ID SN309_YEAST Reviewed; 175 AA. AC Q06091; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUL-2007, entry version 49. DE Pre-mRNA-splicing factor SNT309 (Synergistic to PRP19 mutation protein DE 309) (PRP19-associated complex protein 25). GN Name=SNT309; Synonyms=NTC25; OrderedLocusNames=YPR101W; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=97313271; PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [2] 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., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [3] RP FUNCTION, AND IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX. RX PubMed=9528791; RA Chen H.-R., Jan S.-P., Tsao T.Y., Sheu Y.-J., Banroques J., RA Cheng S.-C.; RT "Snt309p, a component of the Prp19p-associated complex that interacts RT with Prp19p and associates with the spliceosome simultaneously with or RT immediately after dissociation of U4 in the same manner as Prp19p."; RL Mol. Cell. Biol. 18:2196-2204(1998). RN [4] RP FUNCTION. RX PubMed=10318896; DOI=10.1073/pnas.96.10.5406; RA Chen H.-R., Tsao T.Y., Chen C.-H., Tsai W.-Y., Her L.-S., Hsu M.M.-T., RA Cheng S.-C.; RT "Snt309p modulates interactions of Prp19p with its associated RT components to stabilize the Prp19p-associated complex essential for RT pre-mRNA splicing."; RL Proc. Natl. Acad. Sci. U.S.A. 96:5406-5411(1999). RN [5] RP INTERACTION WITH PRP19. RX PubMed=11018040; DOI=10.1074/jbc.M006958200; RA Chen C.-H., Tsai W.-Y., Chen H.-R., Wang C.-H., Cheng S.-C.; RT "Identification and characterization of two novel components of the RT Prp19p-associated complex, Ntc30p and Ntc20p."; RL J. Biol. Chem. 276:488-494(2001). RN [6] RP MASS SPECTROMETRY, AND IDENTIFICATION IN THE CWC COMPLEX. RX MEDLINE=21881936; PubMed=11884590; RX 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 [7] RP INTERACTION WITH PRP19. RX PubMed=12088152; DOI=10.1017/S1355838202025050; RA Ohi M.D., Gould K.L.; RT "Characterization of interactions among the Cef1p-Prp19p-associated RT splicing complex."; RL RNA 8:798-815(2002). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [9] 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). CC -!- FUNCTION: Involved in pre-mRNA splicing by stabilizing the NTC (or CC PRP19-associated complex). As a component of the NTC complex, CC associates to the spliceosome to mediate conformational CC rearrangement or to stabilize the structure of the spliceosome CC after U4 snRNA dissociation, which leads to spliceosome CC maturation. CC -!- SUBUNIT: Belongs to the NTC complex (or PRP19-associated complex), CC composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, CC and PRP19. The NTC complex associates with the spliceosome after CC the release of the U1 and U4 snRNAs and forms the CWC spliceosome CC subcomplex reminiscent of a late-stage spliceosome composed also CC of the U2, U5 and U6 snRNAs and at least BUD13, 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 PRP19. CC -!- INTERACTION: CC Q12309:CLF1; NbExp=1; IntAct=EBI-818, EBI-484; CC P38302:NTC20; NbExp=1; IntAct=EBI-818, EBI-20921; CC P32523:PRP19; NbExp=1; IntAct=EBI-818, EBI-493; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 721 molecules/cell. 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; U32445; AAB68071.1; -; Genomic_DNA. DR EMBL; AY693233; AAT93252.1; -; Genomic_DNA. DR PIR; S59766; S59766. DR DIP; DIP:2864N; -. DR IntAct; Q06091; -. DR Ensembl; YPR101W; Saccharomyces cerevisiae. DR GenomeReviews; U00094_GR; YPR101W. DR KEGG; sce:YPR101W; -. DR CYGD; YPR101w; -. DR SGD; S000006305; SNT309. DR LinkHub; Q06091; -. DR GermOnline; YPR101W; Saccharomyces cerevisiae. DR GO; GO:0005681; C:spliceosome; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IMP:SGD. PE 1: Evidence at protein level; KW Complete proteome; mRNA processing; mRNA splicing; Nucleus; KW Spliceosome. FT CHAIN 1 175 Pre-mRNA-splicing factor SNT309. FT /FTId=PRO_0000071999. SQ SEQUENCE 175 AA; 20709 MW; B781CA65BC9A1918 CRC64; MDGLSFVDKG KIPDGYKNEI DQLVKKEFAN IKREPVHPEI RGILAKRKGA DNSVSTLTNA LYTEYLKQRN NKKRRTPDFN DDDDTLFLEE YRRKYPRIDT SRYIPNESSE VSLLGIVDSY LKHQEIVLDT LLPQTVSNQW RINNDYIRQT CTIVEEMNIQ QRKQINDLEI YRKRL //