SUCLA2 Gene

Name	succinate-CoA ligase, ADP-forming, beta subunit
Description	Succinyl-CoA synthetase (SCS) is a mitochondrial matrix enzyme that acts as a heterodimer, being composed of an invariant alpha subunit and a substrate-specific beta subunit. The protein encoded by this gene is an ATP-specific SCS beta subunit that dimerizes with the SCS alpha subunit to form SCS-A, an essential component of the tricarboxylic acid cycle. SCS-A hydrolyzes ATP to convert succinate to succinyl-CoA. Defects in this gene are a cause of myopathic mitochondrial DNA depletion syndrome. A pseudogene of this gene has been found on chromosome 6. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSUCLA2 encodes the β‐subunit of the ADP‐forming succinyl‐CoA synthetase, a key enzyme in the tricarboxylic acid cycle that catalyzes the reversible conversion of succinyl‐CoA to succinate with concomitant ATP production. This enzyme normally forms a complex with mitochondrial nucleotide diphosphate kinase to support the salvage pathway for mitochondrial deoxyribonucleoside triphosphates, thereby contributing critically to the maintenance of mitochondrial DNA. Disruption of SUCLA2 function—through various mutations—has been linked to mitochondrial DNA depletion syndromes that present as encephalomyopathy, occasionally featuring methylmalonic aciduria and other variable clinical manifestations in both childhood and later life."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical metabolic role, SUCLA2 participates in regulatory processes that influence cell survival and differentiation. For example, under oxidative stress conditions in pancreatic ductal adenocarcinoma cells, phosphorylation of SUCLA2 by p38 MAPK promotes dissociation from glutaminase, thereby enhancing post‐translational succinylation, oligomerization, and activity of the enzyme to increase glutaminolysis and bolster antioxidant defenses. In erythroid cells, SUCLA2 interacts with 5′‐aminolevulinic acid synthase, a connection that appears to be important for the regulation of heme biosynthesis. In parallel, loss of SUCLA2 function leads to pathological accumulation of succinyl‐CoA and widespread protein hypersuccinylation, further underscoring its central role in mitochondrial metabolism."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDetailed studies of tissue‐specific expression have revealed that SUCLA2 is expressed almost exclusively in neurons of the human cerebral cortex, distinguishing it from other subunits such as SUCLG2 that are predominantly located in vascular or non‐neuronal compartments. This neuron‐restricted distribution emphasizes the particular vulnerability of the central nervous system to defects in SUCLA2 function, which likely contributes to the characteristic neurological manifestations observed in affected patients."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional insights have emerged from studies exploring the broader clinical and biological context of SUCLA2 dysfunction. In some cases, atypical presentations—including slower progressive encephalomyopathies or associations with conditions such as retinoblastoma—have been reported, highlighting genotype–phenotype variability. Moreover, deletion of the SUCLA2 gene in advanced prostate cancer creates a metabolic vulnerability that can be exploited therapeutically, while altered expression levels have also been implicated in spermatogenic defects. Complementary studies on other metabolic enzymes, such as xanthine dehydrogenase, further expand the understanding of mitochondrial metabolic networks although SUCLA2 remains a central player in energy homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Orly Elpeleg, Chaya Miller, Eli Hershkovitz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1086/430843"}], "href": "https://doi.org/10.1086/430843"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15877282"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15877282"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Rosalba Carrozzo, Daniela Verrigni, Magnhild Rasmussen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1: phenotype and genotype correlations in 71 patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Inherit Metab Dis (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10545-015-9894-9"}], "href": "https://doi.org/10.1007/s10545-015-9894-9"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26475597"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26475597"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Elsebet Ostergaard, Marianne Schwartz, Mustafa Batbayli, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A novel missense mutation in SUCLG1 associated with mitochondrial DNA depletion, encephalomyopathic form, with methylmalonic aciduria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Pediatr (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00431-009-1007-z"}], "href": "https://doi.org/10.1007/s00431-009-1007-z"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19526370"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19526370"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Costanza Lamperti, Mingyan Fang, Federica Invernizzi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A novel homozygous mutation in SUCLA2 gene identified by exome sequencing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Genet Metab (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ymgme.2012.08.020"}], "href": "https://doi.org/10.1016/j.ymgme.2012.08.020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23010432"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23010432"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Aleix Navarro-Sastre, Frederic Tort, Judit Garcia-Villoria, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial DNA depletion syndrome: new descriptions and the use of citrate synthase as a helpful tool to better characterise the patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Genet Metab (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ymgme.2012.08.018"}], "href": "https://doi.org/10.1016/j.ymgme.2012.08.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22980518"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22980518"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Elham Jaberi, Fereshteh Chitsazian, Gholam Ali Shahidi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The novel mutation p.Asp251Asn in the β-subunit of succinate-CoA ligase causes encephalomyopathy and elevated succinylcarnitine."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Hum Genet (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/jhg.2013.45"}], "href": "https://doi.org/10.1038/jhg.2013.45"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23759946"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23759946"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Sanna Matilainen, Pirjo Isohanni, Liliya Euro, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial encephalomyopathy and retinoblastoma explained by compound heterozygosity of SUCLA2 point mutation and 13q14 deletion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Hum Genet (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ejhg.2014.128"}], "href": "https://doi.org/10.1038/ejhg.2014.128"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24986829"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24986829"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Reem A Alkhater, Saija Ahonen, Berge A Minassian "}, {"type": "b", "children": [{"type": "t", "text": "SUCLA2 Arg407Trp mutation can cause a nonprogressive movement disorder - deafness syndrome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Ann Clin Transl Neurol (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/acn3.51247"}], "href": "https://doi.org/10.1002/acn3.51247"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33231368"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33231368"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Natario L Couser, Daniel S Marchuk, Laurie D Smith, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Co-occurring Down syndrome and SUCLA2-related mitochondrial depletion syndrome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Med Genet A (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ajmg.a.38351"}], "href": "https://doi.org/10.1002/ajmg.a.38351"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28749033"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28749033"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Yingying Tong, Dong Guo, Shu-Hai Lin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "SUCLA2-coupled regulation of GLS succinylation and activity counteracts oxidative stress in tumor cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2021.04.002"}], "href": "https://doi.org/10.1016/j.molcel.2021.04.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33991485"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33991485"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "David F Bishop, Vassili Tchaikovskii, A Victor Hoffbrand, et al. "}, {"type": "b", "children": [{"type": "t", "text": "X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.306423"}], "href": "https://doi.org/10.1074/jbc.M111.306423"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22740690"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22740690"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Philipp Gut, Sanna Matilainen, Jesse G Meyer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-020-19743-4"}], "href": "https://doi.org/10.1038/s41467-020-19743-4"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33230181"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33230181"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Arpád Dobolyi, Elsebet Ostergaard, Attila G Bagó, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Exclusive neuronal expression of SUCLA2 in the human brain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Brain Struct Funct (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00429-013-0643-2"}], "href": "https://doi.org/10.1007/s00429-013-0643-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24085565"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24085565"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Arpád Dobolyi, Attila G Bagó, Aniko Gál, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Localization of SUCLA2 and SUCLG2 subunits of succinyl CoA ligase within the cerebral cortex suggests the absence of matrix substrate-level phosphorylation in glial cells of the human brain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Bioenerg Biomembr (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10863-014-9586-4"}], "href": "https://doi.org/10.1007/s10863-014-9586-4"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25370487"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25370487"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Taraka R Donti, Ruchi Masand, Daryl A Scott, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expanding the phenotypic spectrum of Succinyl-CoA ligase deficiency through functional validation of a new SUCLG1 variant."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Genet Metab (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ymgme.2016.07.007"}], "href": "https://doi.org/10.1016/j.ymgme.2016.07.007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27484306"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27484306"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Susumu Kohno, Paing Linn, Naoko Nagatani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Pharmacologically targetable vulnerability in prostate cancer carrying RB1-SUCLA2 deletion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41388-020-1381-6"}], "href": "https://doi.org/10.1038/s41388-020-1381-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32694611"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32694611"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Soo-Kyung Park, Myunghee Hong, Byong Duk Ye, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Scand J Gastroenterol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3109/00365521.2015.1133698"}], "href": "https://doi.org/10.3109/00365521.2015.1133698"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26863601"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26863601"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Shaoping Huang, Jing Wang, Lei Wang "}, {"type": "b", "children": [{"type": "t", "text": "Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis through injury of the mitochondrial function of cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Folia Histochem Cytobiol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.5603/FHC.a2016.0020"}], "href": "https://doi.org/10.5603/FHC.a2016.0020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27766610"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27766610"}]}]}]}
Synonyms	A-BETA, SCS-BETAA, MTDPS5, A-SCS
Proteins	SUCB1_HUMAN
NCBI Gene ID	8803
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

SUCLA2 has 6,776 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 136 datasets.

Click the + buttons to view associations for SUCLA2 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

SUCLA2 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of SUCLA2 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of SUCLA2 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of SUCLA2 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of SUCLA2 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of SUCLA2 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of SUCLA2 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of SUCLA2 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of SUCLA2 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of SUCLA2 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of SUCLA2 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of SUCLA2 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of SUCLA2 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with SUCLA2 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with SUCLA2 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of SUCLA2 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of SUCLA2 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of SUCLA2 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations	phenotypes associated with SUCLA2 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with SUCLA2 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing SUCLA2 protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of SUCLA2 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing SUCLA2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing SUCLA2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing SUCLA2 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing SUCLA2 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with SUCLA2 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with SUCLA2 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing SUCLA2 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of SUCLA2 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with SUCLA2 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with SUCLA2 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with SUCLA2 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with SUCLA2 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by SUCLA2 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving SUCLA2 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with SUCLA2 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with SUCLA2 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with SUCLA2 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with SUCLA2 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with SUCLA2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.