| IED ID | IndEnz0002004066 |
| Enzyme Type ID | protease004066 |
| Protein Name |
Eukaryotic translation initiation factor 3 subunit F eIF3f Deubiquitinating enzyme eIF3f EC 3.4.19.12 Eukaryotic translation initiation factor 3 subunit 5 eIF-3-epsilon eIF3 p47 |
| Gene Name | EIF3F EIF3S5 |
| 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 | MATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVPDDFETMLNSNINDLLMVTYLANLTQSQIALNEKLVNL |
| Enzyme Length | 357 |
| Uniprot Accession Number | O00303 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:21124883}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling. {ECO:0000269|PubMed:21124883}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (10); Chain (1); Compositional bias (1); Domain (1); Helix (8); Initiator methionine (1); Modified residue (4); Natural variant (3); Region (1); Sequence conflict (1); Turn (4) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Disease variant;Hydrolase;Initiation factor;Mental retardation;Phosphoprotein;Protease;Protein biosynthesis;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | O95994; P54253; P46379-2; Q8TAB5; Q7Z4U5-3; P55212; Q96HB5; A0A1B0GWI1; P21127; P08123; P99999; G5E9A7; O14645; P55884; Itself; O15372; Q7L2H7; A0A0C4DGQ7; Q8WU58; Q969P5; Q53GS7; O14964; P04792; O43464; Q8WXH2; O60333-2; O14901; P13473-2; Q9H000; O15457; Q969H8; Q9NP98; P35240-4; Q7Z3B4; Q9BVL2; Q9BYU1; Q16512; Q7Z3K3; P78424; O75400-2; P60891; P47224; Q13671; Q14D33; Q9Y371; Q7Z699; P51687; Q13148; Q9Y5J6; Q14119; O76024; A0A1U9X8X8; Q9Q2G4; P11223; P59594 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}. |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17322308"; MOD_RES 46; /note="Phosphoserine; by CDK11; in vitro"; /evidence="ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:12446680"; MOD_RES 238; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 258; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11. {ECO:0000269|PubMed:12446680, ECO:0000269|PubMed:17322308}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (8) |
| Cross Reference PDB | 3J8B; 3J8C; 6YBD; 6ZMW; 6ZON; 6ZP4; 6ZVJ; 7A09; |
| Mapped Pubmed ID | 10364207; 10659855; 11018020; 12493757; 12588972; 15161933; 15231748; 15567442; 16169070; 16189514; 16739988; 17353931; 17355907; 17918192; 18354498; 18381585; 18423202; 1856230; 18628297; 18724935; 19237569; 19245811; 19549727; 19738201; 19854136; 20360068; 22190034; 22457825; 23275563; 23455153; 23606334; 23706745; 23725059; 23902751; 24185006; 24189400; 24243016; 24396066; 24502978; 24678890; 24732644; 25171412; 25416956; 25609649; 26496610; 26497985; 26988917; 30573685; 31527668; 32030451; 32680882; 32883864; 33289941; 33736665; 429297; 592399; 641056; 6853548; 6901506; 7000367; 8943342; 9045610; 9732867; 9857202; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,564 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |