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Q07457 (BRE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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:
E3 ubiquitin-protein ligase BRE1

EC=6.3.2.-
Alternative name(s):
Brefeldin A-sensitivity protein 1
Gene names
Name:BRE1
Ordered Locus Names:YDL074C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis. Ref.3 Ref.4 Ref.5 Ref.8 Ref.9

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Forms a complex with the E2 enzyme RAD6/UBC2. May interact with LGE1.

Subcellular location

Nucleus Probable Ref.6.

Miscellaneous

Present with 2980 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the BRE1 family.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing at telomere

Inferred from mutant phenotype Ref.5. Source: SGD

double-strand break repair via homologous recombination

Inferred from genetic interaction PubMed 16783014. Source: SGD

histone monoubiquitination

Inferred from mutant phenotype Ref.4Ref.5. Source: SGD

histone ubiquitination

Inferred from mutant phenotype PubMed 23103252. Source: SGD

intra-S DNA damage checkpoint

Inferred from mutant phenotype PubMed 15632126. Source: SGD

meiotic DNA double-strand break formation

Inferred from mutant phenotype Ref.8. Source: SGD

mitotic G1 DNA damage checkpoint

Inferred from mutant phenotype PubMed 16166626PubMed 16783014. Source: SGD

regulation of DNA-dependent DNA replication initiation

Inferred from mutant phenotype PubMed 23103252. Source: SGD

transcription from RNA polymerase II promoter

Inferred from genetic interaction Ref.9. Source: SGD

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA replication origin binding

Inferred from direct assay PubMed 23103252. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 11087867PubMed 19410543PubMed 19531475PubMed 21179020. Source: IntAct

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 19531475. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself6EBI-31563,EBI-31563
RAD6P061044EBI-31563,EBI-19722

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 700700E3 ubiquitin-protein ligase BRE1
PRO_0000055857

Regions

Zinc finger648 – 68740RING-type
Coiled coil126 – 406281 Potential
Coiled coil555 – 62066 Potential

Experimental info

Mutagenesis6631C → A: Abolishes ability to monoubiquitinate histone H2B. Ref.5
Mutagenesis6651H → A: Abolishes ability to monoubiquitinate histone H2B. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q07457 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FC6B32825970D36F

FASTA70080,692
        10         20         30         40         50         60 
MTAEPATKKI KLELSDPSEP LTQSDVIAFQ KEALFRCINR RRVDFEALRK QYELSRRECI 

        70         80         90        100        110        120 
DVSRKLANIM ALIVTLARFI ETFCTDANEK QLCREIAQGD ETLIVQRSDS FMKLLTKYGK 

       130        140        150        160        170        180 
PNTTDSNTNS NASDHIQELT TELKNLRKSK EELFYENSQL TEEISALKEY YTNIIRKYDR 

       190        200        210        220        230        240 
DESFTIKRVF KEDKTDAVKE LREDEKESNE NNIKSGNKDS SAINGDNTSK KSEKGDELVQ 

       250        260        270        280        290        300 
AEDERKEDAE NEKLELDLKF SDLRAEINSL SSTIKDLENI RRENEEELIK TRSEVSNLKK 

       310        320        330        340        350        360 
QQIAAADQDP DFKSYDHESL LAKIQHLTEQ NAELSEINSS FLSKFQVLAK EKEIYTKKVR 

       370        380        390        400        410        420 
EEFQKSLDSL VEMNSSLEKD VVRIRTARDD LLSKIAILEA EKSKTEVLSD LQHAIDILKE 

       430        440        450        460        470        480 
QWTKIDQRSN DTKSSSTQDA LIKEIQDLEK GFRELSDLTH KKYSEIINHE SVISKLTVEK 

       490        500        510        520        530        540 
TKADQKYFAA MRSKDSILIE IKTLSKSLSK SNELILQLKD SDRLLQQKIG NLHKQLDLSQ 

       550        560        570        580        590        600 
NNERRLIDSS KTETLKIIDL NNTSTKLKRS LEKLQEESNK SIADMTHLET KLNDTEIELK 

       610        620        630        640        650        660 
HFKQKASHLE SKCEKLHDTL FRGNNKNKGS SDEALVEELA NFRTLVYCSL CSKNWKNMAI 

       670        680        690        700 
KTCGHVFCEN CCKERLAARM RKCPTCNKAF SSNDLLTVHL 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p."
Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.
J. Biol. Chem. 278:34739-34742(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"A conserved RING finger protein required for histone H2B monoubiquitination and cell size control."
Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., Madhani H.D.
Mol. Cell 11:261-266(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGE1.
[5]"Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter."
Wood A., Krogan N.J., Dover J., Schneider J., Heidt J., Boateng M.A., Dean K., Golshani A., Zhang Y., Greenblatt J.F., Johnston M., Shilatifard A.
Mol. Cell 11:267-274(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-663 AND HIS-665.
[6]"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].
[7]"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].
[8]"Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks during meiosis."
Yamashita K., Shinohara M., Shinohara A.
Proc. Natl. Acad. Sci. U.S.A. 101:11380-11385(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Histone H2B ubiquitylation is associated with elongating RNA polymerase II."
Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A., Strahl B.D.
Mol. Cell. Biol. 25:637-651(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74122 Genomic DNA. Translation: CAA98640.1.
BK006938 Genomic DNA. Translation: DAA11785.1.
PIRS67610.
RefSeqNP_010209.1. NM_001180133.1.

3D structure databases

ProteinModelPortalQ07457.
SMRQ07457. Positions 639-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31987. 393 interactions.
DIPDIP-2999N.
IntActQ07457. 72 interactions.
MINTMINT-434946.
STRING4932.YDL074C.

Proteomic databases

PaxDbQ07457.
PeptideAtlasQ07457.
PRIDEQ07457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL074C; YDL074C; YDL074C.
GeneID851485.
KEGGsce:YDL074C.

Organism-specific databases

CYGDYDL074c.
SGDS000002232. BRE1.

Phylogenomic databases

eggNOGNOG263074.
GeneTreeENSGT00390000002866.
HOGENOMHOG000095255.
KOK10696.
OMAKEALFRC.
OrthoDBEOG7J9W0C.

Enzyme and pathway databases

BioCycYEAST:G3O-29485-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ07457.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR013956. E3_ubiquit_lig_BRE1.
IPR007087. Znf_C2H2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF08647. BRE1. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968807.
PROQ07457.

Entry information

Entry nameBRE1_YEAST
AccessionPrimary (citable) accession number: Q07457
Secondary accession number(s): D6VRS5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 119 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 IV

Yeast (Saccharomyces cerevisiae) chromosome IV: 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