| IED ID | IndEnz0002016513 |
| Enzyme Type ID | protease016513 |
| Protein Name |
Baculoviral IAP repeat-containing protein 7 EC 2.3.2.27 Kidney inhibitor of apoptosis protein KIAP Livin Melanoma inhibitor of apoptosis protein ML-IAP RING finger protein 50 RING-type E3 ubiquitin transferase BIRC7 Cleaved into: Baculoviral IAP repeat-containing protein 7 30kDa subunit Truncated livin p30-Livin tLivin |
| Gene Name | BIRC7 KIAP LIVIN MLIAP RNF50 UNQ5800/PRO19607/PRO21344 |
| 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 | MGPKDSAKCLHRGPQPSHWAAGDGPTQERCGPRSLGSPVLGLDTCRAWDHVDGQILGQLRPLTEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDPWEEPEDAAPVAPSVPASGYPELPTPRREVQSESAQEPGGVSPAEAQRAWWVLEPPGARDVEAQLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQLCPICRAPVRSRVRTFLS |
| Enzyme Length | 298 |
| Uniprot Accession Number | Q96CA5 |
| 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; Evidence={ECO:0000269|PubMed:16729033}; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control (PubMed:11162435, PubMed:11024045, PubMed:11084335, PubMed:16729033, PubMed:17294084). Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity (PubMed:11024045, PubMed:16729033). As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival (PubMed:16729033). May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions (PubMed:16729033). Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine (PubMed:11162435, PubMed:11084335, PubMed:11865055). Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2 (PubMed:11865055). This activation depends on TAB1 and MAP3K7/TAK1 (PubMed:11865055). In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9 (PubMed:11024045). {ECO:0000269|PubMed:11024045, ECO:0000269|PubMed:11084335, ECO:0000269|PubMed:11162435, ECO:0000269|PubMed:11865055, ECO:0000269|PubMed:16729033, ECO:0000269|PubMed:17294084}.; FUNCTION: [Isoform 1]: Blocks staurosporine-induced apoptosis (PubMed:11322947). Promotes natural killer (NK) cell-mediated killing (PubMed:18034418). {ECO:0000269|PubMed:11322947, ECO:0000269|PubMed:18034418}.; FUNCTION: [Isoform 2]: Blocks etoposide-induced apoptosis (PubMed:11162435, PubMed:11322947). Protects against natural killer (NK) cell-mediated killing (PubMed:18034418). {ECO:0000269|PubMed:11162435, ECO:0000269|PubMed:11322947, ECO:0000269|PubMed:18034418}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (7); Chain (2); Helix (9); Metal binding (4); Mutagenesis (4); Natural variant (1); Region (2); Repeat (1); Site (1); Turn (6); Zinc finger (1) |
| Keywords | 3D-structure;Alternative splicing;Apoptosis;Cytoplasm;Golgi apparatus;Metal-binding;Nucleus;Protease inhibitor;Reference proteome;Thiol protease inhibitor;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | Q9UQB9; Q13490; Q9Y3E2; A0A087WZT3; P55211; P26196; Q9NR28; Q9H5Z6; P52655; O43464; Q63ZY3; Q96JN0-2; P61968; Q96HA8; O43189; O15160; P0CG20; P20618; P47897; P35711-4; Q96N21; Q08117; Q08117-2; O14787-2; Q3SY00; P49638; P61086; O75604; A5D8V6; Q6GPH4 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17294084}. Cytoplasm {ECO:0000269|PubMed:17294084}. Golgi apparatus {ECO:0000269|PubMed:17294084}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively in the cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis. |
| Modified Residue | |
| Post Translational Modification | PTM: Autoubiquitinated and undergoes proteasome-mediated degradation.; PTM: The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (13) |
| Cross Reference PDB | 1OXN; 1OXQ; 1OY7; 1TW6; 2I3H; 2I3I; 3F7G; 3F7H; 3F7I; 3GT9; 3GTA; 3UW5; 4AUQ; |
| Mapped Pubmed ID | 12488298; 12620238; 14614456; 15009721; 15541814; 16026775; 16437214; 16806840; 16840203; 16965834; 16990595; 17035597; 17168540; 17437058; 17519534; 17632732; 17672950; 17968430; 18031611; 18210873; 18278467; 18315896; 18451137; 18476630; 18555709; 18827979; 18837095; 19228017; 19397802; 19549727; 19549891; 19635196; 19690982; 19724862; 19806913; 19914791; 20109966; 20189383; 20237496; 20388502; 20416174; 20460713; 20584688; 20607788; 20691667; 20717925; 21122381; 21700335; 21867615; 22033581; 22086237; 22413863; 22427141; 22711539; 22766624; 22902369; 22930255; 22931613; 22932199; 22938441; 23029054; 23030305; 23069480; 23188704; 23343959; 23404657; 23480510; 23524337; 23563149; 23632777; 23781587; 23906305; 24008725; 24023847; 24220265; 24287698; 24696218; 24767895; 24938471; 25090821; 25242075; 25260751; 25261663; 25339450; 25370472; 25374170; 25416956; 25695324; 26094984; 26122233; 26412467; 26708654; 26823716; 27175933; 27448305; 27677286; 27802195; 28030838; 28109866; 28440463; 28459204; 28470345; 29436592; 30280770; 30376767; 31298372; 31445935; 32119704; 32124942; 32359099; 32395888; 32724797; 32928920; 33234031; 33649820; |
| Motif | |
| Gene Encoded By | |
| Mass | 32,798 |
| Kinetics | |
| Metal Binding | METAL 124; /note=Zinc; METAL 127; /note=Zinc; METAL 144; /note=Zinc; METAL 151; /note=Zinc |
| Rhea ID | |
| Cross Reference Brenda |