HUMAN:FRDA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FXN (synonyms: FRDA, X25)
Protein Name(s)	Frataxin, mitochondrial Friedreich ataxia protein Fxn Frataxin intermediate form i-FXN Frataxin(56-210) m56-FXN Frataxin(78-210) d-FXN m78-FXN Frataxin mature form Frataxin(81-210) m81-FXN
External Links
UniProt	Q16595
EMBL	U43747 U43752 U43748 U43749 U43750 U43751 U43753 U43748 U43749 U43750 U43751 AL162730 BC023633 BC048097 Y13751 AF028240 U93173
CCDS	CCDS43834.1 CCDS55313.1 CCDS6626.1
RefSeq	NP_000135.2 NP_001155178.1 NP_852090.1
UniGene	Hs.20685
PDB	1EKG 1LY7 3S4M 3S5D 3S5E 3S5F 3T3J 3T3K 3T3L 3T3T 3T3X
PDBsum	1EKG 1LY7 3S4M 3S5D 3S5E 3S5F 3T3J 3T3K 3T3L 3T3T 3T3X
DisProt	DP00607
ProteinModelPortal	Q16595
SMR	Q16595
BioGrid	108677
IntAct	Q16595
MINT	MINT-2856590
STRING	9606.ENSP00000366482
ChEMBL	CHEMBL2321640
TCDB	9.B.21.1.1
PhosphoSite	Q16595
OGP	Q16595
MaxQB	Q16595
PaxDb	Q16595
PeptideAtlas	Q16595
PRIDE	Q16595
DNASU	2395
Ensembl	ENST00000377270 ENST00000396364 ENST00000396366
GeneID	2395
KEGG	hsa:2395
UCSC	uc004aha.2 uc011lrr.1
CTD	2395
GeneCards	GC09P071650
GeneReviews	FXN
HGNC	HGNC:3951
HPA	CAB022164
MIM	229300 606829
neXtProt	NX_Q16595
Orphanet	95
PharmGKB	PA28369
eggNOG	COG1965
GeneTree	ENSGT00390000005811
HOGENOM	HOG000190729
HOVERGEN	HBG005745
InParanoid	Q16595
OMA	KQSVCLM
OrthoDB	EOG7HHWVD
PhylomeDB	Q16595
TreeFam	TF318958
Reactome	REACT_118595 REACT_150353
ChiTaRS	FXN
EvolutionaryTrace	Q16595
GeneWiki	Frataxin
GenomeRNAi	2395
NextBio	9641
PRO	PR:Q16595
Proteomes	UP000005640
Bgee	Q16595
CleanEx	HS_FXN
ExpressionAtlas	Q16595
Genevestigator	Q16595
GO	GO:0005829 GO:0005759 GO:0005739 GO:0051537 GO:0008199 GO:0008198 GO:0004322 GO:0034986 GO:0051536 GO:0007628 GO:0009060 GO:0006879 GO:0070301 GO:0009792 GO:0006783 GO:0006811 GO:0018283 GO:0007005 GO:0043066 GO:0040015 GO:0046621 GO:0090201 GO:0006119 GO:0030307 GO:0008284 GO:0051349 GO:0048554 GO:0051353 GO:0051347 GO:0019230 GO:0016540 GO:0010722 GO:0010039 GO:0044281
Gene3D	3.30.920.10
InterPro	IPR017789 IPR002908 IPR020895
PANTHER	PTHR16821
Pfam	PF01491
PRINTS	PR00904
SUPFAM	SSF55387
TIGRFAMs	TIGR03421 TIGR03422
PROSITE	PS01344 PS50810

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:1904234	positive regulation of aconitate hydratase activity	PMID:18160053^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051537	2 iron, 2 sulfur cluster binding	PMID:12785837^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051349	positive regulation of lyase activity	PMID:18160053^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1904231	positive regulation of succinate dehydrogenase activity	PMID:18160053^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043085	positive regulation of catalytic activity	PMID:15509595^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0034986	iron chaperone activity	PMID:15123683^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0030307	positive regulation of cell growth	PMID:15509595^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018283	iron incorporation into metallo-sulfur cluster	PMID:12785837^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:12785837^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010722	regulation of ferrochelatase activity	PMID:15123683^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010039	response to iron ion	PMID:18424449^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:18160053^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:18537827^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:12785837^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008198	ferrous iron binding	PMID:15123683^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008198	ferrous iron binding	PMID:17285345^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008198	ferrous iron binding	PMID:12785837^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	PMID:18160053^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006783	heme biosynthetic process	PMID:15123683^[4]	ECO:0000303	author statement without traceable support used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:17468497^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:17285345^[7]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07540	C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:17468497^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:16608849^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070301	cellular response to hydrogen peroxide	PMID:15641778^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051349	positive regulation of lyase activity	PMID:20053667^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:16608849^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004322	ferroxidase activity	PMID:15641778^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051537	2 iron, 2 sulfur cluster binding	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000423706 UniProtKB:Q16595	F	Seeded From UniProt	complete
enables	GO:0034986	iron chaperone activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0030092 PANTHER:PTN000423706 SGD:S000002278 UniProtKB:Q16595	F	Seeded From UniProt	complete
involved_in	GO:0018283	iron incorporation into metallo-sulfur cluster	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000423706 UniProtKB:Q16595	P	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000423706 UniProtKB:Q16595	F	Seeded From UniProt	complete
enables	GO:0008198	ferrous iron binding	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000423706 SGD:S000002278 UniProtKB:Q16595	F	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1096879 PANTHER:PTN000423706	P	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1096879 PANTHER:PTN000423706 SGD:S000002278 UniProtKB:Q16595	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0030092 MGI:MGI:1096879 PANTHER:PTN000423706 PomBase:SPCC1183.03c RGD:1565754 SGD:S000002278 TAIR:locus:2125477 UniProtKB:Q16595 WB:WBGene00001486	C	Seeded From UniProt	complete
enables	GO:0004322	ferroxidase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000423706 SGD:S000002278 UniProtKB:Q16595	F	Seeded From UniProt	complete
involved_in	GO:0016226	iron-sulfur cluster assembly	PMID:29491838^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:1990221	L-cysteine desulfurase complex	PMID:29491838^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0046621	negative regulation of organ growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0040015	negative regulation of multicellular organism growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0019230	proprioception	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0016226	iron-sulfur cluster assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0009792	embryo development ending in birth or egg hatching	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0009060	aerobic respiration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0007628	adult walking behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
involved_in	GO:0006119	oxidative phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O35943 ensembl:ENSMUSP00000080081	C	Seeded From UniProt	complete
enables	GO:0004322	ferroxidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017789	F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017789	C	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002908 InterPro:IPR036524	F	Seeded From UniProt	complete
involved_in	GO:0016226	iron-sulfur cluster assembly	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002908 InterPro:IPR036524	P	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017789	P	Seeded From UniProt	complete
enables	GO:0004322	ferroxidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.16.3.1	F	Seeded From UniProt	complete
involved_in	GO:0044281	small molecule metabolic process	Reactome:R-HSA-1430728	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-1362416 Reactome:R-HSA-1362408	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0006783	heme biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0350	P	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0409	P	Seeded From UniProt	complete
involved_in	GO:0006811	ion transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0406	P	Seeded From UniProt	complete
involved_in	GO:0055072	iron ion homeostasis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0410	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Zanella, I et al. (2008) The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin. Biochim. Biophys. Acta 1782 90-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Yoon, T & Cowan, JA (2003) Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 125 6078-84 PubMed GONUTS page
↑ ^3.0 ^3.1 Stehling, O et al. (2004) Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet. 13 3007-15 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Yoon, T & Cowan, JA (2004) Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 279 25943-6 PubMed GONUTS page
↑ Li, K et al. (2008) Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia. Hum. Mol. Genet. 17 2265-73 PubMed GONUTS page
↑ Correia, AR et al. (2008) Dynamics, stability and iron-binding activity of frataxin clinical mutants. FEBS J. 275 3680-90 PubMed GONUTS page
↑ ^7.0 ^7.1 Yoon, T et al. (2007) N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins. J. Biol. Inorg. Chem. 12 535-42 PubMed GONUTS page
↑ ^8.0 ^8.1 Condò, I et al. (2007) In vivo maturation of human frataxin. Hum. Mol. Genet. 16 1534-40 PubMed GONUTS page
↑ ^9.0 ^9.1 Condò, I et al. (2006) A pool of extramitochondrial frataxin that promotes cell survival. J. Biol. Chem. 281 16750-6 PubMed GONUTS page
↑ ^10.0 ^10.1 O'Neill, HA et al. (2005) Assembly of human frataxin is a mechanism for detoxifying redox-active iron. Biochemistry 44 537-45 PubMed GONUTS page
↑ Condò, I et al. (2010) Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum. Mol. Genet. 19 1221-9 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 ^12.6 ^12.7 ^12.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^13.0 ^13.1 Marelja, Z et al. (2018) Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Life Cycle by Controlling Cell Metabolism. Front Physiol 9 50 PubMed GONUTS page

[PMID:18160053-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Zanella, I et al. (2008) The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin. Biochim. Biophys. Acta 1782 90-8 PubMed GONUTS page

[PMID:12785837-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Yoon, T & Cowan, JA (2003) Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 125 6078-84 PubMed GONUTS page

[PMID:15509595-3] 3.0 ^3.1 Stehling, O et al. (2004) Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet. 13 3007-15 PubMed GONUTS page

[PMID:15123683-4] 4.0 ^4.1 ^4.2 ^4.3 Yoon, T & Cowan, JA (2004) Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 279 25943-6 PubMed GONUTS page

[PMID:18424449-5] Li, K et al. (2008) Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia. Hum. Mol. Genet. 17 2265-73 PubMed GONUTS page

[PMID:18537827-6] Correia, AR et al. (2008) Dynamics, stability and iron-binding activity of frataxin clinical mutants. FEBS J. 275 3680-90 PubMed GONUTS page

[PMID:17285345-7] 7.0 ^7.1 Yoon, T et al. (2007) N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins. J. Biol. Inorg. Chem. 12 535-42 PubMed GONUTS page

[PMID:17468497-8] 8.0 ^8.1 Condò, I et al. (2007) In vivo maturation of human frataxin. Hum. Mol. Genet. 16 1534-40 PubMed GONUTS page

[PMID:16608849-9] 9.0 ^9.1 Condò, I et al. (2006) A pool of extramitochondrial frataxin that promotes cell survival. J. Biol. Chem. 281 16750-6 PubMed GONUTS page

[PMID:15641778-10] 10.0 ^10.1 O'Neill, HA et al. (2005) Assembly of human frataxin is a mechanism for detoxifying redox-active iron. Biochemistry 44 537-45 PubMed GONUTS page

[PMID:20053667-11] Condò, I et al. (2010) Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum. Mol. Genet. 19 1221-9 PubMed GONUTS page

[PMID:21873635-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 ^12.6 ^12.7 ^12.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:29491838-13] 13.0 ^13.1 Marelja, Z et al. (2018) Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Life Cycle by Controlling Cell Metabolism. Front Physiol 9 50 PubMed GONUTS page

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HUMAN:FRDA

Contents

Annotations

Notes

References

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