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)

P97807

- FUMH_MOUSE

UniProt

P97807 - FUMH_MOUSE

Protein

Fumarate hydratase, mitochondrial

Gene

Fh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei144 – 1441SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fumarate metabolic process Source: InterPro
    2. homeostasis of number of cells within a tissue Source: MGI
    3. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase
    Alternative name(s):
    EF-3
    Gene namesi
    Name:Fh
    Synonyms:Fh1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:95530. Fh1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4141MitochondrionBy similarityAdd
    BLAST
    Chaini42 – 507466Fumarate hydratase, mitochondrialPRO_0000010323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine; alternate1 Publication
    Modified residuei58 – 581N6-succinyllysine; alternate1 Publication
    Modified residuei63 – 631N6-acetyllysine; alternate2 Publications
    Modified residuei63 – 631N6-succinyllysine; alternate1 Publication
    Modified residuei77 – 771N6-acetyllysine; alternate1 Publication
    Modified residuei77 – 771N6-succinyllysine; alternate1 Publication
    Modified residuei112 – 1121N6-acetyllysine; alternate1 Publication
    Modified residuei112 – 1121N6-succinyllysine; alternate1 Publication
    Modified residuei119 – 1191N6-acetyllysine; alternate1 Publication
    Modified residuei119 – 1191N6-succinyllysine; alternate1 Publication
    Modified residuei210 – 2101N6-acetyllysine1 Publication
    Modified residuei220 – 2201N6-acetyllysine; alternate1 Publication
    Modified residuei220 – 2201N6-succinyllysine; alternate1 Publication
    Modified residuei289 – 2891N6-acetyllysine; alternate1 Publication
    Modified residuei289 – 2891N6-succinyllysine; alternate1 Publication
    Modified residuei464 – 4641N6-succinyllysine1 Publication
    Modified residuei470 – 4701N6-succinyllysine1 Publication
    Modified residuei499 – 4991N6-acetyllysine1 Publication

    Post-translational modificationi

    Isoform Cytoplasmic is acetylated at position 2.By similarity
    Acetylation of Lys-474 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP97807.
    PaxDbiP97807.
    PRIDEiP97807.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00759940.
    P97807.

    PTM databases

    PhosphoSiteiP97807.

    Expressioni

    Gene expression databases

    ArrayExpressiP97807.
    BgeeiP97807.
    CleanExiMM_FH1.
    GenevestigatoriP97807.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiP97807. 6 interactions.
    MINTiMINT-1859341.

    Structurei

    3D structure databases

    ProteinModelPortaliP97807.
    SMRiP97807. Positions 46-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 1764B siteBy similarity
    Regioni183 – 1853Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    GeneTreeiENSGT00390000002779.
    HOGENOMiHOG000061736.
    HOVERGENiHBG002183.
    InParanoidiQ3UIA9.
    KOiK01679.
    OMAiMESFNIH.
    OrthoDBiEOG75J0MX.
    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: P97807-1) [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 SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE    50
    FDTFGELKVP TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA 100
    AEVNQEYGLD PKIASAIMKA ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV 150
    NEVISNRAIE MLGGELGSKK PVHPNDHVNK SQSSNDTFPT AMHIAAAVEV 200
    HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT LGQEFSGYVQ 250
    QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL 300
    PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL 350
    GELILPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF 400
    ELNVFKPMMI KNVLHSARLL GDASVSFTDN CVVGIQANTE RINKLMNESL 450
    MLVTALNPHI GYDKAAKIAK TAHKNGSTLK ETAIELGYLT AEQFDEWVKP 500
    KDMLGPK 507
    Length:507
    Mass (Da):54,357
    Last modified:July 27, 2011 - v3
    Checksum:i2F24F7B089608ABE
    GO
    Isoform Cytoplasmic (identifier: P97807-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: Missing.

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

    Show »
    Length:467
    Mass (Da):50,053
    Checksum:i95ECA9B728E029AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti183 – 1831S → N in AK002379. (PubMed:16141072)Curated
    Sequence conflicti236 – 2361A → T in AK002379. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040Missing in isoform Cytoplasmic. CuratedVSP_018967Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002379 mRNA. No translation available.
    AK147000 mRNA. Translation: BAE27597.1.
    CH466555 Genomic DNA. Translation: EDL13210.1.
    BC006048 mRNA. Translation: AAH06048.1.
    U72679 mRNA. Translation: AAB51039.1.
    CCDSiCCDS15547.1. [P97807-1]
    RefSeqiNP_034339.2. NM_010209.2. [P97807-1]
    UniGeneiMm.41502.

    Genome annotation databases

    EnsembliENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526. [P97807-1]
    GeneIDi14194.
    KEGGimmu:14194.
    UCSCiuc007dtn.2. mouse. [P97807-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002379 mRNA. No translation available.
    AK147000 mRNA. Translation: BAE27597.1 .
    CH466555 Genomic DNA. Translation: EDL13210.1 .
    BC006048 mRNA. Translation: AAH06048.1 .
    U72679 mRNA. Translation: AAB51039.1 .
    CCDSi CCDS15547.1. [P97807-1 ]
    RefSeqi NP_034339.2. NM_010209.2. [P97807-1 ]
    UniGenei Mm.41502.

    3D structure databases

    ProteinModelPortali P97807.
    SMRi P97807. Positions 46-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97807. 6 interactions.
    MINTi MINT-1859341.

    PTM databases

    PhosphoSitei P97807.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00759940.
    P97807.

    Proteomic databases

    MaxQBi P97807.
    PaxDbi P97807.
    PRIDEi P97807.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027810 ; ENSMUSP00000027810 ; ENSMUSG00000026526 . [P97807-1 ]
    GeneIDi 14194.
    KEGGi mmu:14194.
    UCSCi uc007dtn.2. mouse. [P97807-1 ]

    Organism-specific databases

    CTDi 14194.
    MGIi MGI:95530. Fh1.

    Phylogenomic databases

    eggNOGi COG0114.
    GeneTreei ENSGT00390000002779.
    HOGENOMi HOG000061736.
    HOVERGENi HBG002183.
    InParanoidi Q3UIA9.
    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG75J0MX.
    TreeFami TF300441.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    Miscellaneous databases

    NextBioi 285416.
    PROi P97807.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97807.
    Bgeei P97807.
    CleanExi MM_FH1.
    Genevestigatori P97807.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart and Kidney.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
    4. "E2a-Pbx1 induces aberrant expression of tissue-specific and developmentally regulated genes when expressed in NIH 3T3 fibroblasts."
      Fu X., Kamps M.P.
      Mol. Cell. Biol. 17:1503-1512(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-282.
    5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 49-71; 85-97; 99-112; 129-157; 181-210; 231-258; 266-283; 294-308; 348-368; 419-441; 445-464 AND 481-501, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-58; LYS-63; LYS-77; LYS-112; LYS-119; LYS-220; LYS-289; LYS-464 AND LYS-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58; LYS-63; LYS-77; LYS-112; LYS-119; LYS-210; LYS-220; LYS-289 AND LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiFUMH_MOUSE
    AccessioniPrimary (citable) accession number: P97807
    Secondary accession number(s): Q3UIA9, Q99JL0, Q9DCX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3