ID DIB1_YEAST Reviewed; 143 AA.
AC Q06819; D6W484;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Spliceosomal protein DIB1;
GN Name=DIB1; Synonyms=CDH1, SNU16; OrderedLocusNames=YPR082C;
GN ORFNames=P9513.12;
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].
RX PubMed=9182666; DOI=10.1083/jcb.137.6.1337;
RA Berry L.D., Gould K.L.;
RT "Fission yeast dim1(+) encodes a functionally conserved polypeptide
RT essential for mitosis.";
RL J. Cell Biol. 137:1337-1354(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Essential role in pre-mRNA splicing. Also essential for entry
CC into mitosis (G2/M progression) as well as for chromosome segregation
CC during mitosis.
CC -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31,
CC PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC {ECO:0000269|PubMed:10449419}.
CC -!- INTERACTION:
CC Q06819; P19735: PRP6; NbExp=3; IntAct=EBI-166, EBI-227;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the DIM1 family. {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; U51033; AAB68131.1; -; Genomic_DNA.
DR EMBL; AY558054; AAS56380.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11500.1; -; Genomic_DNA.
DR PIR; S69068; S69068.
DR RefSeq; NP_015407.1; NM_001184179.1.
DR PDB; 3JCM; EM; 3.80 A; L=1-143.
DR PDB; 5GAN; EM; 3.60 A; D=1-143.
DR PDB; 5GAP; EM; 3.60 A; D=1-143.
DR PDB; 5NRL; EM; 7.20 A; D=1-143.
DR PDB; 5ZWM; EM; 3.40 A; E=1-143.
DR PDB; 5ZWO; EM; 3.90 A; E=1-143.
DR PDBsum; 3JCM; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GAP; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR AlphaFoldDB; Q06819; -.
DR EMDB; EMD-3683; -.
DR EMDB; EMD-6972; -.
DR EMDB; EMD-6974; -.
DR EMDB; EMD-8012; -.
DR EMDB; EMD-8014; -.
DR SMR; Q06819; -.
DR BioGRID; 36253; 166.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-29; U5 small nuclear ribonucleoprotein complex.
DR DIP; DIP-1289N; -.
DR IntAct; Q06819; 16.
DR MINT; Q06819; -.
DR STRING; 4932.YPR082C; -.
DR iPTMnet; Q06819; -.
DR MaxQB; Q06819; -.
DR PaxDb; 4932-YPR082C; -.
DR PeptideAtlas; Q06819; -.
DR EnsemblFungi; YPR082C_mRNA; YPR082C; YPR082C.
DR GeneID; 856197; -.
DR KEGG; sce:YPR082C; -.
DR AGR; SGD:S000006286; -.
DR SGD; S000006286; DIB1.
DR VEuPathDB; FungiDB:YPR082C; -.
DR eggNOG; KOG3414; Eukaryota.
DR GeneTree; ENSGT00390000010779; -.
DR HOGENOM; CLU_117348_0_0_1; -.
DR InParanoid; Q06819; -.
DR OMA; TMFFYRN; -.
DR OrthoDB; 3939228at2759; -.
DR BioCyc; YEAST:G3O-34226-MONOMER; -.
DR BioGRID-ORCS; 856197; 10 hits in 10 CRISPR screens.
DR PRO; PR:Q06819; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06819; Protein.
DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR CDD; cd02954; DIM1; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR004123; Dim1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12052:SF5; THIOREDOXIN-LIKE PROTEIN 4A; 1.
DR PANTHER; PTHR12052; THIOREDOXIN-LIKE PROTEN 4A, 4B; 1.
DR Pfam; PF02966; DIM1; 1.
DR PIRSF; PIRSF017199; mRNA_splic_U5; 1.
DR SMART; SM01410; DIM1; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..143
FT /note="Spliceosomal protein DIB1"
FT /id="PRO_0000218286"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 143 AA; 16776 MW; B8C11278571C57E5 CRC64;
MASVLLPQLR TGWHVDQAIV TETKRLVVIR FGRKNDRQCM IMDELLSSIA ERVRNFAVIY
LCDIDEVSDF DEMYELTDPM TVMFFYHNKH MMCDFGTGNN NKLNFIVDDK QEMIDILETI
FRGARKNKGL VVSPYDYNHK RVS
//
