Centromere-binding protein 1 - Saccharomyces cerevisiae (Baker's yeast)

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Names and origin

Protein names

Recommended name:
    Centromere-binding protein 1
      Short name=CBP-1
Alternative name(s):
    Centromere-binding factor 1
    Centromere promoter factor 1

Gene names

Name:	CBF1
Synonyms:	CEP1, CP1, CPF1
Ordered Locus Names:	YJR060W
ORF Names:	J1730

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	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Required for chromosome stability and methionine prototrophy. It is involved in chromosomal segregation. Binds to a highly conserved DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in several promoters. DNA-binding activity is enhanced by MET28. Required as an auxiliary factor for transcriptional activation of sulfur metabolism together with MET4 and MET28. Ref.7 Ref.8
Subunit structure	Binds DNA as a dimer. Associates with MET4 to form a heteromeric complex which also includes MET28. Ref.9
Subcellular location	Nucleus. Mitochondrion. Centromere Ref.10 Ref.12.
Miscellaneous	Present with 6890 molecules/cell in log phase SD medium. Ref.11
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Centromere Chromosomal protein Mitochondrion Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	chromatin assembly or disassembly Inferred from direct assay. Source: SGD chromosome segregation Ref.1 Inferred from mutant phenotype. Source: SGD methionine biosynthetic process Ref.1 Inferred from mutant phenotype. Source: SGD negative regulation of transcription Inferred from mutant phenotype. Source: SGD positive regulation of gene-specific transcription Inferred from mutant phenotype. Source: SGD response to drug Inferred from mutant phenotype. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	kinetochore Traceable author statement. Source: SGD mitochondrion Ref.12 Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	centromeric DNA binding Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct transcription factor activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-4096,EBI-4096

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 351

351

Centromere-binding protein 1

PRO_0000127161

Regions

Domain

236 – 271

Helix-loop-helix motif

DNA binding

222 – 235

Basic motif

Amino acid modifications

Modified residue

Phosphoserine; by ATM or ATR Ref.14 Ref.15

Modified residue

Phosphoserine Ref.14 Ref.15

Modified residue

Phosphoserine Ref.15

Modified residue

138

Phosphothreonine Ref.15 Ref.13

Modified residue

140

Phosphoserine Ref.15

Modified residue

148

Phosphothreonine Ref.14

Modified residue

149

Phosphoserine Ref.15

Modified residue

154

Phosphothreonine Ref.15

Modified residue

155

Phosphoserine Ref.14

Modified residue

156

Phosphoserine Ref.14 Ref.15

Experimental info

Sequence conflict

144

V → F in CAA36382. Ref.2

Sequence conflict

168

M → T in AAS56245. Ref.6

Sequence conflict

262

C → R Ref.1

Sequence conflict

262

C → R Ref.2

Sequence conflict

262

C → R Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P17106-1 [UniParc].

Last modified February 21, 2006. Version 2.
Checksum: 068F7FA578CB90FC
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FASTA

351

39,388

        10         20         30         40         50         60 
MNSLANNNKL STEDEEIHSA RKRGYNEEQN YSEARKKQRD QGLLSQESND GNIDSALLSE 

        70         80         90        100        110        120 
GATLKGTQSQ YESGLTSNKD EKGSDDEDAS VAEAAVAATV NYTDLIQGQE DSSDAHTSNQ 

       130        140        150        160        170        180 
TNANGEHKDS LNGERAITPS NEGVKPNTSL EGMTSSPMES TQQSKNDMLI PLAEHDRGPE 

       190        200        210        220        230        240 
HQQDDEDNDD ADIDLKKDIS MQPGRRGRKP TTLATTDEWK KQRKDSHKEV ERRRRENINT 

       250        260        270        280        290        300 
AINVLSDLLP VRESSKAAIL ACAAEYIQKL KETDEANIEK WTLQKLLSEQ NASQLASANE 

       310        320        330        340        350 
KLQEELGNAY KEIEYMKRVL RKEGIEYEDM HTHKKQENER KSTRSDNPHE A

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy." Cai M., Davis R.W. Cell 61:437-446(1990) [PubMed: 2185892] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 214-231.
[2]	"CPF1, a yeast protein which functions in centromeres and promoters." Mellor J., Jiang W., Funk M., Rathjen J., Barnes C.A., Hinz T., Hegemann J.H., Philippsen P. EMBO J. 9:4017-4026(1990) [PubMed: 2249662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 44827 / SKQ2N.
[3]	"Isolation of the gene encoding the Saccharomyces cerevisiae centromere-binding protein CP1." Baker R.E., Masison D.C. Mol. Cell. Biol. 10:2458-2467(1990) [PubMed: 2188087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI." Huang M.-E., Manus V., Chuat J.-C., Galibert F. Yeast 12:869-875(1996) [PubMed: 8840504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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.
[7]	"MET4, a leucine zipper protein, and centromere-binding factor 1 are both required for transcriptional activation of sulfur metabolism in Saccharomyces cerevisiae." Thomas D., Jacquemin I., Surdin-Kerjan Y. Mol. Cell. Biol. 12:1719-1727(1992) [PubMed: 1549123] [Abstract] Cited for: FUNCTION.
[8]	"A heteromeric complex containing the centromere binding factor 1 and two basic leucine zipper factors, Met4 and Met28, mediates the transcription activation of yeast sulfur metabolism." Kuras L., Cherest H., Surdin-Kerjan Y., Thomas D. EMBO J. 15:2519-2529(1996) [PubMed: 8665859] [Abstract] Cited for: FUNCTION, INTERACTION WITH MET4.
[9]	"Assembly of a bZIP-bHLH transcription activation complex: formation of the yeast Cbf1-Met4-Met28 complex is regulated through Met28 stimulation of Cbf1 DNA binding." Kuras L., Barbey R., Thomas D. EMBO J. 16:2441-2451(1997) [PubMed: 9171357] [Abstract] Cited for: SUBUNIT.
[10]	"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].
[11]	"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].
[12]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, MASS SPECTROMETRY.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-48; THR-148; SER-155 AND SER-156, MASS SPECTROMETRY.
[15]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-48; SER-84; THR-138; SER-140; SER-149; THR-154 AND SER-156, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	M33620 Genomic DNA. Translation: AAA34490.1. X52137 Genomic DNA. Translation: CAA36382.1. M34070 Genomic DNA. Translation: AAA34524.1. L47993 Genomic DNA. Translation: AAB39286.1. Z49560 Genomic DNA. Translation: CAA89588.1. AY557919 Genomic DNA. Translation: AAS56245.1.
PIR	JSBYP1. S57079.
RefSeq	NP_012594.1.
3D structure databases
SMR	P17106. Positions 220-274.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2239N.
IntAct	P17106. 8 interactions.
STRING	P17106.
Proteomic databases
PeptideAtlas	P17106.
Genome annotation databases
Ensembl	YJR060W; YJR060W; YJR060W; Saccharomyces cerevisiae. [Genome view]
GeneID	853523.
KEGG	sce:YJR060W.
NMPDR	fig\|4932.3.peg.3568.
Organism-specific databases
CYGD	YJR060w.
SGD	S000003821. CBF1.
Phylogenomic databases
eggNOG	fuNOG10728.
OrthoDB	EOG9XPRZ0.
PhylomeDB	P17106.
Gene expression databases
ArrayExpress	P17106.
Genevestigator	P17106.
GermOnline	YJR060W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001092. HLH_DNA-bd_dom. IPR011598. HLH_DNA_bd. [Graphical view]
Gene3D	G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
Pfam	PF00010. HLH. 1 hit. [Graphical view]
SMART	SM00353. HLH. 1 hit. [Graphical view]
PROSITE	PS50888. HLH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974206.

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Entry information

Entry name

CBF1_YEAST

Accession

Primary (citable) accession number: P17106
Secondary accession number(s): P17623, Q6Q5N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 21, 2006
Last modified:	January 19, 2010
This is version 98 of the entry and version 2 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 X

Yeast (Saccharomyces cerevisiae) chromosome X: 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

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

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents