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P07954

- FUMH_HUMAN

UniProt

P07954 - FUMH_HUMAN

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Protein

Fumarate hydratase, mitochondrial

Gene

FH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Also acts as a tumor suppressor.

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471SubstrateBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: Reactome

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. fumarate metabolic process Source: ProtInc
  3. homeostasis of number of cells within a tissue Source: Ensembl
  4. small molecule metabolic process Source: Reactome
  5. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000091483-MONOMER.
BRENDAi4.2.1.2. 2681.
ReactomeiREACT_1785. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:FH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3700. FH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: UniProt
  5. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Fumarase deficiency (FHD) [MIM:606812]: Characterized by progressive encephalopathy, developmental delay, hypotonia, cerebral atrophy and lactic and pyruvic acidemia.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti230 – 2301K → R in FHD and HLRCC. 2 Publications
VAR_002445
Natural varianti308 – 3081A → T in FHD. 2 Publications
VAR_002446
Natural varianti312 – 3121F → C in FHD. 1 Publication
VAR_002447
Natural varianti425 – 4251D → V in FHD. 1 Publication
VAR_002448
Hereditary leiomyomatosis and renal cell cancer (HLRCC) [MIM:150800]: A disorder characterized by predisposition to cutaneous and uterine leiomyomas, and papillary type 2 renal cancer which occurs in about 20% of patients.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071N → T in HLRCC. 1 Publication
VAR_013497
Natural varianti117 – 1171A → P in HLRCC. 1 Publication
VAR_013498
Natural varianti180 – 1801H → R in HLRCC. 1 Publication
VAR_013499
Natural varianti185 – 1851Q → R in HLRCC. 1 Publication
VAR_013500
Natural varianti230 – 2301K → R in FHD and HLRCC. 2 Publications
VAR_002445
Natural varianti233 – 2331R → H in HLRCC. 1 Publication
Corresponds to variant rs28933069 [ dbSNP | Ensembl ].
VAR_013501
Natural varianti282 – 2821G → V in HLRCC. 1 Publication
VAR_013502
Natural varianti328 – 3281M → R in HLRCC. 1 Publication
VAR_013503

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi150800. phenotype.
606812. phenotype.
Orphaneti24. Fumaric aciduria.
523. Hereditary leiomyomatosis and renal cell cancer.
29072. Hereditary pheochromocytoma-paraganglioma.
PharmGKBiPA28139.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4444MitochondrionBy similarityAdd
BLAST
Chaini45 – 510466Fumarate hydratase, mitochondrialPRO_0000010319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N6-acetyllysine; alternateBy similarity
Modified residuei61 – 611N6-succinyllysine; alternateBy similarity
Modified residuei66 – 661N6-acetyllysine; alternate1 Publication
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Modified residuei80 – 801N6-acetyllysine; alternate1 Publication
Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
Modified residuei94 – 941N6-acetyllysine1 Publication
Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
Modified residuei213 – 2131N6-acetyllysineBy similarity
Modified residuei223 – 2231N6-acetyllysine; alternateBy similarity
Modified residuei223 – 2231N6-succinyllysine; alternateBy similarity
Modified residuei256 – 2561N6-acetyllysine1 Publication
Modified residuei292 – 2921N6-acetyllysine; alternate1 Publication
Modified residuei292 – 2921N6-succinyllysine; alternateBy similarity
Modified residuei467 – 4671N6-succinyllysineBy similarity
Modified residuei473 – 4731N6-succinyllysineBy similarity
Modified residuei502 – 5021N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP07954.
PaxDbiP07954.
PRIDEiP07954.

2D gel databases

REPRODUCTION-2DPAGEIPI00296053.
SWISS-2DPAGEP07954.
UCD-2DPAGEP07954.

PTM databases

PhosphoSiteiP07954.

Expressioni

Tissue specificityi

Expressed in red blood cells; underexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.1 Publication

Gene expression databases

BgeeiP07954.
CleanExiHS_FH.
ExpressionAtlasiP07954. baseline and differential.
GenevestigatoriP07954.

Organism-specific databases

HPAiCAB017785.
HPA025770.
HPA025948.
HPA027341.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi108562. 37 interactions.
IntActiP07954. 6 interactions.
MINTiMINT-5005927.
STRINGi9606.ENSP00000355518.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 556Combined sources
Beta strandi58 – 636Combined sources
Helixi70 – 789Combined sources
Helixi84 – 863Combined sources
Helixi90 – 10617Combined sources
Helixi107 – 1104Combined sources
Helixi114 – 12815Combined sources
Helixi133 – 1353Combined sources
Beta strandi139 – 1424Combined sources
Helixi147 – 16418Combined sources
Helixi177 – 1815Combined sources
Turni182 – 1843Combined sources
Helixi187 – 20519Combined sources
Helixi207 – 22418Combined sources
Turni225 – 2273Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi237 – 2437Combined sources
Helixi244 – 26421Combined sources
Turni267 – 2693Combined sources
Beta strandi270 – 2723Combined sources
Turni277 – 2793Combined sources
Helixi289 – 30113Combined sources
Helixi311 – 3166Combined sources
Helixi319 – 34527Combined sources
Beta strandi349 – 3524Combined sources
Helixi375 – 39925Combined sources
Helixi409 – 43325Combined sources
Helixi435 – 4373Combined sources
Helixi442 – 45110Combined sources
Helixi454 – 4596Combined sources
Helixi460 – 4634Combined sources
Helixi465 – 47814Combined sources
Helixi482 – 4887Combined sources
Helixi494 – 5007Combined sources
Helixi503 – 5053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E04X-ray1.95A/B/C/D44-510[»]
ProteinModelPortaliP07954.
SMRiP07954. Positions 49-510.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07954.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 1794B siteBy similarity
Regioni186 – 1883Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0114.
GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
HOVERGENiHBG002183.
InParanoidiP07954.
KOiK01679.
OMAiMFSGPMT.
OrthoDBiEOG75J0MX.
PhylomeDBiP07954.
TreeFamiTF300441.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Mitochondrial (identifier: P07954-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYRALRLLAR SRPLVRAPAA ALASAPGLGG AAVPSFWPPN AARMASQNSF
60 70 80 90 100
RIEYDTFGEL KVPNDKYYGA QTVRSTMNFK IGGVTERMPT PVIKAFGILK
110 120 130 140 150
RAAAEVNQDY GLDPKIANAI MKAADEVAEG KLNDHFPLVV WQTGSGTQTN
160 170 180 190 200
MNVNEVISNR AIEMLGGELG SKIPVHPNDH VNKSQSSNDT FPTAMHIAAA
210 220 230 240 250
IEVHEVLLPG LQKLHDALDA KSKEFAQIIK IGRTHTQDAV PLTLGQEFSG
260 270 280 290 300
YVQQVKYAMT RIKAAMPRIY ELAAGGTAVG TGLNTRIGFA EKVAAKVAAL
310 320 330 340 350
TGLPFVTAPN KFEALAAHDA LVELSGAMNT TACSLMKIAN DIRFLGSGPR
360 370 380 390 400
SGLGELILPE NEPGSSIMPG KVNPTQCEAM TMVAAQVMGN HVAVTVGGSN
410 420 430 440 450
GHFELNVFKP MMIKNVLHSA RLLGDASVSF TENCVVGIQA NTERINKLMN
460 470 480 490 500
ESLMLVTALN PHIGYDKAAK IAKTAHKNGS TLKETAIELG YLTAEQFDEW
510
VKPKDMLGPK
Length:510
Mass (Da):54,637
Last modified:October 1, 1996 - v3
Checksum:i86F91F95DC046F64
GO
Isoform Cytoplasmic (identifier: P07954-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).By similarity

Show »
Length:467
Mass (Da):50,213
Checksum:i5E1AC7903B062540
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071N → T in HLRCC. 1 Publication
VAR_013497
Natural varianti117 – 1171A → P in HLRCC. 1 Publication
VAR_013498
Natural varianti180 – 1801H → R in HLRCC. 1 Publication
VAR_013499
Natural varianti185 – 1851Q → R in HLRCC. 1 Publication
VAR_013500
Natural varianti230 – 2301K → R in FHD and HLRCC. 2 Publications
VAR_002445
Natural varianti233 – 2331R → H in HLRCC. 1 Publication
Corresponds to variant rs28933069 [ dbSNP | Ensembl ].
VAR_013501
Natural varianti282 – 2821G → V in HLRCC. 1 Publication
VAR_013502
Natural varianti308 – 3081A → T in FHD. 2 Publications
VAR_002446
Natural varianti312 – 3121F → C in FHD. 1 Publication
VAR_002447
Natural varianti328 – 3281M → R in HLRCC. 1 Publication
VAR_013503
Natural varianti425 – 4251D → V in FHD. 1 Publication
VAR_002448

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform Cytoplasmic. CuratedVSP_018965Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59309 mRNA. Translation: AAB66354.1.
U48857 mRNA. Translation: AAD00071.1.
BT009839 mRNA. Translation: AAP88841.1.
AK312415 mRNA. Translation: BAG35325.1.
CH471098 Genomic DNA. Translation: EAW70092.1.
BC003108 mRNA. Translation: AAH03108.1.
BC017444 mRNA. Translation: AAH17444.1.
M15502 mRNA. Translation: AAA52483.1.
CCDSiCCDS1617.1. [P07954-1]
PIRiS06213. UFHUM.
RefSeqiNP_000134.2. NM_000143.3. [P07954-1]
UniGeneiHs.592490.

Genome annotation databases

EnsembliENST00000366560; ENSP00000355518; ENSG00000091483. [P07954-1]
GeneIDi2271.
KEGGihsa:2271.
UCSCiuc001hyx.3. human. [P07954-1]

Polymorphism databases

DMDMi1730117.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

TCA Cycle Gene Mutation Database
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59309 mRNA. Translation: AAB66354.1 .
U48857 mRNA. Translation: AAD00071.1 .
BT009839 mRNA. Translation: AAP88841.1 .
AK312415 mRNA. Translation: BAG35325.1 .
CH471098 Genomic DNA. Translation: EAW70092.1 .
BC003108 mRNA. Translation: AAH03108.1 .
BC017444 mRNA. Translation: AAH17444.1 .
M15502 mRNA. Translation: AAA52483.1 .
CCDSi CCDS1617.1. [P07954-1 ]
PIRi S06213. UFHUM.
RefSeqi NP_000134.2. NM_000143.3. [P07954-1 ]
UniGenei Hs.592490.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E04 X-ray 1.95 A/B/C/D 44-510 [» ]
ProteinModelPortali P07954.
SMRi P07954. Positions 49-510.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108562. 37 interactions.
IntActi P07954. 6 interactions.
MINTi MINT-5005927.
STRINGi 9606.ENSP00000355518.

PTM databases

PhosphoSitei P07954.

Polymorphism databases

DMDMi 1730117.

2D gel databases

REPRODUCTION-2DPAGE IPI00296053.
SWISS-2DPAGE P07954.
UCD-2DPAGE P07954.

Proteomic databases

MaxQBi P07954.
PaxDbi P07954.
PRIDEi P07954.

Protocols and materials databases

DNASUi 2271.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366560 ; ENSP00000355518 ; ENSG00000091483 . [P07954-1 ]
GeneIDi 2271.
KEGGi hsa:2271.
UCSCi uc001hyx.3. human. [P07954-1 ]

Organism-specific databases

CTDi 2271.
GeneCardsi GC01M241660.
GeneReviewsi FH.
HGNCi HGNC:3700. FH.
HPAi CAB017785.
HPA025770.
HPA025948.
HPA027341.
MIMi 136850. gene.
150800. phenotype.
606812. phenotype.
neXtProti NX_P07954.
Orphaneti 24. Fumaric aciduria.
523. Hereditary leiomyomatosis and renal cell cancer.
29072. Hereditary pheochromocytoma-paraganglioma.
PharmGKBi PA28139.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0114.
GeneTreei ENSGT00390000002779.
HOGENOMi HOG000061736.
HOVERGENi HBG002183.
InParanoidi P07954.
KOi K01679.
OMAi MFSGPMT.
OrthoDBi EOG75J0MX.
PhylomeDBi P07954.
TreeFami TF300441.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci MetaCyc:ENSG00000091483-MONOMER.
BRENDAi 4.2.1.2. 2681.
Reactomei REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

EvolutionaryTracei P07954.
GenomeRNAii 2271.
NextBioi 9235.
PROi P07954.
SOURCEi Search...

Gene expression databases

Bgeei P07954.
CleanExi HS_FH.
ExpressionAtlasi P07954. baseline and differential.
Genevestigatori P07954.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Gellera C., Baratta S., Cavadini P., Invernizzi F., Lamantea E., Didonato S., Taroni F.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Complete cDNA sequence of the human fumarase."
    Bourgeron T., Parfait B., Chretien D., Rotig A., Munnich A., Rustin P.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Uterus.
  7. "Nucleotide sequence of a cDNA coding for mitochondrial fumarase from human liver."
    Kinsella B.T., Doonan S.
    Biosci. Rep. 6:921-929(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-510.
    Tissue: Liver.
  8. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 269-286 AND 422-444, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-80; LYS-94; LYS-256 AND LYS-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Assessment of the red cell proteome of young patients with unexplained hemolytic anemia by two-dimensional differential in-gel electrophoresis (DIGE)."
    von Lohneysen K., Scott T.M., Soldau K., Xu X., Friedman J.S.
    PLoS ONE 7:E34237-E34237(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of human fumarate hydratase."
    Structural genomics consortium (SGC)
    Submitted (DEC-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 44-510, SUBUNIT.
  14. "Identification of a molecular defect in a fumarase deficient patient and mapping of the fumarase gene."
    Coughlin E.M., Chalmers R.A., Slaugenhaupt S.A., Gusella J.F., Shih V.E., Ramesh V.
    Am. J. Hum. Genet. 53:A896-A896(1993)
    Cited for: VARIANT FHD THR-308.
  15. Cited for: VARIANTS FHD ARG-230; THR-308; CYS-312 AND VAL-425.
  16. Cited for: VARIANTS HLRCC THR-107; PRO-117; ARG-180; ARG-185; ARG-230; HIS-233; VAL-282 AND ARG-328.

Entry informationi

Entry nameiFUMH_HUMAN
AccessioniPrimary (citable) accession number: P07954
Secondary accession number(s): B1ANK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3