Q07457 (BRE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	700 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Ubl conjugation pathway
Cellular component	Nucleus
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin 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 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 transcription from RNA polymerase II promoter Inferred from genetic interaction Ref.9. Source: SGD
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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
itself		4	EBI-31563,EBI-31563

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	E3 ubiquitin-protein ligase BRE1		PRO_0000055857
Regions
	Zinc finger	648 – 687	40	RING-type
	Coiled coil	126 – 406	281	Potential
	Coiled coil	555 – 620	66	Potential
Experimental info
	Mutagenesis	663	1	C → A: Abolishes ability to monoubiquitinate histone H2B. Ref.5
	Mutagenesis	665	1	H → A: Abolishes ability to monoubiquitinate histone H2B. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q07457 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: FC6B32825970D36F	FASTA	700	80,692
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[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.
PIR	S67610.
RefSeq	NP_010209.1. NM_001180133.1.
3D structure databases
ProteinModelPortal	Q07457.
SMR	Q07457. Positions 638-698.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2999N.
IntAct	Q07457. 73 interactions.
MINT	MINT-434946.
STRING	4932.YDL074C.
Proteomic databases
PaxDb	Q07457.
PeptideAtlas	Q07457.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL074C; YDL074C; YDL074C.
GeneID	851485.
KEGG	sce:YDL074C.
Organism-specific databases
CYGD	YDL074c.
SGD	S000002232. BRE1.
Phylogenomic databases
eggNOG	NOG263074.
GeneTree	ENSGT00390000002866.
HOGENOM	HOG000095255.
KO	K10696.
OMA	CSLCSKN.
OrthoDB	EOG4QVGND.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	Q07457.
GermOnline	YDL074C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR013956. E3_ubiquit_lig_BRE1. IPR007087. Znf_C2H2. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF08647. BRE1. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968807.

Entry information

Entry name

BRE1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program