IED ID | IndEnz0002001744 |
Enzyme Type ID | protease001744 |
Protein Name |
Sentrin-specific protease 6 EC 3.4.22.- SUMO-1-specific protease 1 Sentrin/SUMO-specific protease SENP6 |
Gene Name | SENP6 KIAA0797 SSP1 SUSP1 FKSG6 |
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 | MAAGKSGGSAGEITFLEALARSESKRDGGFKNNWSFDHEEESEGDTDKDGTNLLSVDEDEDSETSKGKKLNRRSEIVANSSGEFILKTYVRRNKSESFKTLKGNPIGLNMLSNNKKLSENTQNTSLCSGTVVHGRRFHHAHAQIPVVKTAAQSSLDRKERKEYPPHVQKVEINPVRLSRLQGVERIMKKTEESESQVEPEIKRKVQQKRHCSTYQPTPPLSPASKKCLTHLEDLQRNCRQAITLNESTGPLLRTSIHQNSGGQKSQNTGLTTKKFYGNNVEKVPIDIIVNCDDSKHTYLQTNGKVILPGAKIPKITNLKERKTSLSDLNDPIILSSDDDDDNDRTNRRESISPQPADSACSSPAPSTGKVEAALNENTCRAERELRSIPEDSELNTVTLPRKARMKDQFGNSIINTPLKRRKVFSQEPPDALALSCQSSFDSVILNCRSIRVGTLFRLLIEPVIFCLDFIKIQLDEPDHDPVEIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSIQLQMNKEDKVWNDCKGVNKLTNLEEQYIILIFQNGLDPPANMVFESIINEIGIKNNISNFFAKIPFEEANGRLVACTRTYEESIKGSCGQKENKIKTVSFESKIQLRSKQEFQFFDEEEETGENHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLNEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNHETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVIQKCSTVEDSCISSSASEMESCSQNSSAKPVIKKMLNKKHCIAVIDSNPGQEESDPRYKRNICSVKYSVKKINHTASENEEFNKGESTSQKVADRTKSENGLQNESLSSTHHTDGLSKIRLNYSDESPEAGKMLEDELVDFSEDQDNQDDSSDDGFLADDNCSSEIGQWHLKPTICKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPILSFELPMNLANWFPPPRMRTKREEIRNIILKLQEDQSKEKRKHKDTYSTEAPLGEGTEQYVNSISD |
Enzyme Length | 1112 |
Uniprot Accession Number | Q9GZR1 |
Absorption | |
Active Site | ACT_SITE 765; /evidence=ECO:0000250; ACT_SITE 917; /evidence=ECO:0000250; ACT_SITE 1030; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875, ECO:0000269|PubMed:18799455, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20705237, ECO:0000269|PubMed:21148299}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Protein modification; protein sumoylation. |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (1); Chain (1); Compositional bias (5); Cross-link (1); Erroneous initiation (1); Modified residue (8); Mutagenesis (1); Natural variant (5); Region (6); Sequence conflict (3) |
Keywords | Alternative splicing;Hydrolase;Isopeptide bond;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875}. |
Modified Residue | MOD_RES 42; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21406692; MOD_RES 335; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18669648; MOD_RES 336; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18669648; MOD_RES 350; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18669648; MOD_RES 352; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18669648; MOD_RES 416; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 919; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 1111; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 14563852; 20195357; 20711500; 21878624; 24424631; 28615201; 30631152; 30720688; 31485003; 31597105; 31980633; |
Motif | |
Gene Encoded By | |
Mass | 126,146 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B74; |