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Protein

Protein BFR2

Gene

BFR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in endoplasmic reticulum to Golgi transport. Involved in a protein-transport step blocked by brefeldin A, which disrupts the Golgi apparatus and its incoming protein flux. May also be involved for mass growth or cell proliferation.1 Publication

GO - Biological processi

  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • protein transport Source: UniProtKB-KW
  • rRNA processing Source: SGD
  • vesicle-mediated transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29860-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BFR2
Alternative name(s):
Brefeldin A resistance protein 2
Gene namesi
Name:BFR2
Ordered Locus Names:YDR299W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR299W.
SGDiS000002707. BFR2.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: SGD
  • small-subunit processome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Protein BFR2PRO_0000056634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411PhosphoserineCombined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei366 – 3661PhosphoserineCombined sources
Modified residuei372 – 3721PhosphoserineCombined sources
Modified residuei379 – 3791PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06631.
PRIDEiQ06631.

PTM databases

iPTMnetiQ06631.

Expressioni

Inductioni

Up-regulated during cold stress and following nutrient replenishment by dilution of cells fron exhausted to fresh minimal medium.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ENP2P482348EBI-36432,EBI-23354
HCA4P204485EBI-36432,EBI-5612
MPP10P470833EBI-36432,EBI-11168

Protein-protein interaction databases

BioGridi32351. 48 interactions.
DIPiDIP-1411N.
IntActiQ06631. 21 interactions.
MINTiMINT-391985.

Structurei

3D structure databases

ProteinModelPortaliQ06631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili86 – 16176Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the AATF family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000000288.
HOGENOMiHOG000065940.
InParanoidiQ06631.
KOiK14782.
OMAiQLHPPDE.
OrthoDBiEOG708W9G.

Family and domain databases

InterProiIPR025160. AATF.
IPR012617. AATF_C.
[Graphical view]
PfamiPF13339. AATF-Che1. 1 hit.
PF08164. TRAUB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06631-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSLADQIS DIAIKPVNKD FDIEDEENAS LFQHNEKNGE SDLSDYGNSN
60 70 80 90 100
TEETKKAHYL EVEKSKLRAE KGLELNDPKY TGVKGSRQAL YEEVSENEDE
110 120 130 140 150
EEEEEEEEEK EEDALSFRTD SEDEEVEIDE EESDADGGET EEAQQKRHAL
160 170 180 190 200
SKLIQQETKQ AINKLSQSVQ RDASKGYSIL QQTKLFDNII DLRIKLQKAV
210 220 230 240 250
IAANKLPLTT ESWEEAKMDD SEETKRLLKE NEKLFNNLFN RLINFRIKFQ
260 270 280 290 300
LGDHITQNEE VAKHKLSKKR SLKELYQETN SLDSELKEYR TAVLNKWSTK
310 320 330 340 350
VSSASGNAAL SSNKFKAINL PADVQVENQL SDMSRLMKRT KLNRRNITPL
360 370 380 390 400
YFQKDCANGR LPELISPVVK DSVDDNENSD DGLDIPKNYD PRRKDNNAID
410 420 430 440 450
ITENPYVFDD EDFYRVLLND LIDKKISNAH NSESAAITIT STNARSNNKL
460 470 480 490 500
KKNIDTKASK GRKLNYSVQD PIANYEAPIT SGYKWSDDQI DEFFAGLLGQ
510 520 530
RVNFNENEDE EQHARIENDE ELEAVKNDDI QIFG
Length:534
Mass (Da):61,203
Last modified:November 1, 1996 - v1
Checksum:iAE84AD597C2BBD8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti451 – 4511K → R in AAU09706 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64735.1.
AY723789 Genomic DNA. Translation: AAU09706.1.
BK006938 Genomic DNA. Translation: DAA12138.1.
PIRiS61185.
RefSeqiNP_010585.3. NM_001180607.3.

Genome annotation databases

EnsemblFungiiYDR299W; YDR299W; YDR299W.
GeneIDi851893.
KEGGisce:YDR299W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64735.1.
AY723789 Genomic DNA. Translation: AAU09706.1.
BK006938 Genomic DNA. Translation: DAA12138.1.
PIRiS61185.
RefSeqiNP_010585.3. NM_001180607.3.

3D structure databases

ProteinModelPortaliQ06631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32351. 48 interactions.
DIPiDIP-1411N.
IntActiQ06631. 21 interactions.
MINTiMINT-391985.

PTM databases

iPTMnetiQ06631.

Proteomic databases

MaxQBiQ06631.
PRIDEiQ06631.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR299W; YDR299W; YDR299W.
GeneIDi851893.
KEGGisce:YDR299W.

Organism-specific databases

EuPathDBiFungiDB:YDR299W.
SGDiS000002707. BFR2.

Phylogenomic databases

GeneTreeiENSGT00390000000288.
HOGENOMiHOG000065940.
InParanoidiQ06631.
KOiK14782.
OMAiQLHPPDE.
OrthoDBiEOG708W9G.

Enzyme and pathway databases

BioCyciYEAST:G3O-29860-MONOMER.

Miscellaneous databases

PROiQ06631.

Family and domain databases

InterProiIPR025160. AATF.
IPR012617. AATF_C.
[Graphical view]
PfamiPF13339. AATF-Che1. 1 hit.
PF08164. TRAUB. 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Over-expression of the yeast BFR2 gene partially suppresses the growth defects induced by Brefeldin A and by four ER-to-Golgi mutations."
    Chabane S., Gachet E., Kepes F.
    Curr. Genet. 33:21-28(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Expression of the yeast BFR2 gene is regulated at the transcriptional level and through degradation of its product."
    Chabane S., Kepes F.
    Mol. Gen. Genet. 258:215-221(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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 SER-41; SER-44; SER-366 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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-41; SER-44; SER-366; SER-372 AND SER-379, 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-41; SER-44; SER-366; SER-372 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBFR2_YEAST
AccessioniPrimary (citable) accession number: Q06631
Secondary accession number(s): D6VSS8, Q66RD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 113 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 15400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.