Serine/threonine-protein kinase BUD32 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P53323 (BUD32_YEAST)

Last modified June 16, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase BUD32
    EC=2.7.11.1
Alternative name(s):
    Bud site selection protein BUD32
    piD261
    Low-dye-binding protein 14

Gene names

Name:	BUD32
Synonyms:	LDB14
Ordered Locus Names:	YGR262C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Component of the EKC/KEOPS complex which promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Important for bud site selection. Ref.8 Ref.9
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.
Subcellular location	Cytoplasm. Nucleus. Telomere. Ref.6
Miscellaneous	Present with 3020 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosomal protein Cytoplasm Nucleus Telomere
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular bud site selection Ref.4 Inferred from mutant phenotype. Source: SGD positive regulation of transcription from RNA polymerase II promoter Ref.8 Inferred from physical interaction. Source: SGD protein amino acid phosphorylation Inferred from direct assay. Source: SGD telomere maintenance Ref.9 Inferred from genetic interaction. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	EKC/KEOPS protein complex Ref.8 Ref.9 Inferred from direct assay. Source: SGD chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Ref.6 Inferred from direct assay. Source: SGD nucleus Ref.6 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.9 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from direct assay. Source: SGD protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	P38800	1	EBI-3809,EBI-24597
CGI121	Q03705	1	EBI-3809,EBI-912262
GON7	P46984	1	EBI-3809,EBI-26178
GRX4	P32642	5	EBI-3809,EBI-22211
KAE1	P36132	2	EBI-3809,EBI-26411

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Serine/threonine-protein kinase BUD32

PRO_0000088189

Regions

Domain

16 – 261

246

Protein kinase

Nucleotide binding

22 – 30

ATP By similarity

Sites

Active site

161

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

187

Phosphoserine; by autocatalysis Ref.5

Modified residue

189

Phosphoserine; by autocatalysis Ref.5

Experimental info

Mutagenesis

187

S → A: Reduced kinase activity. Ref.5

Mutagenesis

189

S → A: Reduced kinase activity. Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P53323-1 [UniParc].

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

261

29,936

        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

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References

	« Hide 'large scale' referencesShow '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: 9090059] [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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 11452010] [Abstract] Cited for: INVOLVEMENT IN BUDDING.
[5]	"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: 12023889] [Abstract] Cited for: PHOSPHORYLATION AT SER-187 AND SER-189, MUTAGENESIS OF SER-187 AND SER-189.
[6]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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: 16874308] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS COMPLEX.
[9]	"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: 16564010] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Y07777 Genomic DNA. Translation: CAA69084.1. Z73047 Genomic DNA. Translation: CAA97291.1. AY558547 Genomic DNA. Translation: AAS56873.1.
PIR	S64595.
RefSeq	NP_011778.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5008N.
IntAct	P53323. 41 interactions.
Proteomic databases
PRIDE	P53323.
Genome annotation databases
Ensembl	YGR262C. Saccharomyces cerevisiae. [Contig view]
GeneID	853178.
GenomeReviews	Gene locus YGR262C in contig Y13135_GR.
KEGG	sce:YGR262C.
NMPDR	fig\|4932.3.peg.2907.
Organism-specific databases
CYGD	YGR262c.
SGD	S000003494. BUD32.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53323.
OMA	P53323. VVYFVDY.
Enzyme and pathway databases
BRENDA	2.7.11.1. 250.
Gene expression databases
GermOnline	YGR262C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR008266. Tyr_pkinase_AS. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973311.

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Entry information

Entry name

BUD32_YEAST

Accession

Primary (citable) accession number: P53323

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents