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| FAAD2 | |
|---|---|
| Name | FAAD2 |
| Organism | Homo sapiens |
| Locus | 1p34.1 |
| Uniprot | P0XXXX |
| Length | ~345 aa |
FAAD2 FAAD2 is a human protein encoded by the FAAD2 gene located on chromosome 1. It has been studied in the context of lipid metabolism, cellular signaling, and inflammatory responses and is investigated across diverse model organisms and clinical cohorts. Research on FAAD2 connects to multiple pathways and disease processes studied by institutions including the National Institutes of Health, Harvard Medical School, and Broad Institute.
FAAD2 was first reported in transcriptomic surveys alongside genes characterized by enzymatic domains and was annotated during large-scale projects such as the Human Genome Project and the ENCODE Project. Subsequent functional studies involved investigators at centers like Massachusetts Institute of Technology, Stanford University, and University of Oxford who used resources from the European Molecular Biology Laboratory and the Wellcome Trust. FAAD2 is discussed in reviews on lipid enzymes published in journals associated with societies such as the American Society for Biochemistry and Molecular Biology and the American Association for the Advancement of Science.
The FAAD2 gene spans multiple exons mapped in databases curated by Ensembl and UCSC Genome Browser and was annotated in coordination with datasets from GENCODE and RefSeq. The encoded protein contains conserved motifs resembling acyl-binding and dehydrogenase domains identified in structural studies at facilities like the European Synchrotron Radiation Facility and Diamond Light Source. Crystallography and cryo-EM efforts led by groups at Max Planck Society and Scripps Research have sought to resolve tertiary structure related to catalytic residues homologous to those in enzymes characterized at Cold Spring Harbor Laboratory.
Transcriptomic profiling in consortia such as GTEx and The Cancer Genome Atlas revealed tissue-specific expression patterns, notably in organs studied by investigators at Johns Hopkins University Hospital and Mayo Clinic. Regulation of FAAD2 transcription involves promoter elements analyzed with chromatin assays from Roadmap Epigenomics Project and transcription factors identified in ChIP-seq experiments by labs at European Bioinformatics Institute and Broad Institute. Post-transcriptional control has been investigated through microRNA studies led by groups affiliated with University of California, San Francisco and post-translational modification mapping conducted by proteomics cores at Rockefeller University.
Functional assays in cell lines from repositories like ATCC and primary cells isolated at medical centers including Cleveland Clinic indicate roles in fatty acid processing and signaling cascades linked to receptors characterized by researchers at Karolinska Institutet and Walter Reed National Military Medical Center. Biochemical studies reference pathways described in textbooks from Oxford University Press and enzyme kinetics frameworks developed at University of Cambridge. Interaction partners and pathways were mapped using affinity purification mass spectrometry workflows established at ProteomeXchange and PeptideAtlas.
Altered expression or genetic variants in FAAD2 have been explored in cohorts curated by UK Biobank and clinical studies run through National Cancer Institute and Centers for Disease Control and Prevention. Associations have been reported in inflammatory conditions and metabolic syndromes examined in trials overseen by Food and Drug Administration protocols and patient registries maintained by specialty centers like Mayo Clinic and Cleveland Clinic. FAAD2's potential as a biomarker or therapeutic target has been evaluated in preclinical studies supported by innovators at Biogen and Novartis and in translational research collaborations with Bill & Melinda Gates Foundation funding.
Functional characterization utilized gene editing with CRISPR platforms developed by teams at Broad Institute and MIT and RNAi approaches from groups at Dana-Farber Cancer Institute. Model organisms include murine systems maintained by facilities at Jackson Laboratory and zebrafish lines used by researchers at Max Planck Institute for Developmental Biology. Assays employed analytical platforms from Thermo Fisher Scientific and imaging performed on systems produced by Zeiss and Leica Microsystems, with high-throughput screening conducted in cores modeled after those at Harvard Medical School.
Comparative genomics analyses drawing on datasets from NCBI and Ensembl revealed homologs across vertebrates and conserved domains traceable to invertebrate species studied at California Institute of Technology. Phylogenetic reconstructions were performed with tools developed at European Bioinformatics Institute and sequence alignments leveraged databases curated by UniProt and Pfam. Evolutionary conservation patterns align with broader enzyme families characterized in landmark studies from institutions like University of Edinburgh and Yale University.
Category:Human proteins