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Protein

E3 ubiquitin-protein ligase BRE1

Gene

BRE1

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

Functioni

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.5 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri648 – 68740RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA replication origin binding Source: SGD
  2. identical protein binding Source: IntAct
  3. ligase activity Source: UniProtKB-KW
  4. ubiquitin-protein transferase activity Source: SGD
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin silencing at telomere Source: SGD
  2. double-strand break repair via homologous recombination Source: SGD
  3. histone monoubiquitination Source: SGD
  4. histone ubiquitination Source: SGD
  5. intra-S DNA damage checkpoint Source: SGD
  6. meiotic DNA double-strand break formation Source: SGD
  7. mitotic G1 DNA damage checkpoint Source: SGD
  8. regulation of DNA-dependent DNA replication initiation Source: SGD
  9. telomere maintenance via recombination Source: SGD
  10. transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29485-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase BRE1 (EC:6.3.2.-)
Alternative name(s):
Brefeldin A-sensitivity protein 1
Gene namesi
Name:BRE1
Ordered Locus Names:YDL074C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL074c.
SGDiS000002232. BRE1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi663 – 6631C → A: Abolishes ability to monoubiquitinate histone H2B. 1 Publication
Mutagenesisi665 – 6651H → A: Abolishes ability to monoubiquitinate histone H2B. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 700700E3 ubiquitin-protein ligase BRE1PRO_0000055857Add
BLAST

Proteomic databases

MaxQBiQ07457.
PaxDbiQ07457.
PeptideAtlasiQ07457.
PRIDEiQ07457.

Expressioni

Gene expression databases

GenevestigatoriQ07457.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-31563,EBI-31563
RAD6P061044EBI-31563,EBI-19722

Protein-protein interaction databases

BioGridi31987. 399 interactions.
DIPiDIP-2999N.
IntActiQ07457. 72 interactions.
MINTiMINT-434946.
STRINGi4932.YDL074C.

Structurei

3D structure databases

ProteinModelPortaliQ07457.
SMRiQ07457. Positions 638-698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili126 – 406281Sequence AnalysisAdd
BLAST
Coiled coili555 – 62066Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the BRE1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri648 – 68740RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG263074.
GeneTreeiENSGT00390000002866.
HOGENOMiHOG000095255.
InParanoidiQ07457.
KOiK10696.
OMAiYSREAER.
OrthoDBiEOG7J9W0C.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR013956. E3_ubiquit_lig_BRE1.
IPR007087. Znf_C2H2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF08647. BRE1. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07457-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAEPATKKI KLELSDPSEP LTQSDVIAFQ KEALFRCINR RRVDFEALRK
60 70 80 90 100
QYELSRRECI DVSRKLANIM ALIVTLARFI ETFCTDANEK QLCREIAQGD
110 120 130 140 150
ETLIVQRSDS FMKLLTKYGK PNTTDSNTNS NASDHIQELT TELKNLRKSK
160 170 180 190 200
EELFYENSQL TEEISALKEY YTNIIRKYDR DESFTIKRVF KEDKTDAVKE
210 220 230 240 250
LREDEKESNE NNIKSGNKDS SAINGDNTSK KSEKGDELVQ AEDERKEDAE
260 270 280 290 300
NEKLELDLKF SDLRAEINSL SSTIKDLENI RRENEEELIK TRSEVSNLKK
310 320 330 340 350
QQIAAADQDP DFKSYDHESL LAKIQHLTEQ NAELSEINSS FLSKFQVLAK
360 370 380 390 400
EKEIYTKKVR EEFQKSLDSL VEMNSSLEKD VVRIRTARDD LLSKIAILEA
410 420 430 440 450
EKSKTEVLSD LQHAIDILKE QWTKIDQRSN DTKSSSTQDA LIKEIQDLEK
460 470 480 490 500
GFRELSDLTH KKYSEIINHE SVISKLTVEK TKADQKYFAA MRSKDSILIE
510 520 530 540 550
IKTLSKSLSK SNELILQLKD SDRLLQQKIG NLHKQLDLSQ NNERRLIDSS
560 570 580 590 600
KTETLKIIDL NNTSTKLKRS LEKLQEESNK SIADMTHLET KLNDTEIELK
610 620 630 640 650
HFKQKASHLE SKCEKLHDTL FRGNNKNKGS SDEALVEELA NFRTLVYCSL
660 670 680 690 700
CSKNWKNMAI KTCGHVFCEN CCKERLAARM RKCPTCNKAF SSNDLLTVHL
Length:700
Mass (Da):80,692
Last modified:November 1, 1996 - v1
Checksum:iFC6B32825970D36F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74122 Genomic DNA. Translation: CAA98640.1.
BK006938 Genomic DNA. Translation: DAA11785.1.
PIRiS67610.
RefSeqiNP_010209.1. NM_001180133.1.

Genome annotation databases

EnsemblFungiiYDL074C; YDL074C; YDL074C.
GeneIDi851485.
KEGGisce:YDL074C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74122 Genomic DNA. Translation: CAA98640.1.
BK006938 Genomic DNA. Translation: DAA11785.1.
PIRiS67610.
RefSeqiNP_010209.1. NM_001180133.1.

3D structure databases

ProteinModelPortaliQ07457.
SMRiQ07457. Positions 638-698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31987. 399 interactions.
DIPiDIP-2999N.
IntActiQ07457. 72 interactions.
MINTiMINT-434946.
STRINGi4932.YDL074C.

Proteomic databases

MaxQBiQ07457.
PaxDbiQ07457.
PeptideAtlasiQ07457.
PRIDEiQ07457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL074C; YDL074C; YDL074C.
GeneIDi851485.
KEGGisce:YDL074C.

Organism-specific databases

CYGDiYDL074c.
SGDiS000002232. BRE1.

Phylogenomic databases

eggNOGiNOG263074.
GeneTreeiENSGT00390000002866.
HOGENOMiHOG000095255.
InParanoidiQ07457.
KOiK10696.
OMAiYSREAER.
OrthoDBiEOG7J9W0C.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-29485-MONOMER.

Miscellaneous databases

NextBioi968807.
PROiQ07457.

Gene expression databases

GenevestigatoriQ07457.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR013956. E3_ubiquit_lig_BRE1.
IPR007087. Znf_C2H2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF08647. BRE1. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. 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.

Entry informationi

Entry nameiBRE1_YEAST
AccessioniPrimary (citable) accession number: Q07457
Secondary accession number(s): D6VRS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 126 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 2980 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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 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.