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P53323 (BUD32_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EKC/KEOPS complex subunit BUD32

EC=3.6.-.-
Alternative name(s):
Atypical serine/threonine protein kinase BUD32
EC=2.7.11.1
Bud site selection protein 32
Low-dye-binding protein 14
piD261
Gene names
Name:BUD32
Synonyms:LDB14
Ordered Locus Names:YGR262C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Important for bud site selection. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes. Ref.9 Ref.10

Subcellular location

Cytoplasm. Nucleus. Chromosometelomere Ref.7.

Miscellaneous

Present with 3020 molecules/cell in log phase SD medium.

This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event.

Sequence similarities

Belongs to the protein kinase superfamily. BUD32 family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
tRNA processing
   Cellular componentChromosome
Cytoplasm
Nucleus
Telomere
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Hydrolase
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription from RNA polymerase II promoter

Inferred from physical interaction Ref.9. Source: SGD

protein phosphorylation

Inferred from direct assay PubMed 9305753. Source: SGD

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

telomere maintenance

Inferred from mutant phenotype Ref.10. Source: SGD

threonylcarbamoyladenosine metabolic process

Inferred from mutant phenotype Ref.11. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentEKC/KEOPS complex

Inferred from direct assay Ref.10Ref.9. Source: SGD

chromosome, telomeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 14519092PubMed 16429126Ref.10Ref.9PubMed 18467557PubMed 18719252PubMed 19021767PubMed 19172740PubMed 20489023. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay PubMed 9305753. Source: SGD

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261EKC/KEOPS complex subunit BUD32
PRO_0000088189

Regions

Domain16 – 261246Protein kinase
Nucleotide binding22 – 309ATP By similarity

Sites

Active site1611Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue1871Phosphoserine; by autocatalysis Ref.6
Modified residue1891Phosphoserine; by autocatalysis Ref.6

Experimental info

Mutagenesis1871S → A: Reduced kinase activity. Ref.6
Mutagenesis1891S → A: Reduced kinase activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P53323 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D12E97BAE21B3385

FASTA26129,936
        10         20         30         40         50         60 
MTQEFIDKVS SYLTPDVDIA PISQGAEAIV FTTTTHPYLP RAKDSHQKYI IKYRPPKRYR 

        70         80         90        100        110        120 
HPQIDQALTK HRTLNESRLL AKLYLIPGLC VPQLIACDPY NGFIWLEFLG EDLPGGHGFS 

       130        140        150        160        170        180 
NLKNFLWMHD QDPYSDLVAT TLRKVGRQIG LLHWNDYCHG DLTSSNIVLV RDGARWTPHL 

       190        200        210        220        230        240 
IDFGLGSVSN LVEDKGVDLY VLERAILSTH SKHAEKYNAW IMEGFEEVYR EQGAKGAKKL 

       250        260 
KEVTKRFEEV RLRGRKRSML G 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of an 11.6 kb region from the right arm of chromosome VII of Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the presence of three new genes."
Clemente M.L., Sartori G., Cardazzo B., Carignani G.
Yeast 13:287-290(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae."
Ni L., Snyder M.
Mol. Biol. Cell 12:2147-2170(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BUDDING.
[6]"Structure-function analysis of yeast piD261/Bud32, an atypical protein kinase essential for normal cell life."
Facchin S., Lopreiato R., Stocchetto S., Arrigoni G., Cesaro L., Marin O., Carignani G., Pinna L.A.
Biochem. J. 364:457-463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-187 AND SER-189, MUTAGENESIS OF SER-187 AND SER-189.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Yeast homolog of a cancer-testis antigen defines a new transcription complex."
Kisseleva-Romanova E., Lopreiato R., Baudin-Baillieu A., Rousselle J.-C., Ilan L., Hofmann K., Namane A., Mann C., Libri D.
EMBO J. 25:3576-3585(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"A genome-wide screen identifies the evolutionarily conserved KEOPS complex as a telomere regulator."
Downey M., Houlsworth R., Maringele L., Rollie A., Brehme M., Galicia S., Guillard S., Partington M., Zubko M.K., Krogan N.J., Emili A., Greenblatt J.F., Harrington L., Lydall D., Durocher D.
Cell 124:1155-1168(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
[11]"The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A."
Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W., Sternglanz R.
EMBO J. 30:873-881(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN T(6)A37 FORMATION.
[12]"Gcn4 misregulation reveals a direct role for the evolutionary conserved EKC/KEOPS in the t6A modification of tRNAs."
Daugeron M.C., Lenstra T.L., Frizzarin M., El Yacoubi B., Liu X., Baudin-Baillieu A., Lijnzaad P., Decourty L., Saveanu C., Jacquier A., Holstege F.C., de Crecy-Lagard V., van Tilbeurgh H., Libri D.
Nucleic Acids Res. 39:6148-6160(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN T(6)A37 FORMATION.
[13]"In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya."
Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B., van Tilbeurgh H., Forterre P., Basta T.
Nucleic Acids Res. 41:1953-1964(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN T(6)A TRNA MODIFICATION.
[14]"Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system."
Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I., Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C., Caudy A.A., Durocher D., Sicheri F.
Nucleic Acids Res. 41:6332-6346(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE EKC/KEOPS COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07777 Genomic DNA. Translation: CAA69084.1.
Z73047 Genomic DNA. Translation: CAA97291.1.
AY558547 Genomic DNA. Translation: AAS56873.1.
BK006941 Genomic DNA. Translation: DAA08352.1.
PIRS64595.
RefSeqNP_011778.1. NM_001181391.1.

3D structure databases

ProteinModelPortalP53323.
SMRP53323. Positions 9-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33513. 100 interactions.
DIPDIP-5008N.
IntActP53323. 20 interactions.
MINTMINT-571543.
STRING4932.YGR262C.

Chemistry

ChEMBLCHEMBL4515.

Proteomic databases

MaxQBP53323.
PaxDbP53323.

Protocols and materials databases

DNASU853178.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR262C; YGR262C; YGR262C.
GeneID853178.
KEGGsce:YGR262C.

Organism-specific databases

CYGDYGR262c.
SGDS000003494. BUD32.

Phylogenomic databases

eggNOGCOG3642.
GeneTreeENSGT00390000012914.
HOGENOMHOG000226425.
KOK08851.
OMAPPLEQLN.
OrthoDBEOG7R83CW.

Enzyme and pathway databases

BioCycYEAST:G3O-30931-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorP53323.

Family and domain databases

InterProIPR022495. Bud32.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERPTHR12209. PTHR12209. 1 hit.
PfamPF06293. Kdo. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
TIGRFAMsTIGR03724. arch_bud32. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio973311.
PROP53323.

Entry information

Entry nameBUD32_YEAST
AccessionPrimary (citable) accession number: P53323
Secondary accession number(s): D6VV41
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families