IBD2_YEAST
ID IBD2_YEAST Reviewed; 351 AA.
AC P53892; D6W118;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein IBD2;
DE AltName: Full=Inhibition of bud division protein 2;
GN Name=IBD2; OrderedLocusNames=YNL164C; ORFNames=N1714;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BFA1.
RX PubMed=12072457; DOI=10.1093/genetics/161.2.595;
RA Hwang H.-S., Song K.;
RT "IBD2 encodes a novel component of the Bub2p-dependent spindle checkpoint
RT in the budding yeast Saccharomyces cerevisiae.";
RL Genetics 161:595-609(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-106 AND THR-211, AND
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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Part of a checkpoint which monitors spindle integrity and
CC prevents premature exit from mitosis. This cell-cycle arrest depends
CC upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.
CC {ECO:0000269|PubMed:12072457}.
CC -!- SUBUNIT: Interacts with BFA1. {ECO:0000269|PubMed:12072457}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:12072457}.
CC -!- SIMILARITY: Belongs to the IBD2 family. {ECO:0000305}.
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DR EMBL; X92517; CAA63275.1; -; Genomic_DNA.
DR EMBL; Z71440; CAA96051.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10384.1; -; Genomic_DNA.
DR PIR; S60963; S60963.
DR RefSeq; NP_014235.1; NM_001183002.1.
DR AlphaFoldDB; P53892; -.
DR BioGRID; 35664; 97.
DR DIP; DIP-1994N; -.
DR IntAct; P53892; 2.
DR MINT; P53892; -.
DR STRING; 4932.YNL164C; -.
DR iPTMnet; P53892; -.
DR MaxQB; P53892; -.
DR PaxDb; P53892; -.
DR PRIDE; P53892; -.
DR EnsemblFungi; YNL164C_mRNA; YNL164C; YNL164C.
DR GeneID; 855557; -.
DR KEGG; sce:YNL164C; -.
DR SGD; S000005108; IBD2.
DR VEuPathDB; FungiDB:YNL164C; -.
DR eggNOG; ENOG502RXXW; Eukaryota.
DR HOGENOM; CLU_067888_0_0_1; -.
DR InParanoid; P53892; -.
DR OMA; PKNMIKW; -.
DR BioCyc; YEAST:G3O-33180-MON; -.
DR PRO; PR:P53892; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53892; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; NAS:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR InterPro; IPR026231; IBD2.
DR PRINTS; PR02099; PROTEINIBD2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..351
FT /note="Protein IBD2"
FT /id="PRO_0000203413"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 351 AA; 40016 MW; 8D649A7A6284D59E CRC64;
MTPTNQSSGT TNASVEVLSE DGPMPINVMM QEGVKALTKI LSNQLQDRQA FQNAPHAMQF
VIRNGGKALS NARLEELKDA LPKMDSLSLE DELAKIDGQS AYHIDSAEEK ETFESKIGQI
ASRNSADFII EEDLQNILDD DLKDSELNLD GEEAEIIFDY ESQELDTPDG IGEKISQMIE
SVLPGGFGSE EQGGLRTVTN VEDLDVAEEV TDIDHDTVDA ARLHGDGQHS ISSRKHSRSK
NSKKNGHVRR HDFYDESRDH KSCCPHHHYE NLSKLRNYYY HDFEYISRTE NRVPDFSVLV
NESSPMCLFC EYYMVFGEPP RNMIKWYNRT FGYNRMPNPP RDEQDSRKRN R
