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P48524 (BUL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length976 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPS5P267833EBI-3881,EBI-16150

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 976976Ubiquitin ligase-binding protein BUL1
PRO_0000065022

Regions

Motif156 – 1605PY-motif
Compositional bias631 – 64010Poly-Ser
Compositional bias868 – 8769Poly-Ser

Amino acid modifications

Modified residue581Phosphoserine Ref.19
Modified residue701Phosphoserine Ref.17

Experimental info

Mutagenesis1571P → Q: Abolishes interaction with RSP5 and reduces HSE-mediated gene expression; when associated with A-158. Ref.6 Ref.10
Mutagenesis1581P → A: Abolishes interaction with RSP5 and reduces HSE-mediated gene expression; when associated with Q-157. Ref.6 Ref.10
Sequence conflict351V → A in BAA08787. Ref.1
Sequence conflict773 – 7753YDD → ISN in AAB07266. Ref.5
Sequence conflict9631A → R in CAA61363. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48524 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9253D207B894CE44

FASTA976109,174
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS57725.
RefSeqNP_014002.1. NM_001182782.1.

3D structure databases

ProteinModelPortalP48524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35454. 116 interactions.
DIPDIP-2502N.
IntActP48524. 11 interactions.
MINTMINT-596689.
STRING4932.YMR275C.

Proteomic databases

PaxDbP48524.
PeptideAtlasP48524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR275C; YMR275C; YMR275C.
GeneID855318.
KEGGsce:YMR275C.

Organism-specific databases

CYGDYMR275c.
SGDS000004888. BUL1.

Phylogenomic databases

eggNOGNOG43698.
GeneTreeENSGT00390000010225.
HOGENOMHOG000095282.
OMAFESCLCC.
OrthoDBEOG7PK975.

Enzyme and pathway databases

BioCycYEAST:G3O-32946-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP48524.

Family and domain databases

InterProIPR022794. Bul1_C.
IPR007520. Bul1_C_yeast.
IPR007519. Bul1_N.
[Graphical view]
PfamPF04426. Bul1_C. 1 hit.
PF04425. Bul1_N. 1 hit.
[Graphical view]
ProDomPD024065. Bul1_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

NextBio979017.

Entry information

Entry nameBUL1_YEAST
AccessionPrimary (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: March 19, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways