ID SETD7_HUMAN Reviewed; 366 AA. AC Q8WTS6; Q0VAH3; Q9C0E6; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 26-JUN-2007, entry version 53. DE Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7 DE (EC 2.1.1.43) (Histone H3-K4 methyltransferase) (H3-K4-HMTase) (SET DE domain-containing protein 7) (Set9) (SET7/9). GN Name=SETD7; Synonyms=KIAA1717, SET7; 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 MEDLINE=21638669; 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 MEDLINE=21838688; 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 MRNA]. RC TISSUE=Brain; RX MEDLINE=21082932; 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 [4] 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 [5] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 52-344. RX MEDLINE=22259601; 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 111:105-105(2002). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=22289682; 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 [7] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366. RX MEDLINE=22459284; 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 [8] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-366. RX MEDLINE=22401621; 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). CC -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone CC H3, a specific tag for epigenetic transcriptional activation. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone L-lysine = CC S-adenosyl-L-homocysteine + histone 6-N-methyl-L-lysine. CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DOMAIN: The SET domain is necessary but not sufficient for histone CC methyltransferase activity. CC -!- SIMILARITY: Belongs to the histone-lysine methyltransferase CC family. CC -!- SIMILARITY: Contains 3 MORN repeats. CC -!- SIMILARITY: Contains 1 SET domain. 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; BC121055; AAI21056.1; -; mRNA. DR EMBL; BC121056; AAI21057.1; -; mRNA. DR UniGene; Hs.480792; -. DR PDB; 1H3I; X-ray; A/B=52-344. DR PDB; 1MT6; X-ray; A=58-337. DR PDB; 1MUF; X-ray; A=81-337. DR PDB; 1N6A; X-ray; A=108-366. DR PDB; 1N6C; X-ray; A=70-366. DR PDB; 1O9S; X-ray; A=108-366, B=-. DR PDB; 1XQH; X-ray; A/E=108-366. DR PDB; 2F69; X-ray; A=110-366. DR DIP; DIP:29045N; -. DR Ensembl; ENSG00000145391; Homo sapiens. DR KEGG; hsa:80854; -. DR HGNC; HGNC:30412; SETD7. DR MIM; 606594; gene. DR LinkHub; Q8WTS6; -. DR ArrayExpress; Q8WTS6; -. DR GermOnline; ENSG00000145391; Homo sapiens. DR RZPD-ProtExp; T3450; -. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; NAS:UniProtKB. DR GO; GO:0016568; P:chromatin modification; NAS:UniProtKB. DR InterPro; IPR003409; MORN. DR InterPro; IPR001214; SET. DR Pfam; PF02493; MORN; 3. DR Pfam; PF00856; SET; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. KW 3D-structure; Chromatin regulator; Direct protein sequencing; KW Methyltransferase; Nucleus; Repeat; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 366 Histone-lysine N-methyltransferase, H3 FT lysine-4 specific SET7. FT /FTId=PRO_0000186054. FT REPEAT 36 58 MORN 1. FT REPEAT 59 81 MORN 2. FT REPEAT 106 128 MORN 3. FT DOMAIN 215 340 SET. FT COMPBIAS 51 54 Poly-Phe. FT MUTAGEN 297 297 H->A,G: Abolishes methyltransferase FT activity. FT STRAND 54 56 FT STRAND 61 64 FT STRAND 67 75 FT STRAND 81 87 FT STRAND 90 98 FT STRAND 100 102 FT STRAND 104 111 FT STRAND 119 122 FT STRAND 128 131 FT STRAND 141 147 FT STRAND 151 160 FT STRAND 163 176 FT STRAND 179 184 FT HELIX 210 213 FT STRAND 216 220 FT STRAND 228 234 FT STRAND 241 245 FT STRAND 248 250 FT HELIX 252 256 FT HELIX 260 262 FT STRAND 270 272 FT STRAND 274 276 FT TURN 279 282 FT TURN 284 286 FT HELIX 292 294 FT STRAND 302 310 FT TURN 311 313 FT STRAND 314 323 FT STRAND 330 333 FT HELIX 351 363 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 //