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   27-MAR-2024, entry version 204.
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; 134.
DR   DIP; DIP-2227N; -.
DR   IntAct; P39969; 34.
DR   MINT; P39969; -.
DR   STRING; 4932.YER114C; -.
DR   CarbonylDB; P39969; -.
DR   GlyGen; P39969; 16 sites, 1 O-linked glycan (16 sites).
DR   iPTMnet; P39969; -.
DR   MaxQB; P39969; -.
DR   PaxDb; 4932-YER114C; -.
DR   PeptideAtlas; P39969; -.
DR   EnsemblFungi; YER114C_mRNA; YER114C; YER114C.
DR   GeneID; 856850; -.
DR   KEGG; sce:YER114C; -.
DR   AGR; SGD:S000000916; -.
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; YYGWMKK; -.
DR   OrthoDB; 164125at2759; -.
DR   BioCyc; YEAST:G3O-30278-MONOMER; -.
DR   BioGRID-ORCS; 856850; 0 hits in 10 CRISPR screens.
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; cd13316; PH_Boi; 1.
DR   CDD; cd09535; SAM_BOI-like_fungal; 1.
DR   CDD; cd11886; SH3_BOI; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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:SF27; INOSITOL PHOSPHATASE INTERACTING PROTEIN, ISOFORM A; 1.
DR   PANTHER; PTHR22902; SESQUIPEDALIAN; 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; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//