ESCO2_MOUSE
ID ESCO2_MOUSE Reviewed; 592 AA.
AC Q8CIB9; Q3UMT6; Q6IQX5; Q8BNG9; Q8BQF8; Q9CRI8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=N-acetyltransferase ESCO2;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q56NI9};
DE AltName: Full=Establishment of cohesion 1 homolog 2;
DE Short=ECO1 homolog 2;
GN Name=Esco2;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Lung;
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 MRNA].
RC STRAIN=Czech II; TISSUE=Embryo, 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 [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=32255174; DOI=10.1093/ejo/cjaa023;
RA Kantaputra P.N., Dejkhamron P., Intachai W., Ngamphiw C., Kawasaki K.,
RA Ohazama A., Krisanaprakornkit S., Olsen B., Tongsima S.,
RA Ketudat Cairns J.R.;
RT "Juberg-Hayward syndrome is a cohesinopathy, caused by mutation in ESCO2.";
RL Eur. J. Orthod. 43:45-50(2021).
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 the S phase. Acetylates
CC the cohesin component SMC3. {ECO:0000250|UniProtKB:Q56NI9}.
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:Q56NI9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q56NI9}.
CC Chromosome {ECO:0000250|UniProtKB:Q56NI9}. Note=Nuclear in interphase
CC cells, excluded from chromosomes during metaphase but reassociates with
CC chromosomes in telophase. {ECO:0000250|UniProtKB:Q56NI9}.
CC -!- DEVELOPMENTAL STAGE: At 14.5 dpc the expression is detected in
CC developing murine lip, eyelid, palate, digit, tongue and hair
CC follicles. Its expression is also observed in the long bones of the
CC developing forelimb but not the hindlimb.
CC {ECO:0000269|PubMed:32255174}.
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:Q56NI9}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26905.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK010391; BAB26905.1; ALT_SEQ; mRNA.
DR EMBL; AK050845; BAC34431.1; -; mRNA.
DR EMBL; AK144685; BAE26012.1; -; mRNA.
DR EMBL; BC033303; AAH33303.2; -; mRNA.
DR EMBL; BC071275; AAH71275.1; -; mRNA.
DR CCDS; CCDS27216.1; -.
DR RefSeq; NP_082315.3; NM_028039.2.
DR PDB; 6SP0; X-ray; 1.77 A; A=368-592.
DR PDBsum; 6SP0; -.
DR AlphaFoldDB; Q8CIB9; -.
DR SMR; Q8CIB9; -.
DR STRING; 10090.ENSMUSP00000022613; -.
DR iPTMnet; Q8CIB9; -.
DR PhosphoSitePlus; Q8CIB9; -.
DR EPD; Q8CIB9; -.
DR jPOST; Q8CIB9; -.
DR MaxQB; Q8CIB9; -.
DR PaxDb; Q8CIB9; -.
DR PeptideAtlas; Q8CIB9; -.
DR PRIDE; Q8CIB9; -.
DR ProteomicsDB; 275648; -.
DR Antibodypedia; 23057; 82 antibodies from 17 providers.
DR DNASU; 71988; -.
DR Ensembl; ENSMUST00000022613; ENSMUSP00000022613; ENSMUSG00000022034.
DR GeneID; 71988; -.
DR KEGG; mmu:71988; -.
DR UCSC; uc007ujp.2; mouse.
DR CTD; 157570; -.
DR MGI; MGI:1919238; Esco2.
DR VEuPathDB; HostDB:ENSMUSG00000022034; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000158598; -.
DR HOGENOM; CLU_031546_1_0_1; -.
DR InParanoid; Q8CIB9; -.
DR OMA; FGTTVCK; -.
DR OrthoDB; 1024179at2759; -.
DR PhylomeDB; Q8CIB9; -.
DR TreeFam; TF314027; -.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR BioGRID-ORCS; 71988; 41 hits in 112 CRISPR screens.
DR ChiTaRS; Esco2; mouse.
DR PRO; PR:Q8CIB9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CIB9; protein.
DR Bgee; ENSMUSG00000022034; Expressed in animal zygote and 167 other tissues.
DR ExpressionAtlas; Q8CIB9; baseline and differential.
DR Genevisible; Q8CIB9; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI.
DR GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR GO; GO:0001741; C:XY body; IDA:MGI.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0034421; P:post-translational protein acetylation; ISO:MGI.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell cycle; Chromosome; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..592
FT /note="N-acetyltransferase ESCO2"
FT /id="PRO_0000074543"
FT ZN_FING 384..408
FT /note="CCHH-type"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56NI9"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56NI9"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56NI9"
FT CONFLICT 54..55
FT /note="KE -> RK (in Ref. 2; AAH33303)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="K -> E (in Ref. 1; BAB26905)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="F -> Y (in Ref. 1; BAB26905)"
FT /evidence="ECO:0000305"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:6SP0"
FT HELIX 398..415
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:6SP0"
FT HELIX 443..460
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 483..492
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:6SP0"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:6SP0"
FT HELIX 540..551
FT /evidence="ECO:0007829|PDB:6SP0"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:6SP0"
FT HELIX 570..580
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6SP0"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:6SP0"
SQ SEQUENCE 592 AA; 67273 MW; F1067E8D3D1ED7CF CRC64;
MMATCTPRKR KRYTLNADND DSLLTDISSS KLRCAENLFP SPNKKHNYQS SVQKEDKSCS
HQLHFPSSPL KTTENSRFSF ANHSSLFKPA MSTVSFYSKE KYYLNPLERK LIRECRSICL
ATESGDKPIP SVTENIQRKP VCTKKNKKKQ KSLTAKYQPN YKHIKSKSRN LKNSKPNQVT
YKPVVDQENS CFPAKNYPNS PPRVLSQKIK PQVTLQGGAA FFVRKRNSLK KLPLEDKPLL
LQKNLPEVPE GAPEAKQIPK SLLVDEKSSV KVQNARSKNE EKLRKNPSGA VVSSKECNLD
KHDFPSENSL DENKTISPES VYPIFNVSSV NTKRPEEQSS VGSTACTNFL KQTNVPKNIN
SRDTNKGGKD QLVIDAGQKH FGTTVCKSCG MIYTASNPED EIQHLQHHHR FLEGIKFVGW
KRERVVAEFW DGKIVLVLPR DPSYAIKKVE DVQELVDLEL GFQQTVPVCP DKTKTFLFID
EKRVVGCLIA EPIKQAFRVL SEPSASKECS RAWRCSDVPE PAICGISRIW VFRLKRRKRI
ARRLVDTVRN CFMFGCFLST NEIAFSDPTP DGKLFATKYC NTPNFLVYNF HN
