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P40450 (BNR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BNI1-related protein 1
Gene names
Name:BNR1
Ordered Locus Names:YIL159W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members By similarity. Ref.3

Subunit structure

Interacts with profilin at the FH1 domain.

Domain

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments By similarity.

Miscellaneous

Present with 259 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the formin homology family. BNI1 subfamily.

Contains 1 DAD (diaphanous autoregulatory) domain.

Contains 1 FH1 (formin homology 1) domain.

Contains 1 FH2 (formin homology 2) domain.

Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13751375BNI1-related protein 1
PRO_0000194900

Regions

Domain94 – 490397GBD/FH3
Domain659 – 851193FH1
Domain868 – 1290423FH2
Domain1302 – 133635DAD
Coiled coil520 – 60182 Potential
Compositional bias659 – 839181Pro-rich
Compositional bias1332 – 13354Arg/Lys-rich (basic)

Amino acid modifications

Modified residue6211Phosphoserine Ref.6
Modified residue7511Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P40450 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B16B04A33C9D2F08

FASTA1,375156,852
        10         20         30         40         50         60 
MDSSPNKKTY RYPRRSLSLH ARDRVSEARK LEELNLNDGL VAAGLQLVGV ALEKQGTGSH 

        70         80         90        100        110        120 
IYMKQKNFSA NDVSSSPMVS EEVNGSEMDF NPKCMPQDAS LVERMFDELL KDGTFFWGAA 

       130        140        150        160        170        180 
YKNLQNISLR RKWLLICKIR SSNHWGKKKV TSSTTYSTHL ATNELAENAH FLDGLVRNLS 

       190        200        210        220        230        240 
TGGMKLSKAL YKLEKFLRKQ SFLQLFLKDE IYLTTLIEKT LPLISKELQF VYLRCFKILM 

       250        260        270        280        290        300 
NNPLARIRAL HSEPLIRWFT ELLTDQNSNL KCQLLSMELL LLLTYVEGST GCELIWDQLS 

       310        320        330        340        350        360 
ILFTDWLEWF DKILADDIAI HSSLYLNWNQ LKIDYSTTFL LLINSILQGF NNKTALEILN 

       370        380        390        400        410        420 
FLKKNNIHNT ITFLELAYKD DPNSVVIMEQ IKQFKSKESA IFDSMIKTTN DTNSLHPTKD 

       430        440        450        460        470        480 
IARIESEPLC LENCLLLKAK DSPVEAPINE IIQSLWKILD SQKPYSESIK LLKLINSLLF 

       490        500        510        520        530        540 
YLIDSFQVST NPSFDETLES AENVDYVFQD SVNKLLDSLQ SDEIARRAVT EIDDLNAKIS 

       550        560        570        580        590        600 
HLNEKLNLVE NHDKDHLIAK LDESESLISL KTKEIENLKL QLKATKKRLD QITTHQRLYD 

       610        620        630        640        650        660 
QPPSLASSNL SIAGSIIKNN SHGNIIFQNL AKKQQQQQKI SLPKRSTSLL KSKRVTSLSS 

       670        680        690        700        710        720 
YLTDANNENE SQNESEDKSK DSLFQRSTST INFNIPSMKN ITNMQNVSLN SILSELEFSN 

       730        740        750        760        770        780 
SLGTQPNYQS SPVLSSVSSS PKLFPRLSSD SLDNGIQLVP EVVKLPQLPP PPPPPPPPPL 

       790        800        810        820        830        840 
PQSLLTEAEA KPDGVSCIAA PAPPPLPDLF KTKTCGAVPP PPPPPPLPES LSMNKGPSNH 

       850        860        870        880        890        900 
DLVTPPAPPL PNGLLSSSSV SINPTTTDLK PPPTEKRLKQ IHWDKVEDIK DTLWEDTFQR 

       910        920        930        940        950        960 
QETIKELQTD GIFSQIEDIF KMKSPTKIAN KRNAESSIAL SSNNGKSSNE LKKISFLSRD 

       970        980        990       1000       1010       1020 
LAQQFGINLH MFSQLSDMEF VMKVLNCDND IVQNVNILKF FCKEELVNIP KSMLNKYEPY 

      1030       1040       1050       1060       1070       1080 
SQGKDGKAVS DLQRADRIFL ELCINLRFYW NARSKSLLTL STYERDYYDL IFKLQKIDDA 

      1090       1100       1110       1120       1130       1140 
ISHLNRSPKF KSLMFIITEI GNHMNKRIVK GIKLKSLTKL AFVRSSIDQN VSFLHFIEKV 

      1150       1160       1170       1180       1190       1200 
IRIKYPDIYG FVDDLKNIED LGKISLEHVE SECHEFHKKI EDLVTQFQVG KLSKEENLDP 

      1210       1220       1230       1240       1250       1260 
RDQIIKKVKF KINRAKTKSE LLIGQCKLTL IDLNKLMKYY GEDPKDKESK NEFFQPFIEF 

      1270       1280       1290       1300       1310       1320 
LAMFKKCAKE NIEKEEMERV YEQRKSLLDM RTSSNKKSNG SDENDGEKVN RDAVDLLISK 

      1330       1340       1350       1360       1370 
LREVKKDPEP LRRRKSTKLN EIAINVHEGD VKTRKDEDHV LLERTHAMLN DIQNI 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae."
Imamura H., Tanaka K., Hihara T., Umikawa M., Kamei T., Takahashi K., Sasaki T., Takai Y.
EMBO J. 16:2745-2755(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"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].
[5]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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-621 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38059 Genomic DNA. Translation: CAA86119.1.
BK006942 Genomic DNA. Translation: DAA08393.1.
PIRS48375.
RefSeqNP_012107.1. NM_001179507.1.

3D structure databases

ProteinModelPortalP40450.
SMRP40450. Positions 870-1281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34833. 110 interactions.
DIPDIP-817N.
IntActP40450. 18 interactions.
MINTMINT-606495.
STRING4932.YIL159W.

Proteomic databases

PaxDbP40450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL159W; YIL159W; YIL159W.
GeneID854647.
KEGGsce:YIL159W.

Organism-specific databases

CYGDYIL159w.
SGDS000001421. BNR1.

Phylogenomic databases

eggNOGNOG281286.
GeneTreeENSGT00710000107854.
HOGENOMHOG000095249.
KOK17971.
OMACAKENIE.
OrthoDBEOG7G4QPH.

Enzyme and pathway databases

BioCycYEAST:G3O-31407-MONOMER.

Gene expression databases

GenevestigatorP40450.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR015425. FH2_Formin.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PfamPF02181. FH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977190.

Entry information

Entry nameBNR1_YEAST
AccessionPrimary (citable) accession number: P40450
Secondary accession number(s): D6VVC7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families