ESCO2_HUMAN
ID ESCO2_HUMAN Reviewed; 601 AA.
AC Q56NI9; B3KW59; Q49AP4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=N-acetyltransferase ESCO2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15958495};
DE AltName: Full=Establishment factor-like protein 2;
DE Short=EFO2 {ECO:0000303|PubMed:15958495};
DE Short=EFO2p;
DE Short=hEFO2;
DE AltName: Full=Establishment of cohesion 1 homolog 2;
DE Short=ECO1 homolog 2;
GN Name=ESCO2 {ECO:0000312|HGNC:HGNC:27230};
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT RBS GLY-539.
RX PubMed=15821733; DOI=10.1038/ng1548;
RA Vega H., Waisfisz Q., Gordillo M., Sakai N., Yanagihara I., Yamada M.,
RA van Gosliga D., Kayserili H., Xu C., Ozono K., Wang Jabs E., Inui K.,
RA Joenje H.;
RT "Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast
RT ECO1 that is essential for the establishment of sister chromatid
RT cohesion.";
RL Nat. Genet. 37:468-470(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, AND
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=21111234; DOI=10.1016/j.cell.2010.10.031;
RA Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A.,
RA Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.;
RT "Sororin mediates sister chromatid cohesion by antagonizing wapl.";
RL Cell 143:737-749(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, 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-29; SER-75; SER-223; SER-244;
RP SER-312 AND SER-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 INVOLVEMENT IN RBS.
RX PubMed=16380922; DOI=10.1086/498695;
RA Schuele B., Oviedo A., Johnston K., Pai S., Francke U.;
RT "Inactivating mutations in ESCO2 cause SC phocomelia and Roberts syndrome:
RT no phenotype-genotype correlation.";
RL Am. J. Hum. Genet. 77:1117-1128(2005).
RN [15]
RP VARIANT JHS 552-ARG--SER-601 DEL, AND CHARACTERIZATION OF VARIANT JHS
RP 552-ARG--SER-601 DEL.
RX PubMed=32977150; DOI=10.1016/j.archoralbio.2020.104918;
RA Kantaputra P.N., Dejkhamron P., Tongsima S., Ngamphiw C., Intachai W.,
RA Ngiwsara L., Sawangareetrakul P., Svasti J., Olsen B., Cairns J.R.K.,
RA Bumroongkit K.;
RT "Juberg-Hayward syndrome and Roberts syndrome are allelic, caused by
RT mutations in ESCO2.";
RL Arch. Oral Biol. 119:104918-104918(2020).
RN [16]
RP VARIANT JHS 552-ARG--SER-601 DEL.
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 (PubMed:15821733, PubMed:15958495). 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 the S phase. Acetylates the cohesin component SMC3
CC (PubMed:21111234). {ECO:0000269|PubMed:15821733,
CC ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:19907496,
CC ECO:0000269|PubMed:21111234}.
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:15958495};
CC -!- INTERACTION:
CC Q56NI9; P51114-2: FXR1; NbExp=3; IntAct=EBI-3951849, EBI-11022345;
CC Q56NI9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-3951849, EBI-618309;
CC Q56NI9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3951849, EBI-79165;
CC Q56NI9; Q15276: RABEP1; NbExp=3; IntAct=EBI-3951849, EBI-447043;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15958495,
CC ECO:0000269|PubMed:19907496}. Chromosome {ECO:0000269|PubMed:15958495,
CC ECO:0000269|PubMed:19907496}. Note=Nuclear in interphase cells,
CC excluded from chromosomes during metaphase but reassociates with
CC chromosomes in telophase. {ECO:0000269|PubMed:15958495}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q56NI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56NI9-2; Sequence=VSP_055773, VSP_055774;
CC -!- TISSUE SPECIFICITY: Widely expressed in fetal tissues. In adult, it is
CC expressed in thymus, placenta and small intestine.
CC {ECO:0000269|PubMed:15821733}.
CC -!- DEVELOPMENTAL STAGE: Cell-cycle regulated. Down-regulated when cells
CC enter M phase. Expression increases again when cells enter S phase of
CC the next cell cycle. {ECO:0000269|PubMed:15958495}.
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 -!- DISEASE: Roberts-SC phocomelia syndrome (RBS) [MIM:268300]: An
CC autosomal recessive disorder characterized by pre- and postnatal growth
CC retardation, intellectual disability, microcephaly, bilateral cleft lip
CC and cleft palate, and mesomelic symmetric limb reduction. Severely
CC affected infants may be stillborn or die shortly after birth. Patient
CC chromosomes have a lack of cohesion involving heterochromatic C-banding
CC regions around centromeres and the heterochromatin regions on the 1, 9,
CC 16, and Y chromosomes. These findings are referred to as premature
CC centromere separation (PCS) and heterochromatin repulsion (HR), and
CC they are important for the diagnosis of the syndrome.
CC {ECO:0000269|PubMed:15821733, ECO:0000269|PubMed:16380922}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Juberg-Hayward syndrome (JHS) [MIM:216100]: An autosomal
CC recessive syndrome characterized by cleft lip/palate, microcephaly,
CC ptosis, hypoplasia or aplasia of thumbs, short stature, dislocation of
CC radial head, and fusion of humerus and radius leading to elbow
CC restriction. {ECO:0000269|PubMed:32255174,
CC ECO:0000269|PubMed:32977150}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000305}.
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DR EMBL; AY882862; AAX68677.1; -; mRNA.
DR EMBL; AK124215; BAG54021.1; -; mRNA.
DR EMBL; AC104997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034641; AAH34641.1; -; mRNA.
DR CCDS; CCDS34872.1; -. [Q56NI9-1]
DR RefSeq; NP_001017420.1; NM_001017420.2. [Q56NI9-1]
DR RefSeq; XP_011542723.1; XM_011544421.2. [Q56NI9-1]
DR AlphaFoldDB; Q56NI9; -.
DR SMR; Q56NI9; -.
DR BioGRID; 127605; 68.
DR IntAct; Q56NI9; 18.
DR MINT; Q56NI9; -.
DR STRING; 9606.ENSP00000306999; -.
DR iPTMnet; Q56NI9; -.
DR PhosphoSitePlus; Q56NI9; -.
DR BioMuta; ESCO2; -.
DR DMDM; 67460434; -.
DR EPD; Q56NI9; -.
DR jPOST; Q56NI9; -.
DR MassIVE; Q56NI9; -.
DR MaxQB; Q56NI9; -.
DR PaxDb; Q56NI9; -.
DR PeptideAtlas; Q56NI9; -.
DR PRIDE; Q56NI9; -.
DR ProteomicsDB; 62062; -.
DR ProteomicsDB; 62581; -. [Q56NI9-1]
DR Antibodypedia; 23057; 82 antibodies from 17 providers.
DR DNASU; 157570; -.
DR Ensembl; ENST00000305188.13; ENSP00000306999.8; ENSG00000171320.15. [Q56NI9-1]
DR Ensembl; ENST00000397418.4; ENSP00000380563.2; ENSG00000171320.15. [Q56NI9-2]
DR GeneID; 157570; -.
DR KEGG; hsa:157570; -.
DR MANE-Select; ENST00000305188.13; ENSP00000306999.8; NM_001017420.3; NP_001017420.1.
DR UCSC; uc003xgg.4; human. [Q56NI9-1]
DR CTD; 157570; -.
DR DisGeNET; 157570; -.
DR GeneCards; ESCO2; -.
DR GeneReviews; ESCO2; -.
DR HGNC; HGNC:27230; ESCO2.
DR HPA; ENSG00000171320; Tissue enhanced (bone marrow, intestine, lymphoid tissue, testis).
DR MalaCards; ESCO2; -.
DR MIM; 216100; phenotype.
DR MIM; 268300; phenotype.
DR MIM; 609353; gene.
DR neXtProt; NX_Q56NI9; -.
DR OpenTargets; ENSG00000171320; -.
DR Orphanet; 3103; Roberts syndrome.
DR PharmGKB; PA134891970; -.
DR VEuPathDB; HostDB:ENSG00000171320; -.
DR eggNOG; KOG3014; Eukaryota.
DR GeneTree; ENSGT00940000158598; -.
DR HOGENOM; CLU_031546_1_0_1; -.
DR InParanoid; Q56NI9; -.
DR OMA; FGTTVCK; -.
DR OrthoDB; 1024179at2759; -.
DR PhylomeDB; Q56NI9; -.
DR TreeFam; TF314027; -.
DR PathwayCommons; Q56NI9; -.
DR Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
DR SignaLink; Q56NI9; -.
DR BioGRID-ORCS; 157570; 147 hits in 1080 CRISPR screens.
DR ChiTaRS; ESCO2; human.
DR GeneWiki; ESCO2; -.
DR GenomeRNAi; 157570; -.
DR Pharos; Q56NI9; Tbio.
DR PRO; PR:Q56NI9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q56NI9; protein.
DR Bgee; ENSG00000171320; Expressed in oocyte and 105 other tissues.
DR ExpressionAtlas; Q56NI9; baseline and differential.
DR Genevisible; Q56NI9; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0016407; F:acetyltransferase activity; IDA:UniProtKB.
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:0008080; F:N-acetyltransferase activity; TAS:Reactome.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central.
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:0034421; P:post-translational protein acetylation; IMP:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IMP: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 Acyltransferase; Alternative splicing; Cell cycle; Chromosome;
KW Disease variant; Dwarfism; Intellectual disability; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..601
FT /note="N-acetyltransferase ESCO2"
FT /id="PRO_0000074542"
FT ZN_FING 387..411
FT /note="CCHH-type"
FT REGION 222..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055773"
FT VAR_SEQ 581..601
FT /note="GKLFATKYCNTPNFLVYNFNS -> DCRRLNRYQET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055774"
FT VARIANT 80
FT /note="A -> V (in dbSNP:rs4732748)"
FT /id="VAR_033840"
FT VARIANT 359
FT /note="Q -> P (in dbSNP:rs57479434)"
FT /id="VAR_060994"
FT VARIANT 539
FT /note="W -> G (in RBS; dbSNP:rs80359868)"
FT /evidence="ECO:0000269|PubMed:15821733"
FT /id="VAR_022649"
FT VARIANT 552..601
FT /note="Missing (in JHS; strongly decreased protein levels)"
FT /evidence="ECO:0000269|PubMed:32977150"
FT /id="VAR_085392"
SQ SEQUENCE 601 AA; 68307 MW; A3D10BFD486572AE CRC64;
MAALTPRKRK QDSLKCDSLL HFTENLFPSP NKKHCFYQNS DKNEENLHCS QQEHFVLSAL
KTTEINRLPS ANQGSPFKSA LSTVSFYNQN KWYLNPLERK LIKESRSTCL KTNDEDKSFP
IVTEKMQGKP VCSKKNNKKP QKSLTAKYQP KYRHIKPVSR NSRNSKQNRV IYKPIVEKEN
NCHSAENNSN APRVLSQKIK PQVTLQGGAA FFVRKKSSLR KSSLENEPSL GRTQKSKSEV
IEDSDVETVS EKKTFATRQV PKCLVLEEKL KIGLLSASSK NKEKLIKDSS DDRVSSKEHK
VDKNEAFSSE DSLGENKTIS PKSTVYPIFS ASSVNSKRSL GEEQFSVGSV NFMKQTNIQK
NTNTRDTSKK TKDQLIIDAG QKHFGATVCK SCGMIYTASN PEDEMQHVQH HHRFLEGIKY
VGWKKERVVA EFWDGKIVLV LPHDPSFAIK KVEDVQELVD NELGFQQVVP KCPNKIKTFL
FISDEKRVVG CLIAEPIKQA FRVLSEPIGP ESPSSTECPR AWQCSDVPEP AVCGISRIWV
FRLKRRKRIA RRLVDTLRNC FMFGCFLSTD EIAFSDPTPD GKLFATKYCN TPNFLVYNFN
S
