ID PRP19_YEAST Reviewed; 503 AA. AC P32523; Q07870; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 02-OCT-2007, entry version 64. DE Pre-mRNA-splicing factor 19. GN Name=PRP19; Synonyms=PSO4; OrderedLocusNames=YLL036C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93180836; PubMed=8441419; RA Cheng S.C., Tarn W.Y., Tsao T.Y., Abelson J.; RT "PRP19: a novel spliceosomal component."; RL Mol. Cell. Biol. 13:1876-1882(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97078680; PubMed=8918805; DOI=10.1093/nar/24.20.4009; RA Grey M., Duesterhoeft A., Henriques J.A.P., Brendel M.; RT "Allelism of PSO4 and PRP19 links pre-mRNA processing with RT recombination and error-prone DNA repair in Saccharomyces RT cerevisiae."; RL Nucleic Acids Res. 24:4009-4014(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313267; PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [4] RP CHARACTERIZATION. RX MEDLINE=93180837; PubMed=7680101; RA Tarn W.Y., Lee K.R., Cheng S.C.; RT "The yeast PRP19 protein is not tightly associated with small nuclear RT RNAs, but appears to associate with the spliceosome after binding of RT U2 to the pre-mRNA and prior to formation of the functional RT spliceosome."; RL Mol. Cell. Biol. 13:1883-1891(1993). RN [5] RP SELF-ASSOCIATION, AND IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX. RX PubMed=8194532; RA Tarn W.Y., Hsu C.H., Huang K.T., Chen H.R., Kao H.Y., Lee K.R., RA Cheng S.C.; RT "Functional association of essential splicing factor(s) with PRP19 in RT a protein complex."; RL EMBO J. 13:2421-2431(1994). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP TETRAMERIZATION, ELECTRON MICROSCOPY OF THE TETRAMER, AND INTERACTION RP WITH CEF1. RX PubMed=15601865; DOI=10.1128/MCB.25.1.451-460.2005; RA Ohi M.D., Vander Kooi C.W., Rosenberg J.A., Ren L., Hirsch J.P., RA Chazin W.J., Walz T., Gould K.L.; RT "Structural and functional analysis of essential pre-mRNA splicing RT factor Prp19p."; RL Mol. Cell. Biol. 25:451-460(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [9] RP STRUCTURE BY NMR OF 1-56. RX PubMed=12627222; DOI=10.1038/nsb906; RA Ohi M.D., Vander Kooi C.W., Rosenberg J.A., Chazin W.J., Gould K.L.; RT "Structural insights into the U-box, a domain associated with multi- RT ubiquitination."; RL Nat. Struct. Biol. 10:250-255(2003). CC -!- FUNCTION: Involved in pre-mRNA splicing. Acts a central component CC of the NTC complex (or PRP19-associated complex) that associates CC to the spliceosome to mediate conformational rearrangement or to CC stabilize the structure of the spliceosome after U4 snRNA CC dissociation, which leads to spliceosome maturation. Involved in CC DNA repair. CC -!- SUBUNIT: Forms homotetramers. Belongs to the NTC complex (or CC PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, CC NTC20, SNT309, SYF1, SYF2, and PRP19. CC -!- INTERACTION: CC Q03654:CEF1; NbExp=1; IntAct=EBI-493, EBI-476; CC Q12309:CLF1; NbExp=1; IntAct=EBI-493, EBI-484; CC P21374:ISY1; NbExp=1; IntAct=EBI-493, EBI-9382; CC P38302:NTC20; NbExp=1; IntAct=EBI-493, EBI-20921; CC Q06091:SNT309; NbExp=1; IntAct=EBI-493, EBI-818; CC Q04048:SYF1; NbExp=1; IntAct=EBI-493, EBI-540; CC P53277:SYF2; NbExp=1; IntAct=EBI-493, EBI-23308; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD CC medium. CC -!- MISCELLANEOUS: The tetramer is an elongated particle consisting of CC four globular WD40 domains held together by a central stalk. CC -!- SIMILARITY: Contains 1 U-box domain. CC -!- SIMILARITY: Contains 3 WD repeats. 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; L09721; AAA34912.1; -; Genomic_DNA. DR EMBL; X99770; CAA68103.1; -; Genomic_DNA. DR EMBL; Z73142; CAA97487.1; -; Genomic_DNA. DR PIR; S64787; S64787. DR RefSeq; NP_013064.1; -. DR PDB; 1N87; NMR; A=1-56. DR PDB; 2BAY; X-ray; A/B/C/D/E/F=1-58. DR DIP; DIP:1112N; -. DR IntAct; P32523; -. DR PeptideAtlas; P32523; -. DR Ensembl; YLL036C; Saccharomyces cerevisiae. DR GeneID; 850623; -. DR GenomeReviews; Y13138_GR; YLL036C. DR KEGG; sce:YLL036C; -. DR CYGD; YLL036c; -. DR SGD; S000003959; PRP19. DR LinkHub; P32523; -. DR GermOnline; YLL036C; Saccharomyces cerevisiae. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0005681; C:spliceosome; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0031202; F:RNA splicing factor activity, transesterifi...; IMP:SGD. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IDA:SGD. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IPI:SGD. DR InterPro; IPR013915; Pre-mRNA_splic_Prp19. DR InterPro; IPR003613; Ubox. DR InterPro; IPR001680; WD40. DR Pfam; PF08606; Prp19; 1. DR SMART; SM00504; Ubox; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; KW mRNA processing; mRNA splicing; Nucleus; Phosphorylation; Repeat; KW Spliceosome; Ubl conjugation pathway; WD repeat. FT CHAIN 1 503 Pre-mRNA-splicing factor 19. FT /FTId=PRO_0000058587. FT DOMAIN 1 64 U-box. FT REPEAT 328 367 WD 1. FT REPEAT 372 410 WD 2. FT REPEAT 418 458 WD 3. FT REGION 57 144 Required for self-association. FT REGION 76 134 Interaction with CEF1. FT MOD_RES 141 141 Phosphoserine; by ATM or ATR. FT CONFLICT 239 239 Missing (in Ref. 1). FT TURN 4 6 FT STRAND 11 16 FT TURN 17 20 FT STRAND 21 24 FT HELIX 25 35 FT TURN 39 41 FT HELIX 47 49 SQ SEQUENCE 503 AA; 56570 MW; A44D8C7DD6F64185 CRC64; MLCAISGKVP RRPVLSPKSR TIFEKSLLEQ YVKDTGNDPI TNEPLSIEEI VEIVPSAQQA SLTESTNSAT LKANYSIPNL LTSLQNEWDA IMLENFKLRS TLDSLTKKLS TVMYERDAAK LVAAQLLMEK NEDSKDLPKS SQQAVAITRE EFLQGLLQSS RDFVARGKLK APKWPILKNL ELLQAQNYSR NIKTFPYKEL NKSMYYDKWV CMCRCEDGAL HFTQLKDSKT ITTITTPNPR TGGEHPAIIS RGPCNRLLLL YPGNQITILD SKTNKVLREI EVDSANEIIY MYGHNEVNTE YFIWADNRGT IGFQSYEDDS QYIVHSAKSD VEYSSGVLHK DSLLLALYSP DGILDVYNLS SPDQASSRFP VDEEAKIKEV KFADNGYWMV VECDQTVVCF DLRKDVGTLA YPTYTIPEFK TGTVTYDIDD SGKNMIAYSN ESNSLTIYKF DKKTKNWTKD EESALCLQSD TADFTDMDVV CGDGGIAAIL KTNDSFNIVA LTP //