Gene Ontology annotation through association of InterPro records with GO terms
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
Combined Automated Annotation using Multiple IEA Methods
Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
Expanding the phenotypic spectrum of Succinyl-CoA ligase deficiency through functional validation of a new SUCLG1 variant.
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Fibroblasts lacking SUCLG1 protein have reduced SUCLA2 and SUCLG2 and essentially no succinyl-CoA synthetase activity; wild-type SUCLG1 rescues.
"The patient's cells lack the SUCLG1 protein, with significantly reduced levels of SUCLA2 and SUCLG2 protein."
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ADP-dependent and GDP-dependent succinyl-CoA synthetase activities were assayed separately, and both were restored in patient cells by wild-type SUCLG1.
"Both ADP and GDP-specific SCS activities are completely restored in the patient’s cells with ectopic expression of SUCLG1 (Figure 1B)"
Architecture of the human interactome defines protein communities and disease networks.
Tartryl-CoA inhibits succinyl-CoA synthetase.
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Human GTP-specific succinyl-CoA synthetase is an alpha/beta heterodimer of SUCLG1 and SUCLG2; CoA binds in the alpha subunit.
"The CoA portion binds in the CoA-binding site located in the amino-terminal domain of the α-subunit"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
The immunometabolite itaconate inhibits heme synthesis and remodels cellular metabolism in erythroid precursors.
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Recombinant SCS-A and pig heart SCS-G metabolised succinate.
"Succinate but not itaconate at 10 mM concentrations is metabolized by pig heart SCS-GTP (SCS-G) (A) and recombinant SCS-ATP (SCS-A) (B)."
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Itaconate is not a substrate of SCS-A or pig SCS-G at 10 mM, and it inhibits the enzyme.
"neither ATP- nor GTP-specific SCS is able to use itaconate under the same conditions as succinate in vitro"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
CLYBL averts vitamin B(12) depletion by repairing malyl-CoA.
The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin.
SUCLG1/A2 cleaves succinyl-CoA
SUCLG1/G2 cleaves succinyl-CoA
Mutated SUCLG1 causes mislocalization of SUCLG2 protein, morphological alterations of mitochondria and an early-onset severe neurometabolic disorder.
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The human enzyme is a heterodimer of SUCLG1 with either SUCLA2 (ATP-forming) or SUCLG2 (GTP-forming) in the mitochondrial matrix.
"Succinate-CoA ligase (SUCL) is a heterodimer consisting of an alpha subunit encoded by SUCLG1, and a beta subunit encoded by either SUCLA2 or SUCLG2 catalyzing an ATP- or GTP-forming reaction, respectively, in the mitochondrial matrix."
The severity of phenotype linked to SUCLG1 mutations could be correlated with residual amount of SUCLG1 protein.
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Complete absence of SUCLG1 protein gives a very severe antenatal-onset disorder; residual protein gives a milder, SUCLA2-like phenotype.
"The involvement of SUCLG1 was confirmed by western blot analysis, which showed absence of SUCLG1 protein in fibroblasts."
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Fibroblasts without SUCLG1 protein have no SUCLA2 protein.
"in the absence of SUCLG1 protein, no SUCLA2 protein is found in fibroblasts by western blot analysis"
The interplay between SUCLA2, SUCLG2, and mitochondrial DNA depletion.
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Knockdown of SUCLG2 lowers mtDNA content and mitochondrial NDPK activity in fibroblasts.
"knockdown of SUCLG2 by shRNA in both patient and control fibroblasts resulted in a significant decrease in mtDNA amount, decreased NDPK and cytochrome c oxidase activities, and a marked growth impairment"
SUCLG1 restricts POLRMT succinylation to enhance mitochondrial biogenesis and leukemia progression.
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SUCLG1 lowers succinyl-CoA and thereby limits succinylation of POLRMT in FLT3-mutant leukemia cells.
"Mechanistically, SUCLG1 restricts succinyl-CoA levels to suppress the succinylation of mitochondrial RNA polymerase (POLRMT)."
Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same alpha-subunit.
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ATP- and GTP-specific enzymes share one alpha subunit, so nucleotide specificity resides in the beta subunit.
"Because the two succinyl-CoA synthetases incorporate the same alpha-subunit, the determinants of nucleotide specificity must reside within the beta-subunit"
Evolution of the succinyl-CoA synthetase subunit families (LSC1 / LSC2)
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PAINT node PTN000929335 of the beta-subunit tree holds the characterised GTP-specific beta subunits, pig and human SUCLG2. An alpha subunit has a GDP-forming partner where the genome encodes such a subunit.
"PTN000929335 is the node that holds the experimentally characterised GTP-specific enzymes (pig and human SUCLG2); it is not the limit of Gln20."
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The fungal genomes in the PANTHER tree have no G-type beta gene, so their alpha subunits have no SUCLG2-type partner.
"The 15 fungal genomes in the PANTHER tree (14 Dikarya and the chytrid Batrachochytrium dendrobatidis) have an A-type beta gene and no G-type beta gene."
UniProt entry P53597 (SUCLG1)
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UniProt records itaconyl-CoA and malyl-CoA synthetase activity for the enzyme, citing PMID:40108300.
"Also able to act as an itaconyl- and malyl-CoA synthetase (PubMed:40108300)."
Affinage mechanistic annotation for SUCLG1 (human)
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SUCLG1 is required for the stability of both beta subunits and for succinyl-CoA synthetase activity.
"loss of SUCLG1 protein leads to concurrent loss of the partner beta subunits SUCLA2 and SUCLG2, abolished SCS enzyme activity, mtDNA depletion, and respiration defects, all of which are reversed by ectopic wild-type SUCLG1"
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Affinage grounds the molecular activity partly as catalytic activity acting on a protein.
"GO:0140096 catalytic activity, acting on a protein"