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N-acetyltransferase ESCO1 (EC 2.3.1.-) (CTF7 homolog 1) (Establishment factor-like protein 1) (EFO1p) (hEFO1) (Establishment of cohesion 1 homolog 1) (ECO1 homolog 1) (ESO1 homolog 1)

 ESCO1_HUMAN             Reviewed;         840 AA.
Q5FWF5; B0YJ11; B0YJ12; Q69YG4; Q69YS3; Q6IMD7; Q8N3Z5; Q8NBG2;
Q96PX7;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
28-MAR-2018, entry version 123.
RecName: Full=N-acetyltransferase ESCO1;
EC=2.3.1.- {ECO:0000269|PubMed:27112597, ECO:0000269|PubMed:27803161};
AltName: Full=CTF7 homolog 1;
AltName: Full=Establishment factor-like protein 1;
Short=EFO1p;
Short=hEFO1;
AltName: Full=Establishment of cohesion 1 homolog 1;
Short=ECO1 homolog 1;
Short=ESO1 homolog 1;
Name=ESCO1; Synonyms=EFO1, KIAA1911;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11572484; DOI=10.1093/dnares/8.4.179;
Nagase T., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XXI.
The complete sequences of 60 new cDNA clones from brain which code for
large proteins.";
DNA Res. 8:179-187(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow, and Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 624-840 (ISOFORM 2), AND VARIANT
MET-221.
TISSUE=Lymph, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-840 (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
IDENTIFICATION (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=14576321; DOI=10.1093/nar/gkg811;
Bellows A.M., Kenna M.A., Cassimeris L., Skibbens R.V.;
"Human EFO1p exhibits acetyltransferase activity and is a unique
combination of linker histone and Ctf7p/Eco1p chromatid cohesion
establishment domains.";
Nucleic Acids Res. 31:6334-6343(2003).
[8]
FUNCTION, ASSOCIATION WITH CHROMOSOMES, SUBCELLULAR LOCATION,
PHOSPHORYLATION, AND MUTAGENESIS OF CYS-622.
PubMed=15958495; DOI=10.1091/mbc.E04-12-1063;
Hou F., Zou H.;
"Two human orthologues of Eco1/Ctf7 acetyltransferases are both
required for proper sister-chromatid cohesion.";
Mol. Biol. Cell 16:3908-3918(2005).
[9]
FUNCTION.
PubMed=18614053; DOI=10.1016/j.molcel.2008.06.006;
Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X.,
Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.;
"Acetylation of Smc3 by Eco1 is required for S phase sister chromatid
cohesion in both human and yeast.";
Mol. Cell 31:143-151(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19907496; DOI=10.1038/nature08550;
Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.;
"Cohesin acetylation speeds the replication fork.";
Nature 462:231-234(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-412, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-332, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[15] {ECO:0000244|PDB:5T53}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 599-825 IN COMPLEX WITH
ACETYL-COA AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF PHE-640;
GLN-643; PHE-644; ASP-690; GLU-725; ARG-732; GLU-735; GLU-736;
TRP-756; SER-770; ARG-771; TRP-773; ARG-786; SER-809 AND GLY-815.
PubMed=27803161; DOI=10.1074/jbc.M116.752220;
Rivera-Colon Y., Maguire A., Liszczak G.P., Olia A.S., Marmorstein R.;
"Molecular Basis for Cohesin Acetylation by Establishment of Sister
Chromatid Cohesion N-Acetyltransferase ESCO1.";
J. Biol. Chem. 291:26468-26477(2016).
[16] {ECO:0000244|PDB:4MXE}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 654-836 IN COMPLEX WITH
ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF
GLY-768; ARG-780; GLU-789 AND LYS-803.
PubMed=27112597; DOI=10.1016/j.str.2016.03.021;
Kouznetsova E., Kanno T., Karlberg T., Thorsell A.G., Wisniewska M.,
Kursula P., Sjogren C., Schuler H.;
"Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by
Substrate-Assisted Catalysis.";
Structure 24:789-796(2016).
-!- FUNCTION: Acetyltransferase required for the establishment of
sister chromatid cohesion and couple the processes of cohesion and
DNA replication to ensure that only sister chromatids become
paired together. In contrast to the structural cohesins, the
deposition and establishment factors are required only during S
phase. Acts by mediating the acetylation of cohesin component
SMC3. {ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495,
ECO:0000269|PubMed:18614053, ECO:0000269|PubMed:19907496,
ECO:0000269|PubMed:27112597, ECO:0000269|PubMed:27803161}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=77 uM for acetyl-CoA {ECO:0000269|PubMed:27803161};
-!- SUBUNIT: The subunit structure is controversial. Monomer
(PubMed:27803161). Homodimer (PubMed:27112597).
{ECO:0000269|PubMed:27112597, ECO:0000269|PubMed:27803161,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14576321}.
Chromosome {ECO:0000269|PubMed:15958495}. Note=Nuclear at
interphase, associated with chromosomes during mitosis
(PubMed:15958495).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5FWF5-1; Sequence=Displayed;
Name=2;
IsoId=Q5FWF5-2; Sequence=VSP_014029, VSP_014030;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain,
liver, placenta, lung, kidney and pancreas. Highly expressed in
muscle. {ECO:0000269|PubMed:14576321}.
-!- DOMAIN: The N-terminal region seems to be responsible for the
association with chromosomes, thus excluding any involvement of
the Zn finger in this process.
-!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:15958495}.
-!- SIMILARITY: Belongs to the acetyltransferase family. ECO
subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH36943.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
Sequence=BAB67804.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC03483.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB067498; BAB67804.1; ALT_INIT; mRNA.
EMBL; AL832041; CAH10584.1; -; mRNA.
EMBL; AL834200; CAH10682.1; -; mRNA.
EMBL; EF444976; ACA05989.1; -; Genomic_DNA.
EMBL; EF444976; ACA05990.1; -; Genomic_DNA.
EMBL; CH471088; EAX01128.1; -; Genomic_DNA.
EMBL; CH471088; EAX01127.1; -; Genomic_DNA.
EMBL; BC036943; AAH36943.1; ALT_SEQ; mRNA.
EMBL; BC089426; AAH89426.1; -; mRNA.
EMBL; AK090579; BAC03483.1; ALT_INIT; mRNA.
EMBL; BK001617; DAA02068.1; -; mRNA.
CCDS; CCDS32800.1; -. [Q5FWF5-1]
RefSeq; NP_443143.2; NM_052911.2. [Q5FWF5-1]
RefSeq; XP_011524100.1; XM_011525798.1. [Q5FWF5-1]
UniGene; Hs.464733; -.
PDB; 4MXE; X-ray; 2.60 A; A/B=654-836.
PDB; 5T53; X-ray; 2.70 A; A=599-825.
PDBsum; 4MXE; -.
PDBsum; 5T53; -.
ProteinModelPortal; Q5FWF5; -.
SMR; Q5FWF5; -.
BioGrid; 125360; 23.
CORUM; Q5FWF5; -.
DIP; DIP-56674N; -.
IntAct; Q5FWF5; 14.
STRING; 9606.ENSP00000269214; -.
CarbonylDB; Q5FWF5; -.
iPTMnet; Q5FWF5; -.
PhosphoSitePlus; Q5FWF5; -.
BioMuta; ESCO1; -.
DMDM; 116241355; -.
EPD; Q5FWF5; -.
MaxQB; Q5FWF5; -.
PaxDb; Q5FWF5; -.
PeptideAtlas; Q5FWF5; -.
PRIDE; Q5FWF5; -.
Ensembl; ENST00000269214; ENSP00000269214; ENSG00000141446. [Q5FWF5-1]
Ensembl; ENST00000383276; ENSP00000372763; ENSG00000141446. [Q5FWF5-2]
GeneID; 114799; -.
KEGG; hsa:114799; -.
UCSC; uc002kth.2; human. [Q5FWF5-1]
CTD; 114799; -.
DisGeNET; 114799; -.
EuPathDB; HostDB:ENSG00000141446.10; -.
GeneCards; ESCO1; -.
H-InvDB; HIX0019345; -.
HGNC; HGNC:24645; ESCO1.
HPA; HPA042497; -.
MIM; 609674; gene.
neXtProt; NX_Q5FWF5; -.
OpenTargets; ENSG00000141446; -.
PharmGKB; PA134924215; -.
eggNOG; KOG3014; Eukaryota.
eggNOG; ENOG410XTJX; LUCA.
GeneTree; ENSGT00390000008335; -.
HOVERGEN; HBG081483; -.
InParanoid; Q5FWF5; -.
KO; K11268; -.
OMA; NSNWTKI; -.
OrthoDB; EOG091G0QVI; -.
PhylomeDB; Q5FWF5; -.
TreeFam; TF314027; -.
Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
SIGNOR; Q5FWF5; -.
ChiTaRS; ESCO1; human.
GenomeRNAi; 114799; -.
PRO; PR:Q5FWF5; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141446; -.
CleanEx; HS_ESCO1; -.
ExpressionAtlas; Q5FWF5; baseline and differential.
Genevisible; Q5FWF5; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008080; F:N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0034421; P:post-translational protein acetylation; IMP:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
InterPro; IPR026656; AcTrfase_ESCO1.
InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
InterPro; IPR028009; ESCO_Acetyltransf_dom.
PANTHER; PTHR11076:SF26; PTHR11076:SF26; 1.
Pfam; PF13880; Acetyltransf_13; 1.
Pfam; PF13878; zf-C2H2_3; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing; Cell cycle;
Chromosome; Complete proteome; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 840 N-acetyltransferase ESCO1.
/FTId=PRO_0000074539.
ZN_FING 617 641 CCHH-type. {ECO:0000269|PubMed:27803161}.
REGION 772 774 Acetyl-CoA binding.
{ECO:0000244|PDB:4MXE,
ECO:0000244|PDB:5T53,
ECO:0000269|PubMed:27112597,
ECO:0000269|PubMed:27803161}.
REGION 780 785 Acetyl-CoA binding.
{ECO:0000244|PDB:4MXE,
ECO:0000244|PDB:5T53,
ECO:0000269|PubMed:27112597,
ECO:0000269|PubMed:27803161}.
REGION 812 814 Acetyl-CoA binding.
{ECO:0000244|PDB:4MXE,
ECO:0000244|PDB:5T53,
ECO:0000269|PubMed:27112597,
ECO:0000269|PubMed:27803161}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364}.
VAR_SEQ 652 701 GWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDND
LGFQQAPLM -> VLLINHHECGSEEEFITSLFLSMFNFRY
TQRSFSFPIRFLEGLEERKNSG (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_014029.
VAR_SEQ 702 840 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_014030.
VARIANT 191 191 N -> S (in dbSNP:rs35087820).
/FTId=VAR_048167.
VARIANT 221 221 T -> M (in dbSNP:rs13381941).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_022648.
MUTAGEN 622 622 C->G: No effect on association with
chromosomes.
{ECO:0000269|PubMed:15958495}.
MUTAGEN 640 640 F->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 643 643 Q->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 644 644 F->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 690 690 D->N: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 725 725 E->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 732 732 R->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 735 735 E->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 736 736 E->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 756 756 W->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 768 768 G->D: Loss of autoacetylation.
{ECO:0000269|PubMed:27112597}.
MUTAGEN 770 770 S->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 771 771 R->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 773 773 W->G: Decreased thermal
stability.Strongly decreased enzyme
activity. {ECO:0000269|PubMed:27803161}.
MUTAGEN 780 780 R->A: Nearly abolishes autoacetylation.
{ECO:0000269|PubMed:27112597}.
MUTAGEN 786 786 R->C: Decreased thermal stability.
Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 789 789 E->A: Reduced autoacetylation.
{ECO:0000269|PubMed:27112597}.
MUTAGEN 803 803 K->A: Strongly reduced autoacetylation.
{ECO:0000269|PubMed:27112597}.
MUTAGEN 809 809 S->A: Strongly decreased enzyme activity.
{ECO:0000269|PubMed:27803161}.
MUTAGEN 815 815 G->R: Strongly decreased enzyme activity.
No effect on thermal stability.
{ECO:0000269|PubMed:27803161}.
CONFLICT 384 384 S -> L (in Ref. 1; BAB67804).
{ECO:0000305}.
CONFLICT 432 432 P -> S (in Ref. 2; CAH10682).
{ECO:0000305}.
CONFLICT 805 805 E -> A (in Ref. 6; BAC03483).
{ECO:0000305}.
TURN 620 622 {ECO:0000244|PDB:5T53}.
HELIX 634 648 {ECO:0000244|PDB:5T53}.
STRAND 658 661 {ECO:0000244|PDB:4MXE}.
STRAND 663 670 {ECO:0000244|PDB:4MXE}.
HELIX 676 689 {ECO:0000244|PDB:4MXE}.
HELIX 703 705 {ECO:0000244|PDB:5T53}.
STRAND 707 713 {ECO:0000244|PDB:4MXE}.
STRAND 717 726 {ECO:0000244|PDB:4MXE}.
STRAND 728 739 {ECO:0000244|PDB:4MXE}.
STRAND 752 764 {ECO:0000244|PDB:4MXE}.
STRAND 766 774 {ECO:0000244|PDB:4MXE}.
HELIX 776 778 {ECO:0000244|PDB:4MXE}.
STRAND 780 782 {ECO:0000244|PDB:4MXE}.
HELIX 783 794 {ECO:0000244|PDB:4MXE}.
STRAND 805 810 {ECO:0000244|PDB:4MXE}.
HELIX 813 823 {ECO:0000244|PDB:4MXE}.
STRAND 827 833 {ECO:0000244|PDB:4MXE}.
SEQUENCE 840 AA; 94983 MW; A36BE0EC1BE3EDF2 CRC64;
MMSIQEKSKE NSSKVTKKSD DKNSETEIQD SQKNLAKKSG PKETIKSQAK SSSESKINQP
ELETRMSTRS SKAASNDKAT KSINKNTVTV RGYSQESTKK KLSQKKLVHE NPKANEQLNR
RSQRLQQLTE VSRRSLRSRE IQGQVQAVKQ SLPPTKKEQC SSTQSKSNKT SQKHVKRKVL
EVKSDSKEDE NLVINEVINS PKGKKRKVEH QTACACSSQC TQGSEKCPQK TTRRDETKPV
PVTSEVKRSK MATSVVPKKN EMKKSVHTQV NTNTTLPKSP QPSVPEQSDN ELEQAGKSKR
GSILQLCEEI AGEIESDNVE VKKESSQMES VKEEKPTEIK LEETSVERQI LHQKETNQDV
QCNRFFPSRK TKPVKCILNG INSSAKKNSN WTKIKLSKFN SVQHNKLDSQ VSPKLGLLRT
SFSPPALEMH HPVTQSTFLG TKLHDRNITC QQEKMKEINS EEVKINDITV EINKTTERAP
ENCHLANEIK PSDPPLDNQM KHSFDSASNK NFSQCLESKL ENSPVENVTA ASTLLSQAKI
DTGENKFPGS APQQHSILSN QTSKSSDNRE TPRNHSLPKC NSHLEITIPK DLKLKEAEKT
DEKQLIIDAG QKRFGAVSCN VCGMLYTASN PEDETQHLLF HNQFISAVKY VGWKKERILA
EYPDGRIIMV LPEDPKYALK KVDEIREMVD NDLGFQQAPL MCYSRTKTLL FISNDKKVVG
CLIAEHIQWG YRVIEEKLPV IRSEEEKVRF ERQKAWCCST LPEPAICGIS RIWVFSMMRR
KKIASRMIEC LRSNFIYGSY LSKEEIAFSD PTPDGKLFAT QYCGTGQFLV YNFINGQNST


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