| IED ID | IndEnz0002018545 |
| Enzyme Type ID | protease018545 |
| Protein Name |
Baculoviral IAP repeat-containing protein 7 EC 2.3.2.27 E3 ubiquitin-protein ligase EIAP Embryonic/Egg IAP EIAP/XLX RING-type E3 ubiquitin transferase BIRC7 |
| Gene Name | birc7 |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MRSEAERQRSFRAWPHTCRTVSPAELARSGFYYLGPGDRVQCFSCGGVLRSWEPGDRPDTEHRKFFPSCPFLQVRRGPPGGTDSVDGQILGQLSGEEPDRTWEPVCPQMAGEGDRLGSFSTWPRYANGDPQQLAGAGFFYTGHRDHVKCFHCDGGLRNWEQGDDPWTEHAKWFPMCDFLLQVKGEAFIRSVQESFFSSPETSPESVGSYEGSPVSSPGSPPVCPFLSTSVAQGALQMGFKRNRVSSLMINRFILTGSCYGSVSELVTDLIQAEEIHGTESVSVPRAPTQRERPEPPKEPAPPLSTEEQLRQLKEERMCKVCMDNDVSMVFVPCGHLVVCTECAPNLRHCPICRAAIRGSVRAFMS |
| Enzyme Length | 365 |
| Uniprot Accession Number | A9JTP3 |
| 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:0000250|UniProtKB:Q96CA5}; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: Weak apoptotic suppressor. Has E3 ubiquitin-protein ligase activity. Weak inhibitor of caspase activity. {ECO:0000250|UniProtKB:Q8JHV9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (4); Modified residue (5); Region (2); Repeat (2); Zinc finger (1) |
| Keywords | Apoptosis;Cytoplasm;Developmental protein;Metal-binding;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Thiol protease inhibitor;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P98170}. |
| Modified Residue | MOD_RES 198; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8JHV9; MOD_RES 202; /note=Phosphoserine; by MAPK1; /evidence=ECO:0000250; MOD_RES 212; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8JHV9; MOD_RES 216; /note=Phosphoserine; by MAPK1; /evidence=ECO:0000250; MOD_RES 219; /note=Phosphoserine; by MAPK1; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Auto-ubiquitinated, and degraded in a 2-step mechanism; a caspase-independent first step and a caspase-dependent second step. {ECO:0000250}.; PTM: Phosphorylated via MAPK-dependent and CDK-dependent pathways during oocyte maturation. Phosphorylation does not appear to affect caspase inhibition or autoubiquitination activity. {ECO:0000250|UniProtKB:Q8JHV9}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,517 |
| Kinetics | |
| Metal Binding | METAL 149; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 152; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 169; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 176; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029" |
| Rhea ID | |
| Cross Reference Brenda |