BUL1_YEAST
ID BUL1_YEAST Reviewed; 976 AA.
AC P48524; D6W0A2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ubiquitin ligase-binding protein BUL1;
DE AltName: Full=Respiration deficiency suppressor 1;
GN Name=BUL1; Synonyms=DAG1, RDS1, SMM2; OrderedLocusNames=YMR275C;
GN ORFNames=YM8021.01C, YM8156.17C;
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], FUNCTION, AND INTERACTION WITH RSP5.
RX PubMed=8668140; DOI=10.1128/mcb.16.7.3255;
RA Yashiroda H., Oguchi T., Yasuda Y., Toh-e A., Kikuchi Y.;
RT "Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:3255-3263(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RA Stein T.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-776.
RC STRAIN=ATCC 204508 / S288c;
RA Biggins S., Rose M.D.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DOMAIN, INTERACTION WITH RSP5, AND MUTAGENESIS OF PRO-157 AND
RP PRO-158.
RX PubMed=9931424; DOI=10.1016/s0378-1119(98)00535-6;
RA Yashiroda H., Kaida D., Toh-e A., Kikuchi Y.;
RT "The PY-motif of Bul1 protein is essential for growth of Saccharomyces
RT cerevisiae under various stress conditions.";
RL Gene 225:39-46(1998).
RN [7]
RP FUNCTION.
RX PubMed=10958669; DOI=10.1128/mcb.20.18.6712-6720.2000;
RA Andoh T., Hirata Y., Kikuchi A.;
RT "Yeast glycogen synthase kinase 3 is involved in protein degradation in
RT cooperation with Bul1, Bul2, and Rsp5.";
RL Mol. Cell. Biol. 20:6712-6720(2000).
RN [8]
RP FUNCTION.
RX PubMed=11500494; DOI=10.1074/jbc.m102945200;
RA Soetens O., De Craene J.-O., Andre B.;
RT "Ubiquitin is required for sorting to the vacuole of the yeast general
RT amino acid permease, Gap1.";
RL J. Biol. Chem. 276:43949-43957(2001).
RN [9]
RP FUNCTION.
RX PubMed=11352928; DOI=10.1083/jcb.153.4.649;
RA Helliwell S.B., Losko S., Kaiser C.A.;
RT "Components of a ubiquitin ligase complex specify polyubiquitination and
RT intracellular trafficking of the general amino acid permease.";
RL J. Cell Biol. 153:649-662(2001).
RN [10]
RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX, AND MUTAGENESIS OF PRO-157 AND
RP PRO-158.
RX PubMed=12821147; DOI=10.1016/s0006-291x(03)01090-8;
RA Kaida D., Toh-e A., Kikuchi Y.;
RT "Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in
RT budding yeast.";
RL Biochem. Biophys. Res. Commun. 306:1037-1041(2003).
RN [11]
RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
RX PubMed=14560004; DOI=10.1128/mcb.23.21.7566-7584.2003;
RA Abe F., Iida H.;
RT "Pressure-induced differential regulation of the two tryptophan permeases
RT Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and
RT Bul2.";
RL Mol. Cell. Biol. 23:7566-7584(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
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 [14]
RP FUNCTION.
RX PubMed=15190065; DOI=10.1074/jbc.m406179200;
RA Welsch C.A., Roth L.W.A., Goetschy J.F., Movva N.R.;
RT "Genetic, biochemical, and transcriptional responses of Saccharomyces
RT cerevisiae to the novel immunomodulator FTY720 largely mimic those of the
RT natural sphingolipid phytosphingosine.";
RL J. Biol. Chem. 279:36720-36731(2004).
RN [15]
RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
RX PubMed=15247235; DOI=10.1074/jbc.m407372200;
RA Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B.,
RA Primig M., Hall M.N.;
RT "NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent
RT transcription in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:37512-37517(2004).
RN [16]
RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
RX PubMed=15020711; DOI=10.1091/mbc.e03-10-0727;
RA Pizzirusso M., Chang A.;
RT "Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7,
RT to the endosomal/vacuolar system in yeast.";
RL Mol. Biol. Cell 15:2401-2409(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [18]
RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
RX PubMed=16864574; DOI=10.1074/jbc.m605551200;
RA Feller A., Boeckstaens M., Marini A.-M., Dubois E.;
RT "Transduction of the nitrogen signal activating Gln3-mediated transcription
RT is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 281:28546-28554(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
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: Component of a RSP5 ubiquitin ligase complex which specifies
CC polyubiquitination and intracellular trafficking of the general amino
CC acid permease GAP1 as well as other permeases such as PMA1. The RSP5-
CC BUL1/2 complex is also necessary for the heat-shock element (HSE)-
CC mediated gene expression, nitrogen starvation GLN3-dependent
CC transcription and pressure-induced differential regulation of the 2
CC tryptophan permeases TAT1 and TAT2. {ECO:0000269|PubMed:10958669,
CC ECO:0000269|PubMed:11352928, ECO:0000269|PubMed:11500494,
CC ECO:0000269|PubMed:12821147, ECO:0000269|PubMed:14560004,
CC ECO:0000269|PubMed:15020711, ECO:0000269|PubMed:15190065,
CC ECO:0000269|PubMed:15247235, ECO:0000269|PubMed:16864574,
CC ECO:0000269|PubMed:8668140, ECO:0000269|PubMed:9931424}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the RSP5-BUL1/2 ubiquitin ligase complex composed
CC of at least RSP5 and BUL1 or BUL2.
CC -!- INTERACTION:
CC P48524; P26783: RPS5; NbExp=3; IntAct=EBI-3881, EBI-16150;
CC P48524; P39940: RSP5; NbExp=4; IntAct=EBI-3881, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The PY-motif is required for the interaction with RSP5
CC ubiquitin-ligase and the HSE-mediated gene expression.
CC {ECO:0000269|PubMed:9931424}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BUL1 family. {ECO:0000305}.
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DR EMBL; D50083; BAA08787.1; -; Genomic_DNA.
DR EMBL; X88901; CAA61363.1; -; Genomic_DNA.
DR EMBL; Z49704; CAA89773.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89258.1; -; Genomic_DNA.
DR EMBL; L40587; AAB07266.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10176.1; -; Genomic_DNA.
DR PIR; S57725; S57725.
DR RefSeq; NP_014002.1; NM_001182782.1.
DR AlphaFoldDB; P48524; -.
DR BioGRID; 35454; 240.
DR ComplexPortal; CPX-2921; RSP5-BUL1 ubiquitin ligase complex.
DR DIP; DIP-2502N; -.
DR IntAct; P48524; 12.
DR MINT; P48524; -.
DR STRING; 4932.YMR275C; -.
DR iPTMnet; P48524; -.
DR MaxQB; P48524; -.
DR PaxDb; P48524; -.
DR PRIDE; P48524; -.
DR EnsemblFungi; YMR275C_mRNA; YMR275C; YMR275C.
DR GeneID; 855318; -.
DR KEGG; sce:YMR275C; -.
DR SGD; S000004888; BUL1.
DR VEuPathDB; FungiDB:YMR275C; -.
DR eggNOG; ENOG502QSAC; Eukaryota.
DR GeneTree; ENSGT00940000176311; -.
DR HOGENOM; CLU_010320_0_0_1; -.
DR InParanoid; P48524; -.
DR OMA; LPYWAPS; -.
DR BioCyc; YEAST:G3O-32946-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P48524; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P48524; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990306; C:RSP5-BUL ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IGI:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; IGI:SGD.
DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IC:ComplexPortal.
DR GO; GO:0006513; P:protein monoubiquitination; IMP:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:SGD.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IGI:SGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:ComplexPortal.
DR InterPro; IPR039634; Bul1-like.
DR InterPro; IPR022794; Bul1_C.
DR InterPro; IPR007519; Bul1_N.
DR PANTHER; PTHR31904; PTHR31904; 1.
DR Pfam; PF04426; Bul1_C; 1.
DR Pfam; PF04425; Bul1_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..976
FT /note="Ubiquitin ligase-binding protein BUL1"
FT /id="PRO_0000065022"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..160
FT /note="PY-motif"
FT COMPBIAS 22..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MUTAGEN 157
FT /note="P->Q: Abolishes interaction with RSP5 and reduces
FT HSE-mediated gene expression; when associated with A-158."
FT /evidence="ECO:0000269|PubMed:12821147,
FT ECO:0000269|PubMed:9931424"
FT MUTAGEN 158
FT /note="P->A: Abolishes interaction with RSP5 and reduces
FT HSE-mediated gene expression; when associated with Q-157."
FT /evidence="ECO:0000269|PubMed:12821147,
FT ECO:0000269|PubMed:9931424"
FT CONFLICT 35
FT /note="V -> A (in Ref. 1; BAA08787)"
FT /evidence="ECO:0000305"
FT CONFLICT 773..775
FT /note="YDD -> ISN (in Ref. 5; AAB07266)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="A -> R (in Ref. 2; CAA61363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 109174 MW; 9253D207B894CE44 CRC64;
MAKDLNDSGF PPKRKPLLRP QRSDFTANSS TTMNVNANTR GRGRQKQEGG KGSSRSPSLH
SPKSWIRSAS ATGILGLRRP ELAHSHSHAP STGTPAGGNR SPLRRSTANA TPVETGRSLT
DGDINNVVDV LPSFEMYNTL HRHIPQGNVD PDRHDFPPSY QEANNSTATG AAGSSADLSH
QSLSTDALGA TRSSSTSNLE NLIPLRTEHH SIAAHQSTAV DEDSLDIPPI LDDLNDTDNI
FIDKLYTLPK MSTPIEITIK TTKHAPIPHV KPEEESILKE YTSGDLIHGF ITIENKSQAN
LKFEMFYVTL ESYISIIDKV KSKRTIKRFL RMVDLSASWS YSKIALGSGV DFIPADVDYD
GSVFGLNNSR VLEPGVKYKK FFIFKLPLQL LDVTCKQEHF SHCLLPPSFG IDKYRNNCKY
SGIKVNRVLG CGHLGTKGSP ILTNDMSDDN LSINYTIDAR IVGKDQKASK LYIMKEREYN
LRVIPFGFDA NVVGERTTMS QLNDITKLVQ ERLDALRKIF QRLEKKEPIT NRDIHGADLS
GTIDDSIESD SQEILQRKLD QLHIKNRNNY LVNYNDLKLG HDLDNGRSGN SGHNTDTSRA
WGPFVESELK YKLKNKSNSS SFLNFSHFLN SSSSSMSSSS NAGKNNHDLT GNKERTGLIL
VKAKIPKQGL PYWAPSLLRK TNVFESKSKH DQENWVRLSE LIPEDVKKPL EKLDLQLTCI
ESDNSLPHDP PEIQSITTEL ICITAKSDNS IPIKLNSELL MNKEKLTSIK ALYDDFHSKI
CEYETKFNKN FLELNELYNM NRGDRRPKEL KFTDFITSQL FNDIESICNL KVSVHNLSNI
FKKQVSTLKQ HSKHALSEDS ISHTGNGSSS SPSSASLTPV TSSSKSSLFL PSGSSSTSLK
FTDQIVHKWV RIAPLQYKRD INVNLEFNKD IKETLIPSFE SCLCCRFYCV RVMIKFENHL
GVAKIDIPIS VRQVTK
