BUD27_YEAST
ID BUD27_YEAST Reviewed; 796 AA.
AC P43573; D6VTK7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Bud site selection protein 27;
GN Name=BUD27; Synonyms=URI; OrderedLocusNames=YFL023W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(2001).
RN [4]
RP FUNCTION.
RX PubMed=12663529; DOI=10.1093/genetics/163.3.875;
RA Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
RA Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
RA Bussey H.;
RT "A Saccharomyces cerevisiae genome-wide mutant screen for altered
RT sensitivity to K1 killer toxin.";
RL Genetics 163:875-894(2003).
RN [5]
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 [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 FUNCTION.
RX PubMed=14615539; DOI=10.1126/science.1088401;
RA Gstaiger M., Luke B., Hess D., Oakeley E.J., Wirbelauer C., Blondel M.,
RA Vigneron M., Peter M., Krek W.;
RT "Control of nutrient-sensitive transcription programs by the unconventional
RT prefoldin URI.";
RL Science 302:1208-1212(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, 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-580, 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-580, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Involved in gene expression controlled by TOR kinase and
CC nutrient signaling. May also be involved in positioning the proximal
CC bud pole signal. {ECO:0000269|PubMed:11452010,
CC ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:14615539}.
CC -!- INTERACTION:
CC P43573; P20081: FPR1; NbExp=2; IntAct=EBI-22787, EBI-6961;
CC P43573; P11484: SSB1; NbExp=3; IntAct=EBI-22787, EBI-8627;
CC P43573; P02994: TEF2; NbExp=2; IntAct=EBI-22787, EBI-6314;
CC P43573; P36008: TEF4; NbExp=3; IntAct=EBI-22787, EBI-6329;
CC P43573; P52553: YKE2; NbExp=3; IntAct=EBI-22787, EBI-13260;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Deletion leads to a K1 killer toxin hypersensitivity.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D50617; BAA09215.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12417.1; -; Genomic_DNA.
DR PIR; S56231; S56231.
DR RefSeq; NP_683715.1; NM_001179943.1.
DR AlphaFoldDB; P43573; -.
DR SMR; P43573; -.
DR BioGRID; 31123; 395.
DR DIP; DIP-4929N; -.
DR IntAct; P43573; 21.
DR MINT; P43573; -.
DR STRING; 4932.YFL023W; -.
DR iPTMnet; P43573; -.
DR MaxQB; P43573; -.
DR PaxDb; P43573; -.
DR PRIDE; P43573; -.
DR EnsemblFungi; YFL023W_mRNA; YFL023W; YFL023W.
DR GeneID; 850521; -.
DR KEGG; sce:YFL023W; -.
DR SGD; S000001871; BUD27.
DR VEuPathDB; FungiDB:YFL023W; -.
DR eggNOG; ENOG502QVS0; Eukaryota.
DR HOGENOM; CLU_344512_0_0_1; -.
DR InParanoid; P43573; -.
DR OMA; IGYEYYV; -.
DR BioCyc; YEAST:G3O-30437-MON; -.
DR PRO; PR:P43573; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43573; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IMP:SGD.
DR GO; GO:1990113; P:RNA polymerase I assembly; IMP:SGD.
DR GO; GO:1990114; P:RNA polymerase II core complex assembly; IMP:SGD.
DR GO; GO:1990115; P:RNA polymerase III assembly; IMP:SGD.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR024325; DUF3835.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR Pfam; PF12927; DUF3835; 1.
DR Pfam; PF02996; Prefoldin; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..796
FT /note="Bud site selection protein 27"
FT /id="PRO_0000153693"
FT REGION 152..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 81..121
FT /evidence="ECO:0000255"
FT COMPBIAS 152..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 796 AA; 91422 MW; 7E2EE2CEB4708BC3 CRC64;
MDLLAASVES TLKNLQDKRN FLSEQREHYI DIRSRLVRFI NDNDDGEEEG EGQGMVFGDI
IISTSKIYLS LGYEYYVEKT KEEAITFVDD KLKLMEDAIE QFNLKIEEAK KTLDNLNHME
DGNGIEEDEA NNDEDFLPSM EIREELDDEG NVISSSVTPT TKQPSQSNSK KEQTPAVGPK
EKGLAKEKKS KSFEENLKGK LLKRNDEVKK KVQPSKVDTE NVYTFADLVQ QMDQQDELED
GYIETDEINY DYDAFENSNF KVNDNYEEDD EDEDEEEYLN HSIIPGFEAQ SSFLQQIQRL
RAQKQSQDHE REEGDVNKSL KPILKKSSFA ENSDKKQKKK QVGFASSLEI HEVENLKEEN
KRQMQSFAVP MYETQESTGI ANKMTSDEFD GDLFAKMLGV QEADEVHEKY KEELINQERL
EGEASRSNRR TRVSRFRKDR ASKKENTLST FKQETTRSVE NEVVEKEPVV GDIIEKEPVV
GDVIEKEPVV GDVIEKEPAV TDIVEREPAV NDIVERKPVV GDIIEKEPTI NDIVEKEPEI
NSKSEFETPF KKKKLKSLQK PRSSKSMKKK FDPKILENIS DDDYDDDDDG NKKLLSNKSK
NNTDEQDKFP SKIQEVSRSM AKTGATVGSE PVRITNVDYH ALGGNLDDMV KAYSLGLYDD
DLEEDPGTIV EKLEDFKEYN KQVELLRDEI RDFQLENKPV TMEEEENDGN VMNDIIEHEF
PESYTNDEDE VALHPGRLQE EVAIEYRRLK EATASKWQSS SPAAHTEGEL EPIDKFGNPV
KTSRFRSQRL HMDSKP
