National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
|
|---|---|
| Protein Name | Small ubiquitin-related modifier 1 |
| Accession Code | Q5E9D1 |
| Gene | SUMO1 |
| Organism | Bos taurus | Cattle (Taxonomy: 9913) |
| Part of Reference Proteome? | Yes |
| Sequence (Length: 101) |
Description |
Position in the Nuclear Envelope |
|
|---|---|---|
| Location | Location ID | Description |
| Nuclear Envelope | SL-0178 | The nuclear envelope is a membrane system which surrounds the nucleoplasm of eukaryotic cells. It is composed of the nuclear lamina, nuclear pore complexes and two nuclear membranes. The space between the two membranes is called the nuclear intermembrane space. |
| Nuclear Membrane | SL-0182 | The membrane surrounding the nucleus. This term is used when it is not known if the protein is found in or associated with the inner or outer nuclear membrane. | Membrane Topology |
| Topology | Source | Annotation Type |
| Unknown | UniProt | Sequence Analysis | Assigned Ontology terms |
Description |
|
|---|---|
| Ubiquitin-like protein that can be covalently attached to proteins as a monomer or 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 E3 ligases such as PIAS1-4, RANBP2 or CBX4. 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {By SimilarityUniProtKB:P63165, By SimilarityUniProtKB:P63166}. | Assigned Ontology terms |
National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory