| IED ID | IndEnz0002009091 |
| Enzyme Type ID | protease009091 |
| Protein Name |
Small ubiquitin-related modifier 2 SUMO-2 HSMT3 SMT3 homolog 2 SUMO-3 Sentrin-2 Ubiquitin-like protein SMT3B Smt3B |
| Gene Name | SUMO2 SMT3B SMT3H2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY |
| Enzyme Length | 95 |
| Uniprot Accession Number | P61956 |
| 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, RANBP2, CBX4 or ZNF451 (PubMed:26524494). 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 (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:26524494, ECO:0000269|PubMed:9556629}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (8); Chain (1); Cross-link (9); Domain (1); Helix (1); Modified residue (1); Mutagenesis (4); Natural variant (1); Propeptide (1); Turn (4) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Host-virus interaction;Isopeptide bond;Nucleus;Reference proteome;Ubl conjugation;Ubl conjugation pathway |
| Interact With | P38398; Q12873; Q8IX15-3; P10242; Q8IZL8; Q8N2W9; Q9P0U3; Q9HC62; P23497-2; Q92844; Q13569; P63279; Q9UHP3; Q5W0Q7; Q86T24; O15060; Q96IT1; O88846; Q6DRC5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. |
| Modified Residue | MOD_RES 11; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:19608861 |
| Post Translational Modification | PTM: Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4. {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:23560854}.; PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000269|PubMed:15487983}.; PTM: Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer. {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:23560854}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (9); X-ray crystallography (15) |
| Cross Reference PDB | 1WM2; 1WM3; 1WZ0; 2AWT; 2CKH; 2D07; 2IO0; 2IO3; 2IYD; 2N1W; 2N9E; 2RPQ; 3UIN; 3UIO; 3ZO5; 4BKG; 4NPN; 5D2M; 5ELU; 5EQL; 5GHB; 5GHC; 6JXW; 6JXX; |
| Mapped Pubmed ID | 10187858; 11889051; 11896061; 12032081; 12192048; 12356736; 12641448; 12665592; 14563852; 15161980; 15175327; 15192080; 15192092; 15272016; 15383276; 15456902; 15608651; 15660128; 15829507; 15870296; 16030353; 16055710; 16169070; 16194093; 16253240; 16524884; 16553580; 16608850; 16738315; 16738331; 16904644; 17012228; 17099700; 17164289; 17183683; 17218271; 17369852; 17491593; 17535915; 17591783; 17643372; 18081309; 18259216; 18374647; 18374648; 18381449; 18408014; 18565875; 18617891; 18694876; 18708356; 18842587; 18946085; 19029252; 19041634; 19107418; 19240082; 19332021; 19345186; 19394292; 19443651; 19597476; 19615732; 19635839; 19638612; 19706679; 19779455; 19850744; 19919826; 19956565; 20016594; 20016603; 20098713; 20159957; 20164921; 20176810; 20351170; 20501649; 20663916; 20705237; 20711500; 20797632; 20797634; 20802522; 20881090; 21098080; 21147198; 21212807; 21252943; 21291420; 21326211; 21467194; 21527249; 21554500; 21647297; 21878624; 21900206; 21900752; 21940674; 21988832; 22194619; 22306003; 22370726; 22464730; 22564762; 22635276; 22661229; 22661230; 22685230; 22810585; 22825850; 22878415; 22922005; 22942423; 23077236; 23078246; 23092970; 23358114; 23552691; 23750026; 23751493; 23990779; 23994136; 24027577; 24151981; 24257756; 24267727; 24278015; 24369422; 24424631; 24564702; 24582501; 24656128; 24753249; 24782567; 24811749; 24844634; 24971752; 25047847; 25097252; 25245533; 25367092; 25380826; 25391294; 25406032; 25416956; 25497329; 25533185; 25722289; 25762490; 25880753; 25884224; 26042670; 26060329; 26073453; 26151477; 26152697; 26200910; 26223632; 26223657; 26458400; 26627832; 26719330; 26867680; 26947976; 27084229; 27767176; 27799292; 27814492; 28665748; 28747609; 28784659; 29138295; 29326161; 29891701; 30006506; 30201799; 30232383; 30280191; 30403549; 30559154; 30761470; 30926672; 31045562; 31587348; 32001251; 32641734; 33006472; 33189785; 34086420; 34396430; 9452416; 9920803; |
| Motif | |
| Gene Encoded By | |
| Mass | 10,871 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |