| IED ID | IndEnz0002005387 |
| Enzyme Type ID | protease005387 |
| Protein Name |
COP9 signalosome complex subunit 5 SGN5 Signalosome subunit 5 EC 3.4.-.- Jun activation domain-binding protein 1 |
| Gene Name | COPS5 CSN5 JAB1 |
| 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 | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS |
| Enzyme Length | 334 |
| Uniprot Accession Number | Q92905 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (8); Chain (1); Domain (1); Erroneous initiation (1); Helix (8); Initiator methionine (1); Metal binding (3); Modified residue (1); Motif (1); Mutagenesis (1); Sequence conflict (2); Turn (3) |
| Keywords | 3D-structure;Acetylation;Cell junction;Cytoplasm;Cytoplasmic vesicle;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Signalosome;Synapse;Zinc |
| Interact With | O95273; P46527; Q9UNS2; Q7L5N1; P55085; Q13098; Q969Y2; O14879; Q9H8M7; P35372; Q5VTR2; O15105; P10599; P09936 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9535219}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:21102408}. Note=Nuclear localization is diminished in the presence of IFIT3. {ECO:0000269|PubMed:17050680}. |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:18850735, ECO:0000269|Ref.6" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (4); X-ray crystallography (7) |
| Cross Reference PDB | 4D10; 4D18; 4F7O; 4WSN; 5JOG; 5JOH; 5M5Q; 6R6H; 6R7F; 6R7H; 6R7I; |
| Mapped Pubmed ID | 10391953; 12032852; 12119282; 12860294; 12944386; 14666612; 14707456; 14719054; 14742321; 15154004; 15231748; 15234121; 15304329; 15353483; 15480426; 15671554; 15757663; 15811629; 15882621; 15887118; 15899841; 15994944; 16000397; 16122907; 16187115; 16223728; 16401342; 16410250; 16483597; 16624822; 16713569; 16882664; 16916636; 16936264; 16943200; 17027978; 17052710; 17133595; 17183367; 17583730; 17879958; 17882165; 18006276; 18093314; 18199546; 18246048; 18246793; 18285702; 18346358; 18476592; 18534028; 18593980; 18624398; 18667426; 18926707; 19109893; 19139918; 19246649; 19349901; 19367725; 19400951; 19444310; 19461157; 19549727; 19609301; 19615732; 19748355; 20034471; 20093369; 20360068; 20467437; 20589433; 20698225; 20855601; 20890423; 20936779; 21135142; 21382349; 21388382; 21466889; 21510940; 21625211; 21689417; 21903422; 21935931; 21988832; 21994455; 22028648; 22103747; 22118460; 22190034; 22311264; 22350412; 22668871; 22675932; 22797071; 22867945; 22911848; 22959436; 23238014; 23288897; 23357576; 23453757; 23535662; 23535663; 23583660; 23583719; 23636414; 23689509; 23840749; 23911788; 23926101; 23926111; 24043623; 24049181; 24078030; 24170542; 24421388; 24671224; 24725084; 25043011; 25609649; 25666480; 26035694; 26045788; 26048783; 26352431; 26464677; 26496610; 26606000; 26719032; 26989054; 27029275; 27375289; 27524414; 27640199; 27774986; 27981705; 28173800; 28229932; 28270496; 28479251; 28539160; 28583475; 28919423; 29226323; 29448099; 29596838; 29975923; 30203426; 30244171; 30282449; 30352219; 30870427; 31148579; 31309518; 31434609; 31444342; 31473252; 31560888; 31930655; 31950832; 31991125; 32064781; 32390003; 32977947; 33051821; 33508120; 33707115; 34148879; |
| Motif | MOTIF 138..151; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 37,579 |
| Kinetics | |
| Metal Binding | METAL 138; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 140; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 151; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Rhea ID | |
| Cross Reference Brenda |