BEM1_YEAST
ID BEM1_YEAST Reviewed; 551 AA.
AC P29366; D6VQJ6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Bud emergence protein 1;
DE AltName: Full=Suppressor of RHO3 protein 1;
GN Name=BEM1; Synonyms=SRO1; OrderedLocusNames=YBR200W; ORFNames=YBR1412;
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=1538785; DOI=10.1038/356077a0;
RA Chenevert J., Corrado K., Bender A., Pringle J., Herskowitz I.;
RT "A yeast gene (BEM1) necessary for cell polarization whose product contains
RT two SH3 domains.";
RL Nature 356:77-79(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975899; DOI=10.1002/yea.320100612;
RA Mallet L., Bussereau F., Jacquet M.;
RT "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II
RT including BEM1, a new gene of the WD-40 repeat family and a new member of
RT the KRE2/MNT1 family.";
RL Yeast 10:819-831(1994).
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 INTERACTION WITH BUD5.
RX PubMed=1905981; DOI=10.1016/0092-8674(91)90016-r;
RA Chant J., Corrado K., Pringle J.R., Herskowitz I.;
RT "Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for
RT bud site selection and interacts with bud formation gene BEM1.";
RL Cell 65:1213-1224(1991).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-461, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-461, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP INTERACTION WITH AXL2, AND FUNCTION.
RX PubMed=17460121; DOI=10.1091/mbc.e06-09-0822;
RA Gao X.D., Sperber L.M., Kane S.A., Tong Z., Tong A.H., Boone C., Bi E.;
RT "Sequential and distinct roles of the cadherin domain-containing protein
RT Axl2p in cell polarization in yeast cell cycle.";
RL Mol. Biol. Cell 18:2542-2560(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-461, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-255; SER-258 AND
RP SER-458, AND IDENTIFICATION 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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).
RN [13]
RP STRUCTURE BY NMR OF 472-551.
RX PubMed=11483498; DOI=10.1093/emboj/20.15.3947;
RA Terasawa H., Noda Y., Ito T., Hatanaka H., Ichikawa S., Ogura K.,
RA Sumimoto H., Inagaki F.;
RT "Structure and ligand recognition of the PB1 domain: a novel protein module
RT binding to the PC motif.";
RL EMBO J. 20:3947-3956(2001).
CC -!- FUNCTION: Necessary for cell polarization during vegetative growth. May
CC link the cytoskeleton to morphogenic determinants on the cell surface.
CC {ECO:0000269|PubMed:17460121}.
CC -!- SUBUNIT: Interacts with AXL2 and BUD5. {ECO:0000269|PubMed:17460121,
CC ECO:0000269|PubMed:1905981}.
CC -!- INTERACTION:
CC P29366; P38041: BOI1; NbExp=5; IntAct=EBI-3508, EBI-3719;
CC P29366; P39969: BOI2; NbExp=6; IntAct=EBI-3508, EBI-3727;
CC P29366; P53280: CAF130; NbExp=3; IntAct=EBI-3508, EBI-23322;
CC P29366; P11433: CDC24; NbExp=22; IntAct=EBI-3508, EBI-4220;
CC P29366; P19073: CDC42; NbExp=4; IntAct=EBI-3508, EBI-4274;
CC P29366; P48562: CLA4; NbExp=9; IntAct=EBI-3508, EBI-4750;
CC P29366; P54199: MPS1; NbExp=3; IntAct=EBI-3508, EBI-11224;
CC P29366; Q08229: NBA1; NbExp=6; IntAct=EBI-3508, EBI-36841;
CC P29366; Q03497: STE20; NbExp=11; IntAct=EBI-3508, EBI-18285;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- MISCELLANEOUS: Present with 6490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X63826; CAA45320.1; -; Genomic_DNA.
DR EMBL; Z21487; CAA79687.1; -; Genomic_DNA.
DR EMBL; Z36069; CAA85162.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07316.1; -; Genomic_DNA.
DR PIR; S23400; S23400.
DR RefSeq; NP_009759.3; NM_001178548.3.
DR PDB; 1IP9; NMR; -; A=472-551.
DR PDB; 1IPG; NMR; -; A=472-551.
DR PDB; 2CZO; NMR; -; A=269-418.
DR PDB; 2KFK; NMR; -; A=477-551.
DR PDB; 2RQV; NMR; -; A=156-260.
DR PDB; 2RQW; NMR; -; A=156-260.
DR PDB; 2V6V; X-ray; 1.50 A; A/B=266-413.
DR PDBsum; 1IP9; -.
DR PDBsum; 1IPG; -.
DR PDBsum; 2CZO; -.
DR PDBsum; 2KFK; -.
DR PDBsum; 2RQV; -.
DR PDBsum; 2RQW; -.
DR PDBsum; 2V6V; -.
DR AlphaFoldDB; P29366; -.
DR SMR; P29366; -.
DR BioGRID; 32897; 521.
DR ComplexPortal; CPX-3462; CLA4-BEM1-CDC24 polarity complex.
DR DIP; DIP-688N; -.
DR ELM; P29366; -.
DR IntAct; P29366; 53.
DR MINT; P29366; -.
DR STRING; 4932.YBR200W; -.
DR iPTMnet; P29366; -.
DR MaxQB; P29366; -.
DR PaxDb; P29366; -.
DR PRIDE; P29366; -.
DR EnsemblFungi; YBR200W_mRNA; YBR200W; YBR200W.
DR GeneID; 852499; -.
DR KEGG; sce:YBR200W; -.
DR SGD; S000000404; BEM1.
DR VEuPathDB; FungiDB:YBR200W; -.
DR eggNOG; KOG4773; Eukaryota.
DR HOGENOM; CLU_014957_0_1_1; -.
DR InParanoid; P29366; -.
DR OMA; YWYIIEA; -.
DR BioCyc; YEAST:G3O-29141-MON; -.
DR Reactome; R-SCE-5668599; RHO GTPases Activate NADPH Oxidases.
DR EvolutionaryTrace; P29366; -.
DR PRO; PR:P29366; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P29366; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0120157; C:PAR polarity complex; IPI:ComplexPortal.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0060090; F:molecular adaptor activity; IPI:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IC:ComplexPortal.
DR GO; GO:0000747; P:conjugation with cellular fusion; IBA:GO_Central.
DR GO; GO:0045185; P:maintenance of protein location; IMP:SGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IC:ComplexPortal.
DR CDD; cd06890; PX_Bem1p; 1.
DR CDD; cd11878; SH3_Bem1p_1; 1.
DR CDD; cd11879; SH3_Bem1p_2; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR030507; Bem1/Scd2.
DR InterPro; IPR035550; Bem1/Scd2_PX.
DR InterPro; IPR035548; Bem1/Scd2_SH3_1.
DR InterPro; IPR035549; Bem1/Scd2_SH3_2.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15706:SF2; PTHR15706:SF2; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 2.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..551
FT /note="Bud emergence protein 1"
FT /id="PRO_0000064908"
FT DOMAIN 72..132
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 155..217
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 278..404
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 478..551
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2RQV"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2RQV"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2RQW"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:2RQV"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:2RQV"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:2RQV"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2RQV"
FT STRAND 283..294
FT /evidence="ECO:0007829|PDB:2V6V"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:2V6V"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:2V6V"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:2V6V"
FT TURN 333..337
FT /evidence="ECO:0007829|PDB:2V6V"
FT HELIX 363..381
FT /evidence="ECO:0007829|PDB:2V6V"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2V6V"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:2V6V"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:2V6V"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:2V6V"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:1IP9"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:1IP9"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:1IP9"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:1IP9"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:1IP9"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:1IP9"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:1IP9"
SQ SEQUENCE 551 AA; 61605 MW; FB6C525AE9A19181 CRC64;
MLKNFKLSKR DSNGSKGRIT SADISTPSHD NGSVIKHIKT VPVRYLSSSS TPVKSQRDSS
PKNRHNSKDI TSPEKVIKAK YSYQAQTSKE LSFMEGEFFY VSGDEKDWYK ASNPSTGKEG
VVPKTYFEVF DRTKPSSVNG SNSSSRKVTN DSLNMGSLYA IVLYDFKAEK ADELTTYVGE
NLFICAHHNC EWFIAKPIGR LGGPGLVPVG FVSIIDIATG YATGNDVIED IKSVNLPTVQ
EWKSNIARYK ASNISLGSVE QQQQQSITKP QNKSAKLVDG ELLVKASVES FGLEDEKYWF
LVCCELSNGK TRQLKRYYQD FYDLQVQLLD AFPAEAGKLR DAGGQWSKRI MPYIPGPVPY
VTNSITKKRK EDLNIYVADL VNLPDYISRS EMVHSLFVVL NNGFDREFER DENQNNIKTL
QENDTATFAT ASQTSNFAST NQDNTLTGED LKLNKKLSDL SLSGSKQAPA QSTSGLKTTK
IKFYYKDDIF ALMLKGDTTY KELRSKIAPR IDTDNFKLQT KLFDGSGEEI KTDSQVSNII
QAKLKISVHD I
