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Database: UniProt
Entry: Q8WTS6
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Original site: Q8WTS6 
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   13-FEB-2019, entry version 167.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-44; 108-115;
RP   144-152; 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
RT   4-specific methyltransferase.";
RL   Mol. Cell 8:1207-1217(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-45; 104-115;
RP   144-152; 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
RT   transcription by precluding histone tail modifications required for
RT   heterochromatin 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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
RT   project: 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
RT   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
RT   elongation 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
RT   initial 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.,
RA   Buerckstuemmer T., 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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
RT   methyltransferase 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, AND MUTAGENESIS
RP   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
RT   methyltransferase 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.,
RA   Lee J., Cho Y.;
RT   "Mechanism of histone lysine methyl transfer revealed by the structure
RT   of 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.,
RA   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
CC       monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation. Plays a central role in the transcriptional activation
CC       of genes such as collagenase or insulin. Recruited by IPF1/PDX-1
CC       to the insulin promoter, leading to activate transcription. Has
CC       also methyltransferase activity toward non-histone proteins such
CC       as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding
CC       the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189'
CC       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
CC       activation. {ECO:0000269|PubMed:12540855,
CC       ECO:0000269|PubMed:12588998, ECO:0000269|PubMed:15099517,
CC       ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16141209,
CC       ECO:0000269|PubMed:17108971}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-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:HIST1H3D; 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
CC       islets.
CC   -!- DOMAIN: The SET domain is necessary but not sufficient for histone
CC       methyltransferase activity.
CC   -!- MISCELLANEOUS: Monomethyltransferase activity is achieved by
CC       disrupting the formation at near-attack conformations for the
CC       dimethylation reaction.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00910}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB21808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Hs.480792; -.
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   ProteinModelPortal; Q8WTS6; -.
DR   SMR; Q8WTS6; -.
DR   BioGrid; 123332; 45.
DR   CORUM; Q8WTS6; -.
DR   DIP; DIP-29045N; -.
DR   IntAct; Q8WTS6; 21.
DR   MINT; Q8WTS6; -.
DR   STRING; 9606.ENSP00000274031; -.
DR   BindingDB; Q8WTS6; -.
DR   ChEMBL; CHEMBL5523; -.
DR   DrugBank; DB01752; S-Adenosyl-L-Homocysteine.
DR   GuidetoPHARMACOLOGY; 2703; -.
DR   iPTMnet; Q8WTS6; -.
DR   PhosphoSitePlus; Q8WTS6; -.
DR   BioMuta; SETD7; -.
DR   DMDM; 25091217; -.
DR   EPD; Q8WTS6; -.
DR   jPOST; Q8WTS6; -.
DR   MaxQB; Q8WTS6; -.
DR   PaxDb; Q8WTS6; -.
DR   PeptideAtlas; Q8WTS6; -.
DR   PRIDE; Q8WTS6; -.
DR   ProteomicsDB; 74595; -.
DR   Ensembl; ENST00000274031; ENSP00000274031; ENSG00000145391.
DR   GeneID; 80854; -.
DR   KEGG; hsa:80854; -.
DR   UCSC; uc003ihw.4; human.
DR   CTD; 80854; -.
DR   DisGeNET; 80854; -.
DR   EuPathDB; HostDB:ENSG00000145391.13; -.
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; HOG000074731; -.
DR   HOVERGEN; HBG028309; -.
DR   InParanoid; Q8WTS6; -.
DR   KO; K11431; -.
DR   OMA; SSVYHFD; -.
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   PRO; PR:Q8WTS6; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000145391; Expressed in 209 organ(s), highest expression level in quadriceps femoris.
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   Complete proteome; Direct protein sequencing; Methyltransferase;
KW   Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    366       Histone-lysine N-methyltransferase SETD7.
FT                                /FTId=PRO_0000186054.
FT   REPEAT       36     58       MORN 1.
FT   REPEAT       59     81       MORN 2.
FT   REPEAT      106    128       MORN 3.
FT   DOMAIN      214    336       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      226    228       S-adenosyl-L-methionine binding.
FT   REGION      256    258       Substrate binding.
FT   REGION      266    268       Substrate binding.
FT   REGION      296    297       S-adenosyl-L-methionine binding.
FT   COMPBIAS     51     54       Poly-Phe.
FT   BINDING     245    245       Substrate.
FT   BINDING     317    317       Substrate.
FT   BINDING     335    335       Substrate; via carbonyl oxygen.
FT   BINDING     356    356       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190,
FT                                ECO:0000269|PubMed:12514135,
FT                                ECO:0000269|PubMed:12540855}.
FT   MUTAGEN     220    220       E->A: Increases near-attack
FT                                conformations.
FT                                {ECO:0000269|PubMed:16433545}.
FT   MUTAGEN     228    228       E->A: Increases near-attack
FT                                conformations.
FT                                {ECO:0000269|PubMed:16433545}.
FT   MUTAGEN     245    245       Y->A: Significantly reduces the
FT                                monomethyltransferase activity but
FT                                increases the dimethyltransferase
FT                                activity. {ECO:0000269|PubMed:12540855,
FT                                ECO:0000269|PubMed:16433545}.
FT   MUTAGEN     294    294       K->A: Significantly reduces the catalytic
FT                                activity. {ECO:0000269|PubMed:16433545}.
FT   MUTAGEN     297    297       H->A,G: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11779497,
FT                                ECO:0000269|PubMed:11850410,
FT                                ECO:0000269|PubMed:15099517,
FT                                ECO:0000269|PubMed:15525938,
FT                                ECO:0000269|PubMed:16141209}.
FT   MUTAGEN     317    317       K->A: Induces a reduction in
FT                                methyltransferase activity toward TAF10
FT                                but an increased methyltransferase
FT                                activity for H3 and p53/TP53.
FT                                {ECO:0000269|PubMed:16415881}.
FT   STRAND       54     56       {ECO:0000244|PDB:1H3I}.
FT   STRAND       61     64       {ECO:0000244|PDB:1H3I}.
FT   STRAND       67     75       {ECO:0000244|PDB:1H3I}.
FT   STRAND       81     87       {ECO:0000244|PDB:1H3I}.
FT   STRAND       90     98       {ECO:0000244|PDB:1H3I}.
FT   STRAND      100    102       {ECO:0000244|PDB:1H3I}.
FT   STRAND      104    111       {ECO:0000244|PDB:1H3I}.
FT   HELIX       114    116       {ECO:0000244|PDB:3M58}.
FT   STRAND      119    122       {ECO:0000244|PDB:2F69}.
FT   STRAND      128    131       {ECO:0000244|PDB:2F69}.
FT   STRAND      135    137       {ECO:0000244|PDB:4J83}.
FT   STRAND      141    147       {ECO:0000244|PDB:2F69}.
FT   STRAND      151    160       {ECO:0000244|PDB:2F69}.
FT   STRAND      163    176       {ECO:0000244|PDB:2F69}.
FT   STRAND      179    184       {ECO:0000244|PDB:2F69}.
FT   STRAND      186    188       {ECO:0000244|PDB:1MT6}.
FT   TURN        203    206       {ECO:0000244|PDB:3M57}.
FT   HELIX       210    213       {ECO:0000244|PDB:2F69}.
FT   STRAND      216    220       {ECO:0000244|PDB:2F69}.
FT   TURN        224    226       {ECO:0000244|PDB:1MUF}.
FT   STRAND      228    234       {ECO:0000244|PDB:2F69}.
FT   STRAND      241    245       {ECO:0000244|PDB:2F69}.
FT   STRAND      248    250       {ECO:0000244|PDB:2F69}.
FT   HELIX       252    256       {ECO:0000244|PDB:2F69}.
FT   HELIX       260    262       {ECO:0000244|PDB:2F69}.
FT   STRAND      266    268       {ECO:0000244|PDB:1H3I}.
FT   STRAND      270    272       {ECO:0000244|PDB:2F69}.
FT   STRAND      274    276       {ECO:0000244|PDB:2F69}.
FT   TURN        279    282       {ECO:0000244|PDB:2F69}.
FT   TURN        284    286       {ECO:0000244|PDB:2F69}.
FT   HELIX       292    294       {ECO:0000244|PDB:2F69}.
FT   STRAND      295    300       {ECO:0000244|PDB:1H3I}.
FT   STRAND      302    310       {ECO:0000244|PDB:2F69}.
FT   TURN        311    313       {ECO:0000244|PDB:2F69}.
FT   STRAND      314    323       {ECO:0000244|PDB:2F69}.
FT   STRAND      330    333       {ECO:0000244|PDB:2F69}.
FT   STRAND      338    340       {ECO:0000244|PDB:5YLT}.
FT   STRAND      344    346       {ECO:0000244|PDB:3OS5}.
FT   HELIX       351    363       {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
//
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