Reviewed, UniProtKB/Swiss-Prot Q03758 (BUL2_YEAST)

Names and origin

Protein names

Recommended name:
    Ubiquitin ligase-binding protein BUL2

Gene names

Name:	BUL2
Ordered Locus Names:	YML111W
ORF Names:	YM8339.08

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	920 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other permeases such as PMA1. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription and pressure-induced differential regulation of the 2 tryptophan permeases TAT1 and TAT2.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the RSP5-BUL1/2 ubiquitin ligase complex composed of at least RSP5 and BUL1 or BUL2.
Subcellular location	Cytoplasm.
Domain	The PY-motif is required for the interaction with RSP5 ubiquitin-ligase and the HSE-mediated gene expression.
Miscellaneous	Present with 339 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the BUL1 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein monoubiquitination Ref.2 Inferred from mutant phenotype. Source: SGD protein polyubiquitination Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Ref.8 Inferred from direct assay. Source: SGD ubiquitin ligase complex Ref.5 Inferred from mutant phenotype. Source: SGD
Molecular function	protein binding Ref.2 Inferred from genetic interaction. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 920	920	Ubiquitin ligase-binding protein BUL2
Regions
	Motif	129 – 133	5	PY-motif
Amino acid modifications
	Modified residue	21	1	Phosphoserine
	Modified residue	22	1	Phosphothreonine

Sequences

	Sequence		Length	Mass (Da)
	Q03758-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 4134530BF9C1E697	FASTA	920	104,786
	10 20 30 40 50 60 MTFTFSTSSR KNGRPPLKSV STEDNIHLLR KRRQQQLSSN STDNSLHPNS GQTPRASDSQ 70 80 90 100 110 120 DDDIRSASTT NLDRLRQERE ENSLEMDCTQ SRLSHRANML VDVLPSFEMY NALHRHIPQG 130 140 150 160 170 180 NVDPDRHDFP PSYQEVRTQR MTILPSNDNS VERSQLTAVP GSENACNNAT AHSLTNLHPL 190 200 210 220 230 240 QTQHLTINST RSGGQSLHSS SDTNISQIPF EDDLNDSDNI FIDKLYTLPK LSTPIEIDIR 250 260 270 280 290 300 ITKTASIPHE RPEEQSILKE YTSGDIIHGY CLIENRSSQP LKFEMFYVTL EAYISVIDRQ 310 320 330 340 350 360 KGKRTLKRFL RMVDLSASWS YTNITPSTGI NIVPGERDFD DAIIGLSNSR ELKPNTKYKK 370 380 390 400 410 420 FFMFKLPTQL LDVTCKQEQF SHCLLPPSFG IDKYKNNCKY SGIKVNSVLG CGHLGTKGSP 430 440 450 460 470 480 ILTLDMADDN LSINYTIDAK IVGKDKRTSK LNIMKEKEYN LRVMPFPFAG VTNQQNEKTC 490 500 510 520 530 540 LRQLKNLESL IEDRFEALNK IFKKLELNEA ISNVDIHDTD ISGTLDGNED LDSDEILRRK 550 560 570 580 590 600 LDQLHINNRI DDTASQSPSY DSKNMAPKEN LVETELRYKF KNKNKSNSSL FSHFLSSSET 610 620 630 640 650 660 GSSSTGPHVY NSGLIVLSVK KPQSTLPYWS PSLLRKTNKF EAKSEQEKEN WQRLMGMLPE 670 680 690 700 710 720 GVKTPLTKLD VHLTCIQSNN SAGHKPPEIS SVTTEFVVIT AKSDNSIPIK FCTELLMNEN 730 740 750 760 770 780 RLNKLKTKFL TYQKKVHEYR KKFEENHAKL NELYNRNRDH FTPKELLFTN FISDQINNDI 790 800 810 820 830 840 DSLAGLKVNI IDLHDIFKKQ IHTFEEENED IISKKGSSNP PSASSSNNNF LQATFSNGAS 850 860 870 880 890 900 TATKFTQQIV HEWEKVKPLQ YKRDVTVNLK LNPNIKETLV PNLETCLCCR FYCVRVNIKF 910 920 DNHLGSMKVD IPVDVKKLQI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions." Yashiroda H., Kaida D., Toh-e A., Kikuchi Y. Gene 225:39-46(1998) [PubMed: 9931424] [Abstract] Cited for: FUNCTION, DOMAIN, INTERACTION WITH RSP5.
[3]	"Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5." Andoh T., Hirata Y., Kikuchi A. Mol. Cell. Biol. 20:6712-6720(2000) [PubMed: 10958669] [Abstract] Cited for: FUNCTION.
[4]	"Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1." Soetens O., De Craene J.-O., Andre B. J. Biol. Chem. 276:43949-43957(2001) [PubMed: 11500494] [Abstract] Cited for: FUNCTION.
[5]	"Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease." Helliwell S.B., Losko S., Kaiser C.A. J. Cell Biol. 153:649-662(2001) [PubMed: 11352928] [Abstract] Cited for: FUNCTION.
[6]	"Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast." Kaida D., Toh-e A., Kikuchi Y. Biochem. Biophys. Res. Commun. 306:1037-1041(2003) [PubMed: 12821147] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[7]	"Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2." Abe F., Iida H. Mol. Cell. Biol. 23:7566-7584(2003) [PubMed: 14560004] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Genetic, biochemical, and transcriptional responses of Saccharomyces cerevisiae to the novel immunomodulator FTY720 largely mimic those of the natural sphingolipid phytosphingosine." Welsch C.A., Roth L.W.A., Goetschy J.F., Movva N.R. J. Biol. Chem. 279:36720-36731(2004) [PubMed: 15190065] [Abstract] Cited for: FUNCTION.
[11]	"NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae." Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B., Primig M., Hall M.N. J. Biol. Chem. 279:37512-37517(2004) [PubMed: 15247235] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[12]	"Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast." Pizzirusso M., Chang A. Mol. Biol. Cell 15:2401-2409(2004) [PubMed: 15020711] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[13]	"Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae." Feller A., Boeckstaens M., Marini A.M., Dubois E. J. Biol. Chem. 281:28546-28554(2006) [PubMed: 16864574] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, MASS SPECTROMETRY.
[15]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND THR-22, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49210 Genomic DNA. Translation: CAA89107.1.
PIR	S53961.
RefSeq	NP_013596.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2237N.
IntAct	Q03758.
Proteomic databases
PeptideAtlas	Q03758.
Genome annotation databases
Ensembl	YML111W. Saccharomyces cerevisiae. [Contig view]
GeneID	854929.
GenomeReviews	Gene locus YML111W in contig Z71257_GR.
KEGG	sce:YML111W.
NMPDR	fig|4932.3.peg.4632.
Organism-specific databases
CYGD	YML111w.
SGD	S000004579. BUL2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q03758.
Gene expression databases
ArrayExpress	Q03758.
GermOnline	YML111W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007520. Bul1_C. IPR007519. Bul1_N. [Graphical view]
Pfam	PF04426. Bul1_C. 1 hit. PF04425. Bul1_N. 1 hit. [Graphical view]
ProDom	Q03758. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	Q03758.
ProtoNet	Search...

Entry information

Entry name

BUL2_YEAST

Accession

Primary (citable) accession number: Q03758

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 2, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)