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Protein

N-acetyltransferase eso1

Gene

eso1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. The relevance of acetyltransferase function remains unclear (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri653 – 67725CCHH-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • establishment of mitotic sister chromatid cohesion Source: PomBase
  • peptidyl-lysine N6-acetylation Source: PomBase
  • positive regulation of maintenance of mitotic sister chromatid cohesion, centromeric Source: PomBase
  • protein acetylation Source: PomBase
  • regulation of maintenance of mitotic sister chromatid cohesion Source: PomBase
  • translesion synthesis Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-110320. Translesion Synthesis by POLH.
R-SPO-5656169. Termination of translesion DNA synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyltransferase eso1 (EC:2.3.1.-)
Alternative name(s):
ECO1 homolog
Sister chromatid cohesion protein eso1
Gene namesi
Name:eso1
ORF Names:SPBC16A3.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16A3.11.
PomBaseiSPBC16A3.11. eso1.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleus Source: PomBase
  • site of double-strand break Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 872872N-acetyltransferase eso1PRO_0000173994Add
BLAST

Proteomic databases

MaxQBiO42917.

Interactioni

Subunit structurei

Interacts with pds5.1 Publication

Protein-protein interaction databases

BioGridi276221. 241 interactions.
IntActiO42917. 1 interaction.
MINTiMINT-4673961.

Structurei

3D structure databases

ProteinModelPortaliO42917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 285257UmuCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 591591Polymerase type-YAdd
BLAST
Regioni592 – 872281AcetyltransferaseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the acetyltransferase family. ECO subfamily.Curated
In the N-terminal section; belongs to the DNA polymerase type-Y family.Curated
Contains 1 umuC domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri653 – 67725CCHH-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiO42917.
KOiK03509.
OrthoDBiEOG7RFTT2.
PhylomeDBiO42917.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR028005. AcTrfase_ESCO_Znf_dom.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR028009. ESCO_Acetyltransf_dom.
IPR001126. UmuC.
[Graphical view]
PfamiPF13880. Acetyltransf_13. 1 hit.
PF00817. IMS. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42917-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELGKSKFSW KDLQYCDKAG TQNSPLRVVA HIDQDAFYAQ VESVRLGLDH
60 70 80 90 100
SVPLAVQQWQ GLIAVNYAAR AANISRHETV TEAKKKCPEL CTAHVKTWKA
110 120 130 140 150
GESEAKYHEN PNPNYYKTCL DPYRHESVKI LNIIKKHAPV VKKASIDECF
160 170 180 190 200
IELTSDVKRI VLEEYPYLKI PSEDSNVALP QAPVLLWPAE FGMVIEEEVV
210 220 230 240 250
DRTKEDYERD WDDVFLFYAA KIVKEIRDDI YLQLKYTCSA GVSFNPMLSK
260 270 280 290 300
LVSSRNKPNK QTILTKNAIQ DYLVSLKITD IRMLGGKFGE EIINLLGTDS
310 320 330 340 350
IKDVWNMSMD FLIDKLGQTN GPLVWNLCHG IDNTEITTQV QIKSMLSAKN
360 370 380 390 400
FSQQKVKSEE DAINWFQVFA SDLRSRFLEL EGMRRPKTIC LTVVSRFLRK
410 420 430 440 450
SRSSQIPMNV DISTQFIVEA TSKLLRQLQQ EFDVYPISNL SISFQNIIEV
460 470 480 490 500
DRNSRGIEGF LKKSNDEIYM STSVSPSIEG RAKLLNENMR ENNSFELSSE
510 520 530 540 550
KDIKSPKRLK RGKGKGIFDM LQQTAVSKPT ENSADETYTC EECEQKITLS
560 570 580 590 600
ERNEHEDYHI ALSISRKERY NNLVPPSHDK PKQVKPKTYG RKTGSKHYAP
610 620 630 640 650
LSDETNNKRA FLDAFLGNGG NLTPNWKKQT PKAISNSSDN MTQLHLDLAN
660 670 680 690 700
STVTCSECSM EYNSTSEEDI LLHSRFHSRV LGGVTVSFQC SPIYRVNYGL
710 720 730 740 750
SSDCIYSINS ESSLIDQRKA EEALSFVNNE LSSEPIETIG VDKYTTFLFI
760 770 780 790 800
SDKKCVGLLL AERISSAYIV DELELNNNNS TSSAVYIKNE NLRKGFVLGI
810 820 830 840 850
SRIWVSASRR KQGIASLLLD NALKKFIYGY VISPAEVAFS QPSESGKQFI
860 870
ISWHRSRNNG SSKSLRYAVY ES
Length:872
Mass (Da):98,909
Last modified:June 1, 1998 - v1
Checksum:i36ECCD2BC0AEFE94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB039861 mRNA. Translation: BAA95122.1.
CU329671 Genomic DNA. Translation: CAA16862.1.
PIRiT39541.
RefSeqiNP_596778.1. NM_001023799.2.

Genome annotation databases

EnsemblFungiiSPBC16A3.11.1; SPBC16A3.11.1:pep; SPBC16A3.11.
GeneIDi2539666.
KEGGispo:SPBC16A3.11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB039861 mRNA. Translation: BAA95122.1.
CU329671 Genomic DNA. Translation: CAA16862.1.
PIRiT39541.
RefSeqiNP_596778.1. NM_001023799.2.

3D structure databases

ProteinModelPortaliO42917.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276221. 241 interactions.
IntActiO42917. 1 interaction.
MINTiMINT-4673961.

Proteomic databases

MaxQBiO42917.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16A3.11.1; SPBC16A3.11.1:pep; SPBC16A3.11.
GeneIDi2539666.
KEGGispo:SPBC16A3.11.

Organism-specific databases

EuPathDBiFungiDB:SPBC16A3.11.
PomBaseiSPBC16A3.11. eso1.

Phylogenomic databases

InParanoidiO42917.
KOiK03509.
OrthoDBiEOG7RFTT2.
PhylomeDBiO42917.

Enzyme and pathway databases

ReactomeiR-SPO-110320. Translesion Synthesis by POLH.
R-SPO-5656169. Termination of translesion DNA synthesis.

Miscellaneous databases

NextBioi20800820.
PROiO42917.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR028005. AcTrfase_ESCO_Znf_dom.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR028009. ESCO_Acetyltransf_dom.
IPR001126. UmuC.
[Graphical view]
PfamiPF13880. Acetyltransf_13. 1 hit.
PF00817. IMS. 1 hit.
PF13878. zf-C2H2_3. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fission yeast eso1p is required for establishing sister chromatid cohesion during S phase."
    Tanaka K., Yonekawa T., Kawasaki Y., Kai M., Furuya K., Iwasaki M., Murakami H., Yanagida M., Okayama H.
    Mol. Cell. Biol. 20:3459-3469(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Establishment and maintenance of sister chromatid cohesion in fission yeast by a unique mechanism."
    Tanaka K., Hao Z., Kai M., Okayama H.
    EMBO J. 20:5779-5790(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDS5.
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiESO1_SCHPO
AccessioniPrimary (citable) accession number: O42917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.