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 26-NOV-2014, entry version 136. DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000305}; DE EC=6.3.2.- {ECO:0000269|PubMed:12627222}; 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 204508 / S288c; 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; 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). 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 IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. 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 IDENTIFICATION BY 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP IDENTIFICATION BY 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 RT insights into evolution."; RL Science 325:1682-1686(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP STRUCTURE BY NMR OF 1-56, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. 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: Probable ubiquitin-protein ligase involved in pre-mRNA CC splicing. Acts as a central component of the NTC complex (or CC PRP19-associated complex) that associates to the spliceosome to CC mediate conformational rearrangement or to stabilize the structure CC of the spliceosome after U4 snRNA dissociation, which leads to CC spliceosome maturation. It is also probably involved in DNA CC repair. {ECO:0000269|PubMed:12627222}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:12627222}. CC -!- SUBUNIT: Homotetramer. Component of the NTC complex (or PRP19- CC associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, CC SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the CC spliceosome after the release of the U1 and U4 snRNAs and forms CC 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. {ECO:0000269|PubMed:11884590, CC ECO:0000269|PubMed:15601865, ECO:0000269|PubMed:8194532}. CC -!- INTERACTION: CC P40968:CDC40; NbExp=7; IntAct=EBI-493, EBI-13834; CC Q03654:CEF1; NbExp=8; IntAct=EBI-493, EBI-476; CC Q12309:CLF1; NbExp=9; 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=7; 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 {ECO:0000305}. CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. 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. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 U-box domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 3 WD repeats. {ECO:0000305}. 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 BioGrid; 31217; 162. DR DIP; DIP-1112N; -. DR IntAct; P32523; 56. DR MINT; MINT-632220; -. DR MaxQB; P32523; -. 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 HOGENOM; HOG000115709; -. DR InParanoid; P32523; -. DR KO; K10599; -. DR OMA; HTANDEN; -. DR OrthoDB; EOG7V76GC; -. DR BioCyc; YEAST:G3O-32139-MONOMER; -. DR Reactome; REACT_191574; Processing of Intronless Pre-mRNAs. DR UniPathway; UPA00143; -. DR EvolutionaryTrace; P32523; -. DR NextBio; 966526; -. DR Genevestigator; P32523; -. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005634; C:nucleus; 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:0004842; F:ubiquitin-protein transferase activity; IDA: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; IPR011047; Quinonprotein_ADH-like_supfam. DR InterPro; IPR003613; Ubox_domain. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF08606; Prp19; 1. DR SMART; SM00504; Ubox; 1. DR SUPFAM; SSF50998; SSF50998; 1. DR PROSITE; PS51698; U_BOX; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; Ligase; KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat; KW Spliceosome; Ubl conjugation pathway; WD repeat. FT CHAIN 1 503 Pre-mRNA-processing factor 19. FT /FTId=PRO_0000058587. FT DOMAIN 1 71 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 CONFLICT 239 239 Missing (in Ref. 1; AAA34912). FT {ECO:0000305}. FT TURN 4 6 {ECO:0000244|PDB:2BAY}. FT STRAND 11 16 {ECO:0000244|PDB:2BAY}. FT TURN 17 20 {ECO:0000244|PDB:2BAY}. FT STRAND 21 24 {ECO:0000244|PDB:2BAY}. FT HELIX 25 35 {ECO:0000244|PDB:2BAY}. FT TURN 39 41 {ECO:0000244|PDB:2BAY}. FT HELIX 47 49 {ECO:0000244|PDB:2BAY}. FT STRAND 179 187 {ECO:0000244|PDB:3LRV}. FT STRAND 192 194 {ECO:0000244|PDB:3LRV}. FT STRAND 197 200 {ECO:0000244|PDB:3LRV}. FT STRAND 202 216 {ECO:0000244|PDB:3LRV}. FT STRAND 219 229 {ECO:0000244|PDB:3LRV}. FT STRAND 231 237 {ECO:0000244|PDB:3LRV}. FT STRAND 247 251 {ECO:0000244|PDB:3LRV}. FT STRAND 256 261 {ECO:0000244|PDB:3LRV}. FT TURN 262 264 {ECO:0000244|PDB:3LRV}. FT STRAND 265 270 {ECO:0000244|PDB:3LRV}. FT TURN 271 273 {ECO:0000244|PDB:3LRV}. FT STRAND 276 281 {ECO:0000244|PDB:3LRV}. FT STRAND 288 292 {ECO:0000244|PDB:3LRV}. FT STRAND 301 306 {ECO:0000244|PDB:3LRV}. FT STRAND 311 319 {ECO:0000244|PDB:3LRV}. FT STRAND 321 325 {ECO:0000244|PDB:3LRV}. FT STRAND 335 338 {ECO:0000244|PDB:3LRV}. FT STRAND 344 348 {ECO:0000244|PDB:3LRV}. FT STRAND 354 360 {ECO:0000244|PDB:3LRV}. FT STRAND 377 382 {ECO:0000244|PDB:3LRV}. FT STRAND 386 401 {ECO:0000244|PDB:3LRV}. FT STRAND 409 411 {ECO:0000244|PDB:3LRV}. FT STRAND 424 428 {ECO:0000244|PDB:3LRV}. FT STRAND 432 439 {ECO:0000244|PDB:3LRV}. FT TURN 440 443 {ECO:0000244|PDB:3LRV}. FT STRAND 444 450 {ECO:0000244|PDB:3LRV}. FT TURN 452 454 {ECO:0000244|PDB:3LRV}. FT STRAND 456 464 {ECO:0000244|PDB:3LRV}. FT STRAND 476 482 {ECO:0000244|PDB:3LRV}. FT STRAND 485 491 {ECO:0000244|PDB:3LRV}. FT STRAND 493 502 {ECO:0000244|PDB:3LRV}. 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 //