BUD32_YEAST
ID BUD32_YEAST Reviewed; 261 AA.
AC P53323; D6VV41;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=EKC/KEOPS complex subunit BUD32;
DE EC=3.6.-.- {ECO:0000250|UniProtKB:Q9UYB9};
DE AltName: Full=Atypical serine/threonine protein kinase BUD32;
DE EC=2.7.11.1 {ECO:0000305|PubMed:12023889};
DE AltName: Full=Bud site selection protein 32;
DE AltName: Full=Low-dye-binding protein 14;
DE AltName: Full=piD261;
GN Name=BUD32; Synonyms=LDB14; OrderedLocusNames=YGR262C;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090059;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<287::aid-yea75>3.0.co;2-5;
RA Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the
RT presence of three new genes.";
RL Yeast 13:287-290(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [5]
RP INVOLVEMENT IN BUDDING.
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 PHOSPHORYLATION AT SER-187 AND SER-189, AND MUTAGENESIS OF SER-187 AND
RP SER-189.
RX PubMed=12023889; DOI=10.1042/bj20011376;
RA Facchin S., Lopreiato R., Stocchetto S., Arrigoni G., Cesaro L., Marin O.,
RA Carignani G., Pinna L.A.;
RT "Structure-function analysis of yeast piD261/Bud32, an atypical protein
RT kinase essential for normal cell life.";
RL Biochem. J. 364:457-463(2002).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS COMPLEX,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16874308; DOI=10.1038/sj.emboj.7601235;
RA Kisseleva-Romanova E., Lopreiato R., Baudin-Baillieu A., Rousselle J.-C.,
RA Ilan L., Hofmann K., Namane A., Mann C., Libri D.;
RT "Yeast homolog of a cancer-testis antigen defines a new transcription
RT complex.";
RL EMBO J. 25:3576-3585(2006).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
RX PubMed=16564010; DOI=10.1016/j.cell.2005.12.044;
RA Downey M., Houlsworth R., Maringele L., Rollie A., Brehme M., Galicia S.,
RA Guillard S., Partington M., Zubko M.K., Krogan N.J., Emili A.,
RA Greenblatt J.F., Harrington L., Lydall D., Durocher D.;
RT "A genome-wide screen identifies the evolutionarily conserved KEOPS complex
RT as a telomere regulator.";
RL Cell 124:1155-1168(2006).
RN [11]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21183954; DOI=10.1038/emboj.2010.343;
RA Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W.,
RA Sternglanz R.;
RT "The highly conserved KEOPS/EKC complex is essential for a universal tRNA
RT modification, t6A.";
RL EMBO J. 30:873-881(2011).
RN [12]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21459853; DOI=10.1093/nar/gkr178;
RA Daugeron M.C., Lenstra T.L., Frizzarin M., El Yacoubi B., Liu X.,
RA Baudin-Baillieu A., Lijnzaad P., Decourty L., Saveanu C., Jacquier A.,
RA Holstege F.C., de Crecy-Lagard V., van Tilbeurgh H., Libri D.;
RT "Gcn4 misregulation reveals a direct role for the evolutionary conserved
RT EKC/KEOPS in the t6A modification of tRNAs.";
RL Nucleic Acids Res. 39:6148-6160(2011).
RN [13]
RP FUNCTION IN T(6)A TRNA MODIFICATION.
RX PubMed=23258706; DOI=10.1093/nar/gks1287;
RA Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B.,
RA van Tilbeurgh H., Forterre P., Basta T.;
RT "In vitro biosynthesis of a universal t6A tRNA modification in Archaea and
RT Eukarya.";
RL Nucleic Acids Res. 41:1953-1964(2013).
RN [14]
RP FUNCTION IN THE EKC/KEOPS COMPLEX.
RX PubMed=23620299; DOI=10.1093/nar/gkt322;
RA Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I.,
RA Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C.,
RA Caudy A.A., Durocher D., Sicheri F.;
RT "Reconstitution and characterization of eukaryotic N6-
RT threonylcarbamoylation of tRNA using a minimal enzyme system.";
RL Nucleic Acids Res. 41:6332-6346(2013).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase
CC activity in the context of the EKC/KEOPS complex and likely plays a
CC supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex
CC also promotes both telomere uncapping and telomere elongation. The
CC complex is required for efficient recruitment of transcriptional
CC coactivators. Important for bud site selection.
CC {ECO:0000269|PubMed:16564010, ECO:0000269|PubMed:16874308,
CC ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:21459853,
CC ECO:0000269|PubMed:23258706, ECO:0000269|PubMed:23620299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305|PubMed:12023889};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305|PubMed:12023889};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least BUD32,
CC CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
CC {ECO:0000269|PubMed:16564010, ECO:0000269|PubMed:16874308}.
CC -!- INTERACTION:
CC P53323; Q03705: CGI121; NbExp=9; IntAct=EBI-3809, EBI-912262;
CC P53323; P46984: GON7; NbExp=6; IntAct=EBI-3809, EBI-26178;
CC P53323; Q03835: GRX3; NbExp=3; IntAct=EBI-3809, EBI-22178;
CC P53323; P32642: GRX4; NbExp=11; IntAct=EBI-3809, EBI-22211;
CC P53323; P36132: KAE1; NbExp=21; IntAct=EBI-3809, EBI-26411;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Chromosome, telomere
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: This protein is considered an atypical serine/threonine kinase,
CC because it lacks the conventional structural elements necessary for the
CC substrate recognition as well as a lysine residue that in all other
CC serine/threonine kinases participates in the catalytic event
CC (PubMed:12023889). BUD32 has protein kinase activity in vitro, but in
CC the context of the EKC/KEOPS complex, the catalytic subunit KAE1
CC switches the activity of BUD32 from kinase into ATPase (By similarity).
CC {ECO:0000250|UniProtKB:Q9UYB9, ECO:0000305|PubMed:12023889}.
CC -!- MISCELLANEOUS: Present with 3020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000305}.
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DR EMBL; Y07777; CAA69084.1; -; Genomic_DNA.
DR EMBL; Z73047; CAA97291.1; -; Genomic_DNA.
DR EMBL; AY558547; AAS56873.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08352.1; -; Genomic_DNA.
DR PIR; S64595; S64595.
DR RefSeq; NP_011778.1; NM_001181391.1.
DR PDB; 4WW5; X-ray; 2.00 A; A=1-261.
DR PDB; 4WW7; X-ray; 1.67 A; A=1-261.
DR PDB; 4WW9; X-ray; 1.95 A; A=1-261.
DR PDB; 4WWA; X-ray; 2.95 A; A=1-261.
DR PDBsum; 4WW5; -.
DR PDBsum; 4WW7; -.
DR PDBsum; 4WW9; -.
DR PDBsum; 4WWA; -.
DR AlphaFoldDB; P53323; -.
DR SMR; P53323; -.
DR BioGRID; 33513; 127.
DR ComplexPortal; CPX-995; KEOPS complex.
DR DIP; DIP-5008N; -.
DR IntAct; P53323; 68.
DR MINT; P53323; -.
DR STRING; 4932.YGR262C; -.
DR ChEMBL; CHEMBL4515; -.
DR iPTMnet; P53323; -.
DR MaxQB; P53323; -.
DR PaxDb; P53323; -.
DR PRIDE; P53323; -.
DR DNASU; 853178; -.
DR EnsemblFungi; YGR262C_mRNA; YGR262C; YGR262C.
DR GeneID; 853178; -.
DR KEGG; sce:YGR262C; -.
DR SGD; S000003494; BUD32.
DR VEuPathDB; FungiDB:YGR262C; -.
DR eggNOG; KOG3087; Eukaryota.
DR GeneTree; ENSGT00390000012914; -.
DR HOGENOM; CLU_063953_1_1_1; -.
DR InParanoid; P53323; -.
DR OMA; KPWRHPI; -.
DR BioCyc; YEAST:G3O-30931-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P53323; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53323; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0000282; P:cellular bud site selection; HMP:SGD.
DR GO; GO:1990145; P:maintenance of translational fidelity; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IPI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IMP:SGD.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IC:ComplexPortal.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR12209; PTHR12209; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Chromosome; Cytoplasm; Hydrolase;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transcription;
KW Transcription regulation; Transferase; tRNA processing.
FT CHAIN 1..261
FT /note="EKC/KEOPS complex subunit BUD32"
FT /id="PRO_0000088189"
FT DOMAIN 16..261
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 187
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12023889"
FT MOD_RES 189
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12023889"
FT MUTAGEN 187
FT /note="S->A: Reduced kinase activity."
FT /evidence="ECO:0000269|PubMed:12023889"
FT MUTAGEN 189
FT /note="S->A: Reduced kinase activity."
FT /evidence="ECO:0000269|PubMed:12023889"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4WW7"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4WWA"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 136..154
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 214..230
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 233..253
FT /evidence="ECO:0007829|PDB:4WW7"
SQ SEQUENCE 261 AA; 29936 MW; D12E97BAE21B3385 CRC64;
MTQEFIDKVS SYLTPDVDIA PISQGAEAIV FTTTTHPYLP RAKDSHQKYI IKYRPPKRYR
HPQIDQALTK HRTLNESRLL AKLYLIPGLC VPQLIACDPY NGFIWLEFLG EDLPGGHGFS
NLKNFLWMHD QDPYSDLVAT TLRKVGRQIG LLHWNDYCHG DLTSSNIVLV RDGARWTPHL
IDFGLGSVSN LVEDKGVDLY VLERAILSTH SKHAEKYNAW IMEGFEEVYR EQGAKGAKKL
KEVTKRFEEV RLRGRKRSML G
