E3 ubiquitin-protein ligase DTX3L (EC 2.3.2.27) (B-lymphoma- and BAL-associated protein) (Protein deltex-3-like) (RING-type E3 ubiquitin transferase DTX3L) (Rhysin-2) (Rhysin2)
1_MASHL 6_ RPPSP 11_ LLVRV 16_ YKSGP 21_ RVRRK 26_ LESYF 31_ QSSKS 36_ SGGGE 41_ CTVST 46_ QEHEA 51_ PGTFR 56_ VEFSE 61_ RAAKE 66_ RVLKK 71_ GEHQI 76_ LVDEK 81_ PVPIF 86_ LVPTE 91_ NSIKK 96_ NTRPQ 101_ ISSLT 106_ QSQAE 111_ TPSGD 116_ MHQHE 121_ GHIPN 126_ AVDSC 131_ LQKIF 136_ LTVTA 141_ DLNCN 146_ LFSKE 151_ QRAYI 156_ TTLCP 161_ SIRKM 166_ EGHDG 171_ IEKVC 176_ GDFQD 181_ IERIH 186_ QFLSE 191_ QFLES 196_ EQKQQ 201_ FSPSM 206_ TERKP 211_ LSQQE 216_ RDSCI 221_ SPSEP 226_ ETKAE 231_ QKSNY 236_ FEVPL 241_ PYFEY 246_ FKYIC 251_ PDKIN 256_ SIEKR 261_ FGVNI 266_ EIQES 271_ SPNMV 276_ CLDFT 281_ SSRSG 286_ DLEAA 291_ RESFA 296_ SEFQK 301_ NTEPL 306_ KQECV 311_ SLADS 316_ KQANK 321_ FKQEL 326_ NHQFT 331_ KLLIK 336_ EKGGE 341_ LTLLG 346_ TQDDI 351_ SAAKQ 356_ KISEA 361_ FVKIP 366_ VKLFA 371_ ANYMM 376_ NVIEV 381_ DSAHY 386_ KLLET 391_ ELLQE 396_ ISEIE 401_ KRYDI 406_ CSKVS 411_ EKGQK 416_ TCILF 421_ ESKDR 426_ QVDLS 431_ VHAYA 436_ SFIDA 441_ FQHAS 446_ CQLMR 451_ EVLLL 456_ KSLGK 461_ ERKHL 466_ HQTKF 471_ ADDFR 476_ KRHPN 481_ VHFVL 486_ NQESM 491_ TLTGL 496_ PNHLA 501_ KAKQY 506_ VLKGG 511_ GMSSL 516_ AGKKL 521_ KEGHE 526_ TPMDI 531_ DSDDS 536_ KAASP 541_ PLKGS 546_ VSSEA 551_ SELDK 556_ KEKGI 561_ CVICM 566_ DTISN 571_ KKVLP 576_ KCKHE 581_ FCAPC 586_ INKAM 591_ SYKPI 596_ CPTCQ 601_ TSYGI 606_ QKGNQ 611_ PEGSM 616_ VFTVS 621_ RDSLP 626_ GYESF 631_ GTIVI 636_ TYSMK 641_ AGIQT 646_ EEHPN 651_ PGKRY 656_ PGIQR 661_ TAYLP 666_ DNKEG 671_ RKVLK 676_ LLYRA 681_ FDQKL 686_ IFTVG 691_ YSRVL 696_ GVSDV 701_ ITWND 706_ IHHKT 711_ SRFGG 716_ PEMYG 721_ YPDPS 726_ YLKRV 731_KEELK
1: E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses (PubMed:12670957, PubMed:19818714, PubMed:23230272, PubMed:26479788). Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4 (PubMed:28525742). In response to DNA damage, mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1) (PubMed:19818714). The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me) (PubMed:19818714). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). By monoubiquitinating histone H2B H2BC9/H2BJ and thereby promoting chromatin remodeling, positively regulates STAT1-dependent interferon-stimulated gene transcription and thus STAT1-mediated control of viral replication (PubMed:26479788). Independently of its catalytic activity, promotes the sorting of chemokine receptor CXCR4 from early endosome to lysosome following CXCL12 stimulation by reducing E3 ligase ITCH activity and thus ITCH-mediated ubiquitination of endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (PubMed:24790097). In addition, required for the recruitment of HGS and STAM to early endosomes (PubMed:24790097). In association with PARP9, plays a role in antiviral responses by mediating 'Lys-48'-linked ubiquitination of encephalomyocarditis virus (EMCV) and human rhinovirus (HRV) C3 proteases and thus promoting their proteasomal-mediated degradation (PubMed:26479788)