BNI1/YNL271C Protein Information

Standard Name	Bni1p
Systematic Name	Ynl271cp
Alias	Ppf3p 1 , She5p 2
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 BNR1 (3, 4, 5, 6, 7)
Name Description	Bud Neck Involved 8

Experimental Data
Molecules/cell	166 9

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,953
Molecular Weight (Da)	219,672
Isoelectric Point (pI)	6.49

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Bni1p (InterPro)
Physical Interactions	There are 79 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000006BA96 \| P41832 MIPS: YNL271C NCBI: 1045237 \| 1302334 \| 1705492 \| 2253185 \| 2447041 \| 330443692 \| 347595809 \| 47169356 \| 47169357 \| 47169358 \| 472525 \| 60594133 \| NP_014128.2 GenBank/EMBL/DDBJ: DAA10289.2 \| D38411 \| L31766 \| X92494 \| Z71546 \| Z71547

Amino Acid Sequence (or in FASTA format)
1 MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ 51 HSPVGNEVST SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM 101 NGKLSGDVPV SSQHARSHSM QSKYSYSKRN SSQASNKLTR QHTGQSHSAS 151 SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY EVEVLFEDIM YKRNIFQSLS 201 EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA SRTSMASDHH 251 PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK 301 LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL 351 TSDEMKDLWV TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT 401 KELLEKENSF FKCFRVLSML SQGLYEFSTH RLMTDTVAEG LFSTKLATRK 451 MATEIFVCML EKKNKSRFEA VLTSLDKKFR IGQNLHMIQN FKKMPQYFSH 501 LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG GGENAILEYC 551 QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ 601 IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL 651 VSLVQHLFLS SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM 701 NMAIQRLYDA MQTDEVARRA ILESRALTKK LEEIQAERDS LSEKLSKAEH 751 GLVGQLEDEL HERDRILAKN QRVMQQLEAE LEELKKKHLL EKHQQEVELR 801 KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ DGLSRAKKDY 851 KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP 901 IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALAEI QMESNDISKF 951 NVEERVNELF NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD 1001 VETEEDANYA SLDPKTYQKK LDEINRITDQ LLDIQTQTEH EIQVEEDGES 1051 DLSSSSSDDE SEEIYQDASP TQELRSEHSE LSSGSGPGSF LDALSQKYGT 1101 GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS SAPYLEELTQ 1151 KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG 1201 RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP 1251 AKLFGESLEK EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG 1301 ETPPPPPLPS VLSSSTDGVI PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK 1351 YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE KFADDLYEKG VLADLEKAFA 1401 AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS VADLVKKILN 1451 CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP 1501 EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR 1551 KVDKAVSALQ ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI 1601 KDTTNSMTFL NYVEKIVRLN YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK 1651 DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV LIKTLPVLPE ARKKGDLLED 1701 EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY KKAQAQNLAA 1751 EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV 1801 MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG 1851 SILYSPEAMD PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE 1901 EISDRARMLL KELRGSDTPV KQNSILDEHL EKLRARKERS IGEASTGNRL 1951 SFK*

Amino Acid Sequence (or in FASTA format)

       1  MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ
      51  HSPVGNEVST SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM
     101  NGKLSGDVPV SSQHARSHSM QSKYSYSKRN SSQASNKLTR QHTGQSHSAS
     151  SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY EVEVLFEDIM YKRNIFQSLS
     201  EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA SRTSMASDHH
     251  PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK
     301  LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL
     351  TSDEMKDLWV TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT
     401  KELLEKENSF FKCFRVLSML SQGLYEFSTH RLMTDTVAEG LFSTKLATRK
     451  MATEIFVCML EKKNKSRFEA VLTSLDKKFR IGQNLHMIQN FKKMPQYFSH
     501  LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG GGENAILEYC
     551  QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ
     601  IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL
     651  VSLVQHLFLS SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM
     701  NMAIQRLYDA MQTDEVARRA ILESRALTKK LEEIQAERDS LSEKLSKAEH
     751  GLVGQLEDEL HERDRILAKN QRVMQQLEAE LEELKKKHLL EKHQQEVELR
     801  KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ DGLSRAKKDY
     851  KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP
     901  IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALAEI QMESNDISKF
     951  NVEERVNELF NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD
    1001  VETEEDANYA SLDPKTYQKK LDEINRITDQ LLDIQTQTEH EIQVEEDGES
    1051  DLSSSSSDDE SEEIYQDASP TQELRSEHSE LSSGSGPGSF LDALSQKYGT
    1101  GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS SAPYLEELTQ
    1151  KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG
    1201  RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP
    1251  AKLFGESLEK EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG
    1301  ETPPPPPLPS VLSSSTDGVI PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK
    1351  YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE KFADDLYEKG VLADLEKAFA
    1401  AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS VADLVKKILN
    1451  CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP
    1501  EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR
    1551  KVDKAVSALQ ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI
    1601  KDTTNSMTFL NYVEKIVRLN YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK
    1651  DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV LIKTLPVLPE ARKKGDLLED
    1701  EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY KKAQAQNLAA
    1751  EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV
    1801  MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG
    1851  SILYSPEAMD PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE
    1901  EISDRARMLL KELRGSDTPV KQNSILDEHL EKLRARKERS IGEASTGNRL
    1951  SFK*

external links for Bni1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Bni1p

1)	Yorihuzi T and Ohsumi Y (1994) Saccharomyces cerevisiae MATa mutant cells defective in pointed projection formation in response to alpha-factor at high concentrations. Yeast 10(5):579-94
2)	Jansen RP, et al. (1996) Mother cell-specific HO expression in budding yeast depends on the unconventional myosin myo4p and other cytoplasmic proteins. Cell 84(5):687-97
3)	Chang F and Peter M (2002) Cell biology. Formins set the record straight. Science 297(5581):531-2
4)	Pruyne D, et al. (2002) Role of formins in actin assembly: nucleation and barbed-end association. Science 297(5581):612-5
5)	Sagot I, et al. (2002) An actin nucleation mechanism mediated by Bni1 and profilin. Nat Cell Biol 4(8):626-31
6)	Lew DJ (2002) Formin' actin filament bundles. Nat Cell Biol 4(2):E29-30
7)	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
8)	Zahner JE, et al. (1996) Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Mol Cell Biol 16(4):1857-70
9)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41