| IED ID | IndEnz0002011355 |
| Enzyme Type ID | protease011355 |
| Protein Name |
E3 ubiquitin-protein ligase XIAP EC 2.3.2.27 Baculoviral IAP repeat-containing protein 4 IAP homolog A Inhibitor of apoptosis protein 3 IAP-3 mIAP-3 mIAP3 RING-type E3 ubiquitin transferase XIAP X-linked inhibitor of apoptosis protein X-linked IAP |
| Gene Name | Xiap Aipa Api3 Birc4 Miha |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MTFNSFEGTRTFVLADTNKDEEFVEEFNRLKTFANFPSSSPVSASTLARAGFLYTGEGDTVQCFSCHAAIDRWQYGDSAVGRHRRISPNCRFINGFYFENGAAQSTNPGIQNGQYKSENCVGNRNPFAPDRPPETHADYLLRTGQVVDISDTIYPRNPAMCSEEARLKSFQNWPDYAHLTPRELASAGLYYTGADDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNVNVRSESGVSSDRNFPNSTNSPRNPAMAEYEARIVTFGTWTSSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLDEKGQEYINNIHLTHSLEESLGRTAEKTPSLTKKIDDTIFQNPMVQEAIRMGFSFKDIKKTMEEKIQTSGSSYLSLEVLIADLVSAQKDNTEDESSQTSLQKDISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS |
| Enzyme Length | 496 |
| Uniprot Accession Number | Q60989 |
| 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: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Inhibits apoptosis in intestinal crypt cells, its activity it mitigated via its interaction with SEPTIN4 isoform ARTS (PubMed:30389919). Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Ubiquitinates and therefore mediates the proteosomal degradation of BCL2 in response to apoptosis (By similarity). Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. Positive regulator of dermal wound repair, potentially via its interaction with SEPTIN4 (PubMed:23788729). {ECO:0000250|UniProtKB:P98170, ECO:0000269|PubMed:18761086, ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:23788729, ECO:0000269|PubMed:30389919}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Cross-link (2); Metal binding (4); Modified residue (1); Region (2); Repeat (3); Sequence conflict (10); Zinc finger (1) |
| Keywords | Apoptosis;Cytoplasm;Isopeptide bond;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;S-nitrosylation;Transferase;Ubl conjugation;Ubl conjugation pathway;Wnt signaling pathway;Zinc;Zinc-finger |
| Interact With | P53702; Q9JIY5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=TLE3 promotes its nuclear localization. {ECO:0000250}. |
| Modified Residue | MOD_RES 449; /note=S-nitrosocysteine; /evidence=ECO:0000250|UniProtKB:P98170 |
| Post Translational Modification | PTM: S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity. {ECO:0000250|UniProtKB:P98170}.; PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P98170}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10929712; 11217851; 11313486; 11355574; 11602612; 11604410; 12011074; 12042762; 12153481; 12395105; 12466851; 12520002; 12667469; 12679106; 12812761; 12973017; 14610273; 14623868; 14634619; 14759516; 15102471; 15207275; 15258565; 15540113; 15618518; 15737931; 15798218; 15888033; 15944288; 16115895; 16116448; 16141072; 16154537; 16157589; 16414041; 16543147; 16566922; 16858406; 17148670; 17218959; 17318174; 17562856; 17699753; 17967808; 18025200; 18055022; 18259199; 18363099; 18684108; 18687476; 18692482; 18708583; 18755525; 18769721; 18799693; 19268530; 19273858; 19333375; 19531477; 19570023; 19595300; 19626005; 19735291; 19782107; 19875445; 19897582; 19956646; 20129247; 20154138; 20427267; 20584313; 20660158; 20932476; 20952537; 21099289; 21267068; 21533085; 21695558; 21709246; 21712378; 21768356; 21789165; 22065417; 22117219; 22327219; 22365665; 22576661; 22607974; 22988430; 23384561; 23482492; 23928917; 23954782; 24277699; 24335231; 24378336; 24395041; 24422988; 24882010; 25028717; 25056906; 25190756; 25292199; 25551609; 25693118; 25902529; 26825770; 27129149; 27189977; 27735938; 27767058; 28300832; 28647349; 28656888; 28723569; 28898696; 29073098; 29250796; 29386580; 29605544; 29743550; 29775577; 29899110; 30585320; 30970248; 31438981; 31624230; 31756561; 31841118; 32015347; 32060280; 33713642; 33752931; 33845129; 34739338; 9205126; 9916987; 9990045; 9990849; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,079 |
| Kinetics | |
| Metal Binding | METAL 299; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029; METAL 302; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029; METAL 319; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029; METAL 326; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029 |
| Rhea ID | |
| Cross Reference Brenda |