Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma.
-
Both yeast and human Sdh5 (SDHAF2) interact with the SDH catalytic subunit and are required for SDH-dependent respiration and for flavination (covalent FAD incorporation) of the SDHA/Sdh1 flavoprotein subunit; germline loss-of-function mutations cause hereditary paraganglioma.
"Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor)"
Succinate dehydrogenase 5 (SDH5) regulates glycogen synthase kinase 3β-β-catenin-mediated lung cancer metastasis.
-
Loss of SDH5 initiates EMT and lung-cancer metastasis; SDH5 interacts with GSK-3β, facilitating its Ser-9 dephosphorylation/activation and thereby negatively regulating Wnt/β-catenin signaling.
"The physical interaction between SDH5 and GSK-3β facilitates GSK-3β activation through Ser-9 dephosphorylation"
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein.
-
X-ray structure of the human SDHA–SDHAF2 complex; SDHAF2 works with a small-molecule dicarboxylate to orient the flavin and capping domains of SDHA, adjusting the active site so that covalent FAD attachment is supported — establishing SDHAF2 as a chaperone/assembly factor rather than a catalyst.
"works in synergy with SDHAF2 to properly orient the flavin and capping domains of SDHA"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.