Detail Information for IndEnz0002004716
IED ID IndEnz0002004716
Enzyme Type ID protease004716
Protein Name COP9 signalosome complex subunit 4
SGN4
Signalosome subunit 4
JAB1-containing signalosome subunit 4
Gene Name COPS4 CSN4
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 MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGAEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEIYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
Enzyme Length 406
Uniprot Accession Number Q9BT78
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Component 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 SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, 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. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:9535219}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Beta strand (4); Chain (1); Domain (1); Helix (24); Initiator methionine (1); Modified residue (2); Sequence conflict (2); Turn (2)
Keywords 3D-structure;Acetylation;Alternative splicing;Cell junction;Cytoplasm;Cytoplasmic vesicle;Direct protein sequencing;Nucleus;Reference proteome;Signalosome;Synapse
Interact With Q0VDD7; Q7L5N1; P01100; P08727; Q9BVL2; Q9Y5F1; O75381; Q15831; Q8N6Y0
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:9535219}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:21102408}.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:18850735, ECO:0007744|PubMed:19413330"; MOD_RES 25; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (5); X-ray crystallography (4)
Cross Reference PDB 4D0P; 4D10; 4D18; 4WSN; 6R6H; 6R7F; 6R7H; 6R7I; 6R7N;
Mapped Pubmed ID 10391953; 12944386; 14742321; 15161933; 15811629; 15882621; 16189514; 16223728; 16401342; 16916636; 16943200; 17183367; 17353931; 17882165; 18093314; 18835386; 18926707; 19109893; 19214193; 19367725; 19609301; 19615732; 19748355; 20195357; 20360068; 20855601; 21135142; 21388382; 21903422; 22118460; 22190034; 22653443; 22959436; 23238014; 23453757; 23535662; 23535663; 23583660; 24725084; 25043011; 25416956; 25609649; 25852190; 26496610; 26638075; 27029275; 30896450; 30992253; 31431478; 31444342; 31871319;
Motif
Gene Encoded By
Mass 46,269
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda