BNR1/YIL159W Protein Information Help

Standard Name Bnr1p 1
Systematic Name Yil159wp
ORF Classification Verified
Description Formin, nucleates the formation of linear actin filaments, involved in cell processes such as budding and mitotic spindle orientation which require the formation of polarized actin cables, functionally redundant with BNI1 (2)
Name Description BNi1 Related 1
Experimental Data
Molecules/cell 259 3
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,375
Molecular Weight (Da) 156,850
Isoelectric Point (pI) 7.94

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Bnr1p (InterPro)
Physical Interactions There are 71 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000126A45 | P40450
MIPS: YIL159W
NCBI: 557764 | 6322032 | 731888 | NP_012107.1
GenBank/EMBL/DDBJ: DAA08393.1 | Z38059
Amino Acid Sequence (or in FASTA format)
 
       1  MDSSPNKKTY RYPRRSLSLH ARDRVSEARK LEELNLNDGL VAAGLQLVGV
      51  ALEKQGTGSH IYMKQKNFSA NDVSSSPMVS EEVNGSEMDF NPKCMPQDAS
     101  LVERMFDELL KDGTFFWGAA YKNLQNISLR RKWLLICKIR SSNHWGKKKV
     151  TSSTTYSTHL ATNELAENAH FLDGLVRNLS TGGMKLSKAL YKLEKFLRKQ
     201  SFLQLFLKDE IYLTTLIEKT LPLISKELQF VYLRCFKILM NNPLARIRAL
     251  HSEPLIRWFT ELLTDQNSNL KCQLLSMELL LLLTYVEGST GCELIWDQLS
     301  ILFTDWLEWF DKILADDIAI HSSLYLNWNQ LKIDYSTTFL LLINSILQGF
     351  NNKTALEILN FLKKNNIHNT ITFLELAYKD DPNSVVIMEQ IKQFKSKESA
     401  IFDSMIKTTN DTNSLHPTKD IARIESEPLC LENCLLLKAK DSPVEAPINE
     451  IIQSLWKILD SQKPYSESIK LLKLINSLLF YLIDSFQVST NPSFDETLES
     501  AENVDYVFQD SVNKLLDSLQ SDEIARRAVT EIDDLNAKIS HLNEKLNLVE
     551  NHDKDHLIAK LDESESLISL KTKEIENLKL QLKATKKRLD QITTHQRLYD
     601  QPPSLASSNL SIAGSIIKNN SHGNIIFQNL AKKQQQQQKI SLPKRSTSLL
     651  KSKRVTSLSS YLTDANNENE SQNESEDKSK DSLFQRSTST INFNIPSMKN
     701  ITNMQNVSLN SILSELEFSN SLGTQPNYQS SPVLSSVSSS PKLFPRLSSD
     751  SLDNGIQLVP EVVKLPQLPP PPPPPPPPPL PQSLLTEAEA KPDGVSCIAA
     801  PAPPPLPDLF KTKTCGAVPP PPPPPPLPES LSMNKGPSNH DLVTPPAPPL
     851  PNGLLSSSSV SINPTTTDLK PPPTEKRLKQ IHWDKVEDIK DTLWEDTFQR
     901  QETIKELQTD GIFSQIEDIF KMKSPTKIAN KRNAESSIAL SSNNGKSSNE
     951  LKKISFLSRD LAQQFGINLH MFSQLSDMEF VMKVLNCDND IVQNVNILKF
    1001  FCKEELVNIP KSMLNKYEPY SQGKDGKAVS DLQRADRIFL ELCINLRFYW
    1051  NARSKSLLTL STYERDYYDL IFKLQKIDDA ISHLNRSPKF KSLMFIITEI
    1101  GNHMNKRIVK GIKLKSLTKL AFVRSSIDQN VSFLHFIEKV IRIKYPDIYG
    1151  FVDDLKNIED LGKISLEHVE SECHEFHKKI EDLVTQFQVG KLSKEENLDP
    1201  RDQIIKKVKF KINRAKTKSE LLIGQCKLTL IDLNKLMKYY GEDPKDKESK
    1251  NEFFQPFIEF LAMFKKCAKE NIEKEEMERV YEQRKSLLDM RTSSNKKSNG
    1301  SDENDGEKVN RDAVDLLISK LREVKKDPEP LRRRKSTKLN EIAINVHEGD
    1351  VKTRKDEDHV LLERTHAMLN DIQNI*

external links for Bnr1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
YGOB BioPIXIE MIPS YeastGFP
YOGY CYC2008 (complexes) Pfam domains YeastRC Public Image Repository

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Bnr1p
1) Imamura H, et al.  (1997) Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J 16(10):2745-55
2) Dong Y, et al.  (2003) Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. J Cell Biol 161(6):1081-92
3) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41