ID PRP19_YEAST Reviewed; 503 AA. AC P32523; D6VXW9; Q07870; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 01-MAY-2013, entry version 121. DE RecName: Full=Pre-mRNA-splicing factor 19; GN Name=PRP19; Synonyms=PSO4; OrderedLocusNames=YLL036C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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 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 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 GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP CHARACTERIZATION. RX 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 [6] 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 [7] RP MASS SPECTROMETRY, AND IDENTIFICATION IN THE CWC COMPLEX. RX PubMed=11884590; DOI=10.1128/MCB.22.7.2011-2024.2002; RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.; RT "Proteomics analysis reveals stable multiprotein complexes in both RT fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel RT pre-mRNA splicing factors, and snRNAs."; RL Mol. Cell. Biol. 22:2011-2024(2002). RN [8] 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., 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 [9] 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 [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-141, AND RP MASS SPECTROMETRY. 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [12] 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. The NTC complex associates CC with the spliceosome after the release of the U1 and U4 snRNAs and CC forms the CWC spliceosome subcomplex (or CEF1-associated complex) CC reminiscent of a late-stage spliceosome composed also of the U2, CC U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CC CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, CC HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, CC PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, CC RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20, PRP19, PRP46, CC SYF1 and SYF2. CC -!- INTERACTION: CC P40968:CDC40; NbExp=7; IntAct=EBI-493, EBI-13834; CC Q03654:CEF1; NbExp=9; IntAct=EBI-493, EBI-476; CC Q12309:CLF1; NbExp=10; IntAct=EBI-493, EBI-484; CC Q12046:CWC2; NbExp=9; IntAct=EBI-493, EBI-553; CC P21374:ISY1; NbExp=6; IntAct=EBI-493, EBI-9382; CC P38302:NTC20; NbExp=5; IntAct=EBI-493, EBI-20921; CC Q06091:SNT309; NbExp=8; IntAct=EBI-493, EBI-818; CC Q04048:SYF1; NbExp=6; IntAct=EBI-493, EBI-540; CC P53277:SYF2; NbExp=4; IntAct=EBI-493, EBI-23308; CC Q06525:URN1; NbExp=7; IntAct=EBI-493, EBI-35138; CC Q12208:USB1; NbExp=3; IntAct=EBI-493, EBI-31589; 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: Belongs to the WD repeat PRP19 family. 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 EMBL; BK006945; DAA09285.1; -; Genomic_DNA. DR PIR; S64787; S64787. DR RefSeq; NP_013064.1; NM_001181856.1. DR PDB; 1N87; NMR; -; A=1-56. DR PDB; 2BAY; X-ray; 1.50 A; A/B/C/D/E/F=1-58. DR PDB; 3LRV; X-ray; 2.60 A; A=165-503. DR PDBsum; 1N87; -. DR PDBsum; 2BAY; -. DR PDBsum; 3LRV; -. DR ProteinModelPortal; P32523; -. DR SMR; P32523; 1-57, 171-503. DR DIP; DIP-1112N; -. DR IntAct; P32523; 56. DR MINT; MINT-632220; -. DR PaxDb; P32523; -. DR PeptideAtlas; P32523; -. DR EnsemblFungi; YLL036C; YLL036C; YLL036C. DR GeneID; 850623; -. DR KEGG; sce:YLL036C; -. DR CYGD; YLL036c; -. DR SGD; S000003959; PRP19. DR eggNOG; NOG319177; -. DR GeneTree; ENSGT00700000104487; -. DR HOGENOM; HOG000115709; -. DR KO; K10599; -. DR OMA; YLYSHEN; -. DR OrthoDB; EOG4M0JB3; -. DR ChEMBL; CHEMBL5058; -. DR EvolutionaryTrace; P32523; -. DR NextBio; 966526; -. DR ArrayExpress; P32523; -. DR Genevestigator; P32523; -. DR GermOnline; YLL036C; Saccharomyces cerevisiae. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0000974; C:Prp19 complex; IDA:SGD. DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IMP:SGD. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IMP:SGD. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR013915; Pre-mRNA_splic_Prp19. DR InterPro; IPR003613; Ubox_domain. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR017986; WD40_repeat_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF08606; Prp19; 1. DR SMART; SM00504; Ubox; 1. DR SUPFAM; SSF50978; WD40_like; 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; Phosphoprotein; KW Reference proteome; Repeat; Spliceosome; 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 140 140 Phosphoserine. FT MOD_RES 141 141 Phosphoserine; by ATM or ATR. FT CONFLICT 239 239 Missing (in Ref. 1; AAA34912). 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 FT STRAND 179 187 FT STRAND 192 194 FT STRAND 197 200 FT STRAND 202 216 FT STRAND 219 229 FT STRAND 231 237 FT STRAND 247 251 FT STRAND 256 261 FT TURN 262 264 FT STRAND 265 270 FT TURN 271 273 FT STRAND 276 281 FT STRAND 288 292 FT STRAND 301 306 FT STRAND 311 319 FT STRAND 321 325 FT STRAND 335 338 FT STRAND 344 348 FT STRAND 354 360 FT STRAND 377 382 FT STRAND 386 401 FT STRAND 409 411 FT STRAND 424 428 FT STRAND 432 439 FT TURN 440 443 FT STRAND 444 450 FT TURN 452 454 FT STRAND 456 464 FT STRAND 476 482 FT STRAND 485 491 FT STRAND 493 502 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 //