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Protein

Protein BNI4

Gene

BNI4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

  • asymmetric protein localization Source: SGD
  • barrier septum assembly Source: SGD
  • chitin biosynthetic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33233-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BNI4
Gene namesi
Name:BNI4
Ordered Locus Names:YNL233W
ORF Names:N1146
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL233W.
SGDiS000005177. BNI4.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • cellular bud neck septin collar Source: SGD
  • incipient cellular bud site Source: SGD
  • septin ring Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 892892Protein BNI4PRO_0000064959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei364 – 3641PhosphoserineCombined sources
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei410 – 4101PhosphothreonineCombined sources
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei500 – 5001PhosphoserineCombined sources
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei618 – 6181PhosphoserineCombined sources
Modified residuei703 – 7031PhosphothreonineCombined sources
Modified residuei746 – 7461PhosphoserineCombined sources
Modified residuei825 – 8251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53858.

PTM databases

iPTMnetiP53858.

Interactioni

Subunit structurei

May interact with CHS3 and seems to be an adaptor (along with SKT5) to link CHS3 to septins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GLC7P325984EBI-3704,EBI-13715
HSP82P028292EBI-3704,EBI-8659

Protein-protein interaction databases

BioGridi35605. 127 interactions.
DIPiDIP-1338N.
IntActiP53858. 11 interactions.
MINTiMINT-410655.

Structurei

3D structure databases

ProteinModelPortaliP53858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 1298Poly-Glu
Compositional biasi290 – 2934Poly-Lys
Compositional biasi321 – 3244Poly-Ser
Compositional biasi344 – 3496Poly-Ser

Phylogenomic databases

HOGENOMiHOG000095245.
InParanoidiP53858.
KOiK18638.
OMAiFENEDFN.
OrthoDBiEOG7RFTRP.

Sequencei

Sequence statusi: Complete.

P53858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSISDSKS SELLNSTFYS STSINTLDHA RTFRNSLILK EISDQSLNSS
60 70 80 90 100
IKPCESVLDR DVESSVLQRS FGESNARDSE VQTVNMTTSP SLSALADILN
110 120 130 140 150
ERSKYADQKT RKAQNIESSI IEEEEEAEEQ NNSINYHEDI TGSRLSVREE
160 170 180 190 200
ANENLAMTSP NLIDIDGSNS IQVAPLSLPS FEEPDFLSTP RVKPDSQGPR
210 220 230 240 250
SKVSTRRTIL ERDNNLPVKR EENTIINSET ESTTHSAPFL KEDPKPSPPS
260 270 280 290 300
SKLYNPKVRL NKAEARKYTD SSAQRTTSAG SVLEDTSMHK KKKSIFSFLK
310 320 330 340 350
KKEPKPVIGN NSVTNEKNKM SSSSTFSMNI QTSLKTPEKL KKKSHSSSSI
360 370 380 390 400
FNSFLKGKIE TSDSPRKEPM RQKKRTPKSK DKKQDTEQII DAASVLSTES
410 420 430 440 450
PLLRKNHDDT PVKIDHVTRS IDQRKPTPLN MDLILGGDKQ INTPLQEHVR
460 470 480 490 500
EDDDAKNDLQ LPTKDNFLSL DYEAPSPAFS KHDTGEVLFP KFLDNHEVDS
510 520 530 540 550
IVSLERTRST KSNKRSSMNS QRRSLTDTLS IKAQSEGMFI TEASSVVLST
560 570 580 590 600
PDLTKSPASS ILKNGRFEYS DNFSREHSYE GTTNEDFLDI KDDSGPLKKD
610 620 630 640 650
DIFLESIEQK FDQLVMASDE EKTEVERDVP KPREEPLKKD SERQSVFADD
660 670 680 690 700
DNELISDIME FASFINFGDD DLNLDLDLGD TTASYATETP EPVGNDEVNR
710 720 730 740 750
SGTFDTRNNK EDSYKERETQ SYSAAGATTY GDERQGQLHT FEQDGSEIND
760 770 780 790 800
NEFENEDFNK HIEQPIEVTP RNNAYLPEFE PNRPVSMSFK GLKAPRMNTS
810 820 830 840 850
FIDSMTPDSP VKSDLTSLGE VYVNSNNDQG VRFSSQIILY DTYGEFEYDR
860 870 880 890
HPEISTCNQL TPQLAQMIKL ELNELKSAME VHDDSRCYTH FY
Length:892
Mass (Da):100,590
Last modified:October 1, 1996 - v1
Checksum:i0DF61702AD47B46C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69381 Genomic DNA. Translation: CAA93365.1.
Z71509 Genomic DNA. Translation: CAA96138.1.
BK006947 Genomic DNA. Translation: DAA10325.1.
PIRiS63199.
RefSeqiNP_014166.1. NM_001183071.1.

Genome annotation databases

EnsemblFungiiYNL233W; YNL233W; YNL233W.
GeneIDi855488.
KEGGisce:YNL233W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69381 Genomic DNA. Translation: CAA93365.1.
Z71509 Genomic DNA. Translation: CAA96138.1.
BK006947 Genomic DNA. Translation: DAA10325.1.
PIRiS63199.
RefSeqiNP_014166.1. NM_001183071.1.

3D structure databases

ProteinModelPortaliP53858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35605. 127 interactions.
DIPiDIP-1338N.
IntActiP53858. 11 interactions.
MINTiMINT-410655.

PTM databases

iPTMnetiP53858.

Proteomic databases

MaxQBiP53858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL233W; YNL233W; YNL233W.
GeneIDi855488.
KEGGisce:YNL233W.

Organism-specific databases

EuPathDBiFungiDB:YNL233W.
SGDiS000005177. BNI4.

Phylogenomic databases

HOGENOMiHOG000095245.
InParanoidiP53858.
KOiK18638.
OMAiFENEDFN.
OrthoDBiEOG7RFTRP.

Enzyme and pathway databases

BioCyciYEAST:G3O-33233-MONOMER.

Miscellaneous databases

NextBioi979466.
PROiP53858.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
    Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
    Yeast 12:1071-1076(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall."
    DeMarini D.J., Adams A.E., Fares H., De Virgilio C., Valle G., Chuang J.S., Pringle J.R.
    J. Cell Biol. 139:75-93(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, SUBUNIT.
  5. "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-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-476; SER-503; SER-618; THR-703; SER-746 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-43; SER-133; SER-281; SER-394; THR-410; SER-476; SER-500; SER-503 AND SER-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBNI4_YEAST
AccessioniPrimary (citable) accession number: P53858
Secondary accession number(s): D6W0V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. 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.