ID   BOB1_YEAST              Reviewed;         980 AA.
AC   P38041; D6VPR9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Protein BOB1;
DE   AltName: Full=BEM1-binding protein;
DE   AltName: Full=Growth inhibitory protein 7;
GN   Name=BOI1; Synonyms=BOB1, GIN7; OrderedLocusNames=YBL085W;
GN   ORFNames=YBL0717;
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=8666672; DOI=10.1083/jcb.133.4.879;
RA   Bender L., Lo H.S., Lee H., Kokojan V., Peterson V., Bender A.;
RT   "Associations among PH and SH3 domain-containing proteins and Rho-type
RT   GTPases in Yeast.";
RL   J. Cell Biol. 133:879-894(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7502586; DOI=10.1002/yea.320111112;
RA   Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT   "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT   cerevisiae chromosome II.";
RL   Yeast 11:1103-1112(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-209; SER-528;
RP   SER-644 AND THR-919, 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-735, 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-655, AND IDENTIFICATION BY
RP   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-104; SER-106; SER-128;
RP   THR-151; THR-158; SER-209; SER-393; SER-412; SER-525; SER-528; SER-589;
RP   SER-590; SER-593 AND SER-644, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- FUNCTION: Binds to the BEM1 protein.
CC   -!- INTERACTION:
CC       P38041; P29366: BEM1; NbExp=5; IntAct=EBI-3719, EBI-3508;
CC       P38041; Q00684: CDC14; NbExp=2; IntAct=EBI-3719, EBI-4192;
CC       P38041; P40020: FIR1; NbExp=2; IntAct=EBI-3719, EBI-13431;
CC       P38041; Q08229: NBA1; NbExp=3; IntAct=EBI-3719, EBI-36841;
CC       P38041; Q03780: YDR239C; NbExp=2; IntAct=EBI-3719, EBI-30094;
CC       P38041; P40095: YER158C; NbExp=4; IntAct=EBI-3719, EBI-22734;
CC       P38041; P47115: YJR056C; NbExp=3; IntAct=EBI-3719, EBI-25514;
CC       P38041; P54786: ZDS2; NbExp=3; IntAct=EBI-3719, EBI-29637;
CC   -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L31406; AAB08439.1; -; Genomic_DNA.
DR   EMBL; X79489; CAA56021.1; -; Genomic_DNA.
DR   EMBL; Z35846; CAA84906.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07039.1; -; Genomic_DNA.
DR   PIR; S45444; S45444.
DR   RefSeq; NP_009468.1; NM_001178325.1.
DR   AlphaFoldDB; P38041; -.
DR   SMR; P38041; -.
DR   BioGRID; 32619; 184.
DR   DIP; DIP-2226N; -.
DR   IntAct; P38041; 73.
DR   MINT; P38041; -.
DR   STRING; 4932.YBL085W; -.
DR   GlyGen; P38041; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P38041; -.
DR   MaxQB; P38041; -.
DR   PaxDb; 4932-YBL085W; -.
DR   PeptideAtlas; P38041; -.
DR   EnsemblFungi; YBL085W_mRNA; YBL085W; YBL085W.
DR   GeneID; 852193; -.
DR   KEGG; sce:YBL085W; -.
DR   AGR; SGD:S000000181; -.
DR   SGD; S000000181; BOI1.
DR   VEuPathDB; FungiDB:YBL085W; -.
DR   eggNOG; ENOG502QSRX; Eukaryota.
DR   GeneTree; ENSGT00950000182882; -.
DR   HOGENOM; CLU_003845_0_0_1; -.
DR   InParanoid; P38041; -.
DR   OMA; FGDGWWE; -.
DR   OrthoDB; 164125at2759; -.
DR   BioCyc; YEAST:G3O-28974-MONOMER; -.
DR   BioGRID-ORCS; 852193; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P38041; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38041; Protein.
DR   GO; GO:0005933; C:cellular bud; IDA:SGD.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
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; IDA: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; 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   Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..980
FT                   /note="Protein BOB1"
FT                   /id="PRO_0000064968"
FT   DOMAIN          13..77
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          228..292
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          776..895
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          139..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..702
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..720
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         151
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         528
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         655
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         919
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
SQ   SEQUENCE   980 AA;  109295 MW;  09F1DD1F9EF30F36 CRC64;
     MSLEGNTLGK GAKSFPLYIA VNQYSKRMED ELNMKPGDKI KVITDDGEYN DGWYYGRNLR
     TKEEGLYPAV FTKRIAIEKP ENLHKSPTQE SGNSGVKYGN LNDSASNIGK VSSHQQENRY
     TSLKSTMSDI DKALEELRSG SVEQEVSKSP TRVPEVSTPQ LQDEQTLIQE KTRNEENTTH
     DSLFSSTADL NLSSESLKNI SKSNISTKSL EPSSESVRQL DLKMAKSWSP EEVTDYFSLV
     GFDQSTCNKF KEHQVSGKIL LELELEHLKE LEINSFGIRF QIFKEIRNIK SAIDSSSNKL
     DADYSTFAFE NQAAQLMPAA TVNRDEIQQQ ISSKCNKLSS ESSDRKSSSV TTELQRPSSV
     VVNPNFKLHD PAEQILDMTE VPNLFADKDI FESPGRAPKP PSYPSPVQPP QSPSFNNRYT
     NNNARFPPQT TYPPKNKNPT VYSNGLIPNS STSSDNSTGK FKFPAMNGHD SNSRKTTLTS
     ATIPSINTVN TDESLPAISN ISSNATSHHP NRNSVVYNNH KRTESGSSFV DLFNRISMLS
     PVKSSFDEEE TKQPSKASRA VFDSARRKSS YGHSRDASLS EMKKHRRNSS ILSFFSSKSQ
     SNPTSPTKQT FTIDPAKMTS HSRSQSNSYS HARSQSYSHS RKHSLVTSPL KTSLSPINSK
     SNIALAHSET PTSSNNKEAV SQPSEGKHKH KHKHKSKHKH KNSSSKDGSS EEKSKKKLFS
     STKESFVGSK EFKRSPSELT QKSTKSILPR SNAKKQQTSA FTEGIRSITA KESMQTADCS
     GWMSKKGTGA MGTWKQRFFT LHGTRLSYFT NTNDEKERGL IDITAHRVLP ASDDDRLISL
     YAASLGKGKY CFKLVPPQPG SKKGLTFTEP RVHYFAVENK SEMKAWLSAI IKATIDIDTS
     VPVISSYATP TIPLSKAQTL LEEARLQTQL RDAEEEEGRD QFGWDDTQNK RNSNYPIEQD
     QFETSDYLES SAFEYPGGRL
//