| IED ID | IndEnz0002015781 |
| Enzyme Type ID | protease015781 |
| Protein Name |
NF-kappa-B essential modulator NEMO FIP-3 IkB kinase-associated protein 1 IKKAP1 Inhibitor of nuclear factor kappa-B kinase subunit gamma I-kappa-B kinase subunit gamma IKK-gamma IKKG IkB kinase subunit gamma NF-kappa-B essential modifier |
| Gene Name | IKBKG |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MSRTPWKSQPCEMVQPSGGPAGDQDVLGEESSLGKPTMLHLPSEQGAPETFQRCLEENQELRDAIRQSNQMLRERCEELQRFQGSQREEKEFLMQKFCEARRLVERLSLEKLELRRQREQALQEVELLKTCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQALESRVRATSEQVRQLENEREALQQQHSVQVDQLRLQSQSMEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVSSERNRGLQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREQLAERKELLQEQLEQLQREYSRLKTSCQESARIEDMRKRHVEVSQPTLPPAPAHHSFHPALPSQRRSPPEEPPNFCCPKCQYQAPDMDTLQIHVMECIE |
| Enzyme Length | 419 |
| Uniprot Accession Number | A9QT41 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q9Y6K9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Coiled coil (1); Cross-link (16); Disulfide bond (2); Metal binding (4); Modified residue (6); Region (10); Site (1); Zinc finger (1) |
| Keywords | Coiled coil;Cytoplasm;DNA damage;Disulfide bond;Isopeptide bond;Kinase;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Transferase;Ubl conjugation;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}. |
| Modified Residue | MOD_RES 31; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y6K9; MOD_RES 43; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y6K9; MOD_RES 68; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y6K9; MOD_RES 85; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y6K9; MOD_RES 376; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y6K9; MOD_RES 387; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y6K9 |
| Post Translational Modification | PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Polyubiquitinated on Lys-285 through 'Lys-63'; the ubiquitination is mediated by NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Polyubiquitinated on Lys-399 through 'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Monoubiquitinated on Lys-277 and Lys-309; promotes nuclear export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses. Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation. Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. Ubiquitinated at Lys-326 by MARCHF2 following bacterial and viral infection which leads to its degradation (By similarity). {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: (Microbial infection) Cleaved by porcine reproductive and respiratory syndrome virus serine protease nsp4 after Glu-349. The cleavage inhibits NEMO proper function. {ECO:0000269|PubMed:25008936}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,637 |
| Kinetics | |
| Metal Binding | METAL 397; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01142; METAL 400; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01142; METAL 413; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01142; METAL 417; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01142 |
| Rhea ID | |
| Cross Reference Brenda |