| IED ID | IndEnz0002011654 |
| Enzyme Type ID | protease011654 |
| Protein Name |
Small ubiquitin-related modifier 1 SUMO-1 SMT3 homolog 3 Ubiquitin-homology domain protein PIC1 Ubiquitin-like protein SMT3C Smt3C |
| Gene Name | Sumo1 Smt3c Smt3h3 Ubl1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV |
| Enzyme Length | 101 |
| Uniprot Accession Number | P63166 |
| 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 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 similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:16990542}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Cross-link (11); Domain (1); Initiator methionine (1); Modified residue (4); Propeptide (1); Site (1) |
| Keywords | Acetylation;Cell membrane;Cytoplasm;Isopeptide bond;Membrane;Nucleus;Phosphoprotein;Reference proteome;Stress response;Ubl conjugation;Ubl conjugation pathway |
| Interact With | Q03267; Q505F1; P63015; P26367-1; P18031 |
| Induction | INDUCTION: By hypoxia. {ECO:0000269|PubMed:15225651}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000269|PubMed:18681895}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (PubMed:18681895). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:18681895}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000250|UniProtKB:P63165; MOD_RES 2; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19131326; MOD_RES 9; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P63165; MOD_RES 32; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P63165 |
| Post Translational Modification | PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250|UniProtKB:P63165}.; PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. {ECO:0000250|UniProtKB:P63165}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10068040; 10337614; 10961991; 11129635; 11217851; 11389549; 11591653; 11960997; 12054600; 12387893; 12466851; 12520002; 12904583; 14500579; 14555234; 14610273; 15023536; 15122901; 15173587; 15337742; 15349788; 15569683; 15923632; 15950612; 16162816; 16175636; 16678795; 17060459; 17159996; 17187077; 17496161; 17509614; 17548468; 17823119; 17967808; 17981124; 18573887; 18606847; 18644859; 18682553; 18782761; 18799693; 18955028; 19033381; 19189660; 19200349; 19297320; 19553542; 19931425; 20159957; 20176810; 20233849; 20385780; 20408817; 20417598; 20458745; 20661221; 21084637; 21085687; 21183956; 21267068; 21308649; 21336309; 21563299; 21843595; 21900893; 21931855; 22021037; 22155005; 22303332; 22366399; 22555612; 22560297; 22713753; 22905217; 22975420; 23029315; 23213215; 23270804; 23297408; 23583339; 23651519; 23684609; 23696846; 24194600; 24379443; 24639124; 24690371; 24706897; 24891386; 24893265; 25123474; 25128087; 25299344; 25448527; 25484073; 25617419; 25634095; 25775977; 26022678; 26212320; 26420484; 26471094; 26578773; 26605782; 28598330; 29138280; 29269218; 29472640; 29622681; 29633471; 30355233; 30451821; 30703554; 31433978; 31565897; 31822608; 32233089; 32910521; 33211757; 34110283; 34267330; 8812453; 9489770; 9891849; |
| Motif | |
| Gene Encoded By | |
| Mass | 11,557 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |