BUD20_YEAST
ID BUD20_YEAST Reviewed; 166 AA.
AC Q08004; D6VY75;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Bud site selection protein 20 {ECO:0000303|PubMed:11452010};
GN Name=BUD20 {ECO:0000303|PubMed:11452010}; OrderedLocusNames=YLR074C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 DOMAIN.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRE-60S RIBOSOMAL
RP PARTICLES, AND MUTAGENESIS OF 7-LYS--ARG-16; 12-LYS--ARG-14; 17-ASP--VAL-31
RP AND 18-LEU--LEU-25.
RX PubMed=23045392; DOI=10.1128/mcb.00910-12;
RA Bassler J., Klein I., Schmidt C., Kallas M., Thomson E., Wagner M.A.,
RA Bradatsch B., Rechberger G., Strohmaier H., Hurt E., Bergler H.;
RT "The conserved Bud20 zinc finger protein is a new component of the
RT ribosomal 60S subunit export machinery.";
RL Mol. Cell. Biol. 32:4898-4912(2012).
CC -!- FUNCTION: Involved in pre-60S ribosomal particles maturation by
CC promoting the nuclear export of the 60S ribosome (PubMed:23045392).
CC Involved in positioning the proximal bud pole signal (PubMed:11452010).
CC {ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:23045392}.
CC -!- SUBUNIT: Associates with pre-60S ribosomal particles; released from the
CC pre-60S particle very early in the cytoplasm.
CC {ECO:0000269|PubMed:23045392}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11452010,
CC ECO:0000269|PubMed:23045392}. Cytoplasm {ECO:0000269|PubMed:23045392}.
CC Note=Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000269|PubMed:23045392}.
CC -!- MISCELLANEOUS: Present with 5630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; Z73246; CAA97631.1; -; Genomic_DNA.
DR EMBL; AY558208; AAS56534.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09391.1; -; Genomic_DNA.
DR PIR; S64906; S64906.
DR RefSeq; NP_013175.1; NM_001181961.1.
DR PDB; 3JCT; EM; 3.08 A; I=1-166.
DR PDB; 6FT6; EM; 3.90 A; I=1-166.
DR PDB; 6M62; EM; 3.20 A; I=1-166.
DR PDB; 6N8J; EM; 3.50 A; I=1-166.
DR PDB; 6N8K; EM; 3.60 A; I=1-166.
DR PDB; 6N8L; EM; 3.60 A; I=1-166.
DR PDB; 6YLG; EM; 3.00 A; I=1-166.
DR PDB; 6YLH; EM; 3.10 A; I=1-166.
DR PDB; 6YLY; EM; 3.80 A; I=1-166.
DR PDBsum; 3JCT; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLY; -.
DR AlphaFoldDB; Q08004; -.
DR SMR; Q08004; -.
DR BioGRID; 31348; 247.
DR DIP; DIP-4920N; -.
DR IntAct; Q08004; 89.
DR MINT; Q08004; -.
DR STRING; 4932.YLR074C; -.
DR MaxQB; Q08004; -.
DR PaxDb; Q08004; -.
DR PRIDE; Q08004; -.
DR EnsemblFungi; YLR074C_mRNA; YLR074C; YLR074C.
DR GeneID; 850763; -.
DR KEGG; sce:YLR074C; -.
DR SGD; S000004064; BUD20.
DR VEuPathDB; FungiDB:YLR074C; -.
DR eggNOG; KOG3408; Eukaryota.
DR GeneTree; ENSGT00390000004173; -.
DR HOGENOM; CLU_117291_0_0_1; -.
DR InParanoid; Q08004; -.
DR OMA; FMARVEQ; -.
DR BioCyc; YEAST:G3O-32226-MON; -.
DR PRO; PR:Q08004; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q08004; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Ribosome biogenesis; Zinc; Zinc-finger.
FT CHAIN 1..166
FT /note="Bud site selection protein 20"
FT /id="PRO_0000046803"
FT ZN_FING 49..73
FT /note="C2H2-type"
FT REGION 17..31
FT /note="Nuclear export signal-like (NES-like)"
FT /evidence="ECO:0000269|PubMed:23045392"
FT MOTIF 7..16
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23045392"
FT MUTAGEN 7..16
FT /note="Missing: Increased localization to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:23045392"
FT MUTAGEN 12..14
FT /note="KRR->GGG: Slightly increased localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:23045392"
FT MUTAGEN 17..31
FT /note="Missing: Increased localization to the nucleus."
FT /evidence="ECO:0000269|PubMed:23045392"
FT MUTAGEN 18..25
FT /note="LDLIYNDL->RDLRYNDR: Slightly increased localization
FT to the nucleus."
FT /evidence="ECO:0000269|PubMed:23045392"
SQ SEQUENCE 166 AA; 18517 MW; 77E04027DAC476AC CRC64;
MGRYSVKRYK TKRRTRDLDL IYNDLSTKES VQKLLNQPLD ETKPGLGQHY CIHCAKYMET
AIALKTHLKG KVHKRRVKEL RGVPYTQEVS DAAAGYNLNK FLNRVQEITQ SVGPEKESNE
ALLKEHLDST LANVKTTEPT LPWAAADAEA NTAAVTEAES TASAST
