ID   BRE5_YEAST              Reviewed;         515 AA.
AC   P53741; D6W1M6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 212.
DE   RecName: Full=UBP3-associated protein BRE5;
DE   AltName: Full=Brefeldin-A sensitivity protein 5;
GN   Name=BRE5; OrderedLocusNames=YNR051C; ORFNames=N3465;
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=9169873; DOI=10.1038/387s093;
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-441.
RA   Cusick M.E.;
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=12778054; DOI=10.1038/ncb1003;
RA   Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.;
RT   "Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII
RT   protein, Sec23.";
RL   Nat. Cell Biol. 5:661-667(2003).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-336, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-398, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-340, 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).
RN   [11]
RP   IDENTIFICATION IN A COMPLEX WITH DOA1; UBP3 AND CDC48, INTERACTION WITH
RP   CDC48, AND MUTAGENESIS OF 2-GLY--LYS-146 AND 147-PRO--ASP-515.
RX   PubMed=20508643; DOI=10.1038/embor.2010.74;
RA   Ossareh-Nazari B., Bonizec M., Cohen M., Dokudovskaya S., Delalande F.,
RA   Schaeffer C., Van Dorsselaer A., Dargemont C.;
RT   "Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required
RT   for ribophagy.";
RL   EMBO Rep. 11:548-554(2010).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 1-146 IN COMPLEX WITH UBP3.
RX   PubMed=17632125; DOI=10.1016/j.jmb.2007.06.052;
RA   Li K., Ossareh-Nazari B., Liu X., Dargemont C., Marmorstein R.;
RT   "Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating
RT   enzyme.";
RL   J. Mol. Biol. 372:194-204(2007).
CC   -!- FUNCTION: Has a role in de-ubiquitination. In conjunction with UBP3,
CC       cleaves ubiquitin, leading to the subsequent mono-ubiquitination of
CC       sec23. {ECO:0000269|PubMed:12778054}.
CC   -!- SUBUNIT: Heterotetramer with UBP3; contains two molecules of BRE5 and
CC       two molecules of UBP3 (PubMed:12778054, PubMed:17632125). Forms a
CC       complex composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5
CC       (PubMed:20508643). Within the complex, interacts (via C-terminus) with
CC       CDC48; the interaction is direct and UBP3-independent
CC       (PubMed:20508643). {ECO:0000269|PubMed:12778054,
CC       ECO:0000269|PubMed:17632125, ECO:0000269|PubMed:20508643}.
CC   -!- INTERACTION:
CC       P53741; P53741: BRE5; NbExp=3; IntAct=EBI-28528, EBI-28528;
CC       P53741; P25694: CDC48; NbExp=4; IntAct=EBI-28528, EBI-4308;
CC       P53741; P38074: HMT1; NbExp=2; IntAct=EBI-28528, EBI-8394;
CC       P53741; Q01477: UBP3; NbExp=12; IntAct=EBI-28528, EBI-19834;
CC   -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34833.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA34834.1; Type=Frameshift; Evidence={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; Z71666; CAA96332.1; -; Genomic_DNA.
DR   EMBL; AY692784; AAT92803.1; -; Genomic_DNA.
DR   EMBL; M88607; AAA34833.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; M88607; AAA34834.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006947; DAA10592.1; -; Genomic_DNA.
DR   PIR; S63382; S63382.
DR   RefSeq; NP_014449.1; NM_001183228.1.
DR   PDB; 1ZX2; X-ray; 2.10 A; A/B=1-146.
DR   PDB; 2QIY; X-ray; 1.69 A; A/B=1-146.
DR   AlphaFoldDB; P53741; -.
DR   SMR; P53741; -.
DR   BioGRID; 35876; 1293.
DR   ComplexPortal; CPX-1412; UBP3-BRE5 ubiquitin hydrolase complex.
DR   DIP; DIP-4254N; -.
DR   FunCoup; P53741; 297.
DR   IntAct; P53741; 405.
DR   MINT; P53741; -.
DR   STRING; 4932.YNR051C; -.
DR   GlyGen; P53741; 8 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P53741; -.
DR   PaxDb; 4932-YNR051C; -.
DR   PeptideAtlas; P53741; -.
DR   TopDownProteomics; P53741; -.
DR   EnsemblFungi; YNR051C_mRNA; YNR051C; YNR051C.
DR   GeneID; 855787; -.
DR   KEGG; sce:YNR051C; -.
DR   AGR; SGD:S000005334; -.
DR   SGD; S000005334; BRE5.
DR   VEuPathDB; FungiDB:YNR051C; -.
DR   eggNOG; KOG0116; Eukaryota.
DR   HOGENOM; CLU_036630_0_0_1; -.
DR   InParanoid; P53741; -.
DR   OMA; KTYYQRM; -.
DR   OrthoDB; 339151at2759; -.
DR   BioCyc; YEAST:G3O-33357-MONOMER; -.
DR   BioGRID-ORCS; 855787; 8 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P53741; -.
DR   PRO; PR:P53741; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53741; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0000932; C:P-body; IDA:SGD.
DR   GO; GO:1990861; C:Ubp3-Bre5 deubiquitination complex; IPI:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:1901525; P:negative regulation of mitophagy; IMP:ComplexPortal.
DR   GO; GO:0016579; P:protein deubiquitination; IMP:SGD.
DR   GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR   GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:2000156; P:regulation of retrograde vesicle-mediated transport, Golgi to ER; IMP:SGD.
DR   GO; GO:0034517; P:ribophagy; IMP:SGD.
DR   GO; GO:0034063; P:stress granule assembly; IDA:ComplexPortal.
DR   CDD; cd00780; NTF2; 1.
DR   FunFam; 3.10.450.50:FF:000017; UBP3-associated protein BRE5; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR002075; NTF2_dom.
DR   InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR   InterPro; IPR039539; Ras_GTPase_bind_prot.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR10693:SF20; AT27578P; 1.
DR   PANTHER; PTHR10693; RAS GTPASE-ACTIVATING PROTEIN-BINDING PROTEIN; 1.
DR   Pfam; PF02136; NTF2; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PDBsum; 1ZX2; -.
DR   PDBsum; 2QIY; -.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Reference proteome; RNA-binding;
KW   Ubl conjugation pathway.
FT   CHAIN           1..515
FT                   /note="UBP3-associated protein BRE5"
FT                   /id="PRO_0000194803"
FT   DOMAIN          8..140
FT                   /note="NTF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT   DOMAIN          418..494
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          157..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..166
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..515
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         336
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MUTAGEN         2..146
FT                   /note="Missing: No defect in the interaction with CDC48."
FT                   /evidence="ECO:0000269|PubMed:20508643"
FT   MUTAGEN         147..515
FT                   /note="Missing: Loss of interaction with CDC48."
FT                   /evidence="ECO:0000269|PubMed:20508643"
FT   HELIX           5..22
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   HELIX           24..30
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   STRAND          31..40
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   HELIX           62..71
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   STRAND          79..92
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   STRAND          97..108
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   STRAND          114..124
FT                   /evidence="ECO:0007829|PDB:2QIY"
FT   STRAND          131..141
FT                   /evidence="ECO:0007829|PDB:2QIY"
SQ   SEQUENCE   515 AA;  57674 MW;  462A7D4309A69192 CRC64;
     MGVTVQDICF AFLQNYYERM RTDPSKLAYF YASTAELTHT NYQSKSTNEK DDVLPTVKVT
     GRENINKFFS RNDAKVRSLK LKLDTIDFQY TGHLHKSILI MATGEMFWTG TPVYKFCQTF
     ILLPSSNGST FDITNDIIRF ISNSFKPYVL TDASLSQSNE ENSVSAVEED KIRHESGVEK
     EKEKEKSPEI SKPKAKKETV KDTTAPTESS TQEKPIVDHS QPRAIPVTKE SKIHTETVPS
     STKGNHKQDE VSTEELGNVT KLNEKSHKAE KKAAPIKTKE GSVEAINAVN NSSLPNGKEV
     SDEKPVPGGV KEAETEIKPI EPQVSDAKES GNNASTPSSS PEPVANPPKM TWASKLMNEN
     SDRISKNNTT VEYIRPETLP KKPTERKFEM GNRRDNASAN SKNKKKPVFS TVNKDGFYPI
     YIRGTNGLRE EKLRSALEKE FGKVMRITAA DNFAVVDFET QKSQIDALEK KKKSIDGIEV
     CLERKTVKKP TSNNPPGIFT NGTRSHRKQP LKRKD
//