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UBE2D1 UBE2D1 SKP2 SKP2 FBXO6 FBXO6 UBE2L6 UBE2L6 RNF213 RNF213 ITCH ITCH DTX3L DTX3L UBA7 UBA7 HERC6 HERC6 PARP14 PARP14 PARP9 PARP9
"DTX3L" - E3 ubiquitin-protein ligase DTX3L in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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DTX3LE3 ubiquitin-protein ligase DTX3L; E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses. Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4. In response to DNA damage, mediates monoubiquitination of ’Lys-91’ of histone H4 (H4K91ub1). 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). PARP1-depen [...] (740 aa)    
Predicted Functional Partners:
PARP9
Poly [ADP-ribose] polymerase 9; ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses. Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP- ribose). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP- ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones. During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damag [...] (854 aa)
     
 
  0.996
PARP14
Poly [ADP-ribose] polymerase 14; ADP-ribosyltransferase. By mono-ADP-ribosylating STAT1 at ’Glu-657’ and ’Glu-705’ and thus decreasing STAT1 phosphorylation, negatively regulates pro-inflammatory cytokines production in macrophages in response to IFNG stimulation. Mono-ADP- ribosylates STAT6 (By similarity). Enhances STAT6-dependent transcription (By similarity). In macrophages, positively regulates MRC1 expression in response to IL4 stimulation by promoting STAT6 phosphorylation. Mono-ADP- ribosylates PARP9; Poly(ADP-ribose) polymerases (1801 aa)
     
 
  0.981
UBA7
Ubiquitin-like modifier-activating enzyme 7; Activates ubiquitin by first adenylating with ATP its C- terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin- E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein; Ubiquitin like modifier activating enzymes (1012 aa)
     
 
  0.973
RNF213
E3 ubiquitin-protein ligase RNF213; E3 ubiquitin-protein ligase involved in angiogenesis. Involved in the non-canonical Wnt signaling pathway in vascular development- acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; Ring finger proteins (5207 aa)
     
 
    0.963
ITCH
E3 ubiquitin-protein ligase Itchy homolog; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Catalyzes ’Lys-29’-, ’Lys-48’- and ’Lys-63’-linked ubiquitin conjugation. Involved in the control of inflammatory signaling pathways. Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after [...] (903 aa)
     
  0.962
UBE2D1
Ubiquitin-conjugating enzyme E2 D1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-48’-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubi [...] (147 aa)
       
  0.955
SKP2
S-phase kinase-associated protein 2; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of T [...] (424 aa)
         
  0.945
FBXO6
F-box only protein 6; Substrate-recognition component of some SCF (SKP1-CUL1- F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex- type oligosaccharides. Also recognizes sulfated glycans. Also involved [...] (293 aa)
         
  0.941
UBE2L6
Ubiquitin/ISG15-conjugating enzyme E2 L6; Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3; Ubiquitin conjugating enzymes E2 (153 aa)
     
 
  0.939
HERC6
Probable E3 ubiquitin-protein ligase HERC6; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (1022 aa)
     
 
  0.937
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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