PRP24_YEAST
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 03-AUG-2022, entry version 167.
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}.
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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; 572.
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; P49960; -.
DR PRIDE; P49960; -.
DR EnsemblFungi; YMR268C_mRNA; YMR268C; YMR268C.
DR GeneID; 855310; -.
DR KEGG; sce:YMR268C; -.
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 BioCyc; YEAST:G3O-32941-MON; -.
DR EvolutionaryTrace; P49960; -.
DR PRO; PR:P49960; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P49960; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005688; C:U6 snRNP; IDA:SGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
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; IC: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; 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; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR031766; RRM_occluded.
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; SSF54928; 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
