YJU2_YEAST
ID YJU2_YEAST Reviewed; 278 AA.
AC P28320; D6VXJ3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Splicing factor YJU2 {ECO:0000255|HAMAP-Rule:MF_03226};
GN Name=YJU2 {ECO:0000255|HAMAP-Rule:MF_03226}; Synonyms=CWC16;
GN OrderedLocusNames=YKL095W; ORFNames=YKL442;
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 [GENOMIC DNA], INDUCTION, AND MOTIF.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1626433; DOI=10.1002/yea.320080509;
RA Forrova H., Kolarov J., Ghislain M., Goffeau A.;
RT "Sequence of the novel essential gene YJU2 and two flanking reading frames
RT located within a 3.2 kb EcoRI fragment from chromosome X of Saccharomyces
RT cerevisiae.";
RL Yeast 8:419-422(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8256524; DOI=10.1002/yea.320091016;
RA Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA Bolotin-Fukuhara M.;
RT "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT physically localizes the MRB1 gene and reveals eight new open reading
RT frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL Yeast 9:1149-1155(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS 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 fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
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 [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., 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 [9]
RP IDENTIFICATION IN THE ACTIVATED B COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND FUNCTION.
RX PubMed=19935684; DOI=10.1038/nsmb.1729;
RA Warkocki Z., Odenwaelder P., Schmitzova J., Platzmann F., Stark H.,
RA Urlaub H., Ficner R., Fabrizio P., Luehrmann R.;
RT "Reconstitution of both steps of Saccharomyces cerevisiae splicing with
RT purified spliceosomal components.";
RL Nat. Struct. Mol. Biol. 16:1237-1243(2009).
RN [10]
RP FUNCTION, INTERACTION WITH SYF1, AND INTERACTION WITH CLF1.
RX PubMed=23438600; DOI=10.1128/mcb.00035-13;
RA Chiang T.W., Cheng S.C.;
RT "A weak spliceosome-binding domain of Yju2 functions in the first step and
RT bypasses Prp16 in the second step of splicing.";
RL Mol. Cell. Biol. 33:1746-1755(2013).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) IN COMPLEX WITH ZINC
RP IONS, FUNCTION, IDENTIFICATION IN C COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27459055; DOI=10.1038/nature19316;
RA Galej W.P., Wilkinson M.E., Fica S.M., Oubridge C., Newman A.J., Nagai K.;
RT "Cryo-EM structure of the spliceosome immediately after branching.";
RL Nature 537:197-201(2016).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) IN COMPLEX WITH ZINC
RP IONS, FUNCTION, AND IDENTIFICATION IN C COMPLEX.
RX PubMed=27445308; DOI=10.1126/science.aag2235;
RA Wan R., Yan C., Bai R., Huang G., Shi Y.;
RT "Structure of a yeast catalytic step I spliceosome at 3.4 A resolution.";
RL Science 353:895-904(2016).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN P COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29146871; DOI=10.1126/science.aar3729;
RA Wilkinson M.E., Fica S.M., Galej W.P., Norman C.M., Newman A.J., Nagai K.;
RT "Postcatalytic spliceosome structure reveals mechanism of 3'-splice site
RT selection.";
RL Science 358:1283-1288(2017).
CC -!- FUNCTION: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA (PubMed:19935684, PubMed:27445308, PubMed:27459055,
CC PubMed:29146871). Plays a role (via N-terminus) in stabilizing the
CC structure of the spliceosome catalytic core and docking of the branch
CC helix into the active site, producing 5'-exon and lariat intron-3'-
CC intermediates (PubMed:23438600, PubMed:27459055). Further stabilizes
CC spliceosome conformation for 3'-splice site docking (via C-terminus)
CC promoting exon ligation (PubMed:29146871). {ECO:0000255|HAMAP-
CC Rule:MF_03226, ECO:0000269|PubMed:19935684,
CC ECO:0000269|PubMed:23438600, ECO:0000269|PubMed:27445308,
CC ECO:0000269|PubMed:27459055, ECO:0000269|PubMed:29146871}.
CC -!- SUBUNIT: Component of the spliceosome. Present in the activated B
CC complex, the catalytically activated B* complex which catalyzes the
CC branching, the catalytic step 1 C complex catalyzing the exon ligation,
CC and the postcatalytic P complex containing the ligated exons (mRNA) and
CC the excised lariat intron (PubMed:19935684, PubMed:27445308,
CC PubMed:27459055, PubMed:29146871). Interacts (via C-terminus) with CLF1
CC (PubMed:23438600). Interacts (via N-terminus) with SYF1
CC (PubMed:23438600). Interacts with U2 snRNA; this interaction is direct
CC (PubMed:23438600). Identified in the CWC complex (or CEF1-associated
CC complex), a spliceosome sub-complex reminiscent of a late-stage
CC spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13,
CC BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CC CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8,
CC PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2,
CC SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2
CC (PubMed:11884590). {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:19935684,
CC ECO:0000269|PubMed:23438600, ECO:0000269|PubMed:27445308,
CC ECO:0000269|PubMed:27459055, ECO:0000269|PubMed:29146871}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expressed in exponential-phase cells grown in rich medium.
CC {ECO:0000269|PubMed:1626433}.
CC -!- MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
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; X66245; CAA46970.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50462.1; -; Genomic_DNA.
DR EMBL; Z28095; CAA81933.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09063.1; -; Genomic_DNA.
DR PIR; S25355; S25355.
DR RefSeq; NP_012828.1; NM_001179661.1.
DR PDB; 5GMK; EM; 3.40 A; F=1-278.
DR PDB; 5LJ3; EM; 3.80 A; D=1-278.
DR PDB; 5LJ5; EM; 3.80 A; D=1-278.
DR PDB; 5Y88; EM; 3.70 A; R=1-278.
DR PDB; 6EXN; EM; 3.70 A; D=1-278.
DR PDB; 6J6Q; EM; 3.70 A; F=1-278.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; P28320; -.
DR SMR; P28320; -.
DR BioGRID; 34038; 372.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-1915N; -.
DR IntAct; P28320; 50.
DR MINT; P28320; -.
DR STRING; 4932.YKL095W; -.
DR MaxQB; P28320; -.
DR PaxDb; P28320; -.
DR PRIDE; P28320; -.
DR EnsemblFungi; YKL095W_mRNA; YKL095W; YKL095W.
DR GeneID; 853767; -.
DR KEGG; sce:YKL095W; -.
DR SGD; S000001578; YJU2.
DR VEuPathDB; FungiDB:YKL095W; -.
DR eggNOG; KOG2989; Eukaryota.
DR GeneTree; ENSGT00530000063615; -.
DR HOGENOM; CLU_053603_2_1_1; -.
DR InParanoid; P28320; -.
DR OMA; YIKCITC; -.
DR BioCyc; YEAST:G3O-31886-MON; -.
DR PRO; PR:P28320; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P28320; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:UniProtKB.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IDA:UniProtKB.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR12111; PTHR12111; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome; Zinc.
FT CHAIN 1..278
FT /note="Splicing factor YJU2"
FT /id="PRO_0000203163"
FT REGION 228..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..258
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:1626433"
FT MOTIF 260..278
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:1626433"
FT COMPBIAS 239..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226,
FT ECO:0000269|PubMed:27445308, ECO:0000269|PubMed:27459055"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226,
FT ECO:0000269|PubMed:27445308, ECO:0000269|PubMed:27459055"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226,
FT ECO:0000269|PubMed:27445308, ECO:0000269|PubMed:27459055"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226,
FT ECO:0000269|PubMed:27445308, ECO:0000269|PubMed:27459055"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 101..113
FT /evidence="ECO:0007829|PDB:5GMK"
SQ SEQUENCE 278 AA; 32312 MW; B57F3A173A2113FD CRC64;
MSERKAINKY YPPDYNPLEA EKLSRKMAKK LKTMNKSHAS IRLMTPFSMR CLECNEYIPK
SRKFNGKKEL LKEKYLDSIK IYRLTISCPR CANSIAFRTD PGNSDYVMEV GGVRNYVPQK
PNDDLNAKTA VESIDETLQR LVREKEMEQN EKMGIKEQAD DKMDLLEKRL AKIQQEQEDD
EELENLRKKN LEMSQRAEMI NRSKHAQQEK AVTTDDLDNL VDQVFDNHRQ RTNKPGNNND
EKRTPLFNPT STKGKIQKKS SVRTNPLGIV IKRGKSLK
