| IED ID | IndEnz0002001514 |
| Enzyme Type ID | protease001514 |
| Protein Name |
E3 ubiquitin-protein ligase TRIM22 EC 2.3.2.27 50 kDa-stimulated trans-acting factor RING finger protein 94 RING-type E3 ubiquitin transferase TRIM22 Staf-50 Tripartite motif-containing protein 22 |
| Gene Name | TRIM22 RNF94 STAF50 |
| 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 | MDFSVKVDIEKEVTCPICLELLTEPLSLDCGHSFCQACITAKIKESVIISRGESSCPVCQTRFQPGNLRPNRHLANIVERVKEVKMSPQEGQKRDVCEHHGKKLQIFCKEDGKVICWVCELSQEHQGHQTFRINEVVKECQEKLQVALQRLIKEDQEAEKLEDDIRQERTAWKNYIQIERQKILKGFNEMRVILDNEEQRELQKLEEGEVNVLDNLAAATDQLVQQRQDASTLISDLQRRLRGSSVEMLQDVIDVMKRSESWTLKKPKSVSKKLKSVFRVPDLSGMLQVLKELTDVQYYWVDVMLNPGSATSNVAISVDQRQVKTVRTCTFKNSNPCDFSAFGVFGCQYFSSGKYYWEVDVSGKIAWILGVHSKISSLNKRKSSGFAFDPSVNYSKVYSRYRPQYGYWVIGLQNTCEYNAFEDSSSSDPKVLTLFMAVPPCRIGVFLDYEAGIVSFFNVTNHGALIYKFSGCRFSRPAYPYFNPWNCLVPMTVCPPSS |
| Enzyme Length | 498 |
| Uniprot Accession Number | Q8IYM9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:18389079, ECO:0000269|PubMed:18656448, ECO:0000269|PubMed:19218198, ECO:0000269|PubMed:19585648}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein ubiquitination. |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Metal binding (4); Motif (1); Mutagenesis (3); Natural variant (4); Sequence conflict (1); Zinc finger (2) |
| Keywords | Alternative splicing;Antiviral defense;Coiled coil;Cytoplasm;Host-virus interaction;Metal-binding;Nucleus;Reference proteome;Repressor;Transcription;Transcription regulation;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | Q9H8W4 |
| Induction | INDUCTION: By interferons alpha and beta. Up-regulated by p53/TP53. Dramatically induced by progesterone in MDA-MB-231-derived ABC28 cells and T47D cells. {ECO:0000269|PubMed:15064739, ECO:0000269|PubMed:18389079, ECO:0000269|PubMed:19331816, ECO:0000269|PubMed:7797467}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}. Nucleus {ECO:0000269|PubMed:17156811}. Nucleus speckle. Nucleus, Cajal body. Note=Localizes predominantly to the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to form in the early G0/G1 phase but become speckle-like in the S-phase and completely dispersed in mitosis. 35% of TRIM22 nuclear bodies overlap or are found adjacent to Cajal bodies. |
| Modified Residue | |
| Post Translational Modification | PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18656448}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 1508672; 16713569; 16926043; 17970695; 18362138; 19212762; 19902255; 19943174; 20001730; 20006605; 20711500; 20980524; 21345949; 21651891; 21683060; 21988832; 22509910; 23408607; 23670564; 23818111; 23921607; 24066097; 24183724; 24863734; 24889558; 24983760; 25510414; 25683609; 26237181; 26271984; 26316153; 26683615; 26836588; 27590274; 27704462; 28079123; 28341749; 28782753; 29650252; 29749134; 29762880; 30011088; 31136823; 31863490; 32319602; 32803897; 33299853; 34621686; 7530745; 8176225; 8483949; 8530158; 9143706; |
| Motif | MOTIF 257..275; /note=Nuclear localization signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 56,947 |
| Kinetics | |
| Metal Binding | METAL 97; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00024; METAL 100; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00024; METAL 119; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00024; METAL 125; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00024 |
| Rhea ID | |
| Cross Reference Brenda | 2.3.2.27; |