Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Cloning and characterization of a cDNA encoding human cardiolipin synthase (hCLS1).
Identification and characterization of human cardiolipin synthase.
Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Deleterious variants in CRLS1 lead to cardiolipin deficiency and cause an autosomal recessive multi-system mitochondrial disease.
Mieap forms membrane-less organelles involved in cardiolipin metabolism.
2-acyl LPG is acylated to PG by CRLS1 (IM)
1-acyl LPG is acylated to PG by CRLS1 (IM)
Acyl chain remodelling of PG
PG and CDP-DAG are converted to CL by CRLS1
A novel function of the human CLS1 in phosphatidylglycerol synthesis and remodeling.
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Reports acyl-CoA-dependent LPG acyltransferase activity of recombinant and purified hCLS1, independent of CDP-DAG.
"In this report, we identified a novel function of the hCLS1 enzyme as an acyl-CoA dependent LPG acyltransferase."
Cardiolipin is essential for early embryonic viability and mitochondrial integrity of neurons in mammals.
Cardiolipin synthesizing enzymes form a complex that interacts with cardiolipin-dependent membrane organizing proteins.
De novo synthesis of cardiolipin controls respiratory chain biogenesis in neonatal mouse hearts.
Comparative analysis of mitochondrial proteomes across the tree of life.
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LECA mitochondria likely had both CDP-type and non-homologous PLD-type cardiolipin synthases; humans retain only the CDP-type, and the PLD-type is a candidate pathogen drug target.
"LECA mitochondria also contained multiple pairs of non-homologous enzymes with similar activities"