ID SET7_HUMAN STANDARD; PRT; 366 AA. AC Q8WTS6; Q9C0E6; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Histone-lysine N-methyltransferase, H3 lysine-4 specific (EC 2.1.1.43) DE (Histone H3-K4 methyltransferase) (H3-K4-HMTase) (SET domain- DE containing protein 7) (Set9) (SET7/9). GN SET7 OR KIAA1717. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., SEQUENCE OF 35-44; 108-115; 144-152; 234-258 AND RP 345-358, AND MUTAGENESIS OF HIS-297. RC TISSUE=Brain; RX MEDLINE=21638669; PubMed=11779497; 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 SEQUENCE FROM N.A., SEQUENCE OF 36-45; 104-115; 144-152; 159-169; RP 201-250 AND 324-358, AND MUTAGENESIS OF HIS-297. RC TISSUE=Cervical carcinoma; RX MEDLINE=21838688; PubMed=11850410; 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 SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=21082932; PubMed=11214970; 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; 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; 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; 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; 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 N(6)-methyl-L-lysine. CC -!- SUBCELLULAR LOCATION: Nuclear (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; -. DR EMBL; AF462150; AAL69901.1; -. DR EMBL; AB051504; BAB21808.1; ALT_INIT. DR PDB; 1H3I; 11-NOV-02. DR PDB; 1MT6; 06-NOV-02. DR PDB; 1MUF; 06-NOV-02. DR PDB; 1N6A; 04-FEB-03. DR PDB; 1N6C; 04-FEB-03. DR PDB; 1O9S; 06-FEB-03. DR MIM; 606594; -. 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 Transferase; Methyltransferase; Chromatin regulator; Nuclear protein; KW Repeat; 3D-structure. FT DOMAIN 51 54 Poly-Phe. FT REPEAT 36 58 MORN 1. FT REPEAT 59 81 MORN 2. FT REPEAT 106 128 MORN 3. FT DOMAIN 215 340 SET. FT MUTAGEN 297 297 H->A,G: Abolishes methyltransferase FT activity. FT STRAND 118 122 FT TURN 124 125 FT STRAND 128 132 FT TURN 135 136 FT STRAND 141 147 FT TURN 149 150 FT STRAND 153 160 FT TURN 161 162 FT STRAND 163 176 FT TURN 177 178 FT STRAND 179 184 FT STRAND 190 191 FT TURN 205 206 FT HELIX 210 213 FT TURN 214 215 FT STRAND 216 220 FT TURN 224 225 FT STRAND 228 232 FT STRAND 236 236 FT TURN 238 239 FT STRAND 241 245 FT STRAND 248 250 FT HELIX 252 257 FT HELIX 260 262 FT TURN 264 265 FT STRAND 267 268 FT STRAND 274 276 FT HELIX 279 282 FT TURN 284 286 FT HELIX 292 294 FT STRAND 296 297 FT STRAND 303 310 FT TURN 311 313 FT STRAND 314 321 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 //