BUD21_YEAST
ID BUD21_YEAST Reviewed; 214 AA.
AC Q08492; D6W2E1; O00033;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Bud site selection protein 21;
DE AltName: Full=U three protein 16;
DE AltName: Full=U3 small nucleolar RNA-associated protein 16;
DE Short=U3 snoRNA-associated protein 16;
GN Name=BUD21; Synonyms=UTP16; OrderedLocusNames=YOR078W; ORFNames=YOR29-29;
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 [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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]
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 FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
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 SER-144, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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 SER-65 AND SER-144, AND
RP IDENTIFICATION BY 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-16 AND SER-144, 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).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC Has a role in bud site selection maybe via the regulation of expression
CC of bipolar budding components. {ECO:0000269|PubMed:11452010,
CC ECO:0000269|PubMed:12068309}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC the ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3. {ECO:0000269|PubMed:12068309}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11452010,
CC ECO:0000269|PubMed:12068309}.
CC -!- MISCELLANEOUS: Present with 2120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UTP16 family. {ECO:0000305}.
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DR EMBL; Z74986; CAA99271.1; -; Genomic_DNA.
DR EMBL; Z70678; CAA94563.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10857.1; -; Genomic_DNA.
DR PIR; S66961; S66961.
DR RefSeq; NP_014721.1; NM_001183497.1.
DR PDB; 5WLC; EM; 3.80 A; ND=1-214.
DR PDB; 6KE6; EM; 3.40 A; 5B=1-214.
DR PDB; 6LQP; EM; 3.20 A; 5B=1-214.
DR PDB; 6LQQ; EM; 4.10 A; 5B=1-214.
DR PDB; 6LQR; EM; 8.60 A; 5B=1-214.
DR PDB; 6LQS; EM; 3.80 A; 5B=1-214.
DR PDB; 6LQU; EM; 3.70 A; 5B=1-214.
DR PDB; 6LQV; EM; 4.80 A; 5B=1-214.
DR PDB; 6ND4; EM; 4.30 A; D=1-214.
DR PDB; 6ZQA; EM; 4.40 A; UP=1-214.
DR PDB; 6ZQB; EM; 3.90 A; UP=1-214.
DR PDB; 6ZQC; EM; 3.80 A; UP=1-214.
DR PDB; 6ZQD; EM; 3.80 A; UP=1-214.
DR PDB; 6ZQE; EM; 7.10 A; UP=1-214.
DR PDB; 7AJT; EM; 4.60 A; UP=1-214.
DR PDB; 7AJU; EM; 3.80 A; UP=1-214.
DR PDB; 7D4I; EM; 4.00 A; 5B=1-214.
DR PDB; 7D5S; EM; 4.60 A; 5B=1-214.
DR PDB; 7D63; EM; 12.30 A; 5B=1-214.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ND4; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q08492; -.
DR SMR; Q08492; -.
DR BioGRID; 34477; 374.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-1392N; -.
DR IntAct; Q08492; 40.
DR MINT; Q08492; -.
DR STRING; 4932.YOR078W; -.
DR iPTMnet; Q08492; -.
DR MaxQB; Q08492; -.
DR PaxDb; Q08492; -.
DR PRIDE; Q08492; -.
DR EnsemblFungi; YOR078W_mRNA; YOR078W; YOR078W.
DR GeneID; 854245; -.
DR KEGG; sce:YOR078W; -.
DR SGD; S000005604; BUD21.
DR VEuPathDB; FungiDB:YOR078W; -.
DR eggNOG; ENOG502S51X; Eukaryota.
DR HOGENOM; CLU_077704_0_0_1; -.
DR InParanoid; Q08492; -.
DR OMA; KHIRLDE; -.
DR BioCyc; YEAST:G3O-33615-MON; -.
DR PRO; PR:Q08492; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08492; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR InterPro; IPR013268; U3_snoRNA_assoc.
DR Pfam; PF08297; U3_snoRNA_assoc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..214
FT /note="Bud site selection protein 21"
FT /id="PRO_0000065013"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 214 AA; 24385 MW; 6840F16B355693E4 CRC64;
MSNGHVKFDA DESQASASAV TDRQDDVLVI SKKDKEVHSS SDEESDDDDA PQEEGLHSGK
SEVESQITQR EEAIRLEQSQ LRSKRRKQNE LYAKQKKSVN ETEVTDEVIA ELPEELLKNI
DQKDEGSTQY SSSRHVTFDK LDESDENEEA LAKAIKTKKR KTLKNLRKDS VKRGKFRVQL
LSTTQDSKTL PPKKESSIIR SKDRWLNRKA LNKG
