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Protein

UBP3-associated protein BRE5

Gene

BRE5

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

Has a role in de-ubiquitination. In conjunction with UBP3, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of sec23.1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • protein deubiquitination Source: SGD
  • regulation of ER to Golgi vesicle-mediated transport Source: SGD
  • regulation of retrograde vesicle-mediated transport, Golgi to ER Source: SGD
  • ribophagy Source: SGD
  • transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33357-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
UBP3-associated protein BRE5
Alternative name(s):
Brefeldin-A sensitivity protein 5
Gene namesi
Name:BRE5
Ordered Locus Names:YNR051C
ORF Names:N3465
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNR051C.
SGDiS000005334. BRE5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: SGD
  • Ubp3-Bre5 deubiquitination complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515UBP3-associated protein BRE5PRO_0000194803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei187 – 1871PhosphoserineCombined sources
Modified residuei282 – 2821PhosphoserineCombined sources
Modified residuei336 – 3361PhosphothreonineCombined sources
Modified residuei340 – 3401PhosphoserineCombined sources
Modified residuei398 – 3981PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53741.
PeptideAtlasiP53741.
TopDownProteomicsiP53741.

PTM databases

iPTMnetiP53741.

Interactioni

Subunit structurei

Interacts with UBP3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-28528,EBI-28528
CDC48P256944EBI-28528,EBI-4308
HMT1P380742EBI-28528,EBI-8394
UBP3Q014777EBI-28528,EBI-19834

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi35876. 899 interactions.
DIPiDIP-4254N.
IntActiP53741. 366 interactions.
MINTiMINT-483528.

Structurei

Secondary structure

1
515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2218Combined sources
Helixi24 – 307Combined sources
Beta strandi31 – 4010Combined sources
Beta strandi56 – 616Combined sources
Helixi62 – 7110Combined sources
Helixi73 – 764Combined sources
Beta strandi79 – 9214Combined sources
Helixi93 – 953Combined sources
Beta strandi97 – 10812Combined sources
Beta strandi114 – 12411Combined sources
Beta strandi131 – 14111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZX2X-ray2.10A/B1-146[»]
2QIYX-ray1.69A/B1-146[»]
ProteinModelPortaliP53741.
SMRiP53741. Positions 3-143.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 140133NTF2PROSITE-ProRule annotationAdd
BLAST
Domaini418 – 49477RRMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 NTF2 domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000057133.
InParanoidiP53741.
KOiK19718.
OMAiNEYERNP.
OrthoDBiEOG7HB5NR.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR018222. Nuclear_transport_factor_2_euk.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
PROSITEiPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53741-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVTVQDICF AFLQNYYERM RTDPSKLAYF YASTAELTHT NYQSKSTNEK
60 70 80 90 100
DDVLPTVKVT GRENINKFFS RNDAKVRSLK LKLDTIDFQY TGHLHKSILI
110 120 130 140 150
MATGEMFWTG TPVYKFCQTF ILLPSSNGST FDITNDIIRF ISNSFKPYVL
160 170 180 190 200
TDASLSQSNE ENSVSAVEED KIRHESGVEK EKEKEKSPEI SKPKAKKETV
210 220 230 240 250
KDTTAPTESS TQEKPIVDHS QPRAIPVTKE SKIHTETVPS STKGNHKQDE
260 270 280 290 300
VSTEELGNVT KLNEKSHKAE KKAAPIKTKE GSVEAINAVN NSSLPNGKEV
310 320 330 340 350
SDEKPVPGGV KEAETEIKPI EPQVSDAKES GNNASTPSSS PEPVANPPKM
360 370 380 390 400
TWASKLMNEN SDRISKNNTT VEYIRPETLP KKPTERKFEM GNRRDNASAN
410 420 430 440 450
SKNKKKPVFS TVNKDGFYPI YIRGTNGLRE EKLRSALEKE FGKVMRITAA
460 470 480 490 500
DNFAVVDFET QKSQIDALEK KKKSIDGIEV CLERKTVKKP TSNNPPGIFT
510
NGTRSHRKQP LKRKD
Length:515
Mass (Da):57,674
Last modified:October 1, 1996 - v1
Checksum:i462A7D4309A69192
GO

Sequence cautioni

The sequence AAA34833.1 differs from that shown. Reason: Frameshift at positions 317 and 320. Curated
The sequence AAA34834.1 differs from that shown. Reason: Frameshift at positions 317 and 320. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71666 Genomic DNA. Translation: CAA96332.1.
AY692784 Genomic DNA. Translation: AAT92803.1.
M88607 Genomic DNA. Translation: AAA34833.1. Frameshift.
M88607 Genomic DNA. Translation: AAA34834.1. Frameshift.
BK006947 Genomic DNA. Translation: DAA10592.1.
PIRiS63382.
RefSeqiNP_014449.1. NM_001183228.1.

Genome annotation databases

EnsemblFungiiYNR051C; YNR051C; YNR051C.
GeneIDi855787.
KEGGisce:YNR051C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71666 Genomic DNA. Translation: CAA96332.1.
AY692784 Genomic DNA. Translation: AAT92803.1.
M88607 Genomic DNA. Translation: AAA34833.1. Frameshift.
M88607 Genomic DNA. Translation: AAA34834.1. Frameshift.
BK006947 Genomic DNA. Translation: DAA10592.1.
PIRiS63382.
RefSeqiNP_014449.1. NM_001183228.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZX2X-ray2.10A/B1-146[»]
2QIYX-ray1.69A/B1-146[»]
ProteinModelPortaliP53741.
SMRiP53741. Positions 3-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35876. 899 interactions.
DIPiDIP-4254N.
IntActiP53741. 366 interactions.
MINTiMINT-483528.

PTM databases

iPTMnetiP53741.

Proteomic databases

MaxQBiP53741.
PeptideAtlasiP53741.
TopDownProteomicsiP53741.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR051C; YNR051C; YNR051C.
GeneIDi855787.
KEGGisce:YNR051C.

Organism-specific databases

EuPathDBiFungiDB:YNR051C.
SGDiS000005334. BRE5.

Phylogenomic databases

HOGENOMiHOG000057133.
InParanoidiP53741.
KOiK19718.
OMAiNEYERNP.
OrthoDBiEOG7HB5NR.

Enzyme and pathway databases

BioCyciYEAST:G3O-33357-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53741.
PROiP53741.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR018222. Nuclear_transport_factor_2_euk.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
PROSITEiPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cusick M.E.
    Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-441.
  5. "Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23."
    Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.
    Nat. Cell Biol. 5:661-667(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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 THR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 SER-282 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBRE5_YEAST
AccessioniPrimary (citable) accession number: P53741
Secondary accession number(s): D6W1M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 151 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 11700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.