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P43605 (ECO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyltransferase ECO1

EC=2.3.1.-
Alternative name(s):
Chromosome transmission fidelity protein 7
Establishment of cohesion protein 1
Gene names
Name:ECO1
Synonyms:CTF7
Ordered Locus Names:YFR027W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for establishment of sister chromatid cohesion during S phase but not for its further maintenance during G2 or M phases or for loading the cohesin complex onto DNA. Interacts with the three known alternate replication factor C (RFC) complexes, suggesting that these complexes have essential but redundant activity in cohesion establishment. Acts by acetylating the cohesin complex component SMC3. In vitro, possesses acetyltransferase activity where it can acetylate itself and components of the cohesin complex (MCD1, IRR1 and PDS5), but is unable to acetylate histones. Ref.1 Ref.2 Ref.7 Ref.10

Subunit structure

Binds specifically to CHL12, RFC1, RFC2, RFC3, RFC4, RFC5 and RAD24 when members of an RFC complex. Interacts with CHL1 and MPS3. Ref.7 Ref.8 Ref.9 Ref.11

Subcellular location

Nucleus. Note: Associated with chromatin. Ref.1 Ref.2

Post-translational modification

Autoacetylates in vitro. Ref.6 Ref.11

Sequence similarities

Belongs to the acetyltransferase family. ECO subfamily.

Ontologies

Keywords
   Biological processCell cycle
DNA replication
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from direct assay PubMed 11448778. Source: SGD

DNA replication

Inferred from mutant phenotype Ref.2. Source: SGD

chromosome organization

Inferred from mutant phenotype PubMed 19948494. Source: SGD

double-strand break repair

Inferred from mutant phenotype PubMed 11448778. Source: SGD

establishment of mitotic sister chromatid cohesion

Inferred from mutant phenotype Ref.1Ref.2. Source: SGD

internal peptidyl-lysine acetylation

Inferred from direct assay Ref.11. Source: SGD

mitotic S phase

Inferred from direct assay Ref.1. Source: UniProtKB

mitotic chromosome condensation

Inferred from mutant phenotype PubMed 19948494. Source: SGD

positive regulation of sister chromatid cohesion

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of DNA replication

Inferred from genetic interaction Ref.1. Source: UniProtKB

regulation of mitosis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

tRNA gene clustering

Inferred from mutant phenotype PubMed 19948494. Source: SGD

telomere organization

Inferred from mutant phenotype PubMed 19948494. Source: SGD

   Cellular_componentnuclear chromatin

Inferred from direct assay Ref.2. Source: UniProtKB

nuclear replication fork

Inferred from direct assay PubMed 16962805. Source: SGD

   Molecular_functionacetyltransferase activity

Inferred from direct assay Ref.6. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281N-acetyltransferase ECO1
PRO_0000074550

Regions

Zinc finger33 – 5725CCHH-type

Amino acid modifications

Modified residue2231N6-acetyllysine; by autocatalysis Ref.6

Experimental info

Mutagenesis351C → Y in ctf7-109; loss of function. Ref.10
Mutagenesis531H → Y in ctf7-108; loss of function. Ref.10
Mutagenesis2111G → D: Abolishes acetyltransferase activity; but not chromatid cohesion activity. Ref.6
Mutagenesis222 – 2232RK → GG: Abolishes acetyltransferase activity; but not chromatid cohesion activity.
Mutagenesis2251G → D: Abolishes acetyltransferase activity; but not chromatid cohesion activity. Ref.6
Mutagenesis2321D → G: Abolishes acetyltransferase activity; but not chromatid cohesion activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P43605 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 0AF1B59BE9E71818

FASTA28131,845
        10         20         30         40         50         60 
MKARKSQRKA GSKPNLIQSK LQVNNGSKSN KIVKCDKCEM SYSSTSIEDR AIHEKYHTLQ 

        70         80         90        100        110        120 
LHGRKWSPNW GSIVYTERNH SRTVHLSRST GTITPLNSSP LKKSSPSITH QEEKIVYVRP 

       130        140        150        160        170        180 
DKSNGEVRAM TEIMTLVNNE LNAPHDENVI WNSTTEEKGK AFVYIRNDRA VGIIIIENLY 

       190        200        210        220        230        240 
GGNGKTSSRG RWMVYDSRRL VQNVYPDFKI GISRIWVCRT ARKLGIATKL IDVARENIVY 

       250        260        270        280 
GEVIPRYQVA WSQPTDSGGK LASKYNGIMH KSGKLLLPVY I 

« Hide

References

« Hide 'large scale' references
[1]"Ctf7p is essential for sister chromatid cohesion and links mitotic chromosome structure to the DNA replication machinery."
Skibbens R.V., Corson L.B., Koshland D., Hieter P.
Genes Dev. 13:307-319(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication."
Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.
Genes Dev. 13:320-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: ATCC 200060 / W303.
[3]"Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae."
Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H., Hanaoka F., Murakami Y.
Yeast 12:177-190(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion."
Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H., Nasmyth K.
Curr. Biol. 12:323-328(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-223, ENZYME ACTIVITY, MUTAGENESIS OF GLY-211; 222-ARG-LYS-223; GLY-225 AND ASP-232.
[7]"Mechanical link between cohesion establishment and DNA replication: Ctf7p/Eco1p, a cohesion establishment factor, associates with three different replication factor C complexes."
Kenna M.A., Skibbens R.V.
Mol. Cell. Biol. 23:2999-3007(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHL12; RFC1; RFC2; RFC3; RFC4; RFC5 AND RAD24.
[8]"Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion."
Skibbens R.V.
Genetics 166:33-42(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHL1.
[9]"The spindle pole body assembly component Mps3p/Nep98p functions in sister chromatid cohesion."
Antoniacci L.M., Kenna M.A., Uetz P., Fields S., Skibbens R.V.
J. Biol. Chem. 279:49542-49550(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPS3.
[10]"Ctf7p/Eco1p exhibits acetyltransferase activity -- but does it matter?"
Brands A., Skibbens R.V.
Curr. Biol. 15:R50-R51(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-35 AND HIS-53.
[11]"Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast."
Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X., Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.
Mol. Cell 31:143-151(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, AUTOACETYLATION, INTERACTION WITH SMC3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50617 Genomic DNA. Translation: BAA09266.1.
BK006940 Genomic DNA. Translation: DAA12467.1.
PIRS56282.
RefSeqNP_116683.1. NM_001179992.1.

3D structure databases

ProteinModelPortalP43605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31181. 42 interactions.
DIPDIP-5602N.
IntActP43605. 12 interactions.
MINTMINT-494620.
STRING4932.YFR027W.

Proteomic databases

PeptideAtlasP43605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFR027W; YFR027W; YFR027W.
GeneID850584.
KEGGsce:YFR027W.

Organism-specific databases

CYGDYFR027w.
SGDS000001923. ECO1.

Phylogenomic databases

eggNOGNOG301368.
HOGENOMHOG000093358.
KOK11268.
OMAISRIWVC.
OrthoDBEOG7D2FPZ.

Enzyme and pathway databases

BioCycYEAST:G3O-30476-MONOMER.

Gene expression databases

GenevestigatorP43605.

Family and domain databases

InterProIPR028005. AcTrfase_ESCO_Znf_dom.
IPR016181. Acyl_CoA_acyltransferase.
IPR028009. ESCO_Acetyltransf_dom.
[Graphical view]
PfamPF13880. Acetyltransf_13. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio966420.

Entry information

Entry nameECO1_YEAST
AccessionPrimary (citable) accession number: P43605
Secondary accession number(s): D6VTQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families