SETD7_HUMAN
ID SETD7_HUMAN Reviewed; 366 AA.
AC Q8WTS6; B5WWL3; Q0VAH3; Q4W5A9; Q9C0E6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE EC=2.1.1.364 {ECO:0000255|PROSITE-ProRule:PRU00910, ECO:0000269|PubMed:12540855};
DE AltName: Full=Histone H3-K4 methyltransferase SETD7;
DE Short=H3-K4-HMTase SETD7;
DE AltName: Full=Lysine N-methyltransferase 7;
DE AltName: Full=SET domain-containing protein 7;
DE AltName: Full=SET7/9;
GN Name=SETD7; Synonyms=KIAA1717, KMT7, SET7, SET9;
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], PROTEIN SEQUENCE OF 35-44; 108-115; 144-152;
RP 234-258 AND 345-358, AND MUTAGENESIS OF HIS-297.
RC TISSUE=Brain;
RX PubMed=11779497; DOI=10.1016/s1097-2765(01)00405-1;
RA Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P.,
RA Zhang Y.;
RT "Purification and functional characterization of a histone H3-lysine 4-
RT specific methyltransferase.";
RL Mol. Cell 8:1207-1217(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-45; 104-115; 144-152;
RP 159-169; 201-250 AND 324-358, AND MUTAGENESIS OF HIS-297.
RC TISSUE=Cervix carcinoma;
RX PubMed=11850410; DOI=10.1101/gad.967202;
RA Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D.,
RA Tempst P., Reinberg D.;
RT "Set9, a novel histone H3 methyltransferase that facilitates transcription
RT by precluding histone tail modifications required for heterochromatin
RT formation.";
RL Genes Dev. 16:479-489(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION.
RX PubMed=12588998; DOI=10.1128/mcb.23.5.1808-1816.2003;
RA Martens J.H., Verlaan M., Kalkhoven E., Zantema A.;
RT "Cascade of distinct histone modifications during collagenase gene
RT activation.";
RL Mol. Cell. Biol. 23:1808-1816(2003).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF HIS-297.
RX PubMed=15099517; DOI=10.1016/s1097-2765(04)00182-0;
RA Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.;
RT "Gene-specific modulation of TAF10 function by SET9-mediated methylation.";
RL Mol. Cell 14:175-182(2004).
RN [8]
RP FUNCTION, INTERACTION WITH IPF1, AND MUTAGENESIS OF HIS-297.
RX PubMed=16141209; DOI=10.1074/jbc.m505741200;
RA Francis J., Chakrabarti S.K., Garmey J.C., Mirmira R.G.;
RT "Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation
RT during activation of insulin transcription.";
RL J. Biol. Chem. 280:36244-36253(2005).
RN [9]
RP FUNCTION.
RX PubMed=17108971; DOI=10.1038/nature05287;
RA Huang J., Perez-Burgos L., Placek B.J., Sengupta R., Richter M.,
RA Dorsey J.A., Kubicek S., Opravil S., Jenuwein T., Berger S.L.;
RT "Repression of p53 activity by Smyd2-mediated methylation.";
RL Nature 444:629-632(2006).
RN [10]
RP MUTAGENESIS OF GLU-220; GLU-228; TYR-245 AND LYS-294.
RX PubMed=16433545; DOI=10.1021/ja056153+;
RA Hu P., Zhang Y.;
RT "Catalytic mechanism and product specificity of the histone lysine
RT methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial
RT structures.";
RL J. Am. Chem. Soc. 128:1272-1278(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 52-344.
RX PubMed=12372304; DOI=10.1016/s0092-8674(02)00964-9;
RA Wilson J., Jing C., Walker P., Martin S., Howell S., Blackburn G.,
RA Gamblin S., Xiao B.;
RT "Crystal structure and functional analysis of the histone methyltransferase
RT SET7/9.";
RL Cell 111:105-115(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12389038; DOI=10.1038/nsb861;
RA Jacobs S.A., Harp J.M., Devarakonda S., Kim Y., Rastinejad F.,
RA Khorasanizadeh S.;
RT "The active site of the SET domain is constructed on a knot.";
RL Nat. Struct. Biol. 9:833-838(2002).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND HISTONE PEPTIDE, FUNCTION, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF TYR-245.
RX PubMed=12540855; DOI=10.1038/nature01378;
RA Xiao B., Jing C., Wilson J.R., Walker P.A., Vasisht N., Kelly G.,
RA Howell S., Taylor I.A., Blackburn G.M., Gamblin S.J.;
RT "Structure and catalytic mechanism of the human histone methyltransferase
RT SET7/9.";
RL Nature 421:652-656(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-366 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RX PubMed=12514135; DOI=10.1093/emboj/cdg025;
RA Kwon T., Chang J.H., Kwak E., Lee C.W., Joachimiak A., Kim Y.C., Lee J.,
RA Cho Y.;
RT "Mechanism of histone lysine methyl transfer revealed by the structure of
RT SET7/9-AdoMet.";
RL EMBO J. 22:292-303(2003).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366, FUNCTION, AND
RP MUTAGENESIS OF HIS-297.
RX PubMed=15525938; DOI=10.1038/nature03117;
RA Chuikov S., Kurash J.K., Wilson J.R., Xiao B., Justin N., Ivanov G.S.,
RA McKinney K., Tempst P., Prives C., Gamblin S.J., Barlev N.A., Reinberg D.;
RT "Regulation of p53 activity through lysine methylation.";
RL Nature 432:353-360(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 110-366, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LYS-317.
RX PubMed=16415881; DOI=10.1038/nsmb1045;
RA Couture J.-F., Collazo E., Hauk G., Trievel R.C.;
RT "Structural basis for the methylation site specificity of SET7/9.";
RL Nat. Struct. Mol. Biol. 13:140-146(2006).
CC -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag
CC for epigenetic transcriptional activation. Plays a central role in the
CC transcriptional activation of genes such as collagenase or insulin.
CC Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate
CC transcription. Has also methyltransferase activity toward non-histone
CC proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and
CC binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-
CC 189' of TAF10, leading to increase the affinity of TAF10 for RNA
CC polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing
CC p53/TP53 and increasing p53/TP53-mediated transcriptional activation.
CC {ECO:0000269|PubMed:12540855, ECO:0000269|PubMed:12588998,
CC ECO:0000269|PubMed:15099517, ECO:0000269|PubMed:15525938,
CC ECO:0000269|PubMed:16141209, ECO:0000269|PubMed:17108971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00910,
CC ECO:0000269|PubMed:12540855};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for histone H3 {ECO:0000269|PubMed:16415881};
CC KM=12 uM for TAF10 {ECO:0000269|PubMed:16415881};
CC KM=69 uM for p53/TP53 {ECO:0000269|PubMed:16415881};
CC -!- SUBUNIT: Interacts with IPF1/PDX-1. {ECO:0000269|PubMed:12514135,
CC ECO:0000269|PubMed:12540855, ECO:0000269|PubMed:16141209}.
CC -!- INTERACTION:
CC Q8WTS6; P26358: DNMT1; NbExp=9; IntAct=EBI-1268586, EBI-719459;
CC Q8WTS6; P68431: H3C12; NbExp=3; IntAct=EBI-1268586, EBI-79722;
CC Q8WTS6; Q96RI1: NR1H4; NbExp=5; IntAct=EBI-1268586, EBI-1250177;
CC Q8WTS6; P06400: RB1; NbExp=4; IntAct=EBI-1268586, EBI-491274;
CC Q8WTS6; Q04206: RELA; NbExp=12; IntAct=EBI-1268586, EBI-73886;
CC Q8WTS6; Q9UHV2: SERTAD1; NbExp=2; IntAct=EBI-1268586, EBI-748601;
CC Q8WTS6; Q96EB6: SIRT1; NbExp=11; IntAct=EBI-1268586, EBI-1802965;
CC Q8WTS6; Q12962: TAF10; NbExp=4; IntAct=EBI-1268586, EBI-708376;
CC Q8WTS6; P04637: TP53; NbExp=11; IntAct=EBI-1268586, EBI-366083;
CC Q8WTS6; Q9WVH4: Foxo3; Xeno; NbExp=5; IntAct=EBI-1268586, EBI-6127038;
CC Q8WTS6; P68433: H3c8; Xeno; NbExp=2; IntAct=EBI-1268586, EBI-79743;
CC Q8WTS6; Q04207: Rela; Xeno; NbExp=2; IntAct=EBI-1268586, EBI-644400;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreatic islets.
CC -!- DOMAIN: The SET domain is necessary but not sufficient for histone
CC methyltransferase activity.
CC -!- MISCELLANEOUS: Monomethyltransferase activity is achieved by disrupting
CC the formation at near-attack conformations for the dimethylation
CC reaction.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET7 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00910}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF448510; AAL56579.1; -; mRNA.
DR EMBL; AF462150; AAL69901.1; -; mRNA.
DR EMBL; AB051504; BAB21808.1; ALT_INIT; mRNA.
DR EMBL; AC112236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114743; AAY40937.1; -; Genomic_DNA.
DR EMBL; BC121055; AAI21056.1; -; mRNA.
DR EMBL; BC121056; AAI21057.1; -; mRNA.
DR CCDS; CCDS3748.1; -.
DR RefSeq; NP_001293128.1; NM_001306199.1.
DR RefSeq; NP_085151.1; NM_030648.3.
DR PDB; 1H3I; X-ray; 2.10 A; A/B=52-344.
DR PDB; 1MT6; X-ray; 2.20 A; A=58-337.
DR PDB; 1MUF; X-ray; 2.26 A; A=81-337.
DR PDB; 1N6A; X-ray; 1.70 A; A=108-366.
DR PDB; 1N6C; X-ray; 2.30 A; A=70-366.
DR PDB; 1O9S; X-ray; 1.75 A; A/B=108-366.
DR PDB; 1XQH; X-ray; 1.75 A; A/E=108-366.
DR PDB; 2F69; X-ray; 1.30 A; A=110-366.
DR PDB; 3CBM; X-ray; 1.69 A; A=111-366.
DR PDB; 3CBO; X-ray; 1.65 A; A=111-366.
DR PDB; 3CBP; X-ray; 1.42 A; A=111-366.
DR PDB; 3M53; X-ray; 1.85 A; A=110-366.
DR PDB; 3M54; X-ray; 1.60 A; A=110-366.
DR PDB; 3M55; X-ray; 1.55 A; A=110-366.
DR PDB; 3M56; X-ray; 1.65 A; A=110-366.
DR PDB; 3M57; X-ray; 1.70 A; A=110-366.
DR PDB; 3M58; X-ray; 1.40 A; A=110-366.
DR PDB; 3M59; X-ray; 1.70 A; A=110-366.
DR PDB; 3M5A; X-ray; 1.75 A; A=110-366.
DR PDB; 3OS5; X-ray; 1.69 A; A=111-366.
DR PDB; 3VUZ; X-ray; 2.50 A; A=111-366.
DR PDB; 3VV0; X-ray; 2.00 A; A=111-366.
DR PDB; 4E47; X-ray; 2.00 A; A/B/C/D=109-366.
DR PDB; 4J7F; X-ray; 1.59 A; A=110-366.
DR PDB; 4J7I; X-ray; 2.56 A; A=110-366.
DR PDB; 4J83; X-ray; 1.70 A; A=110-366.
DR PDB; 4J8O; X-ray; 1.63 A; A=110-366.
DR PDB; 4JDS; X-ray; 1.70 A; A/B/C/D=109-366.
DR PDB; 4JLG; X-ray; 1.90 A; A/B=109-366.
DR PDB; 5AYF; X-ray; 2.00 A; A=111-366.
DR PDB; 5EG2; X-ray; 1.55 A; A=110-366.
DR PDB; 5YLT; X-ray; 1.69 A; A=111-366.
DR PDBsum; 1H3I; -.
DR PDBsum; 1MT6; -.
DR PDBsum; 1MUF; -.
DR PDBsum; 1N6A; -.
DR PDBsum; 1N6C; -.
DR PDBsum; 1O9S; -.
DR PDBsum; 1XQH; -.
DR PDBsum; 2F69; -.
DR PDBsum; 3CBM; -.
DR PDBsum; 3CBO; -.
DR PDBsum; 3CBP; -.
DR PDBsum; 3M53; -.
DR PDBsum; 3M54; -.
DR PDBsum; 3M55; -.
DR PDBsum; 3M56; -.
DR PDBsum; 3M57; -.
DR PDBsum; 3M58; -.
DR PDBsum; 3M59; -.
DR PDBsum; 3M5A; -.
DR PDBsum; 3OS5; -.
DR PDBsum; 3VUZ; -.
DR PDBsum; 3VV0; -.
DR PDBsum; 4E47; -.
DR PDBsum; 4J7F; -.
DR PDBsum; 4J7I; -.
DR PDBsum; 4J83; -.
DR PDBsum; 4J8O; -.
DR PDBsum; 4JDS; -.
DR PDBsum; 4JLG; -.
DR PDBsum; 5AYF; -.
DR PDBsum; 5EG2; -.
DR PDBsum; 5YLT; -.
DR AlphaFoldDB; Q8WTS6; -.
DR BMRB; Q8WTS6; -.
DR SMR; Q8WTS6; -.
DR BioGRID; 123332; 70.
DR CORUM; Q8WTS6; -.
DR DIP; DIP-29045N; -.
DR IntAct; Q8WTS6; 39.
DR MINT; Q8WTS6; -.
DR STRING; 9606.ENSP00000274031; -.
DR BindingDB; Q8WTS6; -.
DR ChEMBL; CHEMBL5523; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR DrugCentral; Q8WTS6; -.
DR GuidetoPHARMACOLOGY; 2703; -.
DR GlyGen; Q8WTS6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WTS6; -.
DR PhosphoSitePlus; Q8WTS6; -.
DR BioMuta; SETD7; -.
DR DMDM; 25091217; -.
DR EPD; Q8WTS6; -.
DR jPOST; Q8WTS6; -.
DR MassIVE; Q8WTS6; -.
DR MaxQB; Q8WTS6; -.
DR PaxDb; Q8WTS6; -.
DR PeptideAtlas; Q8WTS6; -.
DR PRIDE; Q8WTS6; -.
DR ProteomicsDB; 74595; -.
DR ABCD; Q8WTS6; 7 sequenced antibodies.
DR Antibodypedia; 16193; 542 antibodies from 40 providers.
DR DNASU; 80854; -.
DR Ensembl; ENST00000274031.8; ENSP00000274031.3; ENSG00000145391.14.
DR GeneID; 80854; -.
DR KEGG; hsa:80854; -.
DR MANE-Select; ENST00000274031.8; ENSP00000274031.3; NM_030648.4; NP_085151.1.
DR UCSC; uc003ihw.4; human.
DR CTD; 80854; -.
DR DisGeNET; 80854; -.
DR GeneCards; SETD7; -.
DR HGNC; HGNC:30412; SETD7.
DR HPA; ENSG00000145391; Low tissue specificity.
DR MIM; 606594; gene.
DR neXtProt; NX_Q8WTS6; -.
DR OpenTargets; ENSG00000145391; -.
DR PharmGKB; PA143485615; -.
DR VEuPathDB; HostDB:ENSG00000145391; -.
DR eggNOG; KOG1079; Eukaryota.
DR GeneTree; ENSGT00390000004827; -.
DR HOGENOM; CLU_803117_0_0_1; -.
DR InParanoid; Q8WTS6; -.
DR OMA; NGIRITH; -.
DR OrthoDB; 675418at2759; -.
DR PhylomeDB; Q8WTS6; -.
DR TreeFam; TF106392; -.
DR BioCyc; MetaCyc:HS07252-MON; -.
DR BRENDA; 2.1.1.364; 2681.
DR PathwayCommons; Q8WTS6; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SABIO-RK; Q8WTS6; -.
DR SignaLink; Q8WTS6; -.
DR BioGRID-ORCS; 80854; 19 hits in 1097 CRISPR screens.
DR ChiTaRS; SETD7; human.
DR EvolutionaryTrace; Q8WTS6; -.
DR GeneWiki; SETD7; -.
DR GenomeRNAi; 80854; -.
DR Pharos; Q8WTS6; Tchem.
DR PRO; PR:Q8WTS6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8WTS6; protein.
DR Bgee; ENSG00000145391; Expressed in tibialis anterior and 193 other tissues.
DR ExpressionAtlas; Q8WTS6; baseline and differential.
DR Genevisible; Q8WTS6; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; IDA:MGI.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd10530; SET_SETD7; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR IDEAL; IID00128; -.
DR InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044436; SETD7_SET.
DR Pfam; PF02493; MORN; 4.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51577; SAM_MT43_SET7; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromatin regulator; Chromosome;
KW Direct protein sequencing; Methyltransferase; Nucleus; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..366
FT /note="Histone-lysine N-methyltransferase SETD7"
FT /id="PRO_0000186054"
FT REPEAT 36..58
FT /note="MORN 1"
FT REPEAT 59..81
FT /note="MORN 2"
FT REPEAT 106..128
FT /note="MORN 3"
FT DOMAIN 214..336
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 226..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 245
FT /ligand="substrate"
FT BINDING 256..258
FT /ligand="substrate"
FT BINDING 266..268
FT /ligand="substrate"
FT BINDING 296..297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 317
FT /ligand="substrate"
FT BINDING 335
FT /ligand="substrate"
FT BINDING 356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855"
FT MUTAGEN 220
FT /note="E->A: Increases near-attack conformations."
FT /evidence="ECO:0000269|PubMed:16433545"
FT MUTAGEN 228
FT /note="E->A: Increases near-attack conformations."
FT /evidence="ECO:0000269|PubMed:16433545"
FT MUTAGEN 245
FT /note="Y->A: Significantly reduces the
FT monomethyltransferase activity but increases the
FT dimethyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12540855,
FT ECO:0000269|PubMed:16433545"
FT MUTAGEN 294
FT /note="K->A: Significantly reduces the catalytic activity."
FT /evidence="ECO:0000269|PubMed:16433545"
FT MUTAGEN 297
FT /note="H->A,G: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11779497,
FT ECO:0000269|PubMed:11850410, ECO:0000269|PubMed:15099517,
FT ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16141209"
FT MUTAGEN 317
FT /note="K->A: Induces a reduction in methyltransferase
FT activity toward TAF10 but an increased methyltransferase
FT activity for H3 and p53/TP53."
FT /evidence="ECO:0000269|PubMed:16415881"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1H3I"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3M58"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4J83"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 163..176
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1MT6"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:3M57"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:2F69"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1MUF"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2F69"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:2F69"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2F69"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:2F69"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2F69"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:1H3I"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:2F69"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:2F69"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5YLT"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3OS5"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:2F69"
SQ 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
