{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q16595","secondaryAccessions":["A8MXJ6","C9JJ89","O15545","O95656","Q15294","Q5VZ01"],"uniProtkbId":"FRDA_HUMAN","entryAudit":{"firstPublicDate":"1999-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1999-07-15","entryVersion":235,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18725397"}],"value":"Frataxin, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15641778"}],"value":"1.16.3.1"}]},"alternativeNames":[{"fullName":{"value":"Friedreich ataxia protein"},"shortNames":[{"value":"Fxn"}]}],"contains":[{"recommendedName":{"fullName":{"value":"Frataxin intermediate form"},"shortNames":[{"value":"i-FXN"}]}},{"recommendedName":{"fullName":{"value":"Frataxin(56-210)"}},"alternativeNames":[{"fullName":{"value":"m56-FXN"}}]},{"recommendedName":{"fullName":{"value":"Frataxin(78-210)"}},"alternativeNames":[{"fullName":{"value":"d-FXN"}},{"fullName":{"value":"m78-FXN"}}]},{"recommendedName":{"fullName":{"value":"Frataxin mature form"}},"alternativeNames":[{"fullName":{"value":"Frataxin(81-210)"}},{"fullName":{"value":"m81-FXN"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20053667"}],"value":"Extramitochondrial frataxin"}}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:3951"}],"value":"FXN"},"synonyms":[{"value":"FRDA"},{"value":"X25"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9H1K1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11823441"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12755598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12785837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123683"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15247478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15641778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16239244"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24971490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29576242"}],"value":"Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly (PubMed:12785837, PubMed:24971490). Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release (PubMed:24971490). Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (PubMed:29576242). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity (PubMed:15641778). May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (PubMed:11823441, PubMed:12755598). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation (PubMed:15247478). May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (PubMed:15123683, PubMed:16239244)"}],"commentType":"FUNCTION","molecule":"Frataxin mature form"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16091420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16608849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20053667"}],"value":"Modulates the RNA-binding activity of ACO1 (PubMed:20053667). May be involved in the cytoplasmic iron-sulfur protein biogenesis (PubMed:16091420). May contribute to oxidative stress resistance and overall cell survival (PubMed:16608849)"}],"commentType":"FUNCTION","molecule":"Extramitochondrial frataxin"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Frataxin mature form","reaction":{"name":"4 Fe(2+) + O2 + 4 H(+) = 4 Fe(3+) + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11148"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"1.16.3.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15641778"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"D3ZYW7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11823441"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12755598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12785837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123683"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15581888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15641778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15961414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17331979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26702583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29576242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31101807"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21298097"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31101807"}],"value":"Component of the mitochondrial core iron-sulfur cluster (ISC) complex composed of NFS1, LYRM4, NDUFAB1, ISCU, FXN, and FDX2; this complex is a heterohexamer containing two copies of each monomer (Probable). Homodimer (PubMed:31101807). Monomer (probable predominant form). Oligomer. Monomers and polymeric aggregates of >1 MDa have been isolated from mitochondria. A small fraction of heterologous overexpressed recombinant frataxin forms high-molecular weight aggregates that incorporate iron (PubMed:11823441, PubMed:12755598, PubMed:15581888, PubMed:15641778). Interacts with LYRM4 (PubMed:17331979). Interacts (via ferrous form) with ISCU; the interaction is possible when both are bound to the dimeric form of the cysteine desulfurase complex (NFS1:LYRM4) and the interaction enhances FXN interaction to the dimeric form of the cysteine desulfurase complex (NFS1:LYRM4) (PubMed:12785837, PubMed:29576242, PubMed:31101807). Interacts with FECH; one iron-bound FXN monomer seems to interact with a FECH homodimer (PubMed:15123683). Interacts with SDHA and SDHB (PubMed:15961414). Interacts with ACO2; the interaction is dependent on citrate (By similarity). Interacts with HSPA9 (PubMed:17331979, PubMed:26702583)"}],"commentType":"SUBUNIT","molecule":"Frataxin mature form"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16091420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20053667"}],"value":"Interacts with ACO1 (PubMed:20053667). Interacts with ISCU (cytoplasmic form) (PubMed:16091420)"}],"commentType":"SUBUNIT","molecule":"Extramitochondrial frataxin"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q9BVU5","geneName":"ARL17","intActId":"EBI-25857117"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q9HC96","geneName":"CAPN10","intActId":"EBI-3915761"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q92828","geneName":"CORO2A","intActId":"EBI-2835660"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q9UN19","geneName":"DAPP1","intActId":"EBI-3918199"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"A6NEM1","geneName":"GOLGA6L9","intActId":"EBI-5916454"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"O75925","geneName":"PIAS1","intActId":"EBI-629434"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q9NS23-4","geneName":"RASSF1","intActId":"EBI-438710"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q8WVD3","geneName":"RNF138","intActId":"EBI-749039"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q96D59","geneName":"RNF183","intActId":"EBI-743938"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q8N6K7-2","geneName":"SAMD3","intActId":"EBI-11528848"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q16595","intActId":"EBI-949340"},"interactantTwo":{"uniProtKBAccession":"Q9GZS3","geneName":"SKIC8","intActId":"EBI-358545"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Frataxin mature form","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15581888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16091420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16608849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18725397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20053667"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21298097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9241270"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9302253"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Extramitochondrial frataxin","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16091420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16608849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20053667"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q16595-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q16595-2"],"sequenceIds":["VSP_001576"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q16595-3"],"sequenceIds":["VSP_047282"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17468497"}],"value":"Expressed in the heart, peripheral blood lymphocytes and dermal fibroblasts"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10545606"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11020385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17468497"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18725397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21298097"}],"value":"Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form (frataxin(81-210)) which is the predominant form (PubMed:21298097). The additional forms, frataxin(56-210) and frataxin(78-210), seem to be produced when the normal maturation process is impaired; their physiological relevance is unsure"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Friedreich ataxia","diseaseAccession":"DI-01630","acronym":"FRDA","description":"Autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.","diseaseCrossReference":{"database":"MIM","id":"229300"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10732799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10874325"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19629184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21298097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24971490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31101807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9150176"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9779809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9989622"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.40"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.7"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.8"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"value":"The unusual migration profile of mature frataxin on SDS-PAGE due to its acidic N-terminus most likely contributed to conflicting reports for the N-terminus of the mature protein. Unlike prokaryotic and yeast frataxin homologs, which self-assemble at high iron concentrations, oligomerization of human frataxin is not induced by iron. The existence of a specialized mitochondrial ferritin in mammalia (FTMT) is suggesting that iron storage would be redundant function, at least in mammalian mitochondria"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Not highly expressed and may be artifactual"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the frataxin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Mitochondrion"},{"type":"Chain","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Frataxin intermediate form","featureId":"PRO_0000010129"},{"type":"Chain","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Frataxin(56-210)","featureId":"PRO_0000010130"},{"type":"Chain","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Frataxin(78-210)","featureId":"PRO_0000399388"},{"type":"Chain","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Extramitochondrial frataxin","featureId":"PRO_0000456947"},{"type":"Chain","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Frataxin mature form","featureId":"PRO_0000289331"},{"type":"Alternative sequence","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"in isoform 2","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8596916"}],"featureId":"VSP_001576","alternativeSequence":{"originalSequence":"SGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA","alternativeSequences":["RLTWLLWLFHP"]}},{"type":"Alternative sequence","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"in isoform 3","evidences":[{"evidenceCode":"ECO:0000305"}],"featureId":"VSP_047282","alternativeSequence":{"originalSequence":"SGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA","alternativeSequences":["RYVVDLSVMTGLGKTGCTPTTACPSMSCWPQSSLKP"]}},{"type":"Natural variant","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"in FRDA; dbSNP:rs104894105","featureCrossReferences":[{"database":"dbSNP","id":"rs104894105"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9779809"}],"featureId":"VAR_016065","alternativeSequence":{"originalSequence":"L","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"in FRDA; does not affect interaction with the core iron-sulfur cluster assembly complex; does not affect mitochondrial localization; does not affect proteolytic processing; dbSNP:rs142157346","featureCrossReferences":[{"database":"dbSNP","id":"rs142157346"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21298097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9989622"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.7"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.8"}],"featureId":"VAR_002428","alternativeSequence":{"originalSequence":"D","alternativeSequences":["Y"]}},{"type":"Natural variant","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"in FRDA; does not affect interaction with the core iron-sulfur cluster assembly complex; does not affect mitochondrial localization; does not affect proteolytic processing.; dbSNP:rs104894107","featureCrossReferences":[{"database":"dbSNP","id":"rs104894107"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10732799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21298097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9150176"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9989622"}],"featureId":"VAR_002429","alternativeSequence":{"originalSequence":"G","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"in FRDA; reduces interaction with the core iron-sulfur cluster assembly complex; does not affect mitochondrial localization; does not affect proteolytic processing; reduces interaction with LYRM4; the interaction is rescued by nickel; a murine cellular FRDA model, deleted for endogenous frataxin and expressing human mutant frataxin cDNA shows defects in mitochondrial structure, mitochondrial iron deposits, decreased enzymatic activity of some mitochondrial and cytoplasmic iron-sulfur cluster-containing enzymes, increased RNA-binding activity of ACO1 and increased sensitivity to oxidative stress; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU; dbSNP:rs104894106","featureCrossReferences":[{"database":"dbSNP","id":"rs104894106"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17331979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19629184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21298097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24971490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8596916"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9150176"}],"featureId":"VAR_087120","alternativeSequence":{"originalSequence":"I","alternativeSequences":["F"]}},{"type":"Natural variant","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"in FRDA; reduces interaction with LYRM4; the interaction is rescued by nickel; drastically decreases affinity for the SDAU complex by > 75-fold; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU; dbSNP:rs138471431","featureCrossReferences":[{"database":"dbSNP","id":"rs138471431"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17331979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24971490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31101807"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.40"}],"featureId":"VAR_087121","alternativeSequence":{"originalSequence":"W","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"in FRDA; mild form; decreases affinity for the SDAU complex by 40-fold; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU; dbSNP:rs138034837","featureCrossReferences":[{"database":"dbSNP","id":"rs138034837"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10732799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24971490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31101807"}],"featureId":"VAR_087122","alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"in FRDA; dbSNP:rs139616452","featureCrossReferences":[{"database":"dbSNP","id":"rs139616452"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10732799"}],"featureId":"VAR_008140","alternativeSequence":{"originalSequence":"L","alternativeSequences":["F"]}},{"type":"Natural variant","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"in FRDA; dbSNP:rs144104124","featureCrossReferences":[{"database":"dbSNP","id":"rs144104124"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10874325"}],"featureId":"VAR_016066","alternativeSequence":{"originalSequence":"L","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"in dbSNP:rs1052195","featureCrossReferences":[{"database":"dbSNP","id":"rs1052195"}],"featureId":"VAR_049100","alternativeSequence":{"originalSequence":"S","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Abolishes cleavage to yield frataxin intermediate form and allows accumulation of frataxin(56-210) and frataxin(78-210).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18725397"}],"alternativeSequence":{"originalSequence":"RR","alternativeSequences":["GG"]}},{"type":"Mutagenesis","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"No effect on processing of wild-type FXN.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17468497"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18725397"}],"alternativeSequence":{"originalSequence":"RR","alternativeSequences":["GG"]}},{"type":"Mutagenesis","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Abolishes cleavage to yield frataxin mature form and allows accumulation of frataxin(56-210) and frataxin(78-210).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18725397"}],"alternativeSequence":{"originalSequence":"LR","alternativeSequences":["GG"]}},{"type":"Mutagenesis","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Abolishes cleavage to yield frataxin mature form and allows the accumulation of frataxin(56-210).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17468497"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18725397"}],"alternativeSequence":{"originalSequence":"RK","alternativeSequences":["GG"]}},{"type":"Mutagenesis","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Does not affect interaction with the core iron-sulfur cluster assembly complex. 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