661
DOI: 10.1261/rna.55406
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20595234
Title: The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome.
PubMed ID: 20595234
DOI: 10.1101/gad.1925010
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 26527271
Title: Crystallization and biochemical characterization of the human spliceosomal Aar2-Prp8(RNaseH) complex.
PubMed ID: 26527271
PubMed ID: 28561026
Title: R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein.
PubMed ID: 28561026
DOI: 10.1038/ncomms15615
PubMed ID: 35167828
Title: C9ORF78 partially localizes to centromeres and plays a role in chromosome segregation.
PubMed ID: 35167828
PubMed ID: 18843295
Title: Structure and function of an RNase H domain at the heart of the spliceosome.
PubMed ID: 18843295
PubMed ID: 18836455
Title: Structural elucidation of a PRP8 core domain from the heart of the spliceosome.
PubMed ID: 18836455
DOI: 10.1038/nsmb.1505
PubMed ID: 26912367
Title: Molecular architecture of the human U4/U6.U5 tri-snRNP.
PubMed ID: 26912367
PubMed ID: 28502770
Title: An Atomic Structure of the Human Spliceosome.
PubMed ID: 28502770
PubMed ID: 28781166
Title: Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.
PubMed ID: 28781166
PubMed ID: 28076346
Title: Cryo-EM structure of a human spliceosome activated for step 2 of splicing.
PubMed ID: 28076346
DOI: 10.1038/nature21079
PubMed ID: 29361316
Title: Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex.
PubMed ID: 29361316
PubMed ID: 30315277
Title: Structures of the human pre-catalytic spliceosome and its precursor spliceosome.
PubMed ID: 30315277
PubMed ID: 29360106
Title: Structure of the human activated spliceosome in three conformational states.
PubMed ID: 29360106
DOI: 10.1038/cr.2018.14
PubMed ID: 29301961
Title: Structure of a human catalytic step I spliceosome.
PubMed ID: 29301961
PubMed ID: 30728453
Title: Structures of the human spliceosomes before and after release of the ligated exon.
PubMed ID: 30728453
PubMed ID: 30705154
Title: A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation.
PubMed ID: 30705154
PubMed ID: 35241646
Title: A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing.
PubMed ID: 35241646
PubMed ID: 35188580
Title: The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling.
PubMed ID: 35188580
DOI: 10.1093/nar/gkac087
PubMed ID: 33509932
Title: Structure of the activated human minor spliceosome.
PubMed ID: 33509932
PubMed ID: 11468273
Title: Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal dominant retinitis pigmentosa (RP13).
PubMed ID: 11468273
PubMed ID: 11910553
Title: Clinical characterization, linkage analysis, and PRPC8 mutation analysis of a family with autosomal dominant retinitis pigmentosa type 13 (RP13).
PubMed ID: 11910553
PubMed ID: 12714658
Title: Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31 in Spanish families with autosomal dominant retinitis pigmentosa.
PubMed ID: 12714658
DOI: 10.1167/iovs.02-0871
PubMed ID: 17317632
Title: Structure of a multipartite protein-protein interaction domain in splicing factor Prp8 and its link to retinitis pigmentosa.
PubMed ID: 17317632
Sequence Information:
- Length: 2335
- Mass: 273600
- Checksum: E823A15C60EA61C9
- Sequence:
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
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.