BUL2_YEAST
ID BUL2_YEAST Reviewed; 920 AA.
AC Q03758; D6W0H3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ubiquitin ligase-binding protein BUL2;
GN Name=BUL2; OrderedLocusNames=YML111W; ORFNames=YM8339.08;
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=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 [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 FUNCTION, DOMAIN, AND INTERACTION WITH RSP5.
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, AND IDENTIFICATION BY
RP 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: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 -!- 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 339 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; Z49210; CAA89107.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09787.1; -; Genomic_DNA.
DR PIR; S53961; S53961.
DR RefSeq; NP_013596.1; NM_001182473.1.
DR AlphaFoldDB; Q03758; -.
DR BioGRID; 35093; 240.
DR ComplexPortal; CPX-2923; RSP5-BUL2 ubiquitin ligase complex.
DR DIP; DIP-2237N; -.
DR IntAct; Q03758; 12.
DR MINT; Q03758; -.
DR STRING; 4932.YML111W; -.
DR iPTMnet; Q03758; -.
DR MaxQB; Q03758; -.
DR PaxDb; Q03758; -.
DR PRIDE; Q03758; -.
DR EnsemblFungi; YML111W_mRNA; YML111W; YML111W.
DR GeneID; 854929; -.
DR KEGG; sce:YML111W; -.
DR SGD; S000004579; BUL2.
DR VEuPathDB; FungiDB:YML111W; -.
DR eggNOG; ENOG502QSAC; Eukaryota.
DR GeneTree; ENSGT00940000176311; -.
DR HOGENOM; CLU_010320_0_0_1; -.
DR InParanoid; Q03758; -.
DR OMA; FFTFKFP; -.
DR BioCyc; YEAST:G3O-32693-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q03758; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03758; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990306; C:RSP5-BUL ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000151; C:ubiquitin ligase complex; IMP:SGD.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; 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: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; Ubl conjugation pathway.
FT CHAIN 1..920
FT /note="Ubiquitin ligase-binding protein BUL2"
FT /id="PRO_0000203241"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..133
FT /note="PY-motif"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 920 AA; 104786 MW; 4134530BF9C1E697 CRC64;
MTFTFSTSSR KNGRPPLKSV STEDNIHLLR KRRQQQLSSN STDNSLHPNS GQTPRASDSQ
DDDIRSASTT NLDRLRQERE ENSLEMDCTQ SRLSHRANML VDVLPSFEMY NALHRHIPQG
NVDPDRHDFP PSYQEVRTQR MTILPSNDNS VERSQLTAVP GSENACNNAT AHSLTNLHPL
QTQHLTINST RSGGQSLHSS SDTNISQIPF EDDLNDSDNI FIDKLYTLPK LSTPIEIDIR
ITKTASIPHE RPEEQSILKE YTSGDIIHGY CLIENRSSQP LKFEMFYVTL EAYISVIDRQ
KGKRTLKRFL RMVDLSASWS YTNITPSTGI NIVPGERDFD DAIIGLSNSR ELKPNTKYKK
FFMFKLPTQL LDVTCKQEQF SHCLLPPSFG IDKYKNNCKY SGIKVNSVLG CGHLGTKGSP
ILTLDMADDN LSINYTIDAK IVGKDKRTSK LNIMKEKEYN LRVMPFPFAG VTNQQNEKTC
LRQLKNLESL IEDRFEALNK IFKKLELNEA ISNVDIHDTD ISGTLDGNED LDSDEILRRK
LDQLHINNRI DDTASQSPSY DSKNMAPKEN LVETELRYKF KNKNKSNSSL FSHFLSSSET
GSSSTGPHVY NSGLIVLSVK KPQSTLPYWS PSLLRKTNKF EAKSEQEKEN WQRLMGMLPE
GVKTPLTKLD VHLTCIQSNN SAGHKPPEIS SVTTEFVVIT AKSDNSIPIK FCTELLMNEN
RLNKLKTKFL TYQKKVHEYR KKFEENHAKL NELYNRNRDH FTPKELLFTN FISDQINNDI
DSLAGLKVNI IDLHDIFKKQ IHTFEEENED IISKKGSSNP PSASSSNNNF LQATFSNGAS
TATKFTQQIV HEWEKVKPLQ YKRDVTVNLK LNPNIKETLV PNLETCLCCR FYCVRVNIKF
DNHLGSMKVD IPVDVKKLQI
