Detail Information for IndEnz0002002415
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