ESCO1_HUMAN
ID ESCO1_HUMAN Reviewed; 840 AA.
AC Q5FWF5; B0YJ11; B0YJ12; Q69YG4; Q69YS3; Q6IMD7; Q8N3Z5; Q8NBG2; Q96PX7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=N-acetyltransferase ESCO1;
DE EC=2.3.1.- {ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:18614053};
DE AltName: Full=CTF7 homolog 1;
DE AltName: Full=Establishment factor-like protein 1 {ECO:0000303|PubMed:14576321};
DE Short=EFO1 {ECO:0000303|PubMed:15958495};
DE Short=EFO1p {ECO:0000303|PubMed:14576321};
DE Short=hEFO1;
DE AltName: Full=Establishment of cohesion 1 homolog 1;
DE Short=ECO1 homolog 1;
DE Short=ESO1 homolog 1;
GN Name=ESCO1; Synonyms=EFO1, KIAA1911;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow, and Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 624-840 (ISOFORM 2), AND VARIANT MET-221.
RC TISSUE=Lymph, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-840 (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP IDENTIFICATION (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14576321; DOI=10.1093/nar/gkg811;
RA Bellows A.M., Kenna M.A., Cassimeris L., Skibbens R.V.;
RT "Human EFO1p exhibits acetyltransferase activity and is a unique
RT combination of linker histone and Ctf7p/Eco1p chromatid cohesion
RT establishment domains.";
RL Nucleic Acids Res. 31:6334-6343(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH CHROMOSOMES, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF CYS-622; GLY-768;
RP 779-ARG-ARG-780; 782-ARG-ILE-783 AND GLU-789.
RX PubMed=15958495; DOI=10.1091/mbc.e04-12-1063;
RA Hou F., Zou H.;
RT "Two human orthologues of Eco1/Ctf7 acetyltransferases are both required
RT for proper sister-chromatid cohesion.";
RL Mol. Biol. Cell 16:3908-3918(2005).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18614053; DOI=10.1016/j.molcel.2008.06.006;
RA Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X.,
RA Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.;
RT "Acetylation of Smc3 by Eco1 is required for S phase sister chromatid
RT cohesion in both human and yeast.";
RL Mol. Cell 31:143-151(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19907496; DOI=10.1038/nature08550;
RA Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.;
RT "Cohesin acetylation speeds the replication fork.";
RL Nature 462:231-234(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-332, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15] {ECO:0007744|PDB:5T53}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 599-825 IN COMPLEX WITH
RP ACETYL-COA AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF PHE-640; GLN-643; PHE-644; ASP-690;
RP GLU-725; ARG-732; GLU-735; GLU-736; TRP-756; SER-770; ARG-771; TRP-773;
RP ARG-786; SER-809 AND GLY-815.
RX PubMed=27803161; DOI=10.1074/jbc.m116.752220;
RA Rivera-Colon Y., Maguire A., Liszczak G.P., Olia A.S., Marmorstein R.;
RT "Molecular Basis for Cohesin Acetylation by Establishment of Sister
RT Chromatid Cohesion N-Acetyltransferase ESCO1.";
RL J. Biol. Chem. 291:26468-26477(2016).
RN [16] {ECO:0007744|PDB:4MXE}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 654-836 IN COMPLEX WITH
RP ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF
RP GLY-768; ARG-780; GLU-789 AND LYS-803.
RX PubMed=27112597; DOI=10.1016/j.str.2016.03.021;
RA Kouznetsova E., Kanno T., Karlberg T., Thorsell A.G., Wisniewska M.,
RA Kursula P., Sjogren C., Schuler H.;
RT "Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by
RT Substrate-Assisted Catalysis.";
RL Structure 24:789-796(2016).
CC -!- FUNCTION: Acetyltransferase required for the establishment of sister
CC chromatid cohesion (PubMed:15958495, PubMed:18614053). Couples the
CC processes of cohesion and DNA replication to ensure that only sister
CC chromatids become paired together. In contrast to the structural
CC cohesins, the deposition and establishment factors are required only
CC during S phase. Acts by mediating the acetylation of cohesin component
CC SMC3 (PubMed:18614053). {ECO:0000269|PubMed:14576321,
CC ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:18614053,
CC ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:27112597,
CC ECO:0000269|PubMed:27803161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495,
CC ECO:0000269|PubMed:18614053};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77 uM for acetyl-CoA {ECO:0000269|PubMed:27803161};
CC -!- SUBUNIT: The subunit structure is controversial. Monomer
CC (PubMed:27803161). Homodimer (PubMed:27112597).
CC {ECO:0000269|PubMed:27112597, ECO:0000269|PubMed:27803161,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q5FWF5-1; Q5FWF5-1: ESCO1; NbExp=3; IntAct=EBI-16205392, EBI-16205392;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14576321,
CC ECO:0000269|PubMed:15958495}. Chromosome {ECO:0000269|PubMed:15958495}.
CC Note=Nuclear at interphase, associated with chromosomes during mitosis.
CC {ECO:0000269|PubMed:15958495}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5FWF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5FWF5-2; Sequence=VSP_014029, VSP_014030;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, liver,
CC placenta, lung, kidney and pancreas. Highly expressed in muscle.
CC {ECO:0000269|PubMed:14576321}.
CC -!- DOMAIN: The N-terminal region seems to be responsible for association
CC with chromosomes, thus excluding any involvement of the Zn finger in
CC this process. {ECO:0000269|PubMed:15958495}.
CC -!- PTM: Phosphorylated during mitosis, when associated with chromosomes.
CC {ECO:0000269|PubMed:15958495}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36943.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAB67804.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB067498; BAB67804.1; ALT_INIT; mRNA.
DR EMBL; AL832041; CAH10584.1; -; mRNA.
DR EMBL; AL834200; CAH10682.1; -; mRNA.
DR EMBL; EF444976; ACA05989.1; -; Genomic_DNA.
DR EMBL; EF444976; ACA05990.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01128.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01127.1; -; Genomic_DNA.
DR EMBL; BC036943; AAH36943.1; ALT_SEQ; mRNA.
DR EMBL; BC089426; AAH89426.1; -; mRNA.
DR EMBL; AK090579; BAC03483.1; ALT_INIT; mRNA.
DR EMBL; BK001617; DAA02068.1; -; mRNA.
DR CCDS; CCDS32800.1; -. [Q5FWF5-1]
DR RefSeq; NP_443143.2; NM_052911.2. [Q5FWF5-1]
DR RefSeq; XP_011524100.1; XM_011525798.1. [Q5FWF5-1]
DR PDB; 4MXE; X-ray; 2.60 A; A/B=654-836.
DR PDB; 5T53; X-ray; 2.70 A; A=599-825.
DR PDBsum; 4MXE; -.
DR PDBsum; 5T53; -.
DR AlphaFoldDB; Q5FWF5; -.
DR SMR; Q5FWF5; -.
DR BioGRID; 125360; 30.
DR CORUM; Q5FWF5; -.
DR DIP; DIP-56674N; -.
DR IntAct; Q5FWF5; 15.
DR STRING; 9606.ENSP00000269214; -.
DR CarbonylDB; Q5FWF5; -.
DR GlyGen; Q5FWF5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5FWF5; -.
DR PhosphoSitePlus; Q5FWF5; -.
DR BioMuta; ESCO1; -.
DR DMDM; 116241355; -.
DR EPD; Q5FWF5; -.
DR jPOST; Q5FWF5; -.
DR MassIVE; Q5FWF5; -.
DR MaxQB; Q5FWF5; -.
DR PaxDb; Q5FWF5; -.
DR PeptideAtlas; Q5FWF5; -.
DR PRIDE; Q5FWF5; -.
DR ProteomicsDB; 62814; -. [Q5FWF5-1]
DR ProteomicsDB; 62815; -. [Q5FWF5-2]
DR Antibodypedia; 21999; 70 antibodies from 19 providers.
DR DNASU; 114799; -.
DR Ensembl; ENST00000269214.10; ENSP00000269214.4; ENSG00000141446.11. [Q5FWF5-1]
DR Ensembl; ENST00000383276.1; ENSP00000372763.1; ENSG00000141446.11. [Q5FWF5-2]
DR GeneID; 114799; -.
DR KEGG; hsa:114799; -.
DR MANE-Select; ENST00000269214.10; ENSP00000269214.4; NM_052911.3; NP_443143.2.
DR UCSC; uc002kth.2; human. [Q5FWF5-1]
DR CTD; 114799; -.
DR DisGeNET; 114799; -.
DR GeneCards; ESCO1; -.
DR HGNC; HGNC:24645; ESCO1.
DR HPA; ENSG00000141446; Low tissue specificity.
DR MIM; 609674; gene.
DR neXtProt; NX_Q5FWF5; -.
DR OpenTargets; ENSG00000141446; -.
DR PharmGKB; PA134924215; -.
DR VEuPathDB; HostDB:ENSG00000141446; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000157762; -.
DR HOGENOM; CLU_012128_0_0_1; -.
DR InParanoid; Q5FWF5; -.
DR OMA; GMPVKCT; -.
DR PhylomeDB; Q5FWF5; -.
DR TreeFam; TF314027; -.
DR PathwayCommons; Q5FWF5; -.
DR Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
DR SignaLink; Q5FWF5; -.
DR SIGNOR; Q5FWF5; -.
DR BioGRID-ORCS; 114799; 19 hits in 1083 CRISPR screens.
DR ChiTaRS; ESCO1; human.
DR GenomeRNAi; 114799; -.
DR Pharos; Q5FWF5; Tbio.
DR PRO; PR:Q5FWF5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q5FWF5; protein.
DR Bgee; ENSG00000141446; Expressed in oviduct epithelium and 184 other tissues.
DR ExpressionAtlas; Q5FWF5; baseline and differential.
DR Genevisible; Q5FWF5; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:UniProtKB.
DR GO; GO:0034421; P:post-translational protein acetylation; IMP:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR InterPro; IPR026656; AcTrfase_ESCO1.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR PANTHER; PTHR45884:SF1; PTHR45884:SF1; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cell cycle;
KW Chromosome; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..840
FT /note="N-acetyltransferase ESCO1"
FT /id="PRO_0000074539"
FT ZN_FING 617..641
FT /note="CCHH-type"
FT /evidence="ECO:0000269|PubMed:27803161"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 772..774
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:27112597,
FT ECO:0000269|PubMed:27803161, ECO:0007744|PDB:4MXE,
FT ECO:0007744|PDB:5T53"
FT BINDING 780..785
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:27112597,
FT ECO:0000269|PubMed:27803161, ECO:0007744|PDB:4MXE,
FT ECO:0007744|PDB:5T53"
FT BINDING 812..814
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:27112597,
FT ECO:0000269|PubMed:27803161, ECO:0007744|PDB:4MXE,
FT ECO:0007744|PDB:5T53"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT VAR_SEQ 652..701
FT /note="GWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLM
FT -> VLLINHHECGSEEEFITSLFLSMFNFRYTQRSFSFPIRFLEGLEERKNSG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_014029"
FT VAR_SEQ 702..840
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_014030"
FT VARIANT 191
FT /note="N -> S (in dbSNP:rs35087820)"
FT /id="VAR_048167"
FT VARIANT 221
FT /note="T -> M (in dbSNP:rs13381941)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_022648"
FT MUTAGEN 622
FT /note="C->G: No effect on association with chromosomes."
FT /evidence="ECO:0000269|PubMed:15958495"
FT MUTAGEN 640
FT /note="F->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 643
FT /note="Q->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 644
FT /note="F->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 690
FT /note="D->N: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 725
FT /note="E->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 732
FT /note="R->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 735
FT /note="E->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 736
FT /note="E->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 756
FT /note="W->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 768
FT /note="G->D: Loss of autoacetylation."
FT /evidence="ECO:0000269|PubMed:15958495,
FT ECO:0000269|PubMed:27112597"
FT MUTAGEN 770
FT /note="S->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 771
FT /note="R->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 773
FT /note="W->G: Decreased thermal stability.Strongly decreased
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 779..780
FT /note="RR->GG: Significant reduction in autoacetylation."
FT /evidence="ECO:0000269|PubMed:15958495"
FT MUTAGEN 780
FT /note="R->A: Nearly abolishes autoacetylation."
FT /evidence="ECO:0000269|PubMed:27112597"
FT MUTAGEN 782..783
FT /note="KI->EV: Significant reduction in autoacetylation."
FT /evidence="ECO:0000269|PubMed:15958495"
FT MUTAGEN 786
FT /note="R->C: Decreased thermal stability. Strongly
FT decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 789
FT /note="E->A: Reduced autoacetylation."
FT /evidence="ECO:0000269|PubMed:15958495,
FT ECO:0000269|PubMed:27112597"
FT MUTAGEN 803
FT /note="K->A: Strongly reduced autoacetylation."
FT /evidence="ECO:0000269|PubMed:27112597"
FT MUTAGEN 809
FT /note="S->A: Strongly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:27803161"
FT MUTAGEN 815
FT /note="G->R: Strongly decreased enzyme activity. No effect
FT on thermal stability."
FT /evidence="ECO:0000269|PubMed:27803161"
FT CONFLICT 384
FT /note="S -> L (in Ref. 1; BAB67804)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="P -> S (in Ref. 2; CAH10682)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="E -> A (in Ref. 6; BAC03483)"
FT /evidence="ECO:0000305"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:5T53"
FT HELIX 634..648
FT /evidence="ECO:0007829|PDB:5T53"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 663..670
FT /evidence="ECO:0007829|PDB:4MXE"
FT HELIX 676..689
FT /evidence="ECO:0007829|PDB:4MXE"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:5T53"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 717..726
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 728..739
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 752..764
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 766..774
FT /evidence="ECO:0007829|PDB:4MXE"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:4MXE"
FT HELIX 783..794
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 805..810
FT /evidence="ECO:0007829|PDB:4MXE"
FT HELIX 813..823
FT /evidence="ECO:0007829|PDB:4MXE"
FT STRAND 827..833
FT /evidence="ECO:0007829|PDB:4MXE"
SQ SEQUENCE 840 AA; 94983 MW; A36BE0EC1BE3EDF2 CRC64;
MMSIQEKSKE NSSKVTKKSD DKNSETEIQD SQKNLAKKSG PKETIKSQAK SSSESKINQP
ELETRMSTRS SKAASNDKAT KSINKNTVTV RGYSQESTKK KLSQKKLVHE NPKANEQLNR
RSQRLQQLTE VSRRSLRSRE IQGQVQAVKQ SLPPTKKEQC SSTQSKSNKT SQKHVKRKVL
EVKSDSKEDE NLVINEVINS PKGKKRKVEH QTACACSSQC TQGSEKCPQK TTRRDETKPV
PVTSEVKRSK MATSVVPKKN EMKKSVHTQV NTNTTLPKSP QPSVPEQSDN ELEQAGKSKR
GSILQLCEEI AGEIESDNVE VKKESSQMES VKEEKPTEIK LEETSVERQI LHQKETNQDV
QCNRFFPSRK TKPVKCILNG INSSAKKNSN WTKIKLSKFN SVQHNKLDSQ VSPKLGLLRT
SFSPPALEMH HPVTQSTFLG TKLHDRNITC QQEKMKEINS EEVKINDITV EINKTTERAP
ENCHLANEIK PSDPPLDNQM KHSFDSASNK NFSQCLESKL ENSPVENVTA ASTLLSQAKI
DTGENKFPGS APQQHSILSN QTSKSSDNRE TPRNHSLPKC NSHLEITIPK DLKLKEAEKT
DEKQLIIDAG QKRFGAVSCN VCGMLYTASN PEDETQHLLF HNQFISAVKY VGWKKERILA
EYPDGRIIMV LPEDPKYALK KVDEIREMVD NDLGFQQAPL MCYSRTKTLL FISNDKKVVG
CLIAEHIQWG YRVIEEKLPV IRSEEEKVRF ERQKAWCCST LPEPAICGIS RIWVFSMMRR
KKIASRMIEC LRSNFIYGSY LSKEEIAFSD PTPDGKLFAT QYCGTGQFLV YNFINGQNST
