ID URN1_YEAST Reviewed; 465 AA.
AC Q06525; D6W4E8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Pre-mRNA-splicing factor URN1;
DE AltName: Full=U2-U5-U6 snRNP, RES complex and NTC-interacting pre-mRNA-splicing factor 1;
GN Name=URN1; OrderedLocusNames=YPR152C;
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=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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX 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 [5]
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 [6]
RP DOMAIN.
RX PubMed=16606443; DOI=10.1186/gb-2006-7-4-r30;
RA Hesselberth J.R., Miller J.P., Golob A., Stajich J.E., Michaud G.A.,
RA Fields S.;
RT "Comparative analysis of Saccharomyces cerevisiae WW domains and their
RT interacting proteins.";
RL Genome Biol. 7:R30.1-R30.15(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, 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 [8]
RP FUNCTION.
RX PubMed=23560879; DOI=10.1111/febs.12277;
RA Dreumont N., Seraphin B.;
RT "Rapid screening of yeast mutants with reporters identifies new splicing
RT phenotypes.";
RL FEBS J. 280:2712-2726(2013).
RN [9]
RP IDENTIFICATION IN THE PRECATALYTIC SPLICEOSOMAL COMPLEX B, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19941820; DOI=10.1016/j.molcel.2009.09.040;
RA Fabrizio P., Dannenberg J., Dube P., Kastner B., Stark H., Urlaub H.,
RA Luhrmann R.;
RT "The evolutionarily conserved core design of the catalytic activation step
RT of the yeast spliceosome.";
RL Mol. Cell 36:593-608(2009).
RN [10]
RP INTERACTION WITH PRP19, AND FUNCTION.
RX PubMed=21386897; DOI=10.1371/journal.pone.0016719;
RA Ren L., McLean J.R., Hazbun T.R., Fields S., Vander Kooi C., Ohi M.D.,
RA Gould K.L.;
RT "Systematic two-hybrid and comparative proteomic analyses reveal novel
RT yeast pre-mRNA splicing factors connected to Prp19.";
RL PLoS ONE 6:E16719-E16719(2011).
RN [11]
RP STRUCTURE BY NMR OF 212-266, AND DOMAIN.
RX PubMed=18536009; DOI=10.1002/prot.22127;
RA Bonet R., Ramirez-Espain X., Macias M.J.;
RT "Solution structure of the yeast URN1 splicing factor FF domain:
RT comparative analysis of charge distributions in FF domain structures-FFs
RT and SURPs, two domains with a similar fold.";
RL Proteins 73:1001-1009(2008).
CC -!- FUNCTION: Component of the spliceosome involved in mRNA processing.
CC {ECO:0000269|PubMed:21386897, ECO:0000269|PubMed:23560879}.
CC -!- SUBUNIT: Component of the precatalytic spliceosomal complex B.
CC Interacts with PRP19. {ECO:0000269|PubMed:19941820,
CC ECO:0000269|PubMed:21386897}.
CC -!- INTERACTION:
CC Q06525; P38305: AIM4; NbExp=6; IntAct=EBI-35138, EBI-20939;
CC Q06525; P32523: PRP19; NbExp=7; IntAct=EBI-35138, EBI-493;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U40829; AAB68289.1; -; Genomic_DNA.
DR EMBL; AY692740; AAT92759.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11564.1; -; Genomic_DNA.
DR PIR; S69038; S69038.
DR RefSeq; NP_015478.1; NM_001184249.1.
DR PDB; 2JUC; NMR; -; A=212-266.
DR PDBsum; 2JUC; -.
DR AlphaFoldDB; Q06525; -.
DR BMRB; Q06525; -.
DR SMR; Q06525; -.
DR BioGRID; 36319; 275.
DR DIP; DIP-2017N; -.
DR IntAct; Q06525; 68.
DR MINT; Q06525; -.
DR STRING; 4932.YPR152C; -.
DR iPTMnet; Q06525; -.
DR MaxQB; Q06525; -.
DR PaxDb; 4932-YPR152C; -.
DR PeptideAtlas; Q06525; -.
DR EnsemblFungi; YPR152C_mRNA; YPR152C; YPR152C.
DR GeneID; 856275; -.
DR KEGG; sce:YPR152C; -.
DR AGR; SGD:S000006356; -.
DR SGD; S000006356; URN1.
DR VEuPathDB; FungiDB:YPR152C; -.
DR eggNOG; KOG0152; Eukaryota.
DR HOGENOM; CLU_039649_0_0_1; -.
DR InParanoid; Q06525; -.
DR OMA; EPTKYHY; -.
DR OrthoDB; 2051897at2759; -.
DR BioCyc; YEAST:G3O-34283-MONOMER; -.
DR BioGRID-ORCS; 856275; 2 hits in 10 CRISPR screens.
DR EvolutionaryTrace; Q06525; -.
DR PRO; PR:Q06525; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06525; Protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0071010; C:prespliceosome; IDA:SGD.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.10.10.440; FF domain; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR045148; TCRG1-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR15377; TRANSCRIPTION ELONGATION REGULATOR 1; 1.
DR PANTHER; PTHR15377:SF3; WW DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01846; FF; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00441; FF; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51676; FF; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..465
FT /note="Pre-mRNA-splicing factor URN1"
FT /id="PRO_0000244477"
FT DOMAIN 1..32
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 212..266
FT /note="FF"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:2JUC"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:2JUC"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2JUC"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2JUC"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:2JUC"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:2JUC"
SQ SEQUENCE 465 AA; 54139 MW; B32285888B7DB772 CRC64;
MRGEWQEFKT PAGKKYYYNK NTKQSRWEKP NLKKGSNLES NAKESQTERK PTFSLELVNG
WHLIIYNDGT KLYFNDDSKE FKNDISQEDD SRCRSLIESL DKEKLVLLIG VARGYTMREE
DIDKILESCN EEIHLFKRNQ DEVERKDEIS EEAGDVKSPL QESHTGLVSG YGSSSGEEDE
EEDEEEDEEN EEQIVNQDIS IIDDLNRIDT DDIDERNIFF ELFDRYKLDK FSTWSLQSKK
IENDPDFYKI RDDTVRESLF EEWCGERSGN ATAEESDSED NSEDDSEVLE PTKYHYLAQI
VANAGTIAPD TIPQDIRKQQ KALYKAYKIK EYIPSKRDQD KFVSQLLFYY KTFDLEQRKE
IFCDCLRDHE RDFTGAVESL RQDKELIDRW QTLLKAPADS SSIEDILLSI EHRCCVSPIV
VTEPRYYVVG ILEKTVVWVR WLAAEVGPSS RFTPVGAGNE PINPE
//
