| IED ID | IndEnz0002001504 |
| Enzyme Type ID | protease001504 |
| Protein Name |
Sentrin-specific protease 1 EC 3.4.22.- Sentrin/SUMO-specific protease SENP1 |
| Gene Name | SENP1 |
| 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 | MDDIADRMRMDAGEVTLVNHNSVFKTHLLPQTGFPEDQLSLSDQQILSSRQGHLDRSFTCSTRSAAYNPSYYSDNPSSDSFLGSGDLRTFGQSANGQWRNSTPSSSSSLQKSRNSRSLYLETRKTSSGLSNSFAGKSNHHCHVSAYEKSFPIKPVPSPSWSGSCRRSLLSPKKTQRRHVSTAEETVQEEEREIYRQLLQMVTGKQFTIAKPTTHFPLHLSRCLSSSKNTLKDSLFKNGNSCASQIIGSDTSSSGSASILTNQEQLSHSVYSLSSYTPDVAFGSKDSGTLHHPHHHHSVPHQPDNLAASNTQSEGSDSVILLKVKDSQTPTPSSTFFQAELWIKELTSVYDSRARERLRQIEEQKALALQLQNQRLQEREHSVHDSVELHLRVPLEKEIPVTVVQETQKKGHKLTDSEDEFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNMLMERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAVVDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQEIPQQMNGSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL |
| Enzyme Length | 644 |
| Uniprot Accession Number | Q9P0U3 |
| Absorption | |
| Active Site | ACT_SITE 533; ACT_SITE 550; ACT_SITE 603; /note=Nucleophile |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway (PubMed:10652325, PubMed:15199155, PubMed:16253240, PubMed:16553580, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. Deconjugates SUMO1 from HIPK2 (PubMed:16253240). Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity (PubMed:21829689). Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity (PubMed:23160374). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Deconjugates SUMO1 from METTL3 (PubMed:29506078). Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed:25406032). Deconjugates SUMO1 from GPS2 (PubMed:24943844). {ECO:0000269|PubMed:10652325, ECO:0000269|PubMed:15199155, ECO:0000269|PubMed:16253240, ECO:0000269|PubMed:16553580, ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:24943844, ECO:0000269|PubMed:25406032, ECO:0000269|PubMed:29506078}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (10); Chain (1); Helix (11); Modified residue (4); Motif (4); Mutagenesis (14); Natural variant (3); Region (5); Turn (3) |
| Keywords | 3D-structure;Alternative splicing;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | P63165; P61956 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25406032}. Cytoplasm. Note=Shuttles between cytoplasm and nucleus. |
| Modified Residue | MOD_RES 57; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 157; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 2CKG; 2CKH; 2G4D; 2IY0; 2IY1; 2IYC; 2IYD; 2XPH; 2XRE; 6NNQ; |
| Mapped Pubmed ID | 11896061; 12192048; 15896780; 16608850; 16738315; 16738331; 17591783; 20233848; 20711500; 21119010; 21505236; 22878415; 25668492; 27278019; 31045562; 31871319; |
| Motif | MOTIF 171..177; /note=Nuclear localization signal; /evidence=ECO:0000305|PubMed:14563852; MOTIF 574..577; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 628..634; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 635..644; /note=Nuclear export signal; /evidence=ECO:0000305 |
| Gene Encoded By | |
| Mass | 73,481 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B70; |