Detail Information for IndEnz0002001717
IED ID IndEnz0002001717
Enzyme Type ID protease001717
Protein Name E3 ubiquitin-protein ligase NRDP1
EC 2.3.2.27
RING finger protein 41
RING-type E3 ubiquitin transferase NRDP1
Gene Name RNF41 FLRF NRDP1 SBBI03
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MGYDVTRFQGDVDEDLICPICSGVLEEPVQAPHCEHAFCNACITQWFSQQQTCPVDRSVVTVAHLRPVPRIMRNMLSKLQIACDNAVFGCSAVVRLDNLMSHLSDCEHNPKRPVTCEQGCGLEMPKDELPNHNCIKHLRSVVQQQQTRIAELEKTSAEHKHQLAEQKRDIQLLKAYMRAIRSVNPNLQNLEETIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIVNELIENAHERSWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGDDMVQEPGLVMIFAHGVEEI
Enzyme Length 317
Uniprot Accession Number Q9H4P4
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
DNA Binding
EC Number 2.3.2.27
Enzyme Function FUNCTION: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus (By similarity). Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PRKN modifier that accelerates its degradation, resulting in a reduction of PRKN activity, influencing the balance of intracellular redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control (PubMed:24949970). {ECO:0000250, ECO:0000250|UniProtKB:Q8BH75, ECO:0000269|PubMed:12411582, ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15632191, ECO:0000269|PubMed:17210635, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:19483718, ECO:0000269|PubMed:24949970}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Protein modification; protein ubiquitination.
nucleotide Binding
Features Alternative sequence (1); Beta strand (6); Chain (1); Erroneous initiation (1); Helix (8); Mutagenesis (3); Turn (3); Zinc finger (2)
Keywords 3D-structure;Alternative splicing;Apoptosis;Autophagy;Metal-binding;Reference proteome;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger
Interact With A0A0C4DG62; Q66PJ3-3; Q9NWX5; Q9NX04; Q9UHY7; Q9NSB8; Q86U28; Q9BRK4; Q6FHY5; Q8N3F0; O15049; P54725; P35249; Itself; Q7LG56; Q9GZT4; Q8N8B7-2; Q99614; P61086; Q8N1B4
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal degradation. Deubiquitinated by USP8 to get stabilized which induces apoptosis. {ECO:0000269|PubMed:15314180, ECO:0000269|PubMed:17210635, ECO:0000269|PubMed:19483718}.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 2FZP; 2GWF;
Mapped Pubmed ID 11358394; 11867753; 12646216; 14676191; 16954532; 19028597; 19489725; 19549727; 19690564; 19800834; 19874575; 20098290; 20360068; 20587519; 20628057; 20711500; 21378310; 21516116; 21576364; 21693106; 22493164; 23750007; 24259665; 24519943; 25036637; 25355637; 25416956; 25519010; 26088461; 26464195; 26496610; 26514267; 26612725; 26846102; 26963794; 27323192; 27648936; 28481871; 28871945; 29180353; 29410345; 30367623;
Motif
Gene Encoded By
Mass 35,905
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda