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Protein

Ubiquitin ligase-binding protein BUL2

Gene

BUL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 TAT2.10 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • ubiquitin-ubiquitin ligase activity Source: SGD

GO - Biological processi

  • protein monoubiquitination Source: SGD
  • protein polyubiquitination Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-32693-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin ligase-binding protein BUL2
Gene namesi
Name:BUL2
Ordered Locus Names:YML111W
ORF Names:YM8339.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML111W.
SGDiS000004579. BUL2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • ubiquitin ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 920920Ubiquitin ligase-binding protein BUL2PRO_0000203241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221PhosphothreonineCombined sources
Modified residuei557 – 5571PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03758.

PTM databases

iPTMnetiQ03758.

Interactioni

Subunit structurei

Component of the RSP5-BUL1/2 ubiquitin ligase complex composed of at least RSP5 and BUL1 or BUL2.

Protein-protein interaction databases

BioGridi35093. 56 interactions.
DIPiDIP-2237N.
IntActiQ03758. 12 interactions.
MINTiMINT-2786678.

Structurei

3D structure databases

ProteinModelPortaliQ03758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi129 – 1335PY-motif

Domaini

The PY-motif is required for the interaction with RSP5 ubiquitin-ligase and the HSE-mediated gene expression.1 Publication

Sequence similaritiesi

Belongs to the BUL1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000010225.
HOGENOMiHOG000095282.
InParanoidiQ03758.
OrthoDBiEOG7PK975.

Family and domain databases

InterProiIPR022794. Bul1_C.
IPR007519. Bul1_N.
[Graphical view]
PfamiPF04426. Bul1_C. 1 hit.
PF04425. Bul1_N. 1 hit.
[Graphical view]
ProDomiPD024065. Bul1_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q03758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFTFSTSSR KNGRPPLKSV STEDNIHLLR KRRQQQLSSN STDNSLHPNS
60 70 80 90 100
GQTPRASDSQ DDDIRSASTT NLDRLRQERE ENSLEMDCTQ SRLSHRANML
110 120 130 140 150
VDVLPSFEMY NALHRHIPQG NVDPDRHDFP PSYQEVRTQR MTILPSNDNS
160 170 180 190 200
VERSQLTAVP GSENACNNAT AHSLTNLHPL QTQHLTINST RSGGQSLHSS
210 220 230 240 250
SDTNISQIPF EDDLNDSDNI FIDKLYTLPK LSTPIEIDIR ITKTASIPHE
260 270 280 290 300
RPEEQSILKE YTSGDIIHGY CLIENRSSQP LKFEMFYVTL EAYISVIDRQ
310 320 330 340 350
KGKRTLKRFL RMVDLSASWS YTNITPSTGI NIVPGERDFD DAIIGLSNSR
360 370 380 390 400
ELKPNTKYKK FFMFKLPTQL LDVTCKQEQF SHCLLPPSFG IDKYKNNCKY
410 420 430 440 450
SGIKVNSVLG CGHLGTKGSP ILTLDMADDN LSINYTIDAK IVGKDKRTSK
460 470 480 490 500
LNIMKEKEYN LRVMPFPFAG VTNQQNEKTC LRQLKNLESL IEDRFEALNK
510 520 530 540 550
IFKKLELNEA ISNVDIHDTD ISGTLDGNED LDSDEILRRK LDQLHINNRI
560 570 580 590 600
DDTASQSPSY DSKNMAPKEN LVETELRYKF KNKNKSNSSL FSHFLSSSET
610 620 630 640 650
GSSSTGPHVY NSGLIVLSVK KPQSTLPYWS PSLLRKTNKF EAKSEQEKEN
660 670 680 690 700
WQRLMGMLPE GVKTPLTKLD VHLTCIQSNN SAGHKPPEIS SVTTEFVVIT
710 720 730 740 750
AKSDNSIPIK FCTELLMNEN RLNKLKTKFL TYQKKVHEYR KKFEENHAKL
760 770 780 790 800
NELYNRNRDH FTPKELLFTN FISDQINNDI DSLAGLKVNI IDLHDIFKKQ
810 820 830 840 850
IHTFEEENED IISKKGSSNP PSASSSNNNF LQATFSNGAS TATKFTQQIV
860 870 880 890 900
HEWEKVKPLQ YKRDVTVNLK LNPNIKETLV PNLETCLCCR FYCVRVNIKF
910 920
DNHLGSMKVD IPVDVKKLQI
Length:920
Mass (Da):104,786
Last modified:November 1, 1997 - v1
Checksum:i4134530BF9C1E697
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49210 Genomic DNA. Translation: CAA89107.1.
BK006946 Genomic DNA. Translation: DAA09787.1.
PIRiS53961.
RefSeqiNP_013596.1. NM_001182473.1.

Genome annotation databases

EnsemblFungiiYML111W; YML111W; YML111W.
GeneIDi854929.
KEGGisce:YML111W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49210 Genomic DNA. Translation: CAA89107.1.
BK006946 Genomic DNA. Translation: DAA09787.1.
PIRiS53961.
RefSeqiNP_013596.1. NM_001182473.1.

3D structure databases

ProteinModelPortaliQ03758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35093. 56 interactions.
DIPiDIP-2237N.
IntActiQ03758. 12 interactions.
MINTiMINT-2786678.

PTM databases

iPTMnetiQ03758.

Proteomic databases

MaxQBiQ03758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML111W; YML111W; YML111W.
GeneIDi854929.
KEGGisce:YML111W.

Organism-specific databases

EuPathDBiFungiDB:YML111W.
SGDiS000004579. BUL2.

Phylogenomic databases

GeneTreeiENSGT00390000010225.
HOGENOMiHOG000095282.
InParanoidiQ03758.
OrthoDBiEOG7PK975.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-32693-MONOMER.

Miscellaneous databases

PROiQ03758.

Family and domain databases

InterProiIPR022794. Bul1_C.
IPR007519. Bul1_N.
[Graphical view]
PfamiPF04426. Bul1_C. 1 hit.
PF04425. Bul1_N. 1 hit.
[Graphical view]
ProDomiPD024065. Bul1_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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.
  4. "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.
  5. "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.
  6. "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.
  7. "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.
  8. "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.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "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].
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBUL2_YEAST
AccessioniPrimary (citable) accession number: Q03758
Secondary accession number(s): D6W0H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 339 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.