| IED ID | IndEnz0002009802 |
| Enzyme Type ID | protease009802 |
| Protein Name |
Sentrin-specific protease 3 EC 3.4.22.- SUMO-1-specific protease 3 Sentrin/SUMO-specific protease SENP3 |
| Gene Name | SENP3 SSP3 SUSP3 |
| 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 | MKETIQGTGSWGPEPPGPGIPPAYSSPRRERLRWPPPPKPRLKSGGGFGPDPGSGTTVPARRLPVPRPSFDASASEEEEEEEEEEDEDEEEEVAAWRLPPRWSQLGTSQRPRPSRPTHRKTCSQRRRRAMRAFRMLLYSKSTSLTFHWKLWGRHRGRRRGLAHPKNHLSPQQGGATPQVPSPCCRFDSPRGPPPPRLGLLGALMAEDGVRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGQSGPEGERSLAPPDASILISNVCSIGDHVAQELFQGSDLGMAEEAERPGEKAGQHSPLREEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKGLVLQLIQSYQRMPGNAMVRGFRVAYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVPEKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTITYFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDCGAFVLQYCKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV |
| Enzyme Length | 574 |
| Uniprot Accession Number | Q9H4L4 |
| Absorption | |
| Active Site | ACT_SITE 465; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 482; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 532; /note=Nucleophile; /evidence=ECO:0000305|PubMed:18259216 |
| Activity Regulation | ACTIVITY REGULATION: On oxidative stress, SENP3 degradation is blocked by inhibition of its ubiquitination, which stabilizes it as it accumulates in the nucleoplasm. {ECO:0000269|PubMed:19680224}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates (PubMed:16608850, PubMed:32832608). Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (PubMed:15743823). Deconjugates SUMO2 and SUMO3 from CDCA8 (PubMed:18946085). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (PubMed:19680224). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (PubMed:19015314). Plays a role in the regulation of sumoylation status of ZNF148 (PubMed:18259216). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (PubMed:32832608). {ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:16608850, ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:18946085, ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224, ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:32832608}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Modified residue (9); Motif (2); Mutagenesis (1); Natural variant (1); Region (3); Sequence conflict (7) |
| Keywords | Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | Q96LK0; P06748; Q8IZL8; Q7Z699; Q9NXF1; P0CG48; Q9BV38; O76024 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19680224}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224}. Cytoplasm {ECO:0000250|UniProtKB:Q9EP97}. Note=Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (PubMed:19680224). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). {ECO:0000250|UniProtKB:Q9EP97, ECO:0000269|PubMed:19680224}. |
| Modified Residue | MOD_RES 54; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 73; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 75; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 169; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 176; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 181; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 188; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 212; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97; MOD_RES 232; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9EP97 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11029585; 15231748; 16043514; 16738141; 17189298; 17353269; 17412707; 18065403; 18438418; 18639523; 19106111; 19423540; 19773279; 19913121; 20181954; 20337593; 20406964; 20438785; 20467437; 20531386; 20628086; 20924358; 21063389; 21182203; 21316347; 21326211; 22094256; 22190735; 22684029; 23467634; 23524851; 24725412; 24930734; 25216525; 25288641; 25609649; 25665578; 26496610; 26511642; 26638075; 27016777; 27181202; 27814492; 28262828; 28351334; 28747609; 29438989; 29576508; 30640896; 30973885; 31914638; 32049023; 33030103; 33558447; 34313310; |
| Motif | MOTIF 125..128; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 153..159; /note=Nuclear localization signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 65,010 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B72; |