IED ID | IndEnz0016000068 |
Enzyme Type ID | tyrosinase000068 |
Protein Name |
Interferon regulatory factor 4 IRF-4 Lymphocyte-specific interferon regulatory factor LSIRF Multiple myeloma oncogene 1 NF-EM5 |
Gene Name | IRF4 MUM1 |
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 | MNLEGGGRGGEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSIFRIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCALNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLEDPQMSMSHPYTMTTPYPSLPAQQVHNYMMPPLDRSWRDYVPDQPHPEIPYQCPMTFGPRGHHWQGPACENGCQVTGTFYACAPPESQAPGVPTEPSIRSAEALAFSDCRLHICLYYREILVKELTTSSPEGCRISHGHTYDASNLDQVLFPYPEDNGQRKNIEKLLSHLERGVVLWMAPDGLYAKRLCQSRIYWDGPLALCNDRPNKLERDQTCKLFDTQQFLSELQAFAHHGRSLPRFQVTLCFGEEFPDPQRQRKLITAHVEPLLARQLYYFAQQNSGHFLRGYDLPEHISNPEDYHRSIRHSSIQE |
Enzyme Length | 451 |
Uniprot Accession Number | Q15306 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | DNA_BIND 21..129; /note=IRF tryptophan pentad repeat; /evidence=ECO:0000255|PROSITE-ProRule:PRU00840 |
EC Number | |
Enzyme Function | FUNCTION: Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes (By similarity). {ECO:0000250|UniProtKB:Q64287}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (1); Beta strand (7); Chain (1); DNA binding (1); Helix (5); Modified residue (2); Sequence conflict (3); Turn (2) |
Keywords | 3D-structure;Activator;Alternative splicing;Chromosomal rearrangement;DNA-binding;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation |
Interact With | O95163; Q8TF65; P51617; Q86UE8; Q7Z6J9; Q9H6S0 |
Induction | INDUCTION: Not induced by interferons. |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus. |
Modified Residue | MOD_RES 447; /note=Phosphoserine; by ROCK2; /evidence=ECO:0000250|UniProtKB:Q64287; MOD_RES 448; /note=Phosphoserine; by ROCK2; /evidence=ECO:0000250|UniProtKB:Q64287 |
Post Translational Modification | PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21 production. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (3); NMR spectroscopy (1) |
Cross Reference PDB | 2DLL; 6TD4; 7JM4; 7O56; |
Mapped Pubmed ID | 11092454; 11337497; 11404376; 12029096; 14712222; 14769151; 15047845; 1508672; 15950906; 16007214; 16009940; 16189514; 1730654; 17427945; 17502719; 17952075; 18362138; 18758461; 19397496; 19773279; 20190752; 20493732; 20711500; 21903422; 21937440; 2211721; 22693070; 23121362; 23455323; 23541952; 24743777; 30485383; 33533913; 34196610; 6162102; 6548414; 7530745; 8176225; 8483949; 8530158; 9096384; 9143706; 9861020; |
Motif | |
Gene Encoded By | |
Mass | 51,772 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |