Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 173 (29 Sep 2021)
Sequence version 4 (27 Jul 2011)
Previous versions | rss
Add a publicationFeedback
Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

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

Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long straight chain fatty acids peroxisomal beta-oxidation pathway. Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species. Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity).

With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (Probable). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (PubMed:24075987).

Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (By similarity).

By similarity1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Enzyme activity enhanced by acetylation.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei99Substrate; via amide nitrogenBy 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>Sitei102Important for catalytic activityBy similarity1
Sitei122Important 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

GO - Biological processi

<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 functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandNAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-390247, Beta-oxidation of very long chain fatty acids
R-MMU-9033241, Peroxisomal protein import

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

More...
UniPathwayi
UPA00659

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000402
SLP:000000491

<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_and_taxonomy_section">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:
Peroxisomal bifunctional enzymeCurated
Short name:
PBE
Short name:
PBFE
Alternative name(s):
L-peroxisomal bifunctional enzyme1 Publication
Short name:
L-PBE1 Publication
Multifunctional enzyme 1
Short name:
MFE1
Multifunctional protein 11 Publication
Short name:
MFP-11 Publication
Including the following 2 domains:
Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.17, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:EhhadhImported
Synonyms:L-pbe1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 16

Organism-specific databases

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

More...
MGIi
MGI:1277964, Ehhadh

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSMUSG00000022853

<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

Peroxisome

<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

Mutant mice fed a normal chow are phenotypically indistinguishable from wild-types. Mutant mice fed coconut oil rapidly lose weight and most of them die within 3 weeks. They overaccumulate dicarboxylic fatty acids, which activate all fatty acid oxidation pathways and lead to liver inflammation, fibrosis, and death.1 Publication

<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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001092481 – 718Peroxisomal bifunctional enzymeAdd BLAST718

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 residuei38N6-succinyllysineCombined sources1
Modified residuei163N6-acetyllysine; alternateBy similarity1
Modified residuei163N6-succinyllysine; alternateCombined sources1
Modified residuei172N6-acetyllysine; alternateCombined sources1
Modified residuei172N6-succinyllysine; alternateCombined sources1
Modified residuei181N6-succinyllysineCombined sources1
Modified residuei189N6-acetyllysine; alternateCombined sources1
Modified residuei189N6-succinyllysine; alternateCombined sources1
Modified residuei217N6-acetyllysine; alternateCombined sources1
Modified residuei217N6-succinyllysine; alternateCombined sources1
Modified residuei240N6-succinyllysineCombined sources1
Modified residuei248N6-acetyllysineCombined sources1
Modified residuei252N6-succinyllysineCombined sources1
Modified residuei274N6-acetyllysine; alternateCombined sources1
Modified residuei274N6-succinyllysine; alternateCombined sources1
Modified residuei278N6-succinyllysineCombined sources1
Modified residuei288N6-succinyllysineCombined sources1
Modified residuei329N6-succinyllysineCombined sources1
Modified residuei344N6-acetyllysineCombined sources1
Modified residuei348N6-acetyllysineCombined sources1
Modified residuei355N6-acetyllysineCombined sources1
Modified residuei459N6-acetyllysineCombined sources1
Modified residuei527N6-succinyllysineCombined sources1
Modified residuei543PhosphothreonineCombined sources1
Modified residuei572N6-succinyllysineCombined sources1
Modified residuei579N6-acetyllysine; alternateCombined sources1
Modified residuei579N6-succinyllysine; alternateCombined sources1
Modified residuei586N6-acetyllysine; alternateCombined sources1
Modified residuei586N6-succinyllysine; alternateCombined sources1
Modified residuei705N6-acetyllysine; alternateCombined sources1
Modified residuei705N6-succinyllysine; alternateCombined sources1
Modified residuei717N6-succinyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-344. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9DBM2

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9DBM2

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9DBM2

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

More...
PaxDbi
Q9DBM2

PeptideAtlas

More...
PeptideAtlasi
Q9DBM2

PRoteomics IDEntifications database

More...
PRIDEi
Q9DBM2

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
277754

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9DBM2

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

More...
PhosphoSitePlusi
Q9DBM2

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9DBM2

<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
ENSMUSG00000022853, Expressed in cortex of kidney and 262 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9DBM2, 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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
216525, 16 interactors

Protein interaction database and analysis system

More...
IntActi
Q9DBM2, 1 interactor

Molecular INTeraction database

More...
MINTi
Q9DBM2

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000023559

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9DBM2, 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
Q9DBM2

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>Regioni1 – 280Enoyl-CoA hydratase / isomeraseAdd BLAST280
Regioni281 – 5673-hydroxyacyl-CoA dehydrogenaseAdd BLAST287

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi716 – 718Microbody targeting signalBy 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

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1683, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157516

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_009834_16_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9DBM2

Identification of Orthologs from Complete Genome Data

More...
OMAi
INGYGWP

Database of Orthologous Groups

More...
OrthoDBi
219667at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9DBM2

TreeFam database of animal gene trees

More...
TreeFami
TF316708

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006180, 3-OHacyl-CoA_DH_CS
IPR006176, 3-OHacyl-CoA_DH_NAD-bd
IPR006108, 3HC_DH_C
IPR008927, 6-PGluconate_DH-like_C_sf
IPR029045, ClpP/crotonase-like_dom_sf
IPR018376, Enoyl-CoA_hyd/isom_CS
IPR001753, Enoyl-CoA_hydra/iso
IPR036291, NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00725, 3HCDH, 2 hits
PF02737, 3HCDH_N, 1 hit
PF00378, ECH_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48179, SSF48179, 2 hits
SSF51735, SSF51735, 1 hit
SSF52096, SSF52096, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00067, 3HCDH, 1 hit
PS00166, ENOYL_COA_HYDRATASE, 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_length">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q9DBM2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEYLRLPHS LAMIRLCNPP VNAISPTVIT EVRNGLQKAS LDHTVRAIVI
60 70 80 90 100
CGANDNFCAG ADIHGFKSPT GLTLGSLVDE IQRYQKPVVA AIQGVALGGG
110 120 130 140 150
LELALGCHYR IANAKARVGF PEVMLGILPG ARGTQLLPRV VGVPVALDLI
160 170 180 190 200
TSGRHISTDE ALKLGILDVV VKSDPVEEAI KFAQTVIGKP IEPRRILNKP
210 220 230 240 250
VPSLPNMDSV FAEAIAKVRK QYPGRLAPET CVRSVQASVK HPYEVAIKEE
260 270 280 290 300
AKLFMYLRGS GQARALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV
310 320 330 340 350
LGLGTMGRGI AISFARVGIP VVAVESDPKQ LDTAKKIITS TLEKEASKSG
360 370 380 390 400
QASAKPNLRF SSSTKELSSV DLVIEAVFED MNLKKKVFAE LSALCKPGAF
410 420 430 440 450
LCTNTSALDV DDIASSTDRP QLVIGTHFFS PAHIMRLLEV IPSRYSSPTT
460 470 480 490 500
IATVMSLSKR IGKIGVVVGN CYGFVGNRML APYYNQGYFL IEEGSKPEDV
510 520 530 540 550
DGVLEEFGFR MGPFRVSDLA GLDVGWKVRK GQGLTGPSLP PGTPTRKRGN
560 570 580 590 600
TRYSPIADML CEAGRFGQKT GKGWYQYDKP LGRIHKPDPW LSEFLSQYRE
610 620 630 640 650
THHIKQRSIS KEEILERCLY SLINEAFRIL EEGMAASPEH IDVIYLHGYG
660 670 680 690 700
WPRHVGGPMY YAASVGLPTV LEKLQKYYRQ NPDIPQLEPS DYLRRLVAQG
710
SPPLKEWQSL AGPHSSKL
Length:718
Mass (Da):78,301
Last modified:July 27, 2011 - v4
<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:iA405717EC7A3EBD9
GO

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 conflicti499D → G in BAB23628 (PubMed:16141072).Curated1

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
AK004867 mRNA Translation: BAB23628.1
BC016899 mRNA Translation: AAH16899.1
CH466521 Genomic DNA Translation: EDK97607.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS28063.1

NCBI Reference Sequences

More...
RefSeqi
NP_076226.2, NM_023737.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
74147

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:74147

UCSC genome browser

More...
UCSCi
uc007yrm.2, mouse

<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
AK004867 mRNA Translation: BAB23628.1
BC016899 mRNA Translation: AAH16899.1
CH466521 Genomic DNA Translation: EDK97607.1
CCDSiCCDS28063.1
RefSeqiNP_076226.2, NM_023737.3

3D structure databases

SMRiQ9DBM2
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi216525, 16 interactors
IntActiQ9DBM2, 1 interactor
MINTiQ9DBM2
STRINGi10090.ENSMUSP00000023559

Chemistry databases

SwissLipidsiSLP:000000402
SLP:000000491

PTM databases

iPTMnetiQ9DBM2
PhosphoSitePlusiQ9DBM2
SwissPalmiQ9DBM2

Proteomic databases

EPDiQ9DBM2
jPOSTiQ9DBM2
MaxQBiQ9DBM2
PaxDbiQ9DBM2
PeptideAtlasiQ9DBM2
PRIDEiQ9DBM2
ProteomicsDBi277754

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
33832, 336 antibodies

The DNASU plasmid repository

More...
DNASUi
74147

Genome annotation databases

EnsembliENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853
GeneIDi74147
KEGGimmu:74147
UCSCiuc007yrm.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1962
MGIiMGI:1277964, Ehhadh
VEuPathDBiHostDB:ENSMUSG00000022853

Phylogenomic databases

eggNOGiKOG1683, Eukaryota
GeneTreeiENSGT00940000157516
HOGENOMiCLU_009834_16_3_1
InParanoidiQ9DBM2
OMAiINGYGWP
OrthoDBi219667at2759
PhylomeDBiQ9DBM2
TreeFamiTF316708

Enzyme and pathway databases

UniPathwayiUPA00659
ReactomeiR-MMU-390247, Beta-oxidation of very long chain fatty acids
R-MMU-9033241, Peroxisomal protein import

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
74147, 1 hit in 63 CRISPR screens

Protein Ontology

More...
PROi
PR:Q9DBM2
RNActiQ9DBM2, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000022853, Expressed in cortex of kidney and 262 other tissues
GenevisibleiQ9DBM2, MM

Family and domain databases

InterProiView protein in InterPro
IPR006180, 3-OHacyl-CoA_DH_CS
IPR006176, 3-OHacyl-CoA_DH_NAD-bd
IPR006108, 3HC_DH_C
IPR008927, 6-PGluconate_DH-like_C_sf
IPR029045, ClpP/crotonase-like_dom_sf
IPR018376, Enoyl-CoA_hyd/isom_CS
IPR001753, Enoyl-CoA_hydra/iso
IPR036291, NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00725, 3HCDH, 2 hits
PF02737, 3HCDH_N, 1 hit
PF00378, ECH_1, 1 hit
SUPFAMiSSF48179, SSF48179, 2 hits
SSF51735, SSF51735, 1 hit
SSF52096, SSF52096, 1 hit
PROSITEiView protein in PROSITE
PS00067, 3HCDH, 1 hit
PS00166, ENOYL_COA_HYDRATASE, 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 nameiECHP_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: Q9DBM2
Secondary accession number(s): Q91W49
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: September 29, 2021
This is version 173 of the entry and version 4 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

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