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Q56NI9

- ESCO2_HUMAN

UniProt

Q56NI9 - ESCO2_HUMAN

Protein

N-acetyltransferase ESCO2

Gene

ESCO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (10 May 2005)
      Previous versions | rss
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    Functioni

    Acetyltransferase required for the establishment of sister chromatid cohesion. Couples 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 the S phase. Acetylates the cohesin component SMC3.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri387 – 41125CCHH-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. transferase activity, transferring acyl groups Source: UniProtKB-KW

    GO - Biological processi

    1. mitotic cell cycle Source: Reactome
    2. post-translational protein acetylation Source: UniProtKB
    3. regulation of DNA replication Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetyltransferase ESCO2 (EC:2.3.1.-)
    Alternative name(s):
    Establishment of cohesion 1 homolog 2
    Short name:
    ECO1 homolog 2
    Gene namesi
    Name:ESCO2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:27230. ESCO2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. Golgi apparatus Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Roberts syndrome (RBS) [MIM:268300]: Rare autosomal recessive disorder characterized by pre- and postnatal growth retardation, microcephaly, bilateral cleft lip and palate, and mesomelic symmetric limb reduction. Severely affected infants may be stillborn or die shortly after birth. RBS chromosomes have a lack of cohesion involving the heterochromatic C-banding regions around centromeres and the distal portion of the long arm of the Y chromosome (known as premature centromere separation, heterochromatin repulsion or puffing, or RS effect).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti539 – 5391W → G in RBS. 1 Publication
    VAR_022649
    SC phocomelia syndrome (SCPS) [MIM:269000]: Has a milder phenotype than RBS, with a lesser degree of symmetric limb reduction and additionally includes flexion contractures of various joints, midfacial hemangioma, hypoplastic cartilage of ears and nose, scant silvery-blond hair, and cloudy corneae. Although microcephaly is present, mental retardation may be mild and survival into adulthood is common.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi268300. phenotype.
    269000. phenotype.
    Orphaneti3103. Roberts syndrome.
    PharmGKBiPA134891970.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 601601N-acetyltransferase ESCO2PRO_0000074542Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei75 – 751Phosphoserine2 Publications
    Modified residuei244 – 2441Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ56NI9.
    PaxDbiQ56NI9.
    PRIDEiQ56NI9.

    PTM databases

    PhosphoSiteiQ56NI9.

    Expressioni

    Tissue specificityi

    Widely expressed in fetal tissues. In adult, it is expressed in thymus, placenta and small intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ56NI9.
    BgeeiQ56NI9.
    CleanExiHS_ESCO2.
    GenevestigatoriQ56NI9.

    Organism-specific databases

    HPAiHPA053679.

    Interactioni

    Protein-protein interaction databases

    BioGridi127605. 11 interactions.
    IntActiQ56NI9. 1 interaction.
    STRINGi9606.ENSP00000306999.

    Structurei

    3D structure databases

    ProteinModelPortaliQ56NI9.
    SMRiQ56NI9. Positions 532-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acetyltransferase family. ECO subfamily.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri387 – 41125CCHH-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG301368.
    HOGENOMiHOG000294103.
    HOVERGENiHBG081482.
    InParanoidiQ56NI9.
    KOiK11268.
    OMAiKIKPQVT.
    OrthoDBiEOG7J9VQQ.
    PhylomeDBiQ56NI9.
    TreeFamiTF314027.

    Family and domain databases

    InterProiIPR028005. AcTrfase_ESCO_Znf_dom.
    IPR028009. ESCO_Acetyltransf_dom.
    [Graphical view]
    PfamiPF13880. Acetyltransf_13. 1 hit.
    PF13878. zf-C2H2_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q56NI9-1) [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

    MAALTPRKRK QDSLKCDSLL HFTENLFPSP NKKHCFYQNS DKNEENLHCS    50
    QQEHFVLSAL KTTEINRLPS ANQGSPFKSA LSTVSFYNQN KWYLNPLERK 100
    LIKESRSTCL KTNDEDKSFP IVTEKMQGKP VCSKKNNKKP QKSLTAKYQP 150
    KYRHIKPVSR NSRNSKQNRV IYKPIVEKEN NCHSAENNSN APRVLSQKIK 200
    PQVTLQGGAA FFVRKKSSLR KSSLENEPSL GRTQKSKSEV IEDSDVETVS 250
    EKKTFATRQV PKCLVLEEKL KIGLLSASSK NKEKLIKDSS DDRVSSKEHK 300
    VDKNEAFSSE DSLGENKTIS PKSTVYPIFS ASSVNSKRSL GEEQFSVGSV 350
    NFMKQTNIQK NTNTRDTSKK TKDQLIIDAG QKHFGATVCK SCGMIYTASN 400
    PEDEMQHVQH HHRFLEGIKY VGWKKERVVA EFWDGKIVLV LPHDPSFAIK 450
    KVEDVQELVD NELGFQQVVP KCPNKIKTFL FISDEKRVVG CLIAEPIKQA 500
    FRVLSEPIGP ESPSSTECPR AWQCSDVPEP AVCGISRIWV FRLKRRKRIA 550
    RRLVDTLRNC FMFGCFLSTD EIAFSDPTPD GKLFATKYCN TPNFLVYNFN 600
    S 601
    Length:601
    Mass (Da):68,307
    Last modified:May 10, 2005 - v1
    Checksum:iA3D10BFD486572AE
    GO
    Isoform 2 (identifier: Q56NI9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-352: Missing.
         581-601: GKLFATKYCNTPNFLVYNFNS → DCRRLNRYQET

    Note: No experimental confirmation available.

    Show »
    Length:239
    Mass (Da):27,500
    Checksum:i054329F214C2BBAE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti80 – 801A → V.
    Corresponds to variant rs4732748 [ dbSNP | Ensembl ].
    VAR_033840
    Natural varianti359 – 3591Q → P.
    Corresponds to variant rs57479434 [ dbSNP | Ensembl ].
    VAR_060994
    Natural varianti539 – 5391W → G in RBS. 1 Publication
    VAR_022649

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 352352Missing in isoform 2. 1 PublicationVSP_055773Add
    BLAST
    Alternative sequencei581 – 60121GKLFA…YNFNS → DCRRLNRYQET in isoform 2. 1 PublicationVSP_055774Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY882862 mRNA. Translation: AAX68677.1.
    AK124215 mRNA. Translation: BAG54021.1.
    AC104997 Genomic DNA. No translation available.
    BC034641 mRNA. Translation: AAH34641.1.
    CCDSiCCDS34872.1.
    RefSeqiNP_001017420.1. NM_001017420.2.
    XP_006716360.1. XM_006716297.1.
    UniGeneiHs.99480.

    Genome annotation databases

    EnsembliENST00000305188; ENSP00000306999; ENSG00000171320. [Q56NI9-1]
    ENST00000397418; ENSP00000380563; ENSG00000171320. [Q56NI9-2]
    GeneIDi157570.
    KEGGihsa:157570.
    UCSCiuc003xgg.3. human.

    Polymorphism databases

    DMDMi67460434.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY882862 mRNA. Translation: AAX68677.1 .
    AK124215 mRNA. Translation: BAG54021.1 .
    AC104997 Genomic DNA. No translation available.
    BC034641 mRNA. Translation: AAH34641.1 .
    CCDSi CCDS34872.1.
    RefSeqi NP_001017420.1. NM_001017420.2.
    XP_006716360.1. XM_006716297.1.
    UniGenei Hs.99480.

    3D structure databases

    ProteinModelPortali Q56NI9.
    SMRi Q56NI9. Positions 532-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127605. 11 interactions.
    IntActi Q56NI9. 1 interaction.
    STRINGi 9606.ENSP00000306999.

    PTM databases

    PhosphoSitei Q56NI9.

    Polymorphism databases

    DMDMi 67460434.

    Proteomic databases

    MaxQBi Q56NI9.
    PaxDbi Q56NI9.
    PRIDEi Q56NI9.

    Protocols and materials databases

    DNASUi 157570.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305188 ; ENSP00000306999 ; ENSG00000171320 . [Q56NI9-1 ]
    ENST00000397418 ; ENSP00000380563 ; ENSG00000171320 . [Q56NI9-2 ]
    GeneIDi 157570.
    KEGGi hsa:157570.
    UCSCi uc003xgg.3. human.

    Organism-specific databases

    CTDi 157570.
    GeneCardsi GC08P027632.
    GeneReviewsi ESCO2.
    H-InvDB HIX0168881.
    HGNCi HGNC:27230. ESCO2.
    HPAi HPA053679.
    MIMi 268300. phenotype.
    269000. phenotype.
    609353. gene.
    neXtProti NX_Q56NI9.
    Orphaneti 3103. Roberts syndrome.
    PharmGKBi PA134891970.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301368.
    HOGENOMi HOG000294103.
    HOVERGENi HBG081482.
    InParanoidi Q56NI9.
    KOi K11268.
    OMAi KIKPQVT.
    OrthoDBi EOG7J9VQQ.
    PhylomeDBi Q56NI9.
    TreeFami TF314027.

    Enzyme and pathway databases

    Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.

    Miscellaneous databases

    GeneWikii ESCO2.
    GenomeRNAii 157570.
    NextBioi 87487.
    PROi Q56NI9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q56NI9.
    Bgeei Q56NI9.
    CleanExi HS_ESCO2.
    Genevestigatori Q56NI9.

    Family and domain databases

    InterProi IPR028005. AcTrfase_ESCO_Znf_dom.
    IPR028009. ESCO_Acetyltransf_dom.
    [Graphical view ]
    Pfami PF13880. Acetyltransf_13. 1 hit.
    PF13878. zf-C2H2_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast ECO1 that is essential for the establishment of sister chromatid cohesion."
      Vega H., Waisfisz Q., Gordillo M., Sakai N., Yanagihara I., Yamada M., van Gosliga D., Kayserili H., Xu C., Ozono K., Wang Jabs E., Inui K., Joenje H.
      Nat. Genet. 37:468-470(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT RBS GLY-539.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Thymus.
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    5. "Inactivating mutations in ESCO2 cause SC phocomelia and Roberts syndrome: no phenotype-genotype correlation."
      Schuele B., Oviedo A., Johnston K., Pai S., Francke U.
      Am. J. Hum. Genet. 77:1117-1128(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SCPS.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Cohesin acetylation speeds the replication fork."
      Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.
      Nature 462:231-234(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: FUNCTION.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiESCO2_HUMAN
    AccessioniPrimary (citable) accession number: Q56NI9
    Secondary accession number(s): B3KW59, Q49AP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3