ID SETD7_HUMAN STANDARD; PRT; 366 AA. AC Q8WTS6; Q9C0E6; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 25-JUL-2006, entry version 42. 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 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 [5] 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 [6] 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 [7] 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 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 Ensembl; ENSG00000145391; Homo sapiens. DR HGNC; HGNC:30412; SETD7. DR MIM; 606594; gene. DR RZPD-ProtExp; T3450; -. DR GO; GO:0005634; C:nucleus; NAS. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; NAS. DR GO; GO:0016568; P:chromatin modification; NAS. 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; Nuclear protein; Repeat; 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 TURN 65 66 FT STRAND 67 75 FT TURN 77 78 FT STRAND 79 79 FT STRAND 81 87 FT TURN 88 89 FT STRAND 90 98 FT STRAND 100 102 FT STRAND 104 111 FT STRAND 118 122 FT TURN 124 125 FT STRAND 126 126 FT STRAND 128 132 FT TURN 135 136 FT STRAND 137 137 FT STRAND 141 147 FT TURN 149 150 FT STRAND 151 160 FT TURN 161 162 FT STRAND 163 176 FT TURN 177 178 FT STRAND 179 184 FT STRAND 186 187 FT STRAND 190 191 FT STRAND 198 199 FT STRAND 203 204 FT TURN 205 206 FT HELIX 210 213 FT TURN 214 215 FT STRAND 216 220 FT STRAND 222 223 FT TURN 224 225 FT STRAND 228 234 FT STRAND 236 236 FT TURN 238 239 FT STRAND 241 245 FT STRAND 248 250 FT HELIX 252 257 FT STRAND 258 258 FT HELIX 260 262 FT TURN 264 265 FT STRAND 267 268 FT STRAND 270 272 FT STRAND 274 276 FT HELIX 279 282 FT STRAND 283 283 FT TURN 284 286 FT STRAND 289 289 FT HELIX 292 294 FT STRAND 296 297 FT STRAND 299 300 FT STRAND 302 310 FT TURN 311 313 FT STRAND 314 323 FT STRAND 325 325 FT TURN 327 328 FT STRAND 330 333 FT HELIX 351 360 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 //