BNI1-related protein 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
BNI1-related protein 1

Gene names

Name:	BNR1
Ordered Locus Names:	YIL159W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1375 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	barbed-end actin filament capping Inferred from direct assay PubMed 15923184. Source: SGD formin-nucleated actin cable assembly Inferred from direct assay PubMed 15923184. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay PubMed 9774458. Source: SGD
Molecular_function	profilin binding Inferred from mutant phenotype PubMed 15923184. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
HOF1	Q05080	3	EBI-3711,EBI-5412
MYO3	P36006	4	EBI-3711,EBI-11670
MYO5	Q04439	3	EBI-3711,EBI-11687

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1375

1375

BNI1-related protein 1

PRO_0000194900

Regions

Domain

94 – 490

397

GBD/FH3

Domain

659 – 851

193

FH1

Domain

868 – 1290

423

FH2

Domain

1302 – 1336

35

DAD

Coiled coil

520 – 601

82

Potential

Compositional bias

659 – 839

181

Pro-rich

Compositional bias

1332 – 1335

4

Arg/Lys-rich (basic)

Amino acid modifications

Modified residue

18

1

Phosphoserine Ref.6

Modified residue

621

1

Phosphoserine Ref.5

Modified residue

687

1

Phosphoserine Ref.6

Modified residue

936

1

Phosphoserine Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P40450 [UniParc].

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

1,375

156,852

        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

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References

	« Hide 'large scale' referencesShow '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. Barrell B.G. Nature 387:84-87(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]	"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]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, MASS SPECTROMETRY.
[6]	"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-18; SER-687 AND SER-936, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z38059 Genomic DNA. Translation: CAA86119.1. BK006942 Genomic DNA. Translation: DAA08393.1.
PIR	S48375.
RefSeq	NP_012107.1. NM_001179507.1.
3D structure databases
ProteinModelPortal	P40450.
SMR	P40450. Positions 870-1281.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-817N.
IntAct	P40450. 14 interactions.
MINT	MINT-606495.
STRING	4932.YIL159W.
Proteomic databases
PaxDb	P40450.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL159W; YIL159W; YIL159W.
GeneID	854647.
KEGG	sce:YIL159W.
Organism-specific databases
CYGD	YIL159w.
SGD	S000001421. BNR1.
Phylogenomic databases
eggNOG	NOG281286.
GeneTree	ENSGT00700000104395.
HOGENOM	HOG000095249.
OMA	CAKENIE.
OrthoDB	EOG42Z7ZW.
Gene expression databases
Genevestigator	P40450.
GermOnline	YIL159W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003104. Actin-bd_FH2/DRF_autoreg. IPR016024. ARM-type_fold. IPR014767. Diaphanous_autoregulatory. IPR015425. FH2_actin-bd. IPR014768. GTPase-bd/formin_homology_3. [Graphical view]
Pfam	PF02181. FH2. 1 hit. [Graphical view]
SMART	SM00498. FH2. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF101447. FH2_actin_bd. 1 hit.
PROSITE	PS51231. DAD. 1 hit. PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977190.

Entry information

Entry name

BNR1_YEAST

Accession

Primary (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:	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

Relevant documents

Yeast

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

Yeast chromosome IX

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents