M-phase phosphoprotein 8 (Two hybrid-associated protein 3 with RanBPM) (Twa3)
1_MEQVA 6_ EGARV 11_ TAVPV 16_ SAADS 21_ TEELA 26_ EVEEG 31_ VGVVG 36_ EDNDA 41_ AARGA 46_ EAFGD 51_ SEEDG 56_ EDVFE 61_ VEKIL 66_ DMKTE 71_ GGKVL 76_ YKVRW 81_ KGYTS 86_ DDDTW 91_ EPEIH 96_ LEDCK 101_ EVLLE 106_ FRKKI 111_ AENKA 116_ KAVRK 121_ DIQRL 126_ SLNND 131_ IFEAN 136_ SDSDQ 141_ QSETK 146_ EDTSP 151_ KKKKK 156_ KLRQR 161_ EEKSP 166_ DDLKK 171_ KKAKA 176_ GKLKD 181_ KSKPD 186_ LESSL 191_ ESLVF 196_ DLRTK 201_ KRISE 206_ AKEEL 211_ KESKK 216_ PKKDE 221_ VKETK 226_ ELKKV 231_ KKGEI 236_ RDLKT 241_ KTRED 246_ PKENR 251_ KTKKE 256_ KFVES 261_ QVESE 266_ SSVLN 271_ DSPFP 276_ EDDSE 281_ GLHSD 286_ SREEK 291_ QNTKS 296_ ARERA 301_ GQDMG 306_ LEHGF 311_ EKPLD 316_ SAMSA 321_ EEDTD 326_ VRGRR 331_ KKKTP 336_ RKAED 341_ TRENR 346_ KLENK 351_ NAFLE 356_ KKTVP 361_ KKQRN 366_ QDRSK 371_ SAAEL 376_ EKLMP 381_ VSAQT 386_ PKGRR 391_ LSGEE 396_ RGLWS 401_ TDSAE 406_ EDKET 411_ KRNES 416_ KEKYQ 421_ KRHDS 426_ DKEEK 431_ GRKEP 436_ KGLKT 441_ LKEIR 446_ NAFDL 451_ FKLTP 456_ EEKND 461_ VSENN 466_ RKREE 471_ IPLDF 476_ KTIDD 481_ HKTKE 486_ NKQSL 491_ KERRN 496_ TRDET 501_ DTWAY 506_ IAAEG 511_ DQEVL 516_ DSVCQ 521_ ADENS 526_ DGRQQ 531_ ILSLG 536_ MDLQL 541_ EWMKL 546_ EDFQK 551_ HLDGK 556_ DENFA 561_ ATDAI 566_ PSNVL 571_ RDAVK 576_ NGDYI 581_ TVKVA 586_ LNSNE 591_ EYNLD 596_ QEDSS 601_ GMTLV 606_ MLAAA 611_ GGQDD 616_ LLRLL 621_ ITKGA 626_ KVNGR 631_ QKNGT 636_ TALIH 641_ AAEKN 646_ FLTTV 651_ AILLE 656_ AGAFV 661_ NVQQS 666_ NGETA 671_ LMKAC 676_ KRGNS 681_ DIVRL 686_ VIECG 691_ ADCNI 696_ LSKHQ 701_ NSALH 706_ FAKQS 711_ NNVLV 716_ YDLLK 721_ NHLET 726_ LSRVA 731_ EETIK 736_ DYFEA 741_ RLALL 746_ EPVFP 751_ IACHR 756_ LCEGP 761_ DFSTD 766_ FNYKP 771_ PQNIP 776_ EGSGI 781_ LLFIF 786_ HANFL 791_ GKEVI 796_ ARLCG 801_ PCSVQ 806_ AVVLN 811_ DKFQL 816_ PVFLD 821_ SHFVY 826_ SFSPV 831_ AGPNK 836_ LFIRL 841_ TEAPS 846_ AKVKL 851_LIGAY
1: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression (PubMed:20871592, PubMed:26022416). Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene (PubMed:20871592). Mediates down-regulation of CDH1 expression (PubMed:20871592). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602)