BOI2_YEAST
ID BOI2_YEAST Reviewed; 1040 AA.
AC P39969; D3DM20;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Protein BOI2;
DE AltName: Full=Protein BEB1;
GN Name=BOI2; Synonyms=BEB1; OrderedLocusNames=YER114C;
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].
RX PubMed=8666671; DOI=10.1083/jcb.133.4.865;
RA Matsui Y., Matsui R., Akada R., Toh-e A.;
RT "Yeast src homology region 3 domain-binding proteins involved in bud
RT formation.";
RL J. Cell Biol. 133:865-878(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-28; SER-450; SER-519;
RP SER-523 AND SER-652, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-519 AND SER-546, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-24; SER-519; SER-523
RP AND SER-546, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Binds to the BEM1 protein. Involved in bud formation.
CC -!- INTERACTION:
CC P39969; P29366: BEM1; NbExp=6; IntAct=EBI-3727, EBI-3508;
CC P39969; P40077: DSE1; NbExp=3; IntAct=EBI-3727, EBI-22676;
CC P39969; P40020: FIR1; NbExp=2; IntAct=EBI-3727, EBI-13431;
CC P39969; Q03780: YDR239C; NbExp=2; IntAct=EBI-3727, EBI-30094;
CC P39969; P40095: YER158C; NbExp=3; IntAct=EBI-3727, EBI-22734;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D38310; BAA07427.1; -; Genomic_DNA.
DR EMBL; U18916; AAC03212.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07774.1; -; Genomic_DNA.
DR PIR; S50617; S50617.
DR RefSeq; NP_011039.1; NM_001179004.1.
DR AlphaFoldDB; P39969; -.
DR SMR; P39969; -.
DR BioGRID; 36859; 127.
DR DIP; DIP-2227N; -.
DR IntAct; P39969; 34.
DR MINT; P39969; -.
DR STRING; 4932.YER114C; -.
DR CarbonylDB; P39969; -.
DR iPTMnet; P39969; -.
DR MaxQB; P39969; -.
DR PaxDb; P39969; -.
DR PRIDE; P39969; -.
DR EnsemblFungi; YER114C_mRNA; YER114C; YER114C.
DR GeneID; 856850; -.
DR KEGG; sce:YER114C; -.
DR SGD; S000000916; BOI2.
DR VEuPathDB; FungiDB:YER114C; -.
DR eggNOG; ENOG502QPMX; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_003845_0_0_1; -.
DR InParanoid; P39969; -.
DR OMA; HYFQVDN; -.
DR BioCyc; YEAST:G3O-30278-MON; -.
DR PRO; PR:P39969; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39969; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISS:SGD.
DR GO; GO:0007015; P:actin filament organization; IGI:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IGI:SGD.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0001881; P:receptor recycling; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IGI:SGD.
DR CDD; cd11886; SH3_BOI; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035551; Boi1/2_SH3.
DR InterPro; IPR045188; Boi1/Boi2-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22902; PTHR22902; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1040
FT /note="Protein BOI2"
FT /id="PRO_0000064970"
FT DOMAIN 43..107
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 266..330
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 768..887
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 733
FT /note="G -> A (in Ref. 1; BAA07427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1040 AA; 115688 MW; 2DC635B1A34E7479 CRC64;
MSNDREVPTL SQLNTTVSRD KDVSDTLSPD FDSKGSATGR DGGNFPMYIA INEYFKRMED
ELDMKPGDKI KVITDDEEYK DGWYFGRNLR TNEEGLYPVV FTQKITVEKA PTLMRAKSTK
RIYSPLTNED PLLSSTFISE NDSNSELPTP QPIETAASIS RTANGKIERN LSLKNTMSDI
DNALLEFKDD SIGPPDRFIN SGRDEEHSIT HETILSATDG LDVVESNSKP TTSSSTGFLN
GDLENQATLI NGIDTTKLNP VEAEFWSPEE ITAYFIMEGY DVQSASRFQK HKISGKILLE
LELVHLKELD INSFGTRFEI FKEIEKIKEA IRTNGRSLNR ASKTNNANIY NQLMPPANVD
QRASYRGHVR KTSQSLEDLP SQQNFIPTPR NTRNSSASKH RPKSLVFDSQ EANANIAPDV
QIPQVVEEMA GNENLFVSPR RAPKPPSYPS PAQPPKSPLL NNTRTSPSPA QLYSWQSPTL
SFSGPKRTSY IDQYSSSDSN FNSRSALPKN NQGGGKALSP IPSPTRNSVR NEDSEGKLTS
SSKRNSVPYY GYAPESSSDR KSSCSSHEEE QFQETMNTFE RPTSSIYADG STIASISNDK
LAHEKEGKKK PTRHSSSLSS KSKSDSRRNS SLKRSSSASR TSSFKKSSFM LSPFRQQFTD
NAARSSSPEE NPITSMPSEK NSSPIVDKKS SKKSRSKRRS VSAKEAEIFT ETVKDDKNKR
SASEAIKGET LKGKSLRQMT ARPVAKKKQT SAFIEGLRSI SVKEAMKDAD FSGWMSKKGS
GAMSTWKTRF FTLHGTRLSY FSSTTDTRER GLIDITAHRV VPAKEDDKLV SLYAASTGKG
RYCFKLLPPQ PGSKKGLTFT QPRTHYFAVD NKEEMRGWMA ALIKTTIDID TSVPIISSYT
TPTVSLSKAQ EMLAEAREET KLREQQMLEN EEDEDQFLWD QQQLQQQQHD NNQGQADRTI
SASTQRTSDE DNTISTPNLS SANNTTIGSN GFSSPFLLAS GLLSPGVARN SSMRGTEKKG
KFSTEEDYFG DNSKHKTDKI
