SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P97807

- FUMH_MOUSE

UniProt

P97807 - FUMH_MOUSE

(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)

Protein
Fumarate hydratase, mitochondrial
Gene
Fh, Fh1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441Substrate By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141Mitochondrion By similarity
Add
BLAST
Chaini42 – 507466Fumarate hydratase, mitochondrialUniRule annotation
PRO_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.UniRule annotation
Acetylation of Lys-474 is observed in liver mitochondria from fasted mice but not from fed mice.UniRule annotation

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.UniRule annotation

Protein-protein interaction databases

IntActiP97807. 6 interactions.
MINTiMINT-1859341.

Structurei

3D structure databases

ProteinModelPortaliP97807.
SMRiP97807. Positions 46-507.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 1764B site By similarity
Regioni183 – 1853Substrate binding By 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).

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040Missing in isoform Cytoplasmic.
VSP_018967Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831S → N in AK002379. 1 Publication
Sequence conflicti236 – 2361A → T in AK002379. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 137 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.

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

Similar proteinsi