FUB1_YEAST
ID FUB1_YEAST Reviewed; 250 AA.
AC P25659; D6VR79;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Silencing boundary-establishment protein FUB1 {ECO:0000305|PubMed:22362029};
DE AltName: Full=Function of boundary protein 1 {ECO:0000303|PubMed:22362029};
DE AltName: Full=Proteasome inhibitor PI31-like protein FUB1 {ECO:0000250|UniProtKB:Q92530, ECO:0000305};
GN Name=FUB1 {ECO:0000303|PubMed:22362029};
GN OrderedLocusNames=YCR076C {ECO:0000312|SGD:S000000672}; ORFNames=YCR76C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 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 [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22362029; DOI=10.1266/ggs.86.305;
RA Hatanaka A., Chen B., Sun J.Q., Mano Y., Funakoshi M., Kobayashi H., Ju Y.,
RA Mizutani T., Shinmyozu K., Nakayama J., Miyamoto K., Uchida H., Oki M.;
RT "Fub1p, a novel protein isolated by boundary screening, binds the
RT proteasome complex.";
RL Genes Genet. Syst. 86:305-314(2011).
CC -!- FUNCTION: Plays a role in the establishment of transcriptional
CC silencing boundaries, preventing the propagation of heterochromatic
CC silencing. {ECO:0000269|PubMed:22362029}.
CC -!- SUBUNIT: Interacts with the 20S proteasome.
CC {ECO:0000269|PubMed:22362029}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC {ECO:0000305}.
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DR EMBL; X59720; CAA42265.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07548.1; -; Genomic_DNA.
DR PIR; S19518; S19518.
DR RefSeq; NP_010001.1; NM_001178785.1.
DR AlphaFoldDB; P25659; -.
DR BioGRID; 31051; 100.
DR DIP; DIP-2637N; -.
DR IntAct; P25659; 3.
DR MINT; P25659; -.
DR STRING; 4932.YCR076C; -.
DR MaxQB; P25659; -.
DR PaxDb; P25659; -.
DR PRIDE; P25659; -.
DR EnsemblFungi; YCR076C_mRNA; YCR076C; YCR076C.
DR GeneID; 850439; -.
DR KEGG; sce:YCR076C; -.
DR SGD; S000000672; FUB1.
DR VEuPathDB; FungiDB:YCR076C; -.
DR eggNOG; ENOG502S4RD; Eukaryota.
DR HOGENOM; CLU_1125080_0_0_1; -.
DR InParanoid; P25659; -.
DR OMA; SHPDWSG; -.
DR BioCyc; YEAST:G3O-29375-MON; -.
DR PRO; PR:P25659; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25659; protein.
DR GO; GO:0070628; F:proteasome binding; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Chromatin regulator; Reference proteome.
FT CHAIN 1..250
FT /note="Silencing boundary-establishment protein FUB1"
FT /id="PRO_0000202574"
FT REGION 179..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 26756 MW; E7AEC69BAFF7FA6F CRC64;
MIENKVELVA ELVLESIGKT EVVSRHTEGT KSCQVSFRIK DSPSEKGSTS FLSELVVIQT
LDDNDKYTVV IRHGTSITMA CVVGYSDFKL PTELKWPLER ESLPVEPDLK PIMTQLKRQT
AGSADMPKFD DEYQAQARQN QGTAPLNPYP GLTVTEPSFA NPAGGYADGD LYPVGTSHPD
WSGGLPNPLG NPSSQGGMIF DPNRRPAPRR EDMPPGWMPG SKYDEPFGPG SGGFGGSGSG
GFGGSGSGFI