ID PRP24_YEAST Reviewed; 444 AA. AC P49960; D6W094; E9P966; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=U4/U6 snRNA-associated-splicing factor PRP24; DE Short=U4/U6 snRNP protein; GN Name=PRP24; OrderedLocusNames=YMR268C; ORFNames=YM8156.10C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-288. RX PubMed=1827420; DOI=10.1101/gad.5.5.773; RA Shannon K.W., Guthrie C.; RT "Suppressors of a U4 snRNA mutation define a novel U6 snRNP protein with RT RNA-binding motifs."; RL Genes Dev. 5:773-785(1991). RN [5] RP CHARACTERIZATION. RX PubMed=7882985; DOI=10.1002/j.1460-2075.1995.tb07060.x; RA Jandrositz A., Guthrie C.; RT "Evidence for a Prp24 binding site in U6 snRNA and in a putative RT intermediate in the annealing of U6 and U4 snRNAs."; RL EMBO J. 14:820-832(1995). RN [6] RP CHARACTERIZATION. RX PubMed=7585243; RA Ghetti A., Company M., Abelson J.; RT "Specificity of Prp24 binding to RNA: a role for Prp24 in the dynamic RT interaction of U4 and U6 snRNAs."; RL RNA 1:132-145(1995). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Binds preferentially to the U4/U6 hybrid snRNAs. Can CC stimulate the annealing of U4 and U6. Could participate in both the CC formation and disassembly of the U4/U6 hybrid during splicing. CC -!- INTERACTION: CC P49960; P47093: LSM8; NbExp=3; IntAct=EBI-212, EBI-313; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z49260; CAA89251.1; -; Genomic_DNA. DR EMBL; AY723858; AAU09775.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10168.1; -; Genomic_DNA. DR PIR; S54480; S54480. DR RefSeq; NP_013995.1; NM_001182775.1. DR PDB; 2GHP; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-291. DR PDB; 2GO9; NMR; -; A=38-197. DR PDB; 2KH9; NMR; -; A=115-197. DR PDB; 2L9W; NMR; -; A=292-400. DR PDB; 4N0T; X-ray; 1.70 A; A=34-400. DR PDB; 5TF6; X-ray; 2.30 A; A/C=34-400. DR PDB; 5VSU; X-ray; 3.10 A; A=1-444. DR PDB; 6ASO; X-ray; 2.71 A; A=28-444. DR PDBsum; 2GHP; -. DR PDBsum; 2GO9; -. DR PDBsum; 2KH9; -. DR PDBsum; 2L9W; -. DR PDBsum; 4N0T; -. DR PDBsum; 5TF6; -. DR PDBsum; 5VSU; -. DR PDBsum; 6ASO; -. DR AlphaFoldDB; P49960; -. DR BMRB; P49960; -. DR SMR; P49960; -. DR BioGRID; 35446; 574. DR ComplexPortal; CPX-24; U6 small nuclear ribonucleoprotein complex. DR DIP; DIP-2570N; -. DR IntAct; P49960; 9. DR MINT; P49960; -. DR STRING; 4932.YMR268C; -. DR iPTMnet; P49960; -. DR MaxQB; P49960; -. DR PaxDb; 4932-YMR268C; -. DR PeptideAtlas; P49960; -. DR EnsemblFungi; YMR268C_mRNA; YMR268C; YMR268C. DR GeneID; 855310; -. DR KEGG; sce:YMR268C; -. DR AGR; SGD:S000004881; -. DR SGD; S000004881; PRP24. DR VEuPathDB; FungiDB:YMR268C; -. DR eggNOG; KOG0128; Eukaryota. DR HOGENOM; CLU_621223_0_0_1; -. DR InParanoid; P49960; -. DR OMA; LPSLRYN; -. DR OrthoDB; 3035286at2759; -. DR BioCyc; YEAST:G3O-32941-MONOMER; -. DR BioGRID-ORCS; 855310; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P49960; -. DR PRO; PR:P49960; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P49960; Protein. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central. DR GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal. DR GO; GO:0005688; C:U6 snRNP; IDA:SGD. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0017069; F:snRNA binding; IPI:SGD. DR GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal. DR GO; GO:0000245; P:spliceosomal complex assembly; IMP:SGD. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:SGD. DR CDD; cd12296; RRM1_Prp24; 1. DR CDD; cd12297; RRM2_Prp24; 1. DR CDD; cd12298; RRM3_Prp24; 1. DR CDD; cd12299; RRM4_Prp24; 1. DR Gene3D; 3.30.70.330; -; 4. DR InterPro; IPR008669; LSM_interact. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR034397; Prp24_RRM1. DR InterPro; IPR034398; Prp24_RRM2. DR InterPro; IPR034540; Prp24_RRM3. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR031766; RRM_occluded. DR PANTHER; PTHR23003; RNA RECOGNITION MOTIF RRM DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF05391; Lsm_interact; 1. DR Pfam; PF00076; RRM_1; 3. DR Pfam; PF16842; RRM_occluded; 1. DR SMART; SM00360; RRM; 4. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 3. PE 1: Evidence at protein level; KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding. FT CHAIN 1..444 FT /note="U4/U6 snRNA-associated-splicing factor PRP24" FT /id="PRO_0000081736" FT DOMAIN 41..116 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 117..195 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 210..289 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT CONFLICT 197 FT /note="E -> G (in Ref. 3; AAU09775)" FT /evidence="ECO:0000305" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:2GO9" FT HELIX 54..61 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 67..74 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 78..89 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 90..97 FT /evidence="ECO:0007829|PDB:4N0T" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 130..139 FT /evidence="ECO:0007829|PDB:4N0T" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:2KH9" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:2GHP" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 168..178 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 204..207 FT /evidence="ECO:0007829|PDB:4N0T" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:2GHP" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 224..231 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:4N0T" FT TURN 244..250 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 252..262 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 263..269 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:5TF6" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 290..302 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 307..310 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 313..318 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 325..334 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 343..349 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 354..361 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 362..372 FT /evidence="ECO:0007829|PDB:4N0T" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:5VSU" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 387..397 FT /evidence="ECO:0007829|PDB:4N0T" FT HELIX 434..444 FT /evidence="ECO:0007829|PDB:5VSU" SQ SEQUENCE 444 AA; 50849 MW; 6BCCE7A9AAC51CE0 CRC64; MEYGHHARPD SKRPLDEGSP AAAGLTSKKA NEALTRNREL TTVLVKNLPK SYNQNKVYKY FKHCGPIIHV DVADSLKKNF RFARIEFARY DGALAAITKT HKVVGQNEII VSHLTECTLW MTNFPPSYTQ RNIRDLLQDI NVVALSIRLP SLRFNTSRRF AYIDVTSKED ARYCVEKLNG LKIEGYTLVT KVSNPLEKSK RTDSATLEGR EIMIRNLSTE LLDENLLRES FEGFGSIEKI NIPAGQKEHS FNNCCAFMVF ENKDSAERAL QMNRSLLGNR EISVSLADKK PFLERNEVKR LLASRNSKEL ETLICLFPLS DKVSPSLICQ FLQEEIHINE KDIRKILLVS DFNGAIIIFR DSKFAAKMLM ILNGSQFQGK VIRSGTINDM KRYYNNQQNH SMKHVKPSCI NMMEKGPNLQ VKKKIPDKQE QMSNDDFRKM FLGE //