| IED ID | IndEnz0002010689 |
| Enzyme Type ID | protease010689 |
| Protein Name |
TRAF family member-associated NF-kappa-B activator TRAF-interacting protein I-TRAF |
| Gene Name | TANK ITRAF TRAF2 |
| 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 | MDKNIGEQLNKAYEAFRQACMDRDSAVKELQQKTENYEQRIREQQEQLSLQQTIIDKLKSQLLLVNSTQDNNYGCVPLLEDSETRKNNLTLDQPQDKVISGIAREKLPKVRRQEVSSPRKETSARSLGSPLLHERGNIEKTFWDLKEEFHKICMLAKAQKDHLSKLNIPDTATETQCSVPIQCTDKTDKQEALFKPQAKDDINRGAPSITSVTPRGLCRDEEDTSFESLSKFNVKFPPMDNDSTFLHSTPERPGILSPATSEAVCQEKFNMEFRDNPGNFVKTEETLFEIQGIDPIASAIQNLKTTDKTKPSNLVNTCIRTTLDRAACLPPGDHNALYVNSFPLLDPSDAPFPSLDSPGKAIRGPQQPIWKPFPNQDSDSVVLSGTDSELHIPRVCEFCQAVFPPSITSRGDFLRHLNSHFNGET |
| Enzyme Length | 425 |
| Uniprot Accession Number | Q92844 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. Negatively regulates NF-kappaB signaling and cell survival upon DNA damage (PubMed:25861989). Plays a role as an adapter to assemble ZC3H12A, USP10 in a deubiquitination complex which plays a negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Promotes UBP10-induced deubiquitination of TRAF6 in response to DNA damage (PubMed:25861989). May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2. {ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:25861989}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Beta strand (1); Chain (1); Coiled coil (1); Metal binding (4); Modified residue (11); Mutagenesis (13); Natural variant (3); Region (4); Sequence conflict (7); Site (4); Zinc finger (1) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Coiled coil;Cytoplasm;DNA damage;Host-virus interaction;Metal-binding;Phosphoprotein;Reference proteome;Zinc;Zinc-finger |
| Interact With | O96018; Q96MT8; P42858; Q14164; Q9Y6K9; P53350; Q05519; P63165; P61956; Q9UHD2; Q13625-3; Q12933; Q13114; Q92574; P03495; P17362; P42858 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 126; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 129; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"; MOD_RES 178; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 208; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 213; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 225; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 228; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 341; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19369195"; MOD_RES 354; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19369195"; MOD_RES 357; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195" |
| Post Translational Modification | PTM: Phosphorylated by IKBKE. {ECO:0000269|PubMed:10759890}.; PTM: (Microbial infection) Cleaved by encephalomyocarditis virus (EMCV) protease 3C (PubMed:26363073). This cleavage allows the virus to disrupt the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (PubMed:28487378). {ECO:0000269|PubMed:26363073, ECO:0000269|PubMed:28487378}.; PTM: (Microbial infection) Cleaved by Seneca Valley virus protease 3C allowing the virus to suppress interferon type-I through both RIG-I and Toll-like receptor-dependent pathways. {ECO:0000269|PubMed:28566380}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1KZZ; 1L0A; 5H10; |
| Mapped Pubmed ID | 10421793; 12692549; 14499357; 14517219; 14517278; 14703513; 14743216; 15210742; 15361868; 16189514; 16336209; 16914100; 17047224; 17157040; 17327220; 17500595; 17526488; 17721511; 17823124; 18307994; 19262425; 19453261; 19479062; 19573080; 19668221; 19773279; 19913121; 20331378; 20484576; 20562859; 20568250; 20628086; 20644899; 20711500; 21212807; 21625535; 21903422; 21988832; 22225470; 22619329; 23286385; 23428248; 23453971; 23524849; 23634849; 24008843; 24189400; 24695225; 24722368; 24841215; 25303530; 25416956; 25852190; 26638075; 28155233; 30721969; 31486084; 33316896; 9566918; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,816 |
| Kinetics | |
| Metal Binding | METAL 396; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01253; METAL 399; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01253; METAL 416; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01253; METAL 420; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01253 |
| Rhea ID | |
| Cross Reference Brenda |