BUD22_YEAST
ID BUD22_YEAST Reviewed; 519 AA.
AC Q04347; D6VZI8; Q6B299;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Bud site selection protein 22;
GN Name=BUD22; OrderedLocusNames=YMR014W; ORFNames=YM9711.01;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-367; THR-371 AND
RP SER-375, 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 THR-257, AND IDENTIFICATION BY
RP 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 THR-257, 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 THR-257; SER-367; THR-371 AND
RP SER-375, 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).
CC -!- FUNCTION: Involved in positioning the proximal bud pole signal.
CC {ECO:0000269|PubMed:11452010}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11452010,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BUD22 family. {ECO:0000305}.
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DR EMBL; Z49211; CAA89115.1; -; Genomic_DNA.
DR EMBL; AY692831; AAT92850.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09912.1; -; Genomic_DNA.
DR PIR; S54014; S54014.
DR RefSeq; NP_013727.1; NM_001182510.1.
DR AlphaFoldDB; Q04347; -.
DR BioGRID; 35185; 22.
DR DIP; DIP-4103N; -.
DR IntAct; Q04347; 20.
DR MINT; Q04347; -.
DR STRING; 4932.YMR014W; -.
DR iPTMnet; Q04347; -.
DR MaxQB; Q04347; -.
DR PaxDb; Q04347; -.
DR PRIDE; Q04347; -.
DR EnsemblFungi; YMR014W_mRNA; YMR014W; YMR014W.
DR GeneID; 855028; -.
DR KEGG; sce:YMR014W; -.
DR SGD; S000004616; BUD22.
DR VEuPathDB; FungiDB:YMR014W; -.
DR eggNOG; ENOG502S6Z4; Eukaryota.
DR HOGENOM; CLU_024653_0_0_1; -.
DR InParanoid; Q04347; -.
DR OMA; PNVNYNE; -.
DR BioCyc; YEAST:G3O-32721-MON; -.
DR PRO; PR:Q04347; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04347; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR InterPro; IPR037393; Bud22/SRFB1.
DR InterPro; IPR015158; Bud22_dom.
DR PANTHER; PTHR23325; PTHR23325; 1.
DR Pfam; PF09073; BUD22; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..519
FT /note="Bud site selection protein 22"
FT /id="PRO_0000065014"
FT REGION 241..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..470
FT /evidence="ECO:0000255"
FT COMPBIAS 266..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 497
FT /note="I -> V (in Ref. 3; AAT92850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 60054 MW; 8142768058BFA264 CRC64;
MPSESSVSIY KLDQLEYQYH YLTKSLQKFE PRYPKTAKLY NCIGKKNKKK IEKLLNSLEL
KTLDKELDES YSKLLNNKIH YYETHLSKCI KEQIQKISKK NSSKVKDAQK NKSPSIDIEK
MLATQLSLDD LALFMTRFRL IKILHQRIKQ KSKKIEGDTN NKTWLNNNDY SGYINDKTSK
WNPSNIWNEV ITKLPSCEKL NALIGQSKIV QNLTESFDLS ICLIFGFDVS AMKAKKYGAR
EKTANANQTH SNIDYDTDDG NEKNAIDSKS NAIGAQTQSN KETTSDNEDL LIKEYEGMLG
SSGDEGEGGG YLNPNINYNE VTDEEPSEAS SDEDDSDERF SDSEENEPRR KKPKLHNLPE
LMAGYYSGND TEEESDEDNK NVKGKKKKRD TAEDRTAREQ MSNEPKRKNR RGQRARRKIW
EKKYGSQAKH VQRELEKEME DRKQRQIEYE ARVAKREAKA ASLEASRSRE REDRRTETNN
KKEKESASTG EEHPSWIAKR LAEEKLQKAK FEGKKIKFD
