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Protein

EKC/KEOPS complex subunit BUD32

Gene

BUD32

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPPROSITE-ProRule annotation
Active sitei161 – 1611Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • protein phosphorylation Source: SGD
  • telomere maintenance Source: SGD
  • telomere maintenance via recombination Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA modification Source: Reactome
  • tRNA threonylcarbamoyladenosine metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator, Hydrolase, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation, tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30931-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:BUD32
Synonyms:LDB14
Ordered Locus Names:YGR262C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR262C.
SGDiS000003494. BUD32.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • cytosol Source: GO_Central
  • EKC/KEOPS complex Source: SGD
  • membrane Source: InterPro
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871S → A: Reduced kinase activity. 1 Publication
Mutagenesisi189 – 1891S → A: Reduced kinase activity. 1 Publication

Chemistry

ChEMBLiCHEMBL4515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261EKC/KEOPS complex subunit BUD32PRO_0000088189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei187 – 1871Phosphoserine; by autocatalysis1 Publication
Modified residuei189 – 1891Phosphoserine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53323.

PTM databases

iPTMnetiP53323.

Interactioni

Subunit structurei

Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CGI121Q037058EBI-3809,EBI-912262
GON7P469846EBI-3809,EBI-26178
GRX4P3264210EBI-3809,EBI-22211
KAE1P3613220EBI-3809,EBI-26411

Protein-protein interaction databases

BioGridi33513. 101 interactions.
DIPiDIP-5008N.
IntActiP53323. 20 interactions.
MINTiMINT-571543.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Beta strandi20 – 245Combined sources
Beta strandi29 – 357Combined sources
Beta strandi37 – 393Combined sources
Beta strandi49 – 535Combined sources
Helixi73 – 8412Combined sources
Beta strandi94 – 985Combined sources
Turni99 – 1024Combined sources
Beta strandi103 – 1075Combined sources
Helixi114 – 1163Combined sources
Beta strandi118 – 1214Combined sources
Helixi122 – 1298Combined sources
Helixi136 – 15419Combined sources
Beta strandi166 – 1727Combined sources
Beta strandi175 – 1806Combined sources
Helixi192 – 20716Combined sources
Helixi214 – 23017Combined sources
Helixi233 – 25321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WW5X-ray2.00A1-261[»]
4WW7X-ray1.67A1-261[»]
4WW9X-ray1.95A1-261[»]
4WWAX-ray2.95A1-261[»]
ProteinModelPortaliP53323.
SMRiP53323. Positions 4-257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 261246Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000012914.
HOGENOMiHOG000226425.
InParanoidiP53323.
KOiK08851.
OMAiSVHPYLP.
OrthoDBiEOG092C484K.

Family and domain databases

InterProiIPR022495. Bud32.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERiPTHR12209. PTHR12209. 1 hit.
PfamiPF06293. Kdo. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR03724. arch_bud32. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQEFIDKVS SYLTPDVDIA PISQGAEAIV FTTTTHPYLP RAKDSHQKYI
60 70 80 90 100
IKYRPPKRYR HPQIDQALTK HRTLNESRLL AKLYLIPGLC VPQLIACDPY
110 120 130 140 150
NGFIWLEFLG EDLPGGHGFS NLKNFLWMHD QDPYSDLVAT TLRKVGRQIG
160 170 180 190 200
LLHWNDYCHG DLTSSNIVLV RDGARWTPHL IDFGLGSVSN LVEDKGVDLY
210 220 230 240 250
VLERAILSTH SKHAEKYNAW IMEGFEEVYR EQGAKGAKKL KEVTKRFEEV
260
RLRGRKRSML G
Length:261
Mass (Da):29,936
Last modified:October 1, 1996 - v1
Checksum:iD12E97BAE21B3385
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07777 Genomic DNA. Translation: CAA69084.1.
Z73047 Genomic DNA. Translation: CAA97291.1.
AY558547 Genomic DNA. Translation: AAS56873.1.
BK006941 Genomic DNA. Translation: DAA08352.1.
PIRiS64595.
RefSeqiNP_011778.1. NM_001181391.1.

Genome annotation databases

EnsemblFungiiYGR262C; YGR262C; YGR262C.
GeneIDi853178.
KEGGisce:YGR262C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07777 Genomic DNA. Translation: CAA69084.1.
Z73047 Genomic DNA. Translation: CAA97291.1.
AY558547 Genomic DNA. Translation: AAS56873.1.
BK006941 Genomic DNA. Translation: DAA08352.1.
PIRiS64595.
RefSeqiNP_011778.1. NM_001181391.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WW5X-ray2.00A1-261[»]
4WW7X-ray1.67A1-261[»]
4WW9X-ray1.95A1-261[»]
4WWAX-ray2.95A1-261[»]
ProteinModelPortaliP53323.
SMRiP53323. Positions 4-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33513. 101 interactions.
DIPiDIP-5008N.
IntActiP53323. 20 interactions.
MINTiMINT-571543.

Chemistry

ChEMBLiCHEMBL4515.

PTM databases

iPTMnetiP53323.

Proteomic databases

MaxQBiP53323.

Protocols and materials databases

DNASUi853178.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR262C; YGR262C; YGR262C.
GeneIDi853178.
KEGGisce:YGR262C.

Organism-specific databases

EuPathDBiFungiDB:YGR262C.
SGDiS000003494. BUD32.

Phylogenomic databases

GeneTreeiENSGT00390000012914.
HOGENOMiHOG000226425.
InParanoidiP53323.
KOiK08851.
OMAiSVHPYLP.
OrthoDBiEOG092C484K.

Enzyme and pathway databases

BioCyciYEAST:G3O-30931-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

PROiP53323.

Family and domain databases

InterProiIPR022495. Bud32.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERiPTHR12209. PTHR12209. 1 hit.
PfamiPF06293. Kdo. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR03724. arch_bud32. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBUD32_YEAST
AccessioniPrimary (citable) accession number: P53323
Secondary accession number(s): D6VV41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3020 molecules/cell in log phase SD medium.1 Publication
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 (PubMed:12023889). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).By similarity1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.