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P53323

- BUD32_YEAST

UniProt

P53323 - BUD32_YEAST

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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: 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

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. lipopolysaccharide biosynthetic process Source: InterPro
  3. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  4. protein phosphorylation Source: SGD
  5. telomere maintenance Source: SGD
  6. telomere maintenance via recombination Source: SGD
  7. threonylcarbamoyladenosine metabolic process Source: SGD
  8. transcription, DNA-templated Source: UniProtKB-KW
  9. tRNA processing Source: UniProtKB-KW
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.

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
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR262c.
SGDiS000003494. BUD32.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. Chromosometelomere 1 Publication

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. EKC/KEOPS complex Source: SGD
  4. membrane Source: InterPro
  5. nucleus Source: UniProtKB-KW
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

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.
PaxDbiP53323.

Expressioni

Gene expression databases

GenevestigatoriP53323.

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.
STRINGi4932.YGR262C.

Structurei

3D structure databases

ProteinModelPortaliP53323.
SMRiP53323. Positions 9-229.
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

eggNOGiCOG3642.
GeneTreeiENSGT00390000012914.
HOGENOMiHOG000226425.
InParanoidiP53323.
KOiK08851.
OMAiPPLEQLN.
OrthoDBiEOG7R83CW.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S64595.
RefSeqi NP_011778.1. NM_001181391.1.

3D structure databases

ProteinModelPortali P53323.
SMRi P53323. Positions 9-229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33513. 101 interactions.
DIPi DIP-5008N.
IntActi P53323. 20 interactions.
MINTi MINT-571543.
STRINGi 4932.YGR262C.

Chemistry

ChEMBLi CHEMBL4515.

Proteomic databases

MaxQBi P53323.
PaxDbi P53323.

Protocols and materials databases

DNASUi 853178.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR262C ; YGR262C ; YGR262C .
GeneIDi 853178.
KEGGi sce:YGR262C.

Organism-specific databases

CYGDi YGR262c.
SGDi S000003494. BUD32.

Phylogenomic databases

eggNOGi COG3642.
GeneTreei ENSGT00390000012914.
HOGENOMi HOG000226425.
InParanoidi P53323.
KOi K08851.
OMAi PPLEQLN.
OrthoDBi EOG7R83CW.

Enzyme and pathway databases

BioCyci YEAST:G3O-30931-MONOMER.
BRENDAi 2.7.11.1. 984.

Miscellaneous databases

NextBioi 973311.
PROi P53323.

Gene expression databases

Genevestigatori P53323.

Family and domain databases

InterProi IPR022495. Bud32.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view ]
PANTHERi PTHR12209. PTHR12209. 1 hit.
Pfami PF06293. Kdo. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
TIGRFAMsi TIGR03724. arch_bud32. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. 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. 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.

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: October 29, 2014
This is version 141 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3