BNI5_YEAST
ID BNI5_YEAST Reviewed; 448 AA.
AC P53890; D6W116;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Bud neck protein 5;
GN Name=BNI5; OrderedLocusNames=YNL166C; ORFNames=N1706;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE GIN4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12058072; DOI=10.1091/mbc.01-10-0500;
RA Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.;
RT "Cell cycle-dependent assembly of a Gin4-septin complex.";
RL Mol. Biol. Cell 13:2091-2105(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH CDC11 AND
RP CDC12.
RX PubMed=12215547; DOI=10.1128/mcb.22.19.6906-6920.2002;
RA Lee P.R., Song S., Ro H.-S., Park C.J., Lippincott J., Li R., Pringle J.R.,
RA De Virgilio C., Longtine M.S., Lee K.S.;
RT "Bni5p, a septin-interacting protein, is required for normal septin
RT function and cytokinesis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 22:6906-6920(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-270; TYR-344;
RP SER-346 AND SER-350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-194 AND SER-340, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-194; THR-257;
RP SER-270; SER-273; THR-274; SER-332; SER-346 AND SER-350, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for normal septin function and cytokinesis.
CC {ECO:0000269|PubMed:12215547}.
CC -!- SUBUNIT: Component of the GIN4 complex composed of at least BNI5, CDC3,
CC CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Interacts directly with CDC11
CC and CDC12. {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:12215547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Bud. Note=Arrives at the bud site
CC approximately coincident with bud emergence and dissociates from the
CC septin scaffold before cytokinesis.
CC -!- INDUCTION: Expression peaks during S phase of the cell cycle.
CC {ECO:0000269|PubMed:12215547}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X92517; CAA63273.1; -; Genomic_DNA.
DR EMBL; Z71442; CAA96053.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10382.1; -; Genomic_DNA.
DR PIR; S60961; S60961.
DR RefSeq; NP_014233.1; NM_001183004.1.
DR AlphaFoldDB; P53890; -.
DR SMR; P53890; -.
DR BioGRID; 35662; 82.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-4333N; -.
DR IntAct; P53890; 4.
DR MINT; P53890; -.
DR STRING; 4932.YNL166C; -.
DR iPTMnet; P53890; -.
DR MaxQB; P53890; -.
DR PaxDb; P53890; -.
DR PRIDE; P53890; -.
DR EnsemblFungi; YNL166C_mRNA; YNL166C; YNL166C.
DR GeneID; 855555; -.
DR KEGG; sce:YNL166C; -.
DR SGD; S000005110; BNI5.
DR VEuPathDB; FungiDB:YNL166C; -.
DR eggNOG; ENOG502S1ET; Eukaryota.
DR HOGENOM; CLU_050570_0_0_1; -.
DR InParanoid; P53890; -.
DR OMA; NEYNHES; -.
DR BioCyc; YEAST:G3O-33182-MON; -.
DR PRO; PR:P53890; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53890; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0032035; F:myosin II tail binding; IPI:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IGI:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ComplexPortal.
DR GO; GO:0072741; P:protein localization to cell division site; IMP:SGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..448
FT /note="Bud neck protein 5"
FT /id="PRO_0000203411"
FT REGION 63..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 344
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 448 AA; 49694 MW; 4861981BE3E15E21 CRC64;
MGLDQDKIKK RLSQIEIDIN QMNQMIDENL QLVEPAEDEA VEDNVKDTGV VDAVKVAETA
LFSGNDGADS NPGDSAQVEE HKTAQVHIPT ENEANKSTDD PSQLSVTQPF IAKEQITHTA
IAIGDSYNSF VANSAGNEKA KDSCTENKED GTVNIDQNRG EADVEIIENN DDEWEDEKSD
VEEGRVDKGT EENSEIESFK SPMPQNNTLG GENKLDAELV LDKFSSANKD LDIQPQTIVV
GGDNEYNHES SRLADQTPHD DNSENCPNRS GGSTPLDSQT KIFIPKKNSK EDGTNINHFN
SDGDGQKKMA NFETRRPTNP FRVISVSSNS NSRNGSRKSS LNKYDSPVSS PITSASELGS
IAKLEKRHDY LSMKCIKLQK EIDYLNKMNA QGSLSMEDGK RLHRAVVKLQ EYLDKKTKEK
YEVGVLLSRH LRKQIDRGEN GQFWIGTK
