BRE5_YEAST
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 03-AUG-2022, entry version 196.
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;
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=11; 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};
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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 PDBsum; 1ZX2; -.
DR PDBsum; 2QIY; -.
DR AlphaFoldDB; P53741; -.
DR SMR; P53741; -.
DR BioGRID; 35876; 1262.
DR ComplexPortal; CPX-1412; UBP3-BRE5 ubiquitin hydrolase complex.
DR DIP; DIP-4254N; -.
DR IntAct; P53741; 367.
DR MINT; P53741; -.
DR STRING; 4932.YNR051C; -.
DR iPTMnet; P53741; -.
DR MaxQB; P53741; -.
DR PaxDb; P53741; -.
DR PRIDE; P53741; -.
DR TopDownProteomics; P53741; -.
DR EnsemblFungi; YNR051C_mRNA; YNR051C; YNR051C.
DR GeneID; 855787; -.
DR KEGG; sce:YNR051C; -.
DR SGD; S000005334; BRE5.
DR VEuPathDB; FungiDB:YNR051C; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_036630_0_0_1; -.
DR InParanoid; P53741; -.
DR OMA; KTYYQRM; -.
DR BioCyc; YEAST:G3O-33357-MON; -.
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: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:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
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 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; PTHR10693; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
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 164..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..505
FT /note="Polar 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 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
