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Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (Lysine N-methyltransferase 7) (SET domain-containing protein 7) (SET7/9)

 SETD7_HUMAN             Reviewed;         366 AA.
Q8WTS6; B5WWL3; Q0VAH3; Q4W5A9; Q9C0E6;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-JUN-2018, entry version 162.
RecName: Full=Histone-lysine N-methyltransferase SETD7;
EC=2.1.1.43;
AltName: Full=Histone H3-K4 methyltransferase SETD7;
Short=H3-K4-HMTase SETD7;
AltName: Full=Lysine N-methyltransferase 7;
AltName: Full=SET domain-containing protein 7;
AltName: Full=SET7/9;
Name=SETD7; Synonyms=KIAA1717, KMT7, SET7, SET9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-44; 108-115;
144-152; 234-258 AND 345-358, AND MUTAGENESIS OF HIS-297.
TISSUE=Brain;
PubMed=11779497; DOI=10.1016/S1097-2765(01)00405-1;
Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P.,
Zhang Y.;
"Purification and functional characterization of a histone H3-lysine
4-specific methyltransferase.";
Mol. Cell 8:1207-1217(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-45; 104-115;
144-152; 159-169; 201-250 AND 324-358, AND MUTAGENESIS OF HIS-297.
TISSUE=Cervix carcinoma;
PubMed=11850410; DOI=10.1101/gad.967202;
Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D.,
Tempst P., Reinberg D.;
"Set9, a novel histone H3 methyltransferase that facilitates
transcription by precluding histone tail modifications required for
heterochromatin formation.";
Genes Dev. 16:479-489(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
FUNCTION.
PubMed=12588998; DOI=10.1128/MCB.23.5.1808-1816.2003;
Martens J.H., Verlaan M., Kalkhoven E., Zantema A.;
"Cascade of distinct histone modifications during collagenase gene
activation.";
Mol. Cell. Biol. 23:1808-1816(2003).
[7]
FUNCTION, AND MUTAGENESIS OF HIS-297.
PubMed=15099517; DOI=10.1016/S1097-2765(04)00182-0;
Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.;
"Gene-specific modulation of TAF10 function by SET9-mediated
methylation.";
Mol. Cell 14:175-182(2004).
[8]
FUNCTION, INTERACTION WITH IPF1, AND MUTAGENESIS OF HIS-297.
PubMed=16141209; DOI=10.1074/jbc.M505741200;
Francis J., Chakrabarti S.K., Garmey J.C., Mirmira R.G.;
"Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II
elongation during activation of insulin transcription.";
J. Biol. Chem. 280:36244-36253(2005).
[9]
FUNCTION.
PubMed=17108971; DOI=10.1038/nature05287;
Huang J., Perez-Burgos L., Placek B.J., Sengupta R., Richter M.,
Dorsey J.A., Kubicek S., Opravil S., Jenuwein T., Berger S.L.;
"Repression of p53 activity by Smyd2-mediated methylation.";
Nature 444:629-632(2006).
[10]
MUTAGENESIS OF GLU-220; GLU-228; TYR-245 AND LYS-294.
PubMed=16433545; DOI=10.1021/ja056153+;
Hu P., Zhang Y.;
"Catalytic mechanism and product specificity of the histone lysine
methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple
initial structures.";
J. Am. Chem. Soc. 128:1272-1278(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 52-344.
PubMed=12372304; DOI=10.1016/S0092-8674(02)00964-9;
Wilson J., Jing C., Walker P., Martin S., Howell S., Blackburn G.,
Gamblin S., Xiao B.;
"Crystal structure and functional analysis of the histone
methyltransferase SET7/9.";
Cell 111:105-115(2002).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=12389038; DOI=10.1038/nsb861;
Jacobs S.A., Harp J.M., Devarakonda S., Kim Y., Rastinejad F.,
Khorasanizadeh S.;
"The active site of the SET domain is constructed on a knot.";
Nat. Struct. Biol. 9:833-838(2002).
[15]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE AND HISTONE PEPTIDE, FUNCTION, AND MUTAGENESIS
OF TYR-245.
PubMed=12540855; DOI=10.1038/nature01378;
Xiao B., Jing C., Wilson J.R., Walker P.A., Vasisht N., Kelly G.,
Howell S., Taylor I.A., Blackburn G.M., Gamblin S.J.;
"Structure and catalytic mechanism of the human histone
methyltransferase SET7/9.";
Nature 421:652-656(2003).
[16]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-366 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE.
PubMed=12514135; DOI=10.1093/emboj/cdg025;
Kwon T., Chang J.H., Kwak E., Lee C.W., Joachimiak A., Kim Y.C.,
Lee J., Cho Y.;
"Mechanism of histone lysine methyl transfer revealed by the structure
of SET7/9-AdoMet.";
EMBO J. 22:292-303(2003).
[17]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366, FUNCTION, AND
MUTAGENESIS OF HIS-297.
PubMed=15525938; DOI=10.1038/nature03117;
Chuikov S., Kurash J.K., Wilson J.R., Xiao B., Justin N., Ivanov G.S.,
McKinney K., Tempst P., Prives C., Gamblin S.J., Barlev N.A.,
Reinberg D.;
"Regulation of p53 activity through lysine methylation.";
Nature 432:353-360(2004).
[18]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 110-366, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF LYS-317.
PubMed=16415881; DOI=10.1038/nsmb1045;
Couture J.-F., Collazo E., Hauk G., Trievel R.C.;
"Structural basis for the methylation site specificity of SET7/9.";
Nat. Struct. Mol. Biol. 13:140-146(2006).
-!- FUNCTION: Histone methyltransferase that specifically
monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation
represents a specific tag for epigenetic transcriptional
activation. Plays a central role in the transcriptional activation
of genes such as collagenase or insulin. Recruited by IPF1/PDX-1
to the insulin promoter, leading to activate transcription. Has
also methyltransferase activity toward non-histone proteins such
as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding
the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189'
of TAF10, leading to increase the affinity of TAF10 for RNA
polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing
p53/TP53 and increasing p53/TP53-mediated transcriptional
activation. {ECO:0000269|PubMed:12540855,
ECO:0000269|PubMed:12588998, ECO:0000269|PubMed:15099517,
ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16141209,
ECO:0000269|PubMed:17108971}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00910}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=29 uM for histone H3 {ECO:0000269|PubMed:16415881};
KM=12 uM for TAF10 {ECO:0000269|PubMed:16415881};
KM=69 uM for p53/TP53 {ECO:0000269|PubMed:16415881};
-!- SUBUNIT: Interacts with IPF1/PDX-1. {ECO:0000269|PubMed:12514135,
ECO:0000269|PubMed:12540855, ECO:0000269|PubMed:16141209}.
-!- INTERACTION:
P26358:DNMT1; NbExp=9; IntAct=EBI-1268586, EBI-719459;
Q9WVH4:Foxo3 (xeno); NbExp=5; IntAct=EBI-1268586, EBI-6127038;
P68431:HIST1H3D; NbExp=3; IntAct=EBI-1268586, EBI-79722;
P68433:Hist1h3i (xeno); NbExp=2; IntAct=EBI-1268586, EBI-79743;
Q96RI1:NR1H4; NbExp=5; IntAct=EBI-1268586, EBI-1250177;
P06400:RB1; NbExp=4; IntAct=EBI-1268586, EBI-491274;
Q04206:RELA; NbExp=12; IntAct=EBI-1268586, EBI-73886;
Q04207:Rela (xeno); NbExp=2; IntAct=EBI-1268586, EBI-644400;
Q9UHV2:SERTAD1; NbExp=2; IntAct=EBI-1268586, EBI-748601;
Q96EB6:SIRT1; NbExp=11; IntAct=EBI-1268586, EBI-1802965;
Q12962:TAF10; NbExp=4; IntAct=EBI-1268586, EBI-708376;
P04637:TP53; NbExp=11; IntAct=EBI-1268586, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreatic
islets.
-!- DOMAIN: The SET domain is necessary but not sufficient for histone
methyltransferase activity.
-!- MISCELLANEOUS: Monomethyltransferase activity is achieved by
disrupting the formation at near-attack conformations for the
dimethylation reaction.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. SET7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00910}.
-!- SEQUENCE CAUTION:
Sequence=BAB21808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF448510; AAL56579.1; -; mRNA.
EMBL; AF462150; AAL69901.1; -; mRNA.
EMBL; AB051504; BAB21808.1; ALT_INIT; mRNA.
EMBL; AC112236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114743; AAY40937.1; -; Genomic_DNA.
EMBL; BC121055; AAI21056.1; -; mRNA.
EMBL; BC121056; AAI21057.1; -; mRNA.
CCDS; CCDS3748.1; -.
RefSeq; NP_001293128.1; NM_001306199.1.
RefSeq; NP_085151.1; NM_030648.3.
UniGene; Hs.480792; -.
PDB; 1H3I; X-ray; 2.10 A; A/B=52-344.
PDB; 1MT6; X-ray; 2.20 A; A=58-337.
PDB; 1MUF; X-ray; 2.26 A; A=81-337.
PDB; 1N6A; X-ray; 1.70 A; A=108-366.
PDB; 1N6C; X-ray; 2.30 A; A=70-366.
PDB; 1O9S; X-ray; 1.75 A; A/B=108-366.
PDB; 1XQH; X-ray; 1.75 A; A/E=108-366.
PDB; 2F69; X-ray; 1.30 A; A=110-366.
PDB; 3CBM; X-ray; 1.69 A; A=111-366.
PDB; 3CBO; X-ray; 1.65 A; A=111-366.
PDB; 3CBP; X-ray; 1.42 A; A=111-366.
PDB; 3M53; X-ray; 1.85 A; A=110-366.
PDB; 3M54; X-ray; 1.60 A; A=110-366.
PDB; 3M55; X-ray; 1.55 A; A=110-366.
PDB; 3M56; X-ray; 1.65 A; A=110-366.
PDB; 3M57; X-ray; 1.70 A; A=110-366.
PDB; 3M58; X-ray; 1.40 A; A=110-366.
PDB; 3M59; X-ray; 1.70 A; A=110-366.
PDB; 3M5A; X-ray; 1.75 A; A=110-366.
PDB; 3OS5; X-ray; 1.69 A; A=111-366.
PDB; 3VUZ; X-ray; 2.50 A; A=111-366.
PDB; 3VV0; X-ray; 2.00 A; A=111-366.
PDB; 4E47; X-ray; 2.00 A; A/B/C/D=109-366.
PDB; 4J7F; X-ray; 1.59 A; A=110-366.
PDB; 4J7I; X-ray; 2.56 A; A=110-366.
PDB; 4J83; X-ray; 1.70 A; A=110-366.
PDB; 4J8O; X-ray; 1.63 A; A=110-366.
PDB; 4JDS; X-ray; 1.70 A; A/B/C/D=109-366.
PDB; 4JLG; X-ray; 1.90 A; A/B=109-366.
PDB; 5AYF; X-ray; 2.00 A; A=111-366.
PDB; 5EG2; X-ray; 1.55 A; A=110-366.
PDBsum; 1H3I; -.
PDBsum; 1MT6; -.
PDBsum; 1MUF; -.
PDBsum; 1N6A; -.
PDBsum; 1N6C; -.
PDBsum; 1O9S; -.
PDBsum; 1XQH; -.
PDBsum; 2F69; -.
PDBsum; 3CBM; -.
PDBsum; 3CBO; -.
PDBsum; 3CBP; -.
PDBsum; 3M53; -.
PDBsum; 3M54; -.
PDBsum; 3M55; -.
PDBsum; 3M56; -.
PDBsum; 3M57; -.
PDBsum; 3M58; -.
PDBsum; 3M59; -.
PDBsum; 3M5A; -.
PDBsum; 3OS5; -.
PDBsum; 3VUZ; -.
PDBsum; 3VV0; -.
PDBsum; 4E47; -.
PDBsum; 4J7F; -.
PDBsum; 4J7I; -.
PDBsum; 4J83; -.
PDBsum; 4J8O; -.
PDBsum; 4JDS; -.
PDBsum; 4JLG; -.
PDBsum; 5AYF; -.
PDBsum; 5EG2; -.
ProteinModelPortal; Q8WTS6; -.
SMR; Q8WTS6; -.
BioGrid; 123332; 45.
CORUM; Q8WTS6; -.
DIP; DIP-29045N; -.
IntAct; Q8WTS6; 21.
MINT; Q8WTS6; -.
STRING; 9606.ENSP00000274031; -.
BindingDB; Q8WTS6; -.
ChEMBL; CHEMBL5523; -.
DrugBank; DB01752; S-Adenosyl-L-Homocysteine.
GuidetoPHARMACOLOGY; 2703; -.
iPTMnet; Q8WTS6; -.
PhosphoSitePlus; Q8WTS6; -.
BioMuta; SETD7; -.
DMDM; 25091217; -.
EPD; Q8WTS6; -.
MaxQB; Q8WTS6; -.
PaxDb; Q8WTS6; -.
PeptideAtlas; Q8WTS6; -.
PRIDE; Q8WTS6; -.
ProteomicsDB; 74595; -.
Ensembl; ENST00000274031; ENSP00000274031; ENSG00000145391.
GeneID; 80854; -.
KEGG; hsa:80854; -.
UCSC; uc003ihw.4; human.
CTD; 80854; -.
DisGeNET; 80854; -.
EuPathDB; HostDB:ENSG00000145391.13; -.
GeneCards; SETD7; -.
HGNC; HGNC:30412; SETD7.
HPA; HPA058111; -.
MIM; 606594; gene.
neXtProt; NX_Q8WTS6; -.
OpenTargets; ENSG00000145391; -.
PharmGKB; PA143485615; -.
eggNOG; KOG1079; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00390000004827; -.
HOGENOM; HOG000074731; -.
HOVERGEN; HBG028309; -.
InParanoid; Q8WTS6; -.
KO; K11431; -.
OMA; GSSVYHF; -.
OrthoDB; EOG091G08JN; -.
PhylomeDB; Q8WTS6; -.
TreeFam; TF106392; -.
BRENDA; 2.1.1.43; 2681.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
SABIO-RK; Q8WTS6; -.
ChiTaRS; SETD7; human.
EvolutionaryTrace; Q8WTS6; -.
GeneWiki; SETD7; -.
GenomeRNAi; 80854; -.
PRO; PR:Q8WTS6; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145391; -.
CleanEx; HS_SETD7; -.
ExpressionAtlas; Q8WTS6; baseline and differential.
Genevisible; Q8WTS6; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
GO; GO:0070828; P:heterochromatin organization; IDA:MGI.
GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0051570; P:regulation of histone H3-K9 methylation; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
InterPro; IPR003409; MORN.
InterPro; IPR001214; SET_dom.
Pfam; PF02493; MORN; 4.
Pfam; PF00856; SET; 1.
PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS51577; SAM_MT43_SET7; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Activator; Chromatin regulator; Chromosome;
Complete proteome; Direct protein sequencing; Methyltransferase;
Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase.
CHAIN 1 366 Histone-lysine N-methyltransferase SETD7.
/FTId=PRO_0000186054.
REPEAT 36 58 MORN 1.
REPEAT 59 81 MORN 2.
REPEAT 106 128 MORN 3.
DOMAIN 214 336 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 226 228 S-adenosyl-L-methionine binding.
REGION 256 258 Substrate binding.
REGION 266 268 Substrate binding.
REGION 296 297 S-adenosyl-L-methionine binding.
COMPBIAS 51 54 Poly-Phe.
BINDING 245 245 Substrate.
BINDING 317 317 Substrate.
BINDING 335 335 Substrate; via carbonyl oxygen.
BINDING 356 356 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00190,
ECO:0000269|PubMed:12514135,
ECO:0000269|PubMed:12540855}.
MUTAGEN 220 220 E->A: Increases near-attack
conformations.
{ECO:0000269|PubMed:16433545}.
MUTAGEN 228 228 E->A: Increases near-attack
conformations.
{ECO:0000269|PubMed:16433545}.
MUTAGEN 245 245 Y->A: Significantly reduces the
monomethyltransferase activity but
increases the dimethyltransferase
activity. {ECO:0000269|PubMed:12540855,
ECO:0000269|PubMed:16433545}.
MUTAGEN 294 294 K->A: Significantly reduces the catalytic
activity. {ECO:0000269|PubMed:16433545}.
MUTAGEN 297 297 H->A,G: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11779497,
ECO:0000269|PubMed:11850410,
ECO:0000269|PubMed:15099517,
ECO:0000269|PubMed:15525938,
ECO:0000269|PubMed:16141209}.
MUTAGEN 317 317 K->A: Induces a reduction in
methyltransferase activity toward TAF10
but an increased methyltransferase
activity for H3 and p53/TP53.
{ECO:0000269|PubMed:16415881}.
STRAND 54 56 {ECO:0000244|PDB:1H3I}.
STRAND 61 64 {ECO:0000244|PDB:1H3I}.
STRAND 67 75 {ECO:0000244|PDB:1H3I}.
STRAND 81 87 {ECO:0000244|PDB:1H3I}.
STRAND 90 98 {ECO:0000244|PDB:1H3I}.
STRAND 100 102 {ECO:0000244|PDB:1H3I}.
STRAND 104 111 {ECO:0000244|PDB:1H3I}.
HELIX 114 116 {ECO:0000244|PDB:3M58}.
STRAND 119 122 {ECO:0000244|PDB:2F69}.
STRAND 128 131 {ECO:0000244|PDB:2F69}.
STRAND 135 137 {ECO:0000244|PDB:4J83}.
STRAND 141 147 {ECO:0000244|PDB:2F69}.
STRAND 151 160 {ECO:0000244|PDB:2F69}.
STRAND 163 176 {ECO:0000244|PDB:2F69}.
STRAND 179 184 {ECO:0000244|PDB:2F69}.
STRAND 186 188 {ECO:0000244|PDB:1MT6}.
TURN 203 206 {ECO:0000244|PDB:3M57}.
HELIX 210 213 {ECO:0000244|PDB:2F69}.
STRAND 216 220 {ECO:0000244|PDB:2F69}.
TURN 224 226 {ECO:0000244|PDB:1MUF}.
STRAND 228 234 {ECO:0000244|PDB:2F69}.
STRAND 241 245 {ECO:0000244|PDB:2F69}.
STRAND 248 250 {ECO:0000244|PDB:2F69}.
HELIX 252 256 {ECO:0000244|PDB:2F69}.
HELIX 260 262 {ECO:0000244|PDB:2F69}.
STRAND 266 268 {ECO:0000244|PDB:1H3I}.
STRAND 270 272 {ECO:0000244|PDB:2F69}.
STRAND 274 276 {ECO:0000244|PDB:2F69}.
TURN 279 282 {ECO:0000244|PDB:2F69}.
TURN 284 286 {ECO:0000244|PDB:2F69}.
HELIX 292 294 {ECO:0000244|PDB:2F69}.
STRAND 295 300 {ECO:0000244|PDB:1H3I}.
STRAND 302 310 {ECO:0000244|PDB:2F69}.
TURN 311 313 {ECO:0000244|PDB:2F69}.
STRAND 314 323 {ECO:0000244|PDB:2F69}.
STRAND 330 333 {ECO:0000244|PDB:2F69}.
STRAND 338 340 {ECO:0000244|PDB:1O9S}.
STRAND 344 346 {ECO:0000244|PDB:3OS5}.
HELIX 351 363 {ECO:0000244|PDB:2F69}.
SEQUENCE 366 AA; 40721 MW; 73A1217079E3BA13 CRC64;
MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE
GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT DGRLIFKGQY KDNIRHGVCW
IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD ERTALYGKFI DGEMIEGKLA TLMSTEEGRP
HFELMPGNSV YHFDKSTSSC ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT
VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF
QATQQK


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