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
Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant.
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CCTalpha resides in the nucleus in addition to associating with the endoplasmic reticulum, distinguishing it from the ER-only CCTbeta isoforms, and has cytidylyltransferase activity in the CDP-choline pathway.
"Using isoform-specific antibodies, both CCTbeta1 and CCTbeta2 localized to the endoplasmic reticulum of cells, in contrast to CCTalpha which resided in the nucleus in addition to associating with the endoplasmic reticulum."
Architecture of the human interactome defines protein communities and disease networks.
Disease-linked mutations in the phosphatidylcholine regulatory enzyme CCTα impair enzymatic activity and fold stability.
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CCT is the key regulatory enzyme in phosphatidylcholine synthesis, activated by binding PC-deficient membranes; disease-linked PCYT1A variants impair enzymatic activity and destabilize the catalytic-domain fold, and an autoinhibitory-helix deletion (E280del) increases constitutive activity.
"CTP:phosphocholine cytidylyltransferase (CCT) is the key regulatory enzyme in phosphatidylcholine (PC) synthesis and is activated by binding to PC-deficient membranes."
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase.
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The cloned human enzyme has lipid-dependent cytidylyltransferase activity; the soluble form is activated several-fold by anionic phospholipids and by oleic acid or diacylglycerol-containing PC vesicles, and it shares an amphipathic membrane-binding helix with lipid-binding proteins.
"The soluble form was activated 3 to 4-fold by anionic phospholipids and by oleic acid or diacylglycerol-containing PC vesicles."
PCho and CTP are condensed to CDP-Cho by PCYT1 dimer