| IED ID | IndEnz0002001748 |
| Enzyme Type ID | protease001748 |
| Protein Name |
Small ubiquitin-related modifier 2-A SUMO-2-A |
| Gene Name | sumo2-a smt3h2 |
| 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 | MADDKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRQTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGSF |
| Enzyme Length | 95 |
| Uniprot Accession Number | Q7ZTK7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i, and can be promoted by an E3 ligase such as pias1-4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. {ECO:0000269|PubMed:14597774, ECO:0000269|PubMed:15933717}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Cross-link (2); Domain (1); Propeptide (1) |
| Keywords | Isopeptide bond;Nucleus;Ubl conjugation;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Polymeric chains can be formed through Lys-11 cross-linking. {ECO:0000250}.; PTM: Cleavage of precursor form by a sentrin-specific protease is necessary for function. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 10,820 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |