Reviewed, UniProtKB/Swiss-Prot P41832 (BNI1_YEAST)

Names and origin

Protein names

Recommended name:
    Protein BNI1
Alternative name(s):
    Synthetic lethal 39
    Sensitive to high expression protein 5

Gene names

Name:	BNI1
Synonyms:	PPF3, SHE5
Ordered Locus Names:	YNL271C
ORF Names:	N0646

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1953 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-actin. May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members. Ref.5 Ref.6
Subunit structure	Homodimer, and possibly also homotetramer. Interacts with PFY1 via the FH1 domain and with actin via the FH2 domain. Ref.6 Ref.12
Subcellular location	Cell membrane. Cell projection › ruffle membrane. Cytoplasm › cytoskeleton.
Miscellaneous	Each FH2 dimer contains binding sites for 4 actin molecules. Present with 166 molecules/cell in log phase SD medium. Ref.7
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
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Domain	Coiled coil
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: SGD actin nucleation Inferred from direct assay. Source: SGD bipolar cellular bud site selection Traceable author statement. Source: SGD budding cell bud growth Traceable author statement. Source: SGD establishment of mitotic spindle orientation Ref.5 Inferred from mutant phenotype. Source: SGD intracellular mRNA localization Inferred from mutant phenotype. Source: SGD mating type switching Inferred from mutant phenotype. Source: SGD pheromone-dependent signal transduction involved in conjugation with cellular fusion Inferred from mutant phenotype. Source: SGD pseudohyphal growth Inferred from mutant phenotype. Source: SGD regulation of initiation of mating projection growth Inferred from mutant phenotype. Source: SGD regulation of protein localization Inferred from mutant phenotype. Source: SGD regulation of termination of mating projection growth Inferred from mutant phenotype. Source: SGD response to osmotic stress Traceable author statement. Source: SGD
Cellular component	actin cap Traceable author statement. Source: SGD actin filament Inferred from direct assay. Source: SGD cellular bud neck Inferred from direct assay. Source: SGD cellular bud tip Inferred from direct assay. Source: SGD incipient cellular bud site Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD polarisome Traceable author statement. Source: SGD ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	Rho GTPase binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletal regulatory protein binding Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYO3	P36006	2	EBI-3692,EBI-11670
MYO5	Q04439	2	EBI-3692,EBI-11687
NUM1	Q00402	1	EBI-3692,EBI-12386

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1953

1953

Protein BNI1

PRO_0000194899

Regions

Domain

174 – 696

523

GBD/FH3

Domain

1053 – 1337

285

FH1

Domain

1348 – 1766

419

FH2

Domain

1792 – 1826

35

DAD

Coiled coil

712 – 807

96

Potential

Coiled coil

864 – 894

31

Potential

Coiled coil

928 – 981

54

Potential

Coiled coil

1732 – 1811

80

Potential

Compositional bias

64 – 67

4

Poly-Ser

Compositional bias

1053 – 1057

5

Poly-Ser

Compositional bias

1239 – 1250

12

Poly-Pro

Compositional bias

1278 – 1291

14

Poly-Pro

Compositional bias

1303 – 1309

7

Poly-Pro

Compositional bias

1751 – 1754

4

Poly-Glu

Amino acid modifications

Modified residue

272

1

Phosphoserine Ref.11

Modified residue

311

1

Phosphoserine Ref.11 Ref.9 Ref.10

Modified residue

325

1

Phosphoserine Ref.11

Modified residue

328

1

Phosphothreonine Ref.11

Modified residue

1076

1

Phosphoserine Ref.10

Modified residue

1079

1

Phosphoserine Ref.11

Modified residue

1085

1

Phosphoserine Ref.10

Modified residue

1141

1

Phosphoserine Ref.11

Modified residue

1170

1

Phosphoserine Ref.11 Ref.9

Modified residue

1175

1

Phosphoserine Ref.11

Modified residue

1302

1

Phosphothreonine Ref.11

Modified residue

1338

1

Phosphoserine Ref.11 Ref.9 Ref.8

Modified residue

1344

1

Phosphoserine Ref.9

Modified residue

1873

1

Phosphothreonine Ref.11

Modified residue

1877

1

Phosphothreonine Ref.11

Modified residue

1889

1

Phosphoserine Ref.11 Ref.10

Experimental info

Sequence conflict

938

1

T → A Ref.1

Sequence conflict

938

1

T → A Ref.2

Sequence conflict

1430

1

G → C in AAA34455. Ref.1

Secondary structure

1

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1953

Helix Strand Turn

Details...

Beta strand

1371 – 1373

3

Helix

1378 – 1388

11

Helix

1391 – 1396

6

Helix

1423 – 1431

9

Helix

1434 – 1436

3

Helix

1441 – 1449

9

Helix

1453 – 1456

4

Helix

1459 – 1464

6

Helix

1468 – 1471

4

Helix

1475 – 1481

7

Helix

1482 – 1484

3

Turn

1494 – 1496

3

Helix

1504 – 1506

3

Helix

1509 – 1516

8

Turn

1517 – 1524

8

Helix

1525 – 1535

11

Helix

1538 – 1560

23

Helix

1563 – 1579

17

Helix

1591 – 1598

8

Beta strand

1603 – 1608

6

Helix

1609 – 1618

10

Helix

1627 – 1629

3

Helix

1633 – 1636

4

Turn

1637 – 1639

3

Helix

1642 – 1665

24

Beta strand

1666 – 1669

4

Helix

1681 – 1683

3

Turn

1684 – 1686

3

Helix

1687 – 1715

29

Helix

1723 – 1745

23

Helix

1747 – 1750

4

Turn

1751 – 1753

3

Beta strand

1754 – 1762

9

Sequences

	Sequence		Length	Mass (Da)
	P41832-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: A85A994780A5858E	FASTA	1,953	219,703
	10 20 30 40 50 60 MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ HSPVGNEVST 70 80 90 100 110 120 SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM NGKLSGDVPV SSQHARSHSM 130 140 150 160 170 180 QSKYSYSKRN SSQASNKLTR QHTGQSHSAS SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY 190 200 210 220 230 240 EVEVLFEDIM YKRNIFQSLS EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA 250 260 270 280 290 300 SRTSMASDHH PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK 310 320 330 340 350 360 LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL TSDEMKDLWV 370 380 390 400 410 420 TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT KELLEKENSF FKCFRVLSML 430 440 450 460 470 480 SQGLYEFSTH RLMTDTVAEG LFSTKLATRK MATEIFVCML EKKNKSRFEA VLTSLDKKFR 490 500 510 520 530 540 IGQNLHMIQN FKKMPQYFSH LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG 550 560 570 580 590 600 GGENAILEYC QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ 610 620 630 640 650 660 IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL VSLVQHLFLS 670 680 690 700 710 720 SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM NMAIQRLYDA MQTDEVARRA 730 740 750 760 770 780 ILESRALTKK LEEIQAERDS LSEKLSKAEH GLVGQLEDEL HERDRILAKN QRVMQQLEAE 790 800 810 820 830 840 LEELKKKHLL EKHQQEVELR KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ 850 860 870 880 890 900 DGLSRAKKDY KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP 910 920 930 940 950 960 IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALTEI QMESNDISKF NVEERVNELF 970 980 990 1000 1010 1020 NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD VETEEDANYA SLDPKTYQKK 1030 1040 1050 1060 1070 1080 LDEINRITDQ LLDIQTQTEH EIQVEEDGES DLSSSSSDDE SEEIYQDASP TQELRSEHSE 1090 1100 1110 1120 1130 1140 LSSGSGPGSF LDALSQKYGT GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS 1150 1160 1170 1180 1190 1200 SAPYLEELTQ KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG 1210 1220 1230 1240 1250 1260 RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP AKLFGESLEK 1270 1280 1290 1300 1310 1320 EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG ETPPPPPLPS VLSSSTDGVI 1330 1340 1350 1360 1370 1380 PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE 1390 1400 1410 1420 1430 1440 KFADDLYEKG VLADLEKAFA AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS 1450 1460 1470 1480 1490 1500 VADLVKKILN CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP 1510 1520 1530 1540 1550 1560 EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR KVDKAVSALQ 1570 1580 1590 1600 1610 1620 ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI KDTTNSMTFL NYVEKIVRLN 1630 1640 1650 1660 1670 1680 YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV 1690 1700 1710 1720 1730 1740 LIKTLPVLPE ARKKGDLLED EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY 1750 1760 1770 1780 1790 1800 KKAQAQNLAA EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV 1810 1820 1830 1840 1850 1860 MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG SILYSPEAMD 1870 1880 1890 1900 1910 1920 PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE EISDRARMLL KELRGSDTPV 1930 1940 1950 KQNSILDEHL EKLRARKERS IGEASTGNRL SFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Synthetic lethals of CDC12." Fares H.F., Pringle J.R. Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A yeast gene necessary for proper establishment of cell polarity for growth." Yorihuzi T., Ohsumi Y. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26109 / X2180.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The sequence of a 24,152 bp segment from the left arm of chromosome XIV from Saccharomyces cerevisiae between the BNI1 and the POL2 genes." Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H. Yeast 12:505-514(1996) [PubMed: 8740425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1553. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p." Lee L., Klee S.K., Evangelista M., Boone C., Pellman D. J. Cell Biol. 144:947-961(1999) [PubMed: 10085293] [Abstract] Cited for: FUNCTION.
[6]	"Formin leaky cap allows elongation in the presence of tight capping proteins." Zigmond S.H., Evangelista M., Boone C., Yang C., Dar A.C., Sicheri F., Forkey J., Pring M. Curr. Biol. 13:1820-1823(2003) [PubMed: 14561409] [Abstract] Cited for: FUNCTION, TETRAMERIZATION.
[7]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1338, MASS SPECTROMETRY.
[9]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-1170; SER-1338 AND SER-1344, MASS SPECTROMETRY.
[10]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-1076; SER-1085 AND SER-1889, MASS SPECTROMETRY.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-311; SER-325; THR-328; SER-1079; SER-1141; SER-1170; SER-1175; THR-1302; SER-1338; THR-1873; THR-1877 AND SER-1889, MASS SPECTROMETRY.
[12]	"Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture." Xu Y., Moseley J.B., Sagot I., Poy F., Pellman D., Goode B.L., Eck M.J. Cell 116:711-723(2004) [PubMed: 15006353] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1350-1760, DIMERIZATION.
[13]	"Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain." Otomo T., Tomchick D.R., Otomo C., Panchal S.C., Machius M., Rosen M.K. Nature 433:488-494(2005) [PubMed: 15635372] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1327-1769 IN COMPLEX WITH ATP AND ACTIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L31766 Genomic DNA. Translation: AAA34455.1.
D38411 Genomic DNA. Translation: BAA22512.1.
Z71546 Genomic DNA. Translation: CAA96178.1.
Z71547 Genomic DNA. Translation: CAA96179.1.
X92494 Genomic DNA. Translation: CAA63225.1.

PIR

S63244.

RefSeq

NP_014128.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UX4	X-ray	3.30	A/B	1352-1765	[»]
1UX5	X-ray	2.50	A	1350-1760	[»]
1Y64	X-ray	3.05	B	1327-1769	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:974N.

IntAct

P41832. 61 interactions.

STRING

P41832.

Proteomic databases

PeptideAtlas

P41832.

PRIDE

P41832.

Genome annotation databases

Ensembl

YNL271C; YNL271C; YNL271C; Saccharomyces cerevisiae. [Genome view]

GeneID

855450.

KEGG

sce:YNL271C.

NMPDR

fig|4932.3.peg.5193.

Organism-specific databases

CYGD

YNL271c.

SGD

S000005215. BNI1.

Phylogenomic databases

HOGENOM

P41832.

OMA

KQLHWEK

OrthoDB

EOG94QVH4

Gene expression databases

ArrayExpress

P41832.

Genevestigator

P41832.

GermOnline

YNL271C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003104. Actin-bd_FH2/DRF_autoreg.
IPR014767. Diaphanous_autoregulatory.
IPR010472. Drf_FH3.
IPR010473. Drf_GTPase_bd.
IPR015425. FH2_actin_bd.
IPR014768. GTPase_bd/formin_homology_3.
[Graphical view]

Pfam

PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]

SMART

SM00498. FH2. 1 hit.
[Graphical view]

PROSITE

PS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

979358.

Entry information

Entry name

BNI1_YEAST

Accession

Primary (citable) accession number: P41832
Secondary accession number(s): O13450

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)