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   02-SEP-2026, entry version 183.
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}.
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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; 433.
DR   DIP; DIP-4929N; -.
DR   FunCoup; P43573; 164.
DR   IntAct; P43573; 38.
DR   MINT; P43573; -.
DR   STRING; 4932.YFL023W; -.
DR   iPTMnet; P43573; -.
DR   PaxDb; 4932-YFL023W; -.
DR   PeptideAtlas; P43573; -.
DR   EnsemblFungi; YFL023W_mRNA; YFL023W; YFL023W.
DR   GeneID; 850521; -.
DR   KEGG; sce:YFL023W; -.
DR   AGR; SGD:S000001871; -.
DR   SGD; S000001871; BUD27.
DR   VEuPathDB; FungiDB:YFL023W; -.
DR   eggNOG; ENOG502QVS0; Eukaryota.
DR   HOGENOM; CLU_344512_0_0_1; -.
DR   InParanoid; P43573; -.
DR   OMA; FKLKQVC; -.
DR   OrthoDB; 21413at2759; -.
DR   BioCyc; YEAST:G3O-30437-MONOMER; -.
DR   BioGRID-ORCS; 850521; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43573; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43573; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IMP:SGD.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IMP:SGD.
DR   GO; GO:2001209; P:positive regulation of transcription elongation by RNA polymerase I; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IMP:SGD.
DR   FunFam; 1.10.287.370:FF:000026; Bud site selection protein; 1.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR024325; DUF3835.
DR   InterPro; IPR011599; PFD_alpha_archaea.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12674; PREFOLDIN SUBUNIT 5; 1.
DR   PANTHER; PTHR12674:SF2; PREFOLDIN SUBUNIT 5; 1.
DR   Pfam; PF12927; DUF3835; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   SUPFAM; SSF46579; 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..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..568
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..589
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..610
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
//