N-lysine methyltransferase KMT5A (EC 2.1.1.-) (H4-K20-HMTase KMT5A) (Histone-lysine N-methyltransferase KMT5A) (EC 2.1.1.361) (Lysine N-methyltransferase 5A) (Lysine-specific methylase 5A) (PR/SET domain-containing protein 07) (PR-Set7) (PR/SET07) (SET domain-containing protein 8)
1_MGEGG 6_ AAAAL 11_ VAAAA 16_ AAAAA 21_ AAAVV 26_ AGQRR 31_ RRLGR 36_ RARCH 41_ GPGRA 46_ AGGKM 51_ SKPCA 56_ VEAAA 61_ AAVAA 66_ TAPGP 71_ EMVER 76_ RGPGR 81_ PRTDG 86_ ENVFT 91_ GQSKI 96_ YSYMS 101_ PNKCS 106_ GMRFP 111_ LQEEN 116_ SVTHH 121_ EVKCQ 126_ GKPLA 131_ GIYRK 136_ REEKR 141_ NAGNA 146_ VRSAM 151_ KSEEQ 156_ KIKDA 161_ RKGPL 166_ VPFPN 171_ QKSEA 176_ AEPPK 181_ TPPSS 186_ CDSTN 191_ AAIAK 196_ QALKK 201_ PIKGK 206_ QAPRK 211_ KAQGK 216_ TQQNR 221_ KLTDF 226_ YPVRR 231_ SSRKS 236_ KAELQ 241_ SEERK 246_ RIDEL 251_ IESGK 256_ EEGMK 261_ IDLID 266_ GKGRG 271_ VIATK 276_ QFSRG 281_ DFVVE 286_ YHGDL 291_ IEITD 296_ AKKRE 301_ ALYAQ 306_ DPSTG 311_ CYMYY 316_ FQYLS 321_ KTYCV 326_ DATRE 331_ TNRLG 336_ RLINH 341_ SKCGN 346_ CQTKL 351_ HDIDG 356_ VPHLI 361_ LIASR 366_ DIAAG 371_ EELLY 376_ DYGDR 381_ SKASI 386_EAHPW
1: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins (PubMed:12086618, PubMed:12121615, PubMed:15964846, PubMed:17707234, PubMed:27338793). Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1) (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599, PubMed:27338793). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Involved in chromosome condensation and proper cytokinesis (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Nucleosomes are preferred as substrate compared to free histones (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes (PubMed:17707234). Plays a negative role in TGF-beta response regulation and a positive role in cell migration (PubMed:23478445)