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 26-FEB-2020, entry version 174. DE RecName: Full=Histone-lysine N-methyltransferase SETD7; DE EC=2.1.1.- {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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00910}; 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 P26358:DNMT1; NbExp=9; IntAct=EBI-1268586, EBI-719459; CC Q9WVH4:Foxo3 (xeno); NbExp=5; IntAct=EBI-1268586, EBI-6127038; CC P68431:HIST1H3F; NbExp=3; IntAct=EBI-1268586, EBI-79722; CC P68433:Hist1h3i (xeno); NbExp=2; IntAct=EBI-1268586, EBI-79743; CC Q96RI1:NR1H4; NbExp=5; IntAct=EBI-1268586, EBI-1250177; CC P06400:RB1; NbExp=4; IntAct=EBI-1268586, EBI-491274; CC Q04206:RELA; NbExp=12; IntAct=EBI-1268586, EBI-73886; CC Q04207:Rela (xeno); NbExp=2; IntAct=EBI-1268586, EBI-644400; CC Q9UHV2:SERTAD1; NbExp=2; IntAct=EBI-1268586, EBI-748601; CC Q96EB6:SIRT1; NbExp=11; IntAct=EBI-1268586, EBI-1802965; CC Q12962:TAF10; NbExp=4; IntAct=EBI-1268586, EBI-708376; CC P04637:TP53; NbExp=11; IntAct=EBI-1268586, EBI-366083; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q8WTS6; -. DR BioGrid; 123332; 47. DR CORUM; Q8WTS6; -. DR DIP; DIP-29045N; -. DR IntAct; Q8WTS6; 24. 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 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; -. DR Ensembl; ENST00000274031; ENSP00000274031; ENSG00000145391. DR GeneID; 80854; -. DR KEGG; hsa:80854; -. DR UCSC; uc003ihw.4; human. DR CTD; 80854; -. DR DisGeNET; 80854; -. DR GeneCards; SETD7; -. DR HGNC; HGNC:30412; SETD7. DR HPA; HPA058111; -. DR MIM; 606594; gene. DR neXtProt; NX_Q8WTS6; -. DR OpenTargets; ENSG00000145391; -. DR PharmGKB; PA143485615; -. DR eggNOG; KOG1079; Eukaryota. DR eggNOG; COG2940; LUCA. DR GeneTree; ENSGT00390000004827; -. DR HOGENOM; CLU_803117_0_0_1; -. DR InParanoid; Q8WTS6; -. DR KO; K11431; -. DR OMA; SFTPNCV; -. DR OrthoDB; 814925at2759; -. DR PhylomeDB; Q8WTS6; -. DR TreeFam; TF106392; -. DR BRENDA; 2.1.1.43; 2681. DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR SABIO-RK; Q8WTS6; -. 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 quadriceps femoris and 208 other tissues. DR ExpressionAtlas; Q8WTS6; baseline and differential. DR Genevisible; Q8WTS6; HS. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. 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:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB. DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET. DR InterPro; IPR003409; MORN. DR InterPro; IPR001214; SET_dom. DR Pfam; PF02493; MORN; 4. DR Pfam; PF00856; SET; 1. DR PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1. DR SMART; SM00317; SET; 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 REGION 226..228 FT /note="S-adenosyl-L-methionine binding" FT REGION 256..258 FT /note="Substrate binding" FT REGION 266..268 FT /note="Substrate binding" FT REGION 296..297 FT /note="S-adenosyl-L-methionine binding" FT COMPBIAS 51..54 FT /note="Poly-Phe" FT BINDING 245 FT /note="Substrate" FT BINDING 317 FT /note="Substrate" FT BINDING 335 FT /note="Substrate; via carbonyl oxygen" FT BINDING 356 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" 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:0000244|PDB:1H3I" FT STRAND 61..64 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 67..75 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 81..87 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 90..98 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 100..102 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 104..111 FT /evidence="ECO:0000244|PDB:1H3I" FT HELIX 114..116 FT /evidence="ECO:0000244|PDB:3M58" FT STRAND 119..122 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 128..131 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 135..137 FT /evidence="ECO:0000244|PDB:4J83" FT STRAND 141..147 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 151..160 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 163..176 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 179..184 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 186..188 FT /evidence="ECO:0000244|PDB:1MT6" FT TURN 203..206 FT /evidence="ECO:0000244|PDB:3M57" FT HELIX 210..213 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 216..220 FT /evidence="ECO:0000244|PDB:2F69" FT TURN 224..226 FT /evidence="ECO:0000244|PDB:1MUF" FT STRAND 228..234 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 241..245 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 248..250 FT /evidence="ECO:0000244|PDB:2F69" FT HELIX 252..256 FT /evidence="ECO:0000244|PDB:2F69" FT HELIX 260..262 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 266..268 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 270..272 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 274..276 FT /evidence="ECO:0000244|PDB:2F69" FT TURN 279..282 FT /evidence="ECO:0000244|PDB:2F69" FT TURN 284..286 FT /evidence="ECO:0000244|PDB:2F69" FT HELIX 292..294 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 295..300 FT /evidence="ECO:0000244|PDB:1H3I" FT STRAND 302..310 FT /evidence="ECO:0000244|PDB:2F69" FT TURN 311..313 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 314..323 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 330..333 FT /evidence="ECO:0000244|PDB:2F69" FT STRAND 338..340 FT /evidence="ECO:0000244|PDB:5YLT" FT STRAND 344..346 FT /evidence="ECO:0000244|PDB:3OS5" FT HELIX 351..363 FT /evidence="ECO:0000244|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 //