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Protein

Centromere-binding protein 1

Gene

CBF1

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

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 MET28.2 Publications

GO - Molecular functioni

  • centromeric DNA binding Source: SGD
  • RNA polymerase II activating transcription factor binding Source: SGD
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: SGD
  • RNA polymerase II repressing transcription factor binding Source: SGD
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: SGD
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: SGD
  • transcription factor activity, RNA polymerase II transcription factor binding Source: SGD

GO - Biological processi

  • chromatin remodeling Source: SGD
  • chromosome segregation Source: SGD
  • negative regulation of ceramide biosynthetic process by negative regulation of transcription from RNA Polymerase II promoter Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of inositol biosynthetic process by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of sulfate assimilation by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to methionine Source: SGD
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31693-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere-binding protein 1
Short name:
CBP-1
Alternative name(s):
Centromere promoter factor 1
Centromere-binding factor 1
Gene namesi
Name:CBF1
Synonyms:CEP1, CP1, CPF1
Ordered Locus Names:YJR060W
ORF Names:J1730
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR060W.
SGDiS000003821. CBF1.

Subcellular locationi

GO - Cellular componenti

  • Cbf1-Met4-Met28 complex Source: SGD
  • chromosome, centromeric region Source: SGD
  • kinetochore Source: SGD
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Centromere-binding protein 1PRO_0000127161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei45 – 451Phosphoserine; by ATM or ATRCombined sources
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources
Modified residuei138 – 1381PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17106.
PeptideAtlasiP17106.

PTM databases

iPTMnetiP17106.

Interactioni

Subunit structurei

Binds DNA as a dimer. Associates with MET4 to form a heteromeric complex which also includes MET28.1 Publication

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD
  • RNA polymerase II repressing transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi33817. 248 interactions.
DIPiDIP-2239N.
IntActiP17106. 4 interactions.
MINTiMINT-433529.

Structurei

3D structure databases

ProteinModelPortaliP17106.
SMRiP17106. Positions 233-271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 27049bHLHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000111343.
InParanoidiP17106.
KOiK09104.
OrthoDBiEOG7HF1X1.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSLANNNKL STEDEEIHSA RKRGYNEEQN YSEARKKQRD QGLLSQESND
60 70 80 90 100
GNIDSALLSE GATLKGTQSQ YESGLTSNKD EKGSDDEDAS VAEAAVAATV
110 120 130 140 150
NYTDLIQGQE DSSDAHTSNQ TNANGEHKDS LNGERAITPS NEGVKPNTSL
160 170 180 190 200
EGMTSSPMES TQQSKNDMLI PLAEHDRGPE HQQDDEDNDD ADIDLKKDIS
210 220 230 240 250
MQPGRRGRKP TTLATTDEWK KQRKDSHKEV ERRRRENINT AINVLSDLLP
260 270 280 290 300
VRESSKAAIL ACAAEYIQKL KETDEANIEK WTLQKLLSEQ NASQLASANE
310 320 330 340 350
KLQEELGNAY KEIEYMKRVL RKEGIEYEDM HTHKKQENER KSTRSDNPHE

A
Length:351
Mass (Da):39,388
Last modified:February 21, 2006 - v2
Checksum:i068F7FA578CB90FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441V → F in CAA36382 (PubMed:2249662).Curated
Sequence conflicti168 – 1681M → T in AAS56245 (PubMed:17322287).Curated
Sequence conflicti262 – 2621C → R (PubMed:2185892).Curated
Sequence conflicti262 – 2621C → R (PubMed:2249662).Curated
Sequence conflicti262 – 2621C → R (PubMed:2188087).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BK006943 Genomic DNA. Translation: DAA08847.1.
PIRiS57079. JSBYP1.
RefSeqiNP_012594.1. NM_001181718.1.

Genome annotation databases

EnsemblFungiiYJR060W; YJR060W; YJR060W.
GeneIDi853523.
KEGGisce:YJR060W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BK006943 Genomic DNA. Translation: DAA08847.1.
PIRiS57079. JSBYP1.
RefSeqiNP_012594.1. NM_001181718.1.

3D structure databases

ProteinModelPortaliP17106.
SMRiP17106. Positions 233-271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33817. 248 interactions.
DIPiDIP-2239N.
IntActiP17106. 4 interactions.
MINTiMINT-433529.

PTM databases

iPTMnetiP17106.

Proteomic databases

MaxQBiP17106.
PeptideAtlasiP17106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR060W; YJR060W; YJR060W.
GeneIDi853523.
KEGGisce:YJR060W.

Organism-specific databases

EuPathDBiFungiDB:YJR060W.
SGDiS000003821. CBF1.

Phylogenomic databases

HOGENOMiHOG000111343.
InParanoidiP17106.
KOiK09104.
OrthoDBiEOG7HF1X1.

Enzyme and pathway databases

BioCyciYEAST:G3O-31693-MONOMER.

Miscellaneous databases

PROiP17106.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 214-231, SUBCELLULAR LOCATION.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MET4.
  10. "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] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  14. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-48 AND SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-48 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCBF1_YEAST
AccessioniPrimary (citable) accession number: P17106
Secondary accession number(s): D6VWN1, P17623, Q6Q5N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 21, 2006
Last modified: June 8, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6890 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.