Detail Information for IndEnz0002010151
IED ID IndEnz0002010151
Enzyme Type ID protease010151
Protein Name Sentrin-specific protease 2
EC 3.4.22.-
Axam2
SUMO-1 protease 1
SuPr-1
SUMO-1/Smt3-specific isopeptidase 2
Smt3ip2
Sentrin/SUMO-specific protease SENP2
Gene Name Senp2 Smt3ip2 Supr1
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 MYRWLAKVLGTILRLCERPAPGARALLKRRRSSSTLFSTAVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVSSACNGTRNVAPSGEVFSNSSSCELMSSGSCSSMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLKSEGYNRRPSGRRHSKSNPESSLTWKPQEQGVTEMISEEGGKGVRRPHCTVEEGVQKDEREKYRKLLERLKEGAHGSTFPPTVSHHSSQRIQMDTLKTKGWVEEQNHGVRTTHFVPKQYRVVETRGPLCSMRSEKRYSKGKADTEKVVGLRFEKEGTRGHQMEPDLSEEVSARLRLGSGSNGLLRRKISVLEIKEKNFPSKEKDRRTEDLFEFTEDMEKEISNALGHGPPDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERSKKQGYPALHAFSTFFYPKLKSGGYQAVKRWTKGVNLFEQELVLVPIHRKVHWSLVVMDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNTDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL
Enzyme Length 588
Uniprot Accession Number Q91ZX6
Absorption
Active Site ACT_SITE 477; /evidence="ECO:0000250|UniProtKB:Q9HC62"; ACT_SITE 494; /evidence="ECO:0000250|UniProtKB:Q9HC62"; ACT_SITE 547; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:11489887, ECO:0000305|PubMed:12419228"
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:11489887, PubMed:20194620). 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 (By similarity). 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 (PubMed:11489887, PubMed:20194620, PubMed:27637147). May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (PubMed:11489887). Deconjugates SUMO2 from MTA1 (By similarity). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed:20194620). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (PubMed:27637147). {ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:11489887, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:27637147}.; FUNCTION: [Isoform 3]: Activates transcription. {ECO:0000269|PubMed:12419228}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (3); Motif (3); Mutagenesis (1); Region (2); Sequence conflict (2)
Keywords Activator;Alternative splicing;Cytoplasm;Cytoplasmic vesicle;Direct protein sequencing;Hydrolase;Membrane;Nuclear pore complex;Nucleus;Phosphoprotein;Protease;Protein transport;Reference proteome;Thiol protease;Transcription;Transcription regulation;Translocation;Transport;Ubl conjugation;Ubl conjugation pathway;Wnt signaling pathway;mRNA transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11489887}. Cytoplasmic vesicle {ECO:0000269|PubMed:11489887}. Note=Found in the cytoplasm and in cytoplasmic vesicles, together with axin. {ECO:0000269|PubMed:11489887}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, PML body {ECO:0000269|PubMed:12419228}.
Modified Residue MOD_RES 32; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9HC62; MOD_RES 332; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9HC62; MOD_RES 343; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9HC62
Post Translational Modification PTM: Polyubiquitinated; which leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q9HC62}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 12693553; 14610273; 15767674; 16602821; 17967808; 17981124; 18799693; 19090619; 19515997; 20417598; 20950277; 21183956; 21554500; 22028379; 22155005; 23381569; 23691130; 24344126; 25189211; 25299344; 25689261; 26142281; 26883797; 28965824; 29272473; 29535048; 30902749; 31433978; 31625212; 32290845; 33182061; 33211757; 33934381; 34509475;
Motif MOTIF 28..31; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 47..52; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 316..331; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:Q9HC62
Gene Encoded By
Mass 67,579
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.B71;