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
//
