BUG1_YEAST
ID BUG1_YEAST Reviewed; 341 AA.
AC Q12191; D6VRQ1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Binder of USO1 and GRH1 protein 1;
GN Name=BUG1 {ECO:0000303|PubMed:16269340}; OrderedLocusNames=YDL099W;
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] {ECO:0000312|EMBL:CAA64914.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679 {ECO:0000312|EMBL:CAA64914.1};
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [2] {ECO:0000312|EMBL:CAA98666.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c {ECO:0000269|PubMed:9169867};
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5] {ECO:0000305}
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH GRH1.
RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S.,
RA Krogan N.J.;
RT "Exploration of the function and organization of the yeast early secretory
RT pathway through an epistatic miniarray profile.";
RL Cell 123:507-519(2005).
RN [7]
RP FUNCTION, INTERACTION WITH GRH1, AND SUBCELLULAR LOCATION.
RX PubMed=17261844; DOI=10.1083/jcb.200607151;
RA Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.;
RT "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein
RT that contributes to ER to Golgi traffic.";
RL J. Cell Biol. 176:255-261(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, 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-87; SER-170 AND THR-292, AND
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Involved in ER to Golgi vesicle-mediated transport by either
CC facilitating USO1-dependent and -independent tethering or increasing
CC target accuracy of fusion events of COPII-coated vesicles.
CC {ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844}.
CC -!- SUBUNIT: Interacts with GRH1 (via C-terminus), probably forming a
CC heterooligomer consisting of a GRH1 dimer and a BUG1 dimer.
CC {ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844}.
CC -!- INTERACTION:
CC Q12191; Q12191: BUG1; NbExp=2; IntAct=EBI-32271, EBI-32271;
CC Q12191; Q04410: GRH1; NbExp=4; IntAct=EBI-32271, EBI-32083;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, cis-Golgi network
CC membrane; Peripheral membrane protein. Note=Localizes to cytoplasm in a
CC punctate pattern. Localizes to cis-Golgi together with GRH1.
CC -!- MISCELLANEOUS: Present with 5220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X95644; CAA64914.1; -; Genomic_DNA.
DR EMBL; Z74147; CAA98666.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11761.1; -; Genomic_DNA.
DR PIR; S67641; S67641.
DR RefSeq; NP_010184.1; NM_001180158.1.
DR AlphaFoldDB; Q12191; -.
DR SMR; Q12191; -.
DR BioGRID; 31963; 246.
DR ComplexPortal; CPX-1125; BUG1-GRH1 complex.
DR DIP; DIP-3001N; -.
DR IntAct; Q12191; 4.
DR MINT; Q12191; -.
DR STRING; 4932.YDL099W; -.
DR iPTMnet; Q12191; -.
DR MaxQB; Q12191; -.
DR PaxDb; Q12191; -.
DR PRIDE; Q12191; -.
DR EnsemblFungi; YDL099W_mRNA; YDL099W; YDL099W.
DR GeneID; 851459; -.
DR KEGG; sce:YDL099W; -.
DR SGD; S000002257; BUG1.
DR VEuPathDB; FungiDB:YDL099W; -.
DR eggNOG; ENOG502S1CR; Eukaryota.
DR HOGENOM; CLU_076662_0_0_1; -.
DR InParanoid; Q12191; -.
DR OMA; NWNVDMT; -.
DR BioCyc; YEAST:G3O-29502-MON; -.
DR PRO; PR:Q12191; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12191; protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:ComplexPortal.
DR GO; GO:0106103; C:COPII vesicles tethering complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0007030; P:Golgi organization; IC:ComplexPortal.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..341
FT /note="Binder of USO1 and GRH1 protein 1"
FT /id="PRO_0000270973"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..41
FT /evidence="ECO:0000255"
FT COILED 188..272
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 341 AA; 38295 MW; E0C5AFBD74062EE9 CRC64;
MSEQESDEVK RMKQLEEARK RVEELKKKKN KKNKGKKNKN SSATGSIGSE TPDLEGTPGE
ESTQEETVKA NSTKSENNDQ NDVDEESEEK EIEQVKSDPS GTTEKDIEEI NSTSSNVGKD
DAENTKKEEV QEVIKNNNDE QTADAGKTIE PQEEKKIVQT QEGNEPSNTS EAADDLFAND
GNEESDFLTT IKKQKEEDEL TKLRAENEKL TQENKQLKFL NMENETTVDD LQDQLQEKED
IINGLQNDLQ TARDELIAAV EKLKLAEAKA ARNTTATPIQ FADFNTSSNN LTPSQSVTNS
GTQVAHGNNM EVDRVMLNKW RQWNVDMTTW RSIGSGPIME F
