P48524 (BUL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin ligase-binding protein BUL1

Alternative name(s):
Respiration deficiency suppressor 1

Gene names

Name:	BUL1
Synonyms:	DAG1, RDS1, SMM2
Ordered Locus Names:	YMR275C
ORF Names:	YM8021.01C, YM8156.17C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	976 AA.
Sequence status	Complete.
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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.18
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 Ref.12.
Domain	The PY-motif is required for the interaction with RSP5 ubiquitin-ligase and the HSE-mediated gene expression. Ref.6
Miscellaneous	Present with 486 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the BUL1 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrion inheritance Inferred from genetic interaction PubMed 10366593. Source: SGD protein monoubiquitination Inferred from physical interaction Ref.1. Source: SGD protein polyubiquitination Inferred from physical interaction Ref.1. Source: SGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from physical interaction Ref.1. Source: SGD ubiquitin ligase complex Inferred from direct assay Ref.6. Source: SGD
Molecular_function	ubiquitin-ubiquitin ligase activity Inferred from genetic interaction Ref.9. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPS5	P26783	3	EBI-3881,EBI-16150
RSP5	P39940	3	EBI-3881,EBI-16219

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 976	976	Ubiquitin ligase-binding protein BUL1		PRO_0000065022
Regions
	Motif	156 – 160	5	PY-motif
	Compositional bias	631 – 640	10	Poly-Ser
	Compositional bias	868 – 876	9	Poly-Ser
Amino acid modifications
	Modified residue	58	1	Phosphoserine Ref.19
	Modified residue	70	1	Phosphoserine Ref.17 Ref.21
	Modified residue	107	1	Phosphothreonine Ref.20 Ref.21
	Modified residue	111	1	Phosphothreonine Ref.20
	Modified residue	184	1	Phosphoserine Ref.21
	Modified residue	194	1	Phosphoserine Ref.21
	Modified residue	195	1	Phosphoserine Ref.21
	Modified residue	619	1	Phosphoserine Ref.21
	Modified residue	896	1	Phosphoserine Ref.21
	Modified residue	897	1	Phosphothreonine Ref.21
	Modified residue	898	1	Phosphoserine Ref.21
Experimental info
	Mutagenesis	157	1	P → Q: Abolishes interaction with RSP5 and reduces HSE-mediated gene expression; when associated with A-158. Ref.6 Ref.10
	Mutagenesis	158	1	P → A: Abolishes interaction with RSP5 and reduces HSE-mediated gene expression; when associated with Q-157. Ref.6 Ref.10
	Sequence conflict	35	1	V → A in BAA08787. Ref.1
	Sequence conflict	773 – 775	3	YDD → ISN in AAB07266. Ref.5
	Sequence conflict	963	1	A → R in CAA61363. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P48524 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 9253D207B894CE44	FASTA	976	109,174
	10 20 30 40 50 60 MAKDLNDSGF PPKRKPLLRP QRSDFTANSS TTMNVNANTR GRGRQKQEGG KGSSRSPSLH 70 80 90 100 110 120 SPKSWIRSAS ATGILGLRRP ELAHSHSHAP STGTPAGGNR SPLRRSTANA TPVETGRSLT 130 140 150 160 170 180 DGDINNVVDV LPSFEMYNTL HRHIPQGNVD PDRHDFPPSY QEANNSTATG AAGSSADLSH 190 200 210 220 230 240 QSLSTDALGA TRSSSTSNLE NLIPLRTEHH SIAAHQSTAV DEDSLDIPPI LDDLNDTDNI 250 260 270 280 290 300 FIDKLYTLPK MSTPIEITIK TTKHAPIPHV KPEEESILKE YTSGDLIHGF ITIENKSQAN 310 320 330 340 350 360 LKFEMFYVTL ESYISIIDKV KSKRTIKRFL RMVDLSASWS YSKIALGSGV DFIPADVDYD 370 380 390 400 410 420 GSVFGLNNSR VLEPGVKYKK FFIFKLPLQL LDVTCKQEHF SHCLLPPSFG IDKYRNNCKY 430 440 450 460 470 480 SGIKVNRVLG CGHLGTKGSP ILTNDMSDDN LSINYTIDAR IVGKDQKASK LYIMKEREYN 490 500 510 520 530 540 LRVIPFGFDA NVVGERTTMS QLNDITKLVQ ERLDALRKIF QRLEKKEPIT NRDIHGADLS 550 560 570 580 590 600 GTIDDSIESD SQEILQRKLD QLHIKNRNNY LVNYNDLKLG HDLDNGRSGN SGHNTDTSRA 610 620 630 640 650 660 WGPFVESELK YKLKNKSNSS SFLNFSHFLN SSSSSMSSSS NAGKNNHDLT GNKERTGLIL 670 680 690 700 710 720 VKAKIPKQGL PYWAPSLLRK TNVFESKSKH DQENWVRLSE LIPEDVKKPL EKLDLQLTCI 730 740 750 760 770 780 ESDNSLPHDP PEIQSITTEL ICITAKSDNS IPIKLNSELL MNKEKLTSIK ALYDDFHSKI 790 800 810 820 830 840 CEYETKFNKN FLELNELYNM NRGDRRPKEL KFTDFITSQL FNDIESICNL KVSVHNLSNI 850 860 870 880 890 900 FKKQVSTLKQ HSKHALSEDS ISHTGNGSSS SPSSASLTPV TSSSKSSLFL PSGSSSTSLK 910 920 930 940 950 960 FTDQIVHKWV RIAPLQYKRD INVNLEFNKD IKETLIPSFE SCLCCRFYCV RVMIKFENHL 970 GVAKIDIPIS VRQVTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae." Yashiroda H., Oguchi T., Yasuda Y., Toh-e A., Kikuchi Y. Mol. Cell. Biol. 16:3255-3263(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RSP5.
[2]	Stein T. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	Biggins S., Rose M.D. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-776. Strain: ATCC 204508 / S288c.
[6]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, INTERACTION WITH RSP5, MUTAGENESIS OF PRO-157 AND PRO-158.
[7]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX, MUTAGENESIS OF PRO-157 AND PRO-158.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[12]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[16]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[17]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, MASS SPECTROMETRY. Strain: YAL6B.
[18]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
[19]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY.
[20]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107 AND THR-111, MASS SPECTROMETRY.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-107; SER-184; SER-194; SER-195; SER-619; SER-896; THR-897 AND SER-898, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50083 Genomic DNA. Translation: BAA08787.1. X88901 Genomic DNA. Translation: CAA61363.1. Z49704 Genomic DNA. Translation: CAA89773.1. Z49260 Genomic DNA. Translation: CAA89258.1. L40587 Genomic DNA. Translation: AAB07266.1. BK006946 Genomic DNA. Translation: DAA10176.1.
PIR	S57725.
RefSeq	NP_014002.1. NM_001182782.1.
3D structure databases
ProteinModelPortal	P48524.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2502N.
IntAct	P48524. 10 interactions.
MINT	MINT-596689.
STRING	4932.YMR275C.
Proteomic databases
PaxDb	P48524.
PeptideAtlas	P48524.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR275C; YMR275C; YMR275C.
GeneID	855318.
KEGG	sce:YMR275C.
Organism-specific databases
CYGD	YMR275c.
SGD	S000004888. BUL1.
Phylogenomic databases
eggNOG	NOG43698.
GeneTree	ENSGT00390000010225.
HOGENOM	HOG000095282.
OMA	FESCLCC.
OrthoDB	EOG451J02.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	P48524.
GermOnline	YMR275C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR022794. Bul1_C. IPR007520. Bul1_C_yeast. IPR007519. Bul1_N. [Graphical view]
Pfam	PF04426. Bul1_C. 1 hit. PF04425. Bul1_N. 1 hit. [Graphical view]
ProDom	PD024065. Bul1_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other
NextBio	979017.

Entry information

Entry name

BUL1_YEAST

Accession

Primary (citable) accession number: P48524
Secondary accession number(s): D6W0A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program