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P53323

- BUD32_YEAST

UniProt

P53323 - BUD32_YEAST

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
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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 binding Source: IntAct
    4. protein serine/threonine kinase activity Source: SGD
    5. protein tyrosine kinase activity Source: InterPro

    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

    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-SubCell
    2. cytoplasm Source: UniProtKB-SubCell
    3. EKC/KEOPS complex Source: SGD
    4. membrane Source: InterPro
    5. nucleus Source: UniProtKB-SubCell

    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. 100 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.
    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

    MTQEFIDKVS SYLTPDVDIA PISQGAEAIV FTTTTHPYLP RAKDSHQKYI    50
    IKYRPPKRYR HPQIDQALTK HRTLNESRLL AKLYLIPGLC VPQLIACDPY 100
    NGFIWLEFLG EDLPGGHGFS NLKNFLWMHD QDPYSDLVAT TLRKVGRQIG 150
    LLHWNDYCHG DLTSSNIVLV RDGARWTPHL IDFGLGSVSN LVEDKGVDLY 200
    VLERAILSTH SKHAEKYNAW IMEGFEEVYR EQGAKGAKKL KEVTKRFEEV 250
    RLRGRKRSML G 261
    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. 100 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.
    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

    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 1, 2014
    This is version 140 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