Detail Information for IndEnz0002012399
IED ID IndEnz0002012399
Enzyme Type ID protease012399
Protein Name Activating signal cointegrator 1
ASC-1
Thyroid receptor-interacting protein 4
TR-interacting protein 4
TRIP-4
Gene Name Trip4
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAVAGAAYREPLVHWCTQQLQKTFALDVSEEIIQYVLSIENAEEIREYVTDLLQGNEGKKGQFIEDLITKWQKNDQEFISDSFQQCLRKDEILDGQRSVDQLKRSRRKGRNKQEVPAFPEPDVAVEVKTPLDLAKAQESNNSVKKKTRFVNLYTREGQDKLAVLLPGRHPCDCLGQKHKLINNCLVCGRIVCEQEGSGPCLFCGSLVCTNEEQDILQRDSNKSQKLLKKLMSGAETSGKVDVSTKDLLPHQESRMKSGLEKAIKHKEKLLEFDRTSIRRTQVIDDESDYFASDSNQWLSKVEREMLQKREEELRELRHASRLSKKVTIDFAGRKILEDENPLAEYHSRLDETIQAIASGTLNQSLVTLDRSCEEPLGVLVNPNMYQASPQWVDNTGSTPQKKTSLSAGPRLEPSLHQHQLRIQDQEFQEGFDGGWCLSMHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDLIDCLSQKQFQEQFPDISQESDSSFVFICKNPQEMVVKFPIKGNPKIWKLDSKIHQGAKKGLMKQNKAV
Enzyme Length 581
Uniprot Accession Number Q9QXN3
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 (By similarity). Also involved in androgen receptor transactivation (PubMed:12077347). 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. May play a role in the development of neuromuscular junction (By similarity). May play a role in late myogenic differentiation (PubMed:27008887). 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 (By similarity). {ECO:0000250|UniProtKB:Q15650, ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:12390891, ECO:0000269|PubMed:27008887}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (3); Region (4); Sequence conflict (4); Zinc finger (1)
Keywords Acetylation;Alternative splicing;Cytoplasm;Cytoskeleton;Direct protein sequencing;Isopeptide bond;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15650}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15650}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15650}. Note=Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome. {ECO:0000250|UniProtKB:Q15650}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q15650; MOD_RES 276; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q15650; MOD_RES 289; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:17947660
Post Translational Modification PTM: Phosphorylated by NEK6. {ECO:0000250}.; 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:0000250|UniProtKB:Q15650, ECO:0000269|PubMed:21494687}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 12520002; 12904583; 14610273; 15226823; 18799693; 20059953; 21267068; 23716698;
Motif
Gene Encoded By
Mass 66,197
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda