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Protein

N-acetyltransferase ESCO1

Gene

ESCO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Acts by mediating the acetylation of cohesin component SMC3.6 Publications

Kineticsi

  1. KM=77 µM for acetyl-CoA1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri617 – 641CCHH-type1 PublicationAdd BLAST25

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • N-acetyltransferase activity Source: UniProtKB
    • peptide-lysine-N-acetyltransferase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • peptidyl-lysine acetylation Source: UniProtKB
    • post-translational protein acetylation Source: UniProtKB
    • regulation of DNA replication Source: UniProtKB
    • sister chromatid cohesion Source: InterPro

    Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processCell cycle
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiR-HSA-2468052. Establishment of Sister Chromatid Cohesion.
    SIGNORiQ5FWF5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetyltransferase ESCO1 (EC:2.3.1.-2 Publications)
    Alternative name(s):
    CTF7 homolog 1
    Establishment factor-like protein 1
    Short name:
    EFO1p
    Short name:
    hEFO1
    Establishment of cohesion 1 homolog 1
    Short name:
    ECO1 homolog 1
    Short name:
    ESO1 homolog 1
    Gene namesi
    Name:ESCO1
    Synonyms:EFO1, KIAA1911
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 18

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000141446.10.
    HGNCiHGNC:24645. ESCO1.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi622C → G: No effect on association with chromosomes. 1 Publication1
    Mutagenesisi640F → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi643Q → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi644F → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi690D → N: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi725E → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi732R → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi735E → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi736E → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi756W → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi768G → D: Loss of autoacetylation. 1 Publication1
    Mutagenesisi770S → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi771R → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi773W → G: Decreased thermal stability.Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi780R → A: Nearly abolishes autoacetylation. 1 Publication1
    Mutagenesisi786R → C: Decreased thermal stability. Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi789E → A: Reduced autoacetylation. 1 Publication1
    Mutagenesisi803K → A: Strongly reduced autoacetylation. 1 Publication1
    Mutagenesisi809S → A: Strongly decreased enzyme activity. 1 Publication1
    Mutagenesisi815G → R: Strongly decreased enzyme activity. No effect on thermal stability. 1 Publication1

    Organism-specific databases

    DisGeNETi114799.
    OpenTargetsiENSG00000141446.
    PharmGKBiPA134924215.

    Polymorphism and mutation databases

    BioMutaiESCO1.
    DMDMi116241355.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000745391 – 840N-acetyltransferase ESCO1Add BLAST840

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei200PhosphoserineCombined sources1
    Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei412PhosphoserineCombined sources1

    Post-translational modificationi

    Phosphorylated during mitosis.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiQ5FWF5.
    MaxQBiQ5FWF5.
    PaxDbiQ5FWF5.
    PeptideAtlasiQ5FWF5.
    PRIDEiQ5FWF5.

    PTM databases

    iPTMnetiQ5FWF5.
    PhosphoSitePlusiQ5FWF5.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in heart, brain, liver, placenta, lung, kidney and pancreas. Highly expressed in muscle.1 Publication

    Gene expression databases

    BgeeiENSG00000141446.
    CleanExiHS_ESCO1.
    ExpressionAtlasiQ5FWF5. baseline and differential.
    GenevisibleiQ5FWF5. HS.

    Organism-specific databases

    HPAiHPA042497.

    Interactioni

    Subunit structurei

    The subunit structure is controversial. Monomer (PubMed:27803161). Homodimer (PubMed:27112597).Curated2 Publications

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi125360. 22 interactors.
    CORUMiQ5FWF5.
    DIPiDIP-56674N.
    IntActiQ5FWF5. 14 interactors.
    STRINGi9606.ENSP00000269214.

    Structurei

    Secondary structure

    1840
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni620 – 622Combined sources3
    Helixi634 – 648Combined sources15
    Beta strandi658 – 661Combined sources4
    Beta strandi663 – 670Combined sources8
    Helixi676 – 689Combined sources14
    Helixi703 – 705Combined sources3
    Beta strandi707 – 713Combined sources7
    Beta strandi717 – 726Combined sources10
    Beta strandi728 – 739Combined sources12
    Beta strandi752 – 764Combined sources13
    Beta strandi766 – 774Combined sources9
    Helixi776 – 778Combined sources3
    Beta strandi780 – 782Combined sources3
    Helixi783 – 794Combined sources12
    Beta strandi805 – 810Combined sources6
    Helixi813 – 823Combined sources11
    Beta strandi827 – 833Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4MXEX-ray2.60A/B654-836[»]
    5T53X-ray2.70A599-825[»]
    ProteinModelPortaliQ5FWF5.
    SMRiQ5FWF5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni772 – 774Acetyl-CoA bindingCombined sources2 Publications3
    Regioni780 – 785Acetyl-CoA bindingCombined sources2 Publications6
    Regioni812 – 814Acetyl-CoA bindingCombined sources2 Publications3

    Domaini

    The N-terminal region seems to be responsible for the association with chromosomes, thus excluding any involvement of the Zn finger in this process.

    Sequence similaritiesi

    Belongs to the acetyltransferase family. ECO subfamily.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri617 – 641CCHH-type1 PublicationAdd BLAST25

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiKOG3014. Eukaryota.
    ENOG410XTJX. LUCA.
    GeneTreeiENSGT00390000008335.
    HOVERGENiHBG081483.
    InParanoidiQ5FWF5.
    KOiK11268.
    OMAiNSNWTKI.
    OrthoDBiEOG091G0QVI.
    PhylomeDBiQ5FWF5.
    TreeFamiTF314027.

    Family and domain databases

    InterProiView protein in InterPro
    IPR026656. AcTrfase_ESCO1.
    IPR028005. AcTrfase_ESCO_Znf_dom.
    IPR028009. ESCO_Acetyltransf_dom.
    PANTHERiPTHR11076:SF26. PTHR11076:SF26. 1 hit.
    PfamiView protein in Pfam
    PF13880. Acetyltransf_13. 1 hit.
    PF13878. zf-C2H2_3. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q5FWF5-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MMSIQEKSKE NSSKVTKKSD DKNSETEIQD SQKNLAKKSG PKETIKSQAK
    60 70 80 90 100
    SSSESKINQP ELETRMSTRS SKAASNDKAT KSINKNTVTV RGYSQESTKK
    110 120 130 140 150
    KLSQKKLVHE NPKANEQLNR RSQRLQQLTE VSRRSLRSRE IQGQVQAVKQ
    160 170 180 190 200
    SLPPTKKEQC SSTQSKSNKT SQKHVKRKVL EVKSDSKEDE NLVINEVINS
    210 220 230 240 250
    PKGKKRKVEH QTACACSSQC TQGSEKCPQK TTRRDETKPV PVTSEVKRSK
    260 270 280 290 300
    MATSVVPKKN EMKKSVHTQV NTNTTLPKSP QPSVPEQSDN ELEQAGKSKR
    310 320 330 340 350
    GSILQLCEEI AGEIESDNVE VKKESSQMES VKEEKPTEIK LEETSVERQI
    360 370 380 390 400
    LHQKETNQDV QCNRFFPSRK TKPVKCILNG INSSAKKNSN WTKIKLSKFN
    410 420 430 440 450
    SVQHNKLDSQ VSPKLGLLRT SFSPPALEMH HPVTQSTFLG TKLHDRNITC
    460 470 480 490 500
    QQEKMKEINS EEVKINDITV EINKTTERAP ENCHLANEIK PSDPPLDNQM
    510 520 530 540 550
    KHSFDSASNK NFSQCLESKL ENSPVENVTA ASTLLSQAKI DTGENKFPGS
    560 570 580 590 600
    APQQHSILSN QTSKSSDNRE TPRNHSLPKC NSHLEITIPK DLKLKEAEKT
    610 620 630 640 650
    DEKQLIIDAG QKRFGAVSCN VCGMLYTASN PEDETQHLLF HNQFISAVKY
    660 670 680 690 700
    VGWKKERILA EYPDGRIIMV LPEDPKYALK KVDEIREMVD NDLGFQQAPL
    710 720 730 740 750
    MCYSRTKTLL FISNDKKVVG CLIAEHIQWG YRVIEEKLPV IRSEEEKVRF
    760 770 780 790 800
    ERQKAWCCST LPEPAICGIS RIWVFSMMRR KKIASRMIEC LRSNFIYGSY
    810 820 830 840
    LSKEEIAFSD PTPDGKLFAT QYCGTGQFLV YNFINGQNST
    Length:840
    Mass (Da):94,983
    Last modified:October 17, 2006 - v3
    Checksum:iA36BE0EC1BE3EDF2
    GO
    Isoform 2 (identifier: Q5FWF5-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         652-701: GWKKERILAE...DLGFQQAPLM → VLLINHHECG...EGLEERKNSG
         702-840: Missing.

    Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
    Show »
    Length:701
    Mass (Da):78,987
    Checksum:iEA85A22EAD7134C0
    GO

    Sequence cautioni

    The sequence AAH36943 differs from that shown. Wrong choice of frame.Curated
    The sequence BAB67804 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAC03483 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti384S → L in BAB67804 (PubMed:11572484).Curated1
    Sequence conflicti432P → S in CAH10682 (PubMed:17974005).Curated1
    Sequence conflicti805E → A in BAC03483 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_048167191N → S. Corresponds to variant dbSNP:rs35087820Ensembl.1
    Natural variantiVAR_022648221T → M1 PublicationCorresponds to variant dbSNP:rs13381941Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_014029652 – 701GWKKE…QAPLM → VLLINHHECGSEEEFITSLF LSMFNFRYTQRSFSFPIRFL EGLEERKNSG in isoform 2. 2 PublicationsAdd BLAST50
    Alternative sequenceiVSP_014030702 – 840Missing in isoform 2. 2 PublicationsAdd BLAST139

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB067498 mRNA. Translation: BAB67804.1. Different initiation.
    AL832041 mRNA. Translation: CAH10584.1.
    AL834200 mRNA. Translation: CAH10682.1.
    EF444976 Genomic DNA. Translation: ACA05989.1.
    EF444976 Genomic DNA. Translation: ACA05990.1.
    CH471088 Genomic DNA. Translation: EAX01128.1.
    CH471088 Genomic DNA. Translation: EAX01127.1.
    BC036943 mRNA. Translation: AAH36943.1. Sequence problems.
    BC089426 mRNA. Translation: AAH89426.1.
    AK090579 mRNA. Translation: BAC03483.1. Different initiation.
    BK001617 mRNA. Translation: DAA02068.1.
    CCDSiCCDS32800.1. [Q5FWF5-1]
    RefSeqiNP_443143.2. NM_052911.2. [Q5FWF5-1]
    XP_011524100.1. XM_011525798.1. [Q5FWF5-1]
    UniGeneiHs.464733.

    Genome annotation databases

    EnsembliENST00000269214; ENSP00000269214; ENSG00000141446. [Q5FWF5-1]
    ENST00000383276; ENSP00000372763; ENSG00000141446. [Q5FWF5-2]
    GeneIDi114799.
    KEGGihsa:114799.
    UCSCiuc002kth.2. human. [Q5FWF5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiESCO1_HUMAN
    AccessioniPrimary (citable) accession number: Q5FWF5
    Secondary accession number(s): B0YJ11
    , B0YJ12, Q69YG4, Q69YS3, Q6IMD7, Q8N3Z5, Q8NBG2, Q96PX7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: October 17, 2006
    Last modified: October 25, 2017
    This is version 121 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-2 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families