CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011499
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase BRE1 
Protein Synonyms/Alias
 Brefeldin A-sensitivity protein 1 
Gene Name
 BRE1 
Gene Synonyms/Alias
 YDL074C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
11EPATKKIKLELSDPSacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 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. 
Sequence Annotation
 ZN_FING 648 687 RING-type.  
Keyword
 Chromatin regulator; Coiled coil; Complete proteome; Ligase; Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 700 AA 
Protein Sequence
MTAEPATKKI KLELSDPSEP LTQSDVIAFQ KEALFRCINR RRVDFEALRK QYELSRRECI 60
DVSRKLANIM ALIVTLARFI ETFCTDANEK QLCREIAQGD ETLIVQRSDS FMKLLTKYGK 120
PNTTDSNTNS NASDHIQELT TELKNLRKSK EELFYENSQL TEEISALKEY YTNIIRKYDR 180
DESFTIKRVF KEDKTDAVKE LREDEKESNE NNIKSGNKDS SAINGDNTSK KSEKGDELVQ 240
AEDERKEDAE NEKLELDLKF SDLRAEINSL SSTIKDLENI RRENEEELIK TRSEVSNLKK 300
QQIAAADQDP DFKSYDHESL LAKIQHLTEQ NAELSEINSS FLSKFQVLAK EKEIYTKKVR 360
EEFQKSLDSL VEMNSSLEKD VVRIRTARDD LLSKIAILEA EKSKTEVLSD LQHAIDILKE 420
QWTKIDQRSN DTKSSSTQDA LIKEIQDLEK GFRELSDLTH KKYSEIINHE SVISKLTVEK 480
TKADQKYFAA MRSKDSILIE IKTLSKSLSK SNELILQLKD SDRLLQQKIG NLHKQLDLSQ 540
NNERRLIDSS KTETLKIIDL NNTSTKLKRS LEKLQEESNK SIADMTHLET KLNDTEIELK 600
HFKQKASHLE SKCEKLHDTL FRGNNKNKGS SDEALVEELA NFRTLVYCSL CSKNWKNMAI 660
KTCGHVFCEN CCKERLAARM RKCPTCNKAF SSNDLLTVHL 700 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IMP:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
 GO:0000724; P:double-strand break repair via homologous recombination; IGI:SGD.
 GO:0010390; P:histone monoubiquitination; IMP:SGD.
 GO:0031573; P:intra-S DNA damage checkpoint; IMP:SGD.
 GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
 GO:0031571; P:mitotic G1 DNA damage checkpoint; IMP:SGD.
 GO:0006366; P:transcription from RNA polymerase II promoter; IGI:SGD. 
Interpro
 IPR013956; E3_ubiquit_lig_BRE1.
 IPR007087; Znf_C2H2.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF08647; BRE1 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS