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Protein

Protein BNI1

Gene

BNI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • profilin binding Source: SGD

GO - Biological processi

  • actin filament bundle assembly Source: SGD
  • actin nucleation Source: SGD
  • actomyosin contractile ring actin filament bundle assembly Source: SGD
  • barbed-end actin filament capping Source: SGD
  • budding cell apical bud growth Source: SGD
  • establishment of mitotic spindle orientation Source: SGD
  • formin-nucleated actin cable assembly Source: SGD
  • positive regulation of actin cytoskeleton reorganization Source: SGD
  • regulation of protein localization Source: SGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33265-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BNI1
Alternative name(s):
Pointed projection formation protein 3
Sensitive to high expression protein 5
Synthetic lethal 39
Gene namesi
Name:BNI1
Synonyms:PPF3, SHE5
Ordered Locus Names:YNL271C
ORF Names:N0646
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL271C.
SGDiS000005215. BNI1.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: SGD
  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
  • polarisome Source: SGD
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19531953Protein BNI1PRO_0000194899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei311 – 3111PhosphoserineCombined sources
Modified residuei325 – 3251PhosphoserineCombined sources
Modified residuei1085 – 10851PhosphoserineCombined sources
Modified residuei1170 – 11701PhosphoserineCombined sources
Modified residuei1338 – 13381PhosphoserineCombined sources
Modified residuei1344 – 13441PhosphoserineCombined sources
Modified residuei1918 – 19181PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41832.
PeptideAtlasiP41832.

PTM databases

iPTMnetiP41832.

Interactioni

Subunit structurei

Homodimer, and possibly also homotetramer. Interacts with PFY1 via the FH1 domain and with actin via the FH2 domain.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-3692,EBI-3692
MYO3P360063EBI-3692,EBI-11670

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • profilin binding Source: SGD

Protein-protein interaction databases

BioGridi35569. 410 interactions.
DIPiDIP-974N.
IntActiP41832. 26 interactions.
MINTiMINT-582139.

Structurei

Secondary structure

1
1953
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1371 – 13733Combined sources
Helixi1378 – 138811Combined sources
Helixi1391 – 13988Combined sources
Beta strandi1400 – 14023Combined sources
Helixi1405 – 14139Combined sources
Turni1414 – 14163Combined sources
Helixi1423 – 143210Combined sources
Helixi1434 – 14363Combined sources
Helixi1441 – 14499Combined sources
Turni1450 – 14523Combined sources
Helixi1453 – 14564Combined sources
Helixi1459 – 14646Combined sources
Helixi1468 – 14714Combined sources
Helixi1475 – 14806Combined sources
Helixi1482 – 14843Combined sources
Helixi1494 – 14963Combined sources
Helixi1504 – 15063Combined sources
Helixi1509 – 15168Combined sources
Turni1517 – 15248Combined sources
Helixi1525 – 153511Combined sources
Helixi1538 – 156023Combined sources
Helixi1563 – 157917Combined sources
Helixi1582 – 15843Combined sources
Helixi1591 – 15966Combined sources
Beta strandi1597 – 15993Combined sources
Beta strandi1603 – 16086Combined sources
Helixi1609 – 162012Combined sources
Helixi1622 – 16265Combined sources
Helixi1627 – 16304Combined sources
Helixi1632 – 16376Combined sources
Helixi1642 – 166524Combined sources
Turni1667 – 16693Combined sources
Turni1671 – 16733Combined sources
Helixi1680 – 171536Combined sources
Beta strandi1720 – 17223Combined sources
Helixi1723 – 175735Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UX4X-ray3.30A/B1352-1765[»]
1UX5X-ray2.50A1350-1760[»]
1Y64X-ray3.05B1327-1769[»]
ProteinModelPortaliP41832.
SMRiP41832. Positions 1350-1760.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini174 – 696523GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini1053 – 1337285FH1Add
BLAST
Domaini1348 – 1766419FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1792 – 182635DADPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili712 – 80796Sequence analysisAdd
BLAST
Coiled coili864 – 89431Sequence analysisAdd
BLAST
Coiled coili928 – 98154Sequence analysisAdd
BLAST
Coiled coili1732 – 181180Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi64 – 674Poly-Ser
Compositional biasi1053 – 10575Poly-Ser
Compositional biasi1239 – 125012Poly-ProAdd
BLAST
Compositional biasi1278 – 129114Poly-ProAdd
BLAST
Compositional biasi1303 – 13097Poly-Pro
Compositional biasi1751 – 17544Poly-Glu

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the formin homology family. BNI1 subfamily.Curated
Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00710000107854.
HOGENOMiHOG000095244.
InParanoidiP41832.
KOiK11238.
OMAiIMELFRM.
OrthoDBiEOG7G4QPH.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM01139. Drf_FH3. 1 hit.
SM01140. Drf_GBD. 1 hit.
SM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41832-1 [UniParc]FASTAAdd to basket

« Hide

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

SFK
Length:1,953
Mass (Da):219,673
Last modified:September 21, 2011 - v3
Checksum:i0C5A9D5280A5858F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti938 – 9381A → T in CAA96178 (PubMed:9169873).Curated
Sequence conflicti938 – 9381A → T in CAA96179 (PubMed:9169873).Curated
Sequence conflicti938 – 9381A → T in CAA63225 (PubMed:8740425).Curated
Sequence conflicti1430 – 14301G → C in AAA34455 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BK006947 Genomic DNA. Translation: DAA10289.2.
PIRiS63244.
RefSeqiNP_014128.2. NM_001183109.2.

Genome annotation databases

EnsemblFungiiYNL271C; YNL271C; YNL271C.
GeneIDi855450.
KEGGisce:YNL271C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BK006947 Genomic DNA. Translation: DAA10289.2.
PIRiS63244.
RefSeqiNP_014128.2. NM_001183109.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UX4X-ray3.30A/B1352-1765[»]
1UX5X-ray2.50A1350-1760[»]
1Y64X-ray3.05B1327-1769[»]
ProteinModelPortaliP41832.
SMRiP41832. Positions 1350-1760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35569. 410 interactions.
DIPiDIP-974N.
IntActiP41832. 26 interactions.
MINTiMINT-582139.

PTM databases

iPTMnetiP41832.

Proteomic databases

MaxQBiP41832.
PeptideAtlasiP41832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL271C; YNL271C; YNL271C.
GeneIDi855450.
KEGGisce:YNL271C.

Organism-specific databases

EuPathDBiFungiDB:YNL271C.
SGDiS000005215. BNI1.

Phylogenomic databases

GeneTreeiENSGT00710000107854.
HOGENOMiHOG000095244.
InParanoidiP41832.
KOiK11238.
OMAiIMELFRM.
OrthoDBiEOG7G4QPH.

Enzyme and pathway databases

BioCyciYEAST:G3O-33265-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP41832.
NextBioi979358.
PROiP41832.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM01139. Drf_FH3. 1 hit.
SM01140. Drf_GBD. 1 hit.
SM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Saccharomyces cerevisiae MATa mutant cells defective in pointed projection formation in response to alpha-factor at high concentrations."
    Yorihuzi T., Ohsumi Y.
    Yeast 10:579-594(1994) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 938.
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1553.
    Strain: ATCC 96604 / S288c / FY1679.
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TETRAMERIZATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-1170; SER-1338 AND SER-1344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-311 AND SER-1170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-325; SER-1085; SER-1170 AND THR-1918, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1327-1769 IN COMPLEX WITH ATP AND ACTIN.

Entry informationi

Entry nameiBNI1_YEAST
AccessioniPrimary (citable) accession number: P41832
Secondary accession number(s): D6W0S3, O13450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 21, 2011
Last modified: May 11, 2016
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Each FH2 dimer contains binding sites for 4 actin molecules.
Present with 166 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.