| IED ID | IndEnz0002011321 |
| Enzyme Type ID | protease011321 |
| Protein Name |
Activating signal cointegrator 1 ASC-1 Thyroid receptor-interacting protein 4 TR-interacting protein 4 TRIP-4 |
| Gene Name | TRIP4 RQT4 |
| 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 | MAVAGAVSGEPLVHWCTQQLRKTFGLDVSEEIIQYVLSIESAEEIREYVTDLLQGNEGKKGQFIEELITKWQKNDQELISDPLQQCFKKDEILDGQKSGDHLKRGRKKGRNRQEVPAFTEPDTTAEVKTPFDLAKAQENSNSVKKKTKFVNLYTREGQDRLAVLLPGRHPCDCLGQKHKLINNCLICGRIVCEQEGSGPCLFCGTLVCTHEEQDILQRDSNKSQKLLKKLMSGVENSGKVDISTKDLLPHQELRIKSGLEKAIKHKDKLLEFDRTSIRRTQVIDDESDYFASDSNQWLSKLERETLQKREEELRELRHASRLSKKVTIDFAGRKILEEENSLAEYHSRLDETIQAIANGTLNQPLTKLDRSSEEPLGVLVNPNMYQSPPQWVDHTGAASQKKAFRSSGFGLEFNSFQHQLRIQDQEFQEGFDGGWCLSVHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDLIDCLSQKQFKEQFPDISQESDSPFVFICKNPQEMVVKFPIKGNPKIWKLDSKIHQGAKKGLMKQNKAV |
| Enzyme Length | 581 |
| Uniprot Accession Number | Q15650 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (PubMed:10454579, PubMed:25219498). Also involved in androgen receptor transactivation (By similarity). Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B (PubMed:12077347). May play a role in the development of neuromuscular junction (PubMed:26924529). May play a role in late myogenic differentiation (By similarity). Also functions as part of the RQC trigger (RQT) complex that activates the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:32099016). {ECO:0000250|UniProtKB:Q9QXN3, ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:32099016}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (6); Chain (1); Cross-link (4); Domain (1); Frameshift (1); Helix (5); Initiator methionine (1); Modified residue (4); Region (3); Sequence conflict (4); Turn (1); Zinc finger (1) |
| Keywords | 3D-structure;Acetylation;Congenital muscular dystrophy;Cytoplasm;Cytoskeleton;Isopeptide bond;Metal-binding;Neurodegeneration;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:26924529}. Cytoplasm, cytosol {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:20873783}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20873783}. Note=Cytoplasmic under conditions of serum deprivation (PubMed:10454579). Colocalizes with NEK6 in the centrosome (PubMed:20873783). {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:20873783}. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:19413330; MOD_RES 276; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 289; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q9QXN3; MOD_RES 341; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163 |
| Post Translational Modification | PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}.; PTM: Polyufmylated by the UFM1-conjugating system composed of the enzymes UBA5, UFC1 and UFL1. Deufmylated by the protease UFSP2. Ufmylation of TRIP4 is promoted by ligand-bound nuclear receptors that compete with UFSP2 for interaction with TRIP4. Nuclear receptors-induced ufmylation promotes the recruitment of additional transcriptional coactivators like EP300 and NCOA1 and therefore the assembly of a coactivator complex facilitating nuclear receptor-mediated transcription. {ECO:0000269|PubMed:25219498}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 2E5O; |
| Mapped Pubmed ID | 19074642; 20711500; 21988832; 24495969; 26496610; 28899685; 30905820; 31794073; 32298598; 34204919; |
| Motif | |
| Gene Encoded By | |
| Mass | 66,146 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |