ID G1P7T3_MYOLU Unreviewed; 616 AA.
AC G1P7T3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Establishment of sister chromatid cohesion N-acetyltransferase 2 {ECO:0000313|Ensembl:ENSMLUP00000006196.2};
GN Name=ESCO2 {ECO:0000313|Ensembl:ENSMLUP00000006196.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006196.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000006196.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000006196.2}
RP IDENTIFICATION.
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 EMBL; AAPE02002005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02002006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02002007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P7T3; -.
DR STRING; 59463.ENSMLUP00000006196; -.
DR Ensembl; ENSMLUT00000006787.2; ENSMLUP00000006196.2; ENSMLUG00000006782.2.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000158598; -.
DR HOGENOM; CLU_031546_1_0_1; -.
DR InParanoid; G1P7T3; -.
DR OMA; HIQYHHR; -.
DR TreeFam; TF314027; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
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: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: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: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:UP000001074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 389..428
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 544..612
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 298..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 69923 MW; 8793B6AC4F5A3CF9 CRC64;
KMSAFTPRKR KQNSLNCDSF HSLLSDIPSK KLILDFTENI FSSPNKKYIC QRNEENVHCS
QQGHFTSSLL KTTKEDRLPS ANQGSPFKSC LSTVSFYNKN TSKCYLNPLE RKMIKESRSI
CLKTNNEDTS FPSVTEKKQE KPICSKKMKK KPQKSLTAKC QPSYKCNKPV SKNSKNSKQN
RVAYKPIVEK ENSCYSAENN LNAPRVLSQK VKPQVTLQGG AAFFVRKKSS LRKLSLENKP
LLGLNQENKS EVIKDSDVET VNERKSFETR QVPKCLLLEK ELNIELLGIR NKNEEKLIKD
SSSGVVSSRE NKPEENKCYS SGDSHSENKA VSSESIVYPI FSASSVNTKR SLVGEQSSVA
SITPTNFLKQ TNTQKSINAR DANKEMKNQL IIDAGQKHFG ATMCKSCGMI YSASNPEDEL
QHVQHHHRFL EGIKYTGWKR ERVVAEFWDG KIVLVLPHDP SYAIKKAEEV QELVDNELGF
QQVVPRCPNK TKTFLFISDE KKVVGCLIAE PIQQAFRVLS EPTSPESPNS KECHRAWQCS
NVPVPAVCGI SRIWVFRFKR RKRIARRLVD TLRNRFMFGC FLSTNEIAFS DPTPDGKLFA
AKYCNTPNFL VYNFNS
//
