Skip Header

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

UniProtKB - P97807 (FUMH_MOUSE)

Entry version 188 (02 Jun 2021)
Sequence version 3 (27 Jul 2011)
Previous versions | rss
Add a publicationFeedback
Protein

Fumarate hydratase, mitochondrial

Gene

Fh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:23643539).

Experiments in different species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable).

Curated1 Publication

Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH.

By similarity

Catalyzes the dehydration of L-malate to fumarate (PubMed:23643539).

Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism (PubMed:23643539).

Also plays a role in DNA repair by promoting non-homologous end-joining (NHEJ) (By similarity).

In response to DNA damage and phosphorylation by PRKDC, translocates to the nucleus and accumulates at DNA double-strand breaks (DSBs): acts by catalyzing formation of fumarate, an inhibitor of KDM2B histone demethylase activity, resulting in enhanced dimethylation of histone H3 'Lys-36' (H3K36me2) (By similarity).

By similarity1 Publication

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.By similarity This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei231SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei232Proton donor/acceptorBy similarity1
Active sitei362By similarity1
Binding sitei363SubstrateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei375Important for catalytic activityBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processDNA damage, DNA repair, Tricarboxylic acid cycle

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-71403, Citric acid cycle (TCA cycle)

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00223;UER01007

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fumarate hydratase, mitochondrial1 Publication (EC:4.2.1.21 Publication)
Short name:
Fumarase1 Publication
Alternative name(s):
EF-3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Fh1 PublicationImported
Synonyms:Fh11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:95530, Fh1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chromosome, Cytoplasm, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic lethality (PubMed:17418408). Conditional deletion in the kidney leads to the development of renal cysts, reminiscent of hereditary leiomyomatosis and renal cell cancer (HLRCC) phenotype in human (PubMed:17418408). Renal cysts are caused by accumulation of fumarate that promotes the formation of non-enzymatic post-translational modification cysteine S-succination (S-(2-succinyl)cysteine) on proteins, such as Keap1 (PubMed:22014577).2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 41MitochondrionBy similarityAdd BLAST41
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001032342 – 507Fumarate hydratase, mitochondrialAdd BLAST466
Isoform Cytoplasmic (identifier: P97807-2)
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei58N6-acetyllysine; alternateCombined sources1
Modified residuei58N6-succinyllysine; alternateCombined sources1
Modified residuei63N6-acetyllysine; alternateCombined sources1
Modified residuei63N6-succinyllysine; alternateCombined sources1
Modified residuei77N6-acetyllysine; alternateCombined sources1
Modified residuei77N6-succinyllysine; alternateCombined sources1
Modified residuei82PhosphothreonineCombined sources1
Modified residuei112N6-acetyllysine; alternateCombined sources1
Modified residuei112N6-succinyllysine; alternateCombined sources1
Modified residuei119N6-acetyllysine; alternateCombined sources1
Modified residuei119N6-succinyllysine; alternateCombined sources1
Modified residuei210N6-acetyllysineCombined sources1
Modified residuei220N6-acetyllysine; alternateCombined sources1
Modified residuei220N6-succinyllysine; alternateCombined sources1
Modified residuei233PhosphothreonineBy similarity1
Modified residuei289N6-acetyllysine; alternateCombined sources1
Modified residuei289N6-succinyllysine; alternateCombined sources1
Modified residuei363PhosphoserineCombined sources1
Modified residuei464N6-succinyllysineCombined sources1
Modified residuei470N6-succinyllysineCombined sources1
Modified residuei499N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Thr-233 by PRKDC in response to DNA damage promotes translocation to the nucleus and recruitment to DNA double-strand breaks (DSBs).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3579

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P97807

MaxQB - The MaxQuant DataBase

More...MaxQBi		P97807

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P97807

PeptideAtlas

More...PeptideAtlasi		P97807

PRoteomics IDEntifications database

More...PRIDEi		P97807

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		271643 [P97807-1]
271644 [P97807-2]

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00759940
P97807

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P97807

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P97807

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P97807

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000026526, Expressed in brown adipose tissue and 325 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P97807, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

Interacts with H2AZ1.

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		199665, 22 interactors

Protein interaction database and analysis system

More...IntActi		P97807, 6 interactors

Molecular INTeraction database

More...MINTi		P97807

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000027810

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P97807, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P97807

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni142 – 144Substrate bindingBy similarity3
Regioni173 – 176Substrate binding (B site)By similarity4
Regioni183 – 185Substrate bindingBy similarity3
Regioni368 – 370Substrate bindingBy similarity3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1317, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183122

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021594_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P97807

Identification of Orthologs from Complete Genome Data

More...OMAi		HDSMGEV

Database of Orthologous Groups

More...OrthoDBi		1022919at2759

TreeFam database of animal gene trees

More...TreeFami		TF300441

Family and domain databases

Conserved Domains Database

More...CDDi		cd01362, Fumarase_classII, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.275.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00743, FumaraseC, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
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

The PANTHER Classification System

More...PANTHERi		PTHR11444, PTHR11444, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10415, FumaraseC_C, 1 hit
PF00206, Lyase_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00149, FUMRATELYASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48557, SSF48557, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00979, fumC_II, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00163, FUMARATE_LYASES, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform Mitochondrial (identifier: P97807-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE 
        60         70         80         90        100
FDTFGELKVP TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA 
       110        120        130        140        150
AEVNQEYGLD PKIASAIMKA ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV 
       160        170        180        190        200
NEVISNRAIE MLGGELGSKK PVHPNDHVNK SQSSNDTFPT AMHIAAAVEV 
       210        220        230        240        250
HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT LGQEFSGYVQ 
       260        270        280        290        300
QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL 
       310        320        330        340        350
PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL 
       360        370        380        390        400
GELILPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF 
       410        420        430        440        450
ELNVFKPMMI KNVLHSARLL GDASVSFTDN CVVGIQANTE RINKLMNESL 
       460        470        480        490        500
MLVTALNPHI GYDKAAKIAK TAHKNGSTLK ETAIELGYLT AEQFDEWVKP 

KDMLGPK
Length:507
Mass (Da):54,357
Last modified:July 27, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BKG7H3BKG7_MOUSE
Fumarate hydratase 1
Fh1
167Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BJV5H3BJV5_MOUSE
Fumarate hydratase 1
Fh1
61Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti183S → N in AK002379 (PubMed:16141072).Curated1
Sequence conflicti236A → T in AK002379 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0189671 – 40Missing in isoform Cytoplasmic. CuratedAdd BLAST40

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS15547.1 [P97807-1]

NCBI Reference Sequences

More...RefSeqi		NP_034339.2, NM_010209.2 [P97807-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526 [P97807-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		14194

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:14194

UCSC genome browser

More...UCSCi		uc007dtn.2, mouse [P97807-1]

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

3D structure databases

SMRiP97807
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi199665, 22 interactors
IntActiP97807, 6 interactors
MINTiP97807
STRINGi10090.ENSMUSP00000027810

PTM databases

iPTMnetiP97807
PhosphoSitePlusiP97807
SwissPalmiP97807

2D gel databases

REPRODUCTION-2DPAGEiIPI00759940
P97807

Proteomic databases

CPTACinon-CPTAC-3579
jPOSTiP97807
MaxQBiP97807
PaxDbiP97807
PeptideAtlasiP97807
PRIDEiP97807
ProteomicsDBi271643 [P97807-1]
271644 [P97807-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		34701, 647 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		14194
MGIiMGI:95530, Fh1

Phylogenomic databases

eggNOGiKOG1317, Eukaryota
GeneTreeiENSGT00950000183122
HOGENOMiCLU_021594_4_1_1
InParanoidiP97807
OMAiHDSMGEV
OrthoDBi1022919at2759
TreeFamiTF300441

Enzyme and pathway databases

UniPathwayiUPA00223;UER01007
ReactomeiR-MMU-71403, Citric acid cycle (TCA cycle)

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		14194, 19 hits in 54 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Fh1, mouse

Protein Ontology

More...PROi		PR:P97807
RNActiP97807, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000026526, Expressed in brown adipose tissue and 325 other tissues
GenevisibleiP97807, MM

Family and domain databases

CDDicd01362, Fumarase_classII, 1 hit
Gene3Di1.10.275.10, 1 hit
HAMAPiMF_00743, FumaraseC, 1 hit
InterProiView protein in InterPro
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
PANTHERiPTHR11444, PTHR11444, 1 hit
PfamiView protein in Pfam
PF10415, FumaraseC_C, 1 hit
PF00206, Lyase_1, 1 hit
PRINTSiPR00149, FUMRATELYASE
SUPFAMiSSF48557, SSF48557, 1 hit
TIGRFAMsiTIGR00979, fumC_II, 1 hit
PROSITEiView protein in PROSITE
PS00163, FUMARATE_LYASES, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFUMH_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P97807
Secondary accession number(s): Q3UIA9, Q99JL0, Q9DCX0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: June 2, 2021
This is version 188 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again