BEM2_YEAST
ID BEM2_YEAST Reviewed; 2167 AA.
AC P39960; D3DM62;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=GTPase-activating protein BEM2/IPL2;
DE AltName: Full=Bud emergence protein 2;
GN Name=BEM2; Synonyms=IPL2, SUP9; OrderedLocusNames=YER155C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7962097; DOI=10.1083/jcb.127.5.1381;
RA Kim Y., Francisco L., Chen G., Marcotte E., Chan C.S.;
RT "Control of cellular morphogenesis by the Ip12/Bem2 GTPase-activating
RT protein: possible role of protein phosphorylation.";
RL J. Cell Biol. 127:1381-1394(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7962098; DOI=10.1083/jcb.127.5.1395;
RA Peterson J., Zheng Y., Bender L., Myers A., Cerione R., Bender A.;
RT "Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-
RT type GTPases in yeast.";
RL J. Cell Biol. 127:1395-1406(1994).
RN [3]
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 [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 CHARACTERIZATION.
RX PubMed=8293973; DOI=10.1093/genetics/135.3.677;
RA Chan C.S., Botstein D.;
RT "Isolation and characterization of chromosome-gain and increase-in-ploidy
RT mutants in yeast.";
RL Genetics 135:677-691(1993).
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-1012; SER-1016 AND SER-1046,
RP AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1012; SER-1046 AND SER-1054,
RP AND IDENTIFICATION BY 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-129 AND SER-283, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-283; THR-1038 AND
RP SER-1128, 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 [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: GTPase-activating protein (GAP) for RHO1 and RHO2. Involved
CC in the control of cellular morphogenesis. Required for proper bud site
CC selection and bud emergence.
CC -!- INTERACTION:
CC P39960; P27637: BUD14; NbExp=3; IntAct=EBI-3517, EBI-20747;
CC -!- MISCELLANEOUS: Present with 1230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z35159; CAA84524.1; -; Genomic_DNA.
DR EMBL; L33832; AAA57132.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64682.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07816.1; -; Genomic_DNA.
DR PIR; S50658; S50658.
DR RefSeq; NP_011082.3; NM_001179045.3.
DR AlphaFoldDB; P39960; -.
DR SMR; P39960; -.
DR BioGRID; 36905; 581.
DR DIP; DIP-6580N; -.
DR IntAct; P39960; 48.
DR MINT; P39960; -.
DR STRING; 4932.YER155C; -.
DR iPTMnet; P39960; -.
DR MaxQB; P39960; -.
DR PaxDb; P39960; -.
DR PRIDE; P39960; -.
DR EnsemblFungi; YER155C_mRNA; YER155C; YER155C.
DR GeneID; 856899; -.
DR KEGG; sce:YER155C; -.
DR SGD; S000000957; BEM2.
DR VEuPathDB; FungiDB:YER155C; -.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_002085_0_0_1; -.
DR InParanoid; P39960; -.
DR OMA; LEDDRWF; -.
DR BioCyc; YEAST:G3O-30316-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9013423; RAC3 GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR Reactome; R-SCE-9035034; RHOF GTPase cycle.
DR PRO; PR:P39960; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39960; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IMP:SGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF48366; SSF48366; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..2167
FT /note="GTPase-activating protein BEM2/IPL2"
FT /id="PRO_0000068858"
FT DOMAIN 592..859
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 1846..1948
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1967..2165
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1038
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 2167 AA; 245430 MW; DB7F4CD417E898F0 CRC64;
MKGLLWSKNR KSSTASASSS STSTSHKTTT ASTASSSSPS SSSQTIRNST SGASPYMHSH
HHHGQGHSHH RGEDNNRDKR KSSVFPPSKQ YTSTSSSQVN LGMYHSDTNT RSSRSIASTL
KDDSPSVCSE DEISNSSSQK SNAQDETPIA YKKSAHSKDS LLPSRSSSLS PPQSRCSTGT
TLEKSLNTSG ISNSSGTNNN NSNNNNDNEQ KQRNVIHLNS ENYDTTVFKT GWVNKSHGQT
VATNYNSSMT APSSSSSSSS QNLRNDAYSR NRESRFYGND GSSLKNDDSS STTATNSGND
VASARSSMAI DPQMLVPDYR LYRAQLKGCV LNLYKSGLNS NIKFFDPTLP ASNSSIANEN
HQQKKQQTNN QAQAEALHQK QSFGQMGEPI TLDLKYLSEV YPHPDLRQDS DGKIISGTIE
SLCHTVLFYP GPKQSDVPNE KSLSKTHRAV INLLLMFPLL DHFIKFLKVF NQFGLSFTKN
KSRLTNNSTQ FYNISPAVDD SMTQRLALTA KTILDVFPGF LLDEPMLKTI ISLLDTISLH
NDEISNNLKI KIANKHNELM KLTAFTRSLP MATSSTHELE IILDPSHFLS LDITTLADEV
HHINLKFDKV WAPKFDYSLL YDSKFINRRI VSLNPLVFNN DQNIHFLGRL LISHLFPTNP
EFSKKVTPKV RAELLDKWVQ IGCRFEHLGD MVSWLAVATI ICSIPVLRSS SWKYVPDQSL
KTIFKDWVPT IIQLERRQRT SKSTSSVFIL APPNLDDDFT RANVISYFGD LLIHADDLPS
DTKFKYLEKK INRTKNAFHK WQQRLQAIDS TRHKTNSTEN VRDNDSPNNV VYQLWKFHLS
QPPLNIEGIM KLSVQHEPPI IDQKAYSTIG SQRSALVTGS YLPILFNELF PNYSLFPKNT
LVGAASDAKL PPPRSSARLS KSLSISEPIP IASNSHTMGS LTDDAMSSKN DNNKVTGVGK
IDGPVIKEMS SKQSNKQRLL KSVRDVFNID MDVFHISDEL VFKSVYDNDG KSRPASMVIE
TPKRFSQHSS MLINNPATPN QKMRDSLDTT GRLSKTLENM DFFNNIGQVS DSLKESIIRV
VLKSSSLEKI FDLLVLTSNI FSKLVDTKDL ENYYYHQRQR GHSTRGLSDD NIGLLDYAFV
KLTMDNDIFT ETFFNTYKSF TTTTTVLENM AKRYVGAKSC SVSISKILDR SDDSKMKINE
DTNLVSSSLY DQNFPVWDMK VTDDENINLI YMAKIQIGAA EAILHLVKNH YSDFTDDLCN
NSTLLDIIKI MEQEVSTEWP TRIANSKLQK SLPENFVIET ENLLTTLTDL FHGIKSAYQK
QLYRPIGVNR TQKRITDILN SFNTFSFTDL NNIIDDPSFS DDMIRSFQKL HSTNYEDILE
WIYQLDNFIS KKFNLVSKKD WIVLFQELEL LSKESLVSFF NYPLHFKSSK LINPGYLQLH
EFEISNLFTW ISTLILKDDN GTESLFFEKL PQSIKLLIKL HTSLTTFFVM EISNVNKSSS
ERLTTCKVIL QILNYIRWKN GSLDLFDSEE DESPHAICPH IPAFIETAIA HAIISPESRN
YELSWIKASE KLSDPTKGTQ NLRSISNVLE KIDDIHIKRF IEIDDVFSKN CKNLCPCPGW
FISRLLEISQ FVPNMSITNS KLINFDKRRF VNNIISNVLD LIPNEREFPL DIEMSDENPS
KRTTFGRILF NNFEDVNKVY RKKTKKVSES EAISERFQEQ GVFNEILVNE IEKIKREARK
LEVLLDQEKI LKNSAALHQA VPKKNRKSVI ISGTHSDNDH SYNINKNTGQ TPSLGSVMES
NNSARNRRDS RASFSTNRSS VVSNSSHNGV SKKIGGFFRR PFSIGGFNTS SSNYSLNSIL
SQEVSSNKSI LPSILPEVDS MQLHDLKPSY SLKTFEIKSI MEIINHRNIP AYYYAFKIVM
QNGHEYLIQT ASSSDLTEWI KMIKASKRFS FHSKKYKGKT HNKIFGVPLE DVCERENTLI
PTIVVKLLEE IELRGLDEVG LYRIPGSIGS INALKNAFDE EGATDNSFTL EDDRWFEVNA
IAGCFKMYLR ELPDSLFSHA MVNDFTDLAI KYKAHAMVNE EYKRMMNELL QKLPTCYYQT
LKRIVFHLNK VHQHVVNNKM DASNLAIVFS MSFINQEDLA NSMGSRLGAV QTILQDFIKN
PNDYFKQ
