ESCO1_MOUSE
ID ESCO1_MOUSE Reviewed; 843 AA.
AC Q69Z69; B9EKQ9; Q8BQI2; Q8BR47; Q922F5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=N-acetyltransferase ESCO1;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5FWF5};
DE AltName: Full=Establishment of cohesion 1 homolog 1;
DE Short=ECO1 homolog 1;
GN Name=Esco1; Synonyms=Kiaa1911;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-234 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 411-843 (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-691 (ISOFORM 1).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
CC -!- FUNCTION: Acetyltransferase required for the establishment of sister
CC chromatid cohesion. Couples the processes of cohesion and DNA
CC replication to ensure that only sister chromatids become paired
CC together. In contrast to the structural cohesins, the deposition and
CC establishment factors are required only during S phase. Acts by
CC mediating the acetylation of cohesin component SMC3.
CC {ECO:0000250|UniProtKB:Q5FWF5}.
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:0000250|UniProtKB:Q5FWF5};
CC -!- SUBUNIT: The subunit structure is controversial. Monomer. Homodimer.
CC {ECO:0000250|UniProtKB:Q5FWF5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FWF5}.
CC Chromosome {ECO:0000250|UniProtKB:Q5FWF5}. Note=Nuclear at interphase,
CC associated with chromosomes during mitosis.
CC {ECO:0000250|UniProtKB:Q5FWF5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q69Z69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69Z69-2; Sequence=VSP_014031, VSP_014032;
CC Name=3;
CC IsoId=Q69Z69-3; Sequence=VSP_014033, VSP_014034;
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:0000250|UniProtKB:Q5FWF5}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q5FWF5}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC33830.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD32575.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK045656; BAC32447.1; -; mRNA.
DR EMBL; AK049589; BAC33830.1; ALT_FRAME; mRNA.
DR EMBL; AC102441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173297; BAD32575.1; ALT_INIT; mRNA.
DR EMBL; BC008220; AAH08220.1; ALT_INIT; mRNA.
DR EMBL; BC151069; AAI51070.1; -; mRNA.
DR EMBL; BC151077; AAI51078.1; -; mRNA.
DR CCDS; CCDS37737.1; -. [Q69Z69-1]
DR RefSeq; NP_001074691.1; NM_001081222.1. [Q69Z69-1]
DR AlphaFoldDB; Q69Z69; -.
DR SMR; Q69Z69; -.
DR BioGRID; 218936; 3.
DR IntAct; Q69Z69; 2.
DR STRING; 10090.ENSMUSP00000025142; -.
DR iPTMnet; Q69Z69; -.
DR PhosphoSitePlus; Q69Z69; -.
DR EPD; Q69Z69; -.
DR MaxQB; Q69Z69; -.
DR PaxDb; Q69Z69; -.
DR PRIDE; Q69Z69; -.
DR ProteomicsDB; 275676; -. [Q69Z69-1]
DR ProteomicsDB; 275677; -. [Q69Z69-2]
DR ProteomicsDB; 275678; -. [Q69Z69-3]
DR Antibodypedia; 21999; 70 antibodies from 19 providers.
DR DNASU; 77805; -.
DR Ensembl; ENSMUST00000025142; ENSMUSP00000025142; ENSMUSG00000024293. [Q69Z69-1]
DR Ensembl; ENSMUST00000115864; ENSMUSP00000111530; ENSMUSG00000024293. [Q69Z69-2]
DR Ensembl; ENSMUST00000127099; ENSMUSP00000157382; ENSMUSG00000024293. [Q69Z69-3]
DR GeneID; 77805; -.
DR KEGG; mmu:77805; -.
DR UCSC; uc008eav.1; mouse. [Q69Z69-1]
DR UCSC; uc008eaw.1; mouse. [Q69Z69-2]
DR CTD; 114799; -.
DR MGI; MGI:1925055; Esco1.
DR VEuPathDB; HostDB:ENSMUSG00000024293; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000157762; -.
DR HOGENOM; CLU_012128_0_0_1; -.
DR InParanoid; Q69Z69; -.
DR OrthoDB; 1024179at2759; -.
DR PhylomeDB; Q69Z69; -.
DR TreeFam; TF314027; -.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR BioGRID-ORCS; 77805; 3 hits in 111 CRISPR screens.
DR ChiTaRS; Esco1; mouse.
DR PRO; PR:Q69Z69; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q69Z69; protein.
DR Bgee; ENSMUSG00000024293; Expressed in cleaving embryo and 246 other tissues.
DR ExpressionAtlas; Q69Z69; baseline and differential.
DR Genevisible; Q69Z69; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0034421; P:post-translational protein acetylation; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; ISS: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 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Cell cycle; Chromosome;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..843
FT /note="N-acetyltransferase ESCO1"
FT /id="PRO_0000074540"
FT ZN_FING 620..644
FT /note="CCHH-type"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 775..777
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF5"
FT BINDING 783..788
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF5"
FT BINDING 815..817
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF5"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF5"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF5"
FT CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5FWF5"
FT VAR_SEQ 1..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014031"
FT VAR_SEQ 525..550
FT /note="TNPLENTAAASTLLSQAKIDEDRTFP -> MLQIHQHPVAVDFRRKNFSEIL
FT SKQT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014032"
FT VAR_SEQ 655..690
FT /note="GWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIRE -> VLLINHHECGSE
FT EEFITSLFLSMSNFRYTQRSLLPY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014033"
FT VAR_SEQ 691..843
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014034"
FT CONFLICT 690..691
FT /note="EM -> DG (in Ref. 4; BAD32575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 843 AA; 94999 MW; DAA24CFFB10FA435 CRC64;
MSIQEKSKEN SSIVTKESED ENLEEEVESS QNSPTKKSGS KEAVKTPVRF SNKSKTNESE
FGMRMSTRSA SCSADKTATN SFNKNTVTLK GQSQESSKTK KLCQEKLSLG ILKGNEQLHR
RSQRLQQLTE CTTRSLRSRE IHGQIQTVKQ NQQSARREQC NSTQSKCNKV KVNQKHVKRK
VLEIKSDCKE DRHSVTNEVI NSPKGKKRKV QHQTTSTCSS QCNQGSEKCL QKTSRKEEIK
PVPVTADIRK LKAATSVVSK KNELRKSAHT QVSTSTKRPQ IPLPLVPEHS DDQELEQAGK
SKRGSILQLC EEIAGEIESD TVEVKKESSC VESVKEEKPA EVKLQGTDAE RQILHHKEAN
QDVRSNRFFP SRKTKPVKCV LNGINSSTKK NSNWTKIKLS KFNSVQQHKL DSQVSPKLNL
LQTGLSTSVL EMPHPVSQST FLEMKAHGNV TCQRDKMKGI KSEEVKINNI AIEINKATKR
DPGNCNLDNH IKPSPDSSLD NQMKLSCESA PDQNFSICSA SEVETNPLEN TAAASTLLSQ
AKIDEDRTFP GSAPNQQHSV LSDEASINRK NRDVPPNHSQ LKHDSHLEIT IPKSLKLKDS
EKVDEKQLVI DAGHKRFGAV SCNICGMLYT ASNPEDETQH LLFHNQFISA VKYVGWKKER
ILAEYPDGRI IMVLPEDPKY ALKKVDEIRE MVDNDLGFQQ APLMCYSRTK TLLFISNDKK
VVGCLIAEHI QWGYRVIEEK LPVIRSEEEK VRFERQKAWC CSTLPEPAIC GISRIWVFSM
MRRKKIASRM IECLRSNFIY GSYLSKEEIA FSDPTPDGKL FATQYCGTGQ FLVYNFINGQ
NTT
