P43605 (ECO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the acetyltransferase family. GCN5 subfamily.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from mutant phenotype Ref.2. Source: SGD S phase of mitotic cell cycle Inferred from direct assay Ref.1. Source: UniProtKB 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 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_component	cytoplasm Inferred from direct assay PubMed 22842922. Source: SGD nuclear chromatin Inferred from direct assay Ref.2. Source: UniProtKB nuclear replication fork Inferred from direct assay PubMed 16962805. Source: SGD
Molecular_function	acetyltransferase 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

With	Entry	#Exp.	IntAct	Notes
CHL1	P22516	2	EBI-22988,EBI-4600
CTF18	P49956	2	EBI-22988,EBI-4560
MPS3	P47069	5	EBI-22988,EBI-25811

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 281	281	N-acetyltransferase ECO1		PRO_0000074550
Regions
	Zinc finger	33 – 57	25	CCHH-type
Amino acid modifications
	Modified residue	223	1	N6-acetyllysine; by autocatalysis Ref.6
Experimental info
	Mutagenesis	35	1	C → Y in ctf7-109; loss of function. Ref.10
	Mutagenesis	53	1	H → Y in ctf7-108; loss of function. Ref.10
	Mutagenesis	211	1	G → D: Abolishes acetyltransferase activity; but not chromatid cohesion activity. Ref.6
	Mutagenesis	222 – 223	2	RK → GG: Abolishes acetyltransferase activity; but not chromatid cohesion activity.
	Mutagenesis	225	1	G → D: Abolishes acetyltransferase activity; but not chromatid cohesion activity. Ref.6
	Mutagenesis	232	1	D → G: Abolishes acetyltransferase activity; but not chromatid cohesion activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P43605 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 0AF1B59BE9E71818	FASTA	281	31,845
	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

References

	« Hide 'large scale' referencesShow '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 204511 / S288c / AB972.
[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.
PIR	S56282.
RefSeq	NP_116683.1. NM_001179992.1.
3D structure databases
ProteinModelPortal	P43605.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5602N.
IntAct	P43605. 12 interactions.
MINT	MINT-494620.
STRING	4932.YFR027W.
Proteomic databases
PeptideAtlas	P43605.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YFR027W; YFR027W; YFR027W.
GeneID	850584.
KEGG	sce:YFR027W.
Organism-specific databases
CYGD	YFR027w.
SGD	S000001923. ECO1.
Phylogenomic databases
eggNOG	NOG301368.
GeneTree	ENSGT00390000008335.
HOGENOM	HOG000093358.
KO	K11268.
OMA	ISRIWVC.
OrthoDB	EOG46X2JS.
Gene expression databases
Genevestigator	P43605.
GermOnline	YFR027W. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other
NextBio	966420.

Entry information

Entry name

ECO1_YEAST

Accession

Primary (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 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program