| IED ID | IndEnz0002002415 |
| Enzyme Type ID | protease002415 |
| Protein Name |
Baculoviral IAP repeat-containing protein 7-B EC 2.3.2.27 E3 ubiquitin-protein ligase EIAP-B Embryonic/Egg IAP-B EIAP/XLX-B RING-type E3 ubiquitin transferase EIAP-B |
| Gene Name | birc7-b |
| Organism | Xenopus laevis (African clawed frog) |
| 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 Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MSRWSVSQGCGNSHKALRMSGNREQLLSGWGAPGMLRPSMRSEAERQRSFRAWPRSCPQLSPVELARSGFYYLGPGDRVQCFSCGGVLRSWEPGDRPDTEHRKFFPSCPFLQQQQRGPGATDSVDGQVLGQLSGEEPDRTWEPVYPEMSEEQVRLGSFSTWPLDVPGSPEVLAGAGFFYTGHRDHVKCFHCDGGLQNWEQGDDPWTEHAKWFPMCDFLLQVKGEAFIRSVQESLFSSPEPSPESLGSYDYDRSLASSTESVSVPRAPTPGERSEPPKVSGPPLSTEEQLQRLKEERMCKVCMDKDVSMLFVPCGHLVVCTECAPNLRHCPICRAAIRGSVRAFMS |
| Enzyme Length | 345 |
| Uniprot Accession Number | A9ULZ2 |
| 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:Q8JHV9}; |
| 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); Erroneous initiation (1); Metal binding (4); Modified residue (4); Region (1); Repeat (2); Zinc finger (1) |
| Keywords | Apoptosis;Cytoplasm;Developmental protein;Metal-binding;Phosphoprotein;Protease inhibitor;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 237; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8JHV9; MOD_RES 241; /note=Phosphoserine; by MAPK1; /evidence=ECO:0000250; MOD_RES 253; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8JHV9; MOD_RES 257; /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|UniProtKB:Q8JHV9}.; 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 | 38,484 |
| Kinetics | |
| Metal Binding | METAL 188; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 191; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 208; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 215; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029" |
| Rhea ID | |
| Cross Reference Brenda |