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Database: UniProt
Entry: F7FUZ4_MACMU
LinkDB: F7FUZ4_MACMU
Original site: F7FUZ4_MACMU 
ID   F7FUZ4_MACMU            Unreviewed;       600 AA.
AC   F7FUZ4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Establishment of sister chromatid cohesion N-acetyltransferase 2 {ECO:0000313|Ensembl:ENSMMUP00000021066.2};
GN   Name=ESCO2 {ECO:0000313|Ensembl:ENSMMUP00000021066.2,
GN   ECO:0000313|VGNC:VGNC:72374};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000021066.2, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000021066.2}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000021066.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000636};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC       {ECO:0000256|ARBA:ARBA00005816}.
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DR   RefSeq; XP_015000526.1; XM_015145040.1.
DR   AlphaFoldDB; F7FUZ4; -.
DR   SMR; F7FUZ4; -.
DR   STRING; 9544.ENSMMUP00000021066; -.
DR   PaxDb; 9544-ENSMMUP00000021066; -.
DR   Ensembl; ENSMMUT00000022519.4; ENSMMUP00000021066.2; ENSMMUG00000016018.4.
DR   GeneID; 713186; -.
DR   CTD; 157570; -.
DR   VEuPathDB; HostDB:ENSMMUG00000016018; -.
DR   VGNC; VGNC:72374; ESCO2.
DR   eggNOG; KOG3014; Eukaryota.
DR   GeneTree; ENSGT00940000158598; -.
DR   HOGENOM; CLU_031546_1_0_1; -.
DR   InParanoid; F7FUZ4; -.
DR   OMA; HIQYHHR; -.
DR   OrthoDB; 22809at2759; -.
DR   TreeFam; TF314027; -.
DR   Proteomes; UP000006718; Chromosome 8.
DR   Bgee; ENSMMUG00000016018; Expressed in spermatocyte and 5 other cell types or tissues.
DR   ExpressionAtlas; F7FUZ4; baseline.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0001741; C:XY body; IEA:Ensembl.
DR   GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR   InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR   InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR   PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1.
DR   PANTHER; PTHR45884:SF3; N-ACETYLTRANSFERASE ESCO2; 1.
DR   Pfam; PF13880; Acetyltransf_13; 1.
DR   Pfam; PF13878; zf-C2H2_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          373..412
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          528..596
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
FT   REGION          279..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  68009 MW;  D8B66160A97367FE CRC64;
     MAALTPRKRK QDSLNCDSLL HFTENLFPSP NKKHCFNQNS DKNEENLHCS QQGHFVLSAL
     KTTEINRLPS ANQGSQFKSS VSTVSFYNQN KWYLNPLERK LIKESRSTCL KTNDEDISFP
     IVTEKMQGKP VCSKNNNKKP QKSLTAKYQP RYRHIKPVSR NSRNPKQNRV IYKPIMEKEN
     NCHSAENNPS APRVLSQKIK PQVTLQGGAA FFVSRKKSSL RKWSLENELS QGTQKNKSAV
     IEDSDVKTVS EKKAFETRQV PKCLILEEKL NIGLSASSKN QEELIKDSSD DRVSSKEHKV
     DKNEAFPSED SLGENKTISP KSTVYPIFSA SSVNSKRSLG EEQLSVGSIN FLKQTNIQKN
     TNTRDTSKKT KDQLIIDAGQ KHFGATVCKS CGMIYTASNP EDEMQHVQHH HRFLEGIKYV
     GWKKERVVAE FWDGKIVLVL PHDPSFAIKK VEDVQELVDN ELGFQQVVPK CANKIKTFLF
     ISDEKRVVGC LIAEPIKQAF RVLSEPAGPG SPTSTECSRA WQCSDVPEPA VCGISRIWVF
     RLKRRKRIAR RLVDTLRNCF MFGCFLSTDE IAFSDPTPDG KLFATKYCNT PNFLVYNFNS
//
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