HUMAN:FUMH

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FH
Protein Name(s)	Fumarate hydratase, mitochondrial Fumarase
External Links
UniProt	P07954
EMBL	U59309 U48857 BT009839 AK312415 CH471098 BC003108 BC017444 M15502
CCDS	CCDS1617.1
PIR	S06213
RefSeq	NP_000134.2
UniGene	Hs.592490
PDB	3E04 5D6B 5UPP
PDBsum	3E04 5D6B 5UPP
ProteinModelPortal	P07954
SMR	P07954
BioGrid	108562
DIP	DIP-46920N
IntAct	P07954
STRING	9606.ENSP00000355518
iPTMnet	P07954
PhosphoSitePlus	P07954
SwissPalm	P07954
BioMuta	FH
DMDM	1730117
REPRODUCTION-2DPAGE	IPI00296053
SWISS-2DPAGE	P07954
UCD-2DPAGE	P07954
EPD	P07954
MaxQB	P07954
PaxDb	P07954
PeptideAtlas	P07954
PRIDE	P07954
TopDownProteomics	P07954-2
DNASU	2271
Ensembl	ENST00000366560
GeneID	2271
KEGG	hsa:2271
UCSC	uc001hyx.4
CTD	2271
DisGeNET	2271
EuPathDB	HostDB:ENSG00000091483.6
GeneCards	FH
GeneReviews	FH
HGNC	HGNC:3700
HPA	CAB017785 HPA025770 HPA025948 HPA027341
MalaCards	FH
MIM	136850 150800 606812
neXtProt	NX_P07954
OpenTargets	ENSG00000091483
Orphanet	24 523 29072
PharmGKB	PA28139
eggNOG	KOG1317 COG0114
GeneTree	ENSGT00390000002779
HOGENOM	HOG000061736
HOVERGEN	HBG002183
InParanoid	P07954
KO	K01679
OMA	VSFTDNC
OrthoDB	EOG091G05UL
PhylomeDB	P07954
TreeFam	TF300441
BioCyc	MetaCyc:ENSG00000091483-MONOMER
BRENDA	4.2.1.2
Reactome	R-HSA-71403
UniPathway	UPA00223
EvolutionaryTrace	P07954
GenomeRNAi	2271
PRO	PR:P07954
Proteomes	UP000005640
Bgee	ENSG00000091483
CleanEx	HS_FH
ExpressionAtlas	P07954
Genevisible	P07954
GO	GO:0005737 GO:0070062 GO:0005759 GO:0005739 GO:0045239 GO:0004333 GO:0006106 GO:0048873 GO:0006108 GO:0006099
CDD	cd01362
Gene3D	1.10.275.10
HAMAP	MF_00743
InterPro	IPR005677 IPR024083 IPR018951 IPR020557 IPR000362 IPR022761 IPR008948
PANTHER	PTHR11444
Pfam	PF10415 PF00206
PRINTS	PR00149
SUPFAM	SSF48557
TIGRFAMs	TIGR00979
PROSITE	PS00163

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004333	fumarate hydratase activity	PMID:29456767^[1]	ECO:0000315			F		Figure 5 shows the HsFH mutants, A308T and H318Y, decrease in enzyme function.	complete CACAO 13248
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	PMID:27554470^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P97807	P		Seeded From UniProt	complete
involved_in	GO:0006106	fumarate metabolic process	PMID:30761759^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006108	malate metabolic process	PMID:30761759^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	PMID:30761759^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20833797^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001134)	Seeded From UniProt	complete
involved_in	GO:0006108	malate metabolic process	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154499 RGD:2614	P		Seeded From UniProt	complete
involved_in	GO:0006106	fumarate metabolic process	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154499 RGD:2614 SGD:S000006183 UniProtKB:Q9FI53	P		Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154499 RGD:2614 SGD:S000006183	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000154501 RGD:2614 SGD:S000006183 TAIR:locus:2061966 UniProtKB:P07954 UniProtKB:Q9FI53	C		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10358 PANTHER:PTN000154499 RGD:2614 SGD:S000006183 UniProtKB:P07954 UniProtKB:Q9FI53	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97807 ensembl:ENSMUSP00000027810	P		Seeded From UniProt	complete
involved_in	GO:0048873	homeostasis of number of cells within a tissue	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97807 ensembl:ENSMUSP00000027810	P		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008948 InterPro:IPR020557	F		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005677	F		Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018951	P		Seeded From UniProt	complete
involved_in	GO:0006106	fumarate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005677	P		Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018951	F		Seeded From UniProt	complete
part_of	GO:0045239	tricarboxylic acid cycle enzyme complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005677	C		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.1.2	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:27037871^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000821	regulation of arginine metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P97807-2	P		Seeded From UniProt	complete
acts_upstream_of	GO:0000050	urea cycle	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P97807-2	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:20231875^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:20231875^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20231875^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:27037871^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006106	fumarate metabolic process	PMID:30718813^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	PMID:30718813^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:26237645^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0S5	F		Seeded From UniProt	complete
involved_in	GO:0000415	negative regulation of histone H3-K36 methylation	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:2001034	positive regulation of double-strand break repair via nonhomologous end joining	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006106	fumarate metabolic process	PMID:26237645^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006106	fumarate metabolic process	PMID:8200987^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:8200987^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:8200987^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004333	fumarate hydratase activity	PMID:3828494^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	Reactome:R-HSA-71403	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-70982 Reactome:R-HSA-451033	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F		Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0816 UniPathway:UPA00223	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
edit table

Notes

References

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

↑ Bulku, A et al. (2018) Biochemical Characterization of Two Clinically-Relevant Human Fumarase Variants Defective for Oligomerization. Open Biochem J 12 1-15 PubMed GONUTS page
↑ Yang, H et al. (2016) Adipose-Specific Deficiency of Fumarate Hydratase in Mice Protects Against Obesity, Hepatic Steatosis, and Insulin Resistance. Diabetes 65 3396-3409 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Ajalla Aleixo, MA et al. (2019) Structural, biochemical and biophysical characterization of recombinant human fumarate hydratase. FEBS J. PubMed GONUTS page
↑ ^4.0 ^4.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^7.0 ^7.1 Dik, E et al. (2016) Human Fumarate Hydratase Is Dual Localized by an Alternative Transcription Initiation Mechanism. Traffic 17 720-32 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Yogev, O et al. (2010) Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response. PLoS Biol. 8 e1000328 PubMed GONUTS page
↑ ^9.0 ^9.1 Kulkarni, RA et al. (2019) A chemoproteomic portrait of the oncometabolite fumarate. Nat. Chem. Biol. 15 391-400 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 Jiang, Y et al. (2015) Local generation of fumarate promotes DNA repair through inhibition of histone H3 demethylation. Nat. Cell Biol. 17 1158-68 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Bourgeron, T et al. (1994) Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency. J. Clin. Invest. 93 2514-8 PubMed GONUTS page
↑ Kinsella, BT & Doonan, S (1986) Nucleotide sequence of a cDNA coding for mitochondrial fumarase from human liver. Biosci. Rep. 6 921-9 PubMed GONUTS page

[PMID:29456767-1] Bulku, A et al. (2018) Biochemical Characterization of Two Clinically-Relevant Human Fumarase Variants Defective for Oligomerization. Open Biochem J 12 1-15 PubMed GONUTS page

[PMID:27554470-2] Yang, H et al. (2016) Adipose-Specific Deficiency of Fumarate Hydratase in Mice Protects Against Obesity, Hepatic Steatosis, and Insulin Resistance. Diabetes 65 3396-3409 PubMed GONUTS page

[PMID:30761759-3] 3.0 ^3.1 ^3.2 Ajalla Aleixo, MA et al. (2019) Structural, biochemical and biophysical characterization of recombinant human fumarate hydratase. FEBS J. PubMed GONUTS page

[PMID:20458337-4] 4.0 ^4.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:20833797-5] Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page

[PMID:21873635-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 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:27037871-7] 7.0 ^7.1 Dik, E et al. (2016) Human Fumarate Hydratase Is Dual Localized by an Alternative Transcription Initiation Mechanism. Traffic 17 720-32 PubMed GONUTS page

[PMID:20231875-8] 8.0 ^8.1 ^8.2 Yogev, O et al. (2010) Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response. PLoS Biol. 8 e1000328 PubMed GONUTS page

[PMID:30718813-9] 9.0 ^9.1 Kulkarni, RA et al. (2019) A chemoproteomic portrait of the oncometabolite fumarate. Nat. Chem. Biol. 15 391-400 PubMed GONUTS page

[PMID:26237645-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 Jiang, Y et al. (2015) Local generation of fumarate promotes DNA repair through inhibition of histone H3 demethylation. Nat. Cell Biol. 17 1158-68 PubMed GONUTS page

[PMID:8200987-11] 11.0 ^11.1 ^11.2 Bourgeron, T et al. (1994) Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency. J. Clin. Invest. 93 2514-8 PubMed GONUTS page

[PMID:3828494-12] Kinsella, BT & Doonan, S (1986) Nucleotide sequence of a cDNA coding for mitochondrial fumarase from human liver. Biosci. Rep. 6 921-9 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

HUMAN:FUMH

Contents

Annotations

Notes

References

c

d

e

f

h

l

m

n

o

p

r

s

t

u

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools