Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P07954

- FUMH_HUMAN

UniProt

P07954 - FUMH_HUMAN

Protein

Fumarate hydratase, mitochondrial

Gene

FH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 3 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.
    Orphaneti523. Familial leiomyomatosis.
    24. Fumaric aciduria.
    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

    ArrayExpressiP07954.
    BgeeiP07954.
    CleanExiHS_FH.
    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 – 556
    Beta strandi58 – 636
    Helixi70 – 789
    Helixi84 – 863
    Helixi90 – 10617
    Helixi107 – 1104
    Helixi114 – 12815
    Helixi133 – 1353
    Beta strandi139 – 1424
    Helixi147 – 16418
    Helixi177 – 1815
    Turni182 – 1843
    Helixi187 – 20519
    Helixi207 – 22418
    Turni225 – 2273
    Beta strandi229 – 2346
    Beta strandi237 – 2437
    Helixi244 – 26421
    Turni267 – 2693
    Beta strandi270 – 2723
    Turni277 – 2793
    Helixi289 – 30113
    Helixi311 – 3166
    Helixi319 – 34527
    Beta strandi349 – 3524
    Helixi375 – 39925
    Helixi409 – 43325
    Helixi435 – 4373
    Helixi442 – 45110
    Helixi454 – 4596
    Helixi460 – 4634
    Helixi465 – 47814
    Helixi482 – 4887
    Helixi494 – 5007
    Helixi503 – 5053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MYRALRLLAR SRPLVRAPAA ALASAPGLGG AAVPSFWPPN AARMASQNSF    50
    RIEYDTFGEL KVPNDKYYGA QTVRSTMNFK IGGVTERMPT PVIKAFGILK 100
    RAAAEVNQDY GLDPKIANAI MKAADEVAEG KLNDHFPLVV WQTGSGTQTN 150
    MNVNEVISNR AIEMLGGELG SKIPVHPNDH VNKSQSSNDT FPTAMHIAAA 200
    IEVHEVLLPG LQKLHDALDA KSKEFAQIIK IGRTHTQDAV PLTLGQEFSG 250
    YVQQVKYAMT RIKAAMPRIY ELAAGGTAVG TGLNTRIGFA EKVAAKVAAL 300
    TGLPFVTAPN KFEALAAHDA LVELSGAMNT TACSLMKIAN DIRFLGSGPR 350
    SGLGELILPE NEPGSSIMPG KVNPTQCEAM TMVAAQVMGN HVAVTVGGSN 400
    GHFELNVFKP MMIKNVLHSA RLLGDASVSF TENCVVGIQA NTERINKLMN 450
    ESLMLVTALN PHIGYDKAAK IAKTAHKNGS TLKETAIELG YLTAEQFDEW 500
    VKPKDMLGPK 510
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 523. Familial leiomyomatosis.
    24. Fumaric aciduria.
    PharmGKBi PA28139.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0114.
    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

    ArrayExpressi P07954.
    Bgeei P07954.
    CleanExi HS_FH.
    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

    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: October 1, 2014
    This is version 174 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