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Protein

Enoyl-CoA hydratase, mitochondrial

Gene

ECHS1

Organism
Homo sapiens (Human)
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

Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. Has high substrate specificity for crotonyl-CoA and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA and methacrylyl-CoA. It is noteworthy that binds tiglyl-CoA, but hydrates only a small amount of this substrate.1 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 ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=12.75 µM for crotonyl-CoA1 Publication
  2. KM=34.04 µM for acryloyl-CoA1 Publication
  3. KM=45.83 µM for 3-Methylcrotonyl-CoA1 Publication
  4. KM=57.87 µM for tiglyl-CoA1 Publication
  1. Vmax=54.64 µmol/min/mg enzyme toward crotonyl-CoA1 Publication
  2. Vmax=42.92 µmol/min/mg enzyme toward acryloyl-CoA1 Publication
  3. Vmax=49.02 µmol/min/mg enzyme toward 3-Methylcrotonyl-CoA1 Publication
  4. Vmax=6.66 µmol/min/mg enzyme toward tiglyl-CoA1 Publication

<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.1 Publication
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 ‘Function’ 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 sitei141Substrate; via amide nitrogen1
<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>Sitei164Important 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

  • enoyl-CoA hydratase activity Source: UniProtKB

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 functionLyase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS05132-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
4.2.1.17 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-HSA-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-HSA-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-HSA-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA
R-HSA-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P30084

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:000001471

<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:
Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.171 Publication)
Alternative name(s):
Enoyl-CoA hydratase 1
Short-chain enoyl-CoA hydratase
Short name:
SCEH
<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:ECHS1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000127884.4

Human Gene Nomenclature Database

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HGNCi
HGNC:3151 ECHS1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602292 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P30084

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Mitochondrial short-chain enoyl-CoA hydratase 1 deficiency (ECHS1D)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe, autosomal recessive inborn error affecting valine metabolism. Disease features include brain lesions in the basal ganglia, neurodegeneration, delayed psychomotor development, hypotonia, spasticity, and increased lactic acid in serum and cerebral serum fluid.
See also OMIM:616277
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0733732A → V in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs587776498EnsemblClinVar.1
Natural variantiVAR_07618533F → S in ECHS1D. 2 Publications1
Natural variantiVAR_07618654R → H in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs375266808Ensembl.1
Natural variantiVAR_07618759N → S in ECHS1D; decreases significantly enoyl-CoA hydratase activity; decreases significantly protein expression. 3 PublicationsCorresponds to variant dbSNP:rs201865375EnsemblClinVar.1
Natural variantiVAR_07618866I → T in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs371063211Ensembl.1
Natural variantiVAR_07618977E → Q in ECHS1D. 1 Publication1
Natural variantiVAR_07619090G → R in ECHS1D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1085307550Ensembl.1
Natural variantiVAR_076191132A → T in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs770931871EnsemblClinVar.1
Natural variantiVAR_076479138A → V in ECHS1D; decreases enoyl-CoA hydratase activity of 70%; decreases significantly protein expression. 1 PublicationCorresponds to variant dbSNP:rs864309656EnsemblClinVar.1
Natural variantiVAR_076192150D → G in ECHS1D. 1 Publication1
Natural variantiVAR_073374158A → D in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs786204001EnsemblClinVar.1
Natural variantiVAR_076193159Q → R in ECHS1D. 2 PublicationsCorresponds to variant dbSNP:rs375032130EnsemblClinVar.1
Natural variantiVAR_076194195G → S in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs761989177Ensembl.1
Natural variantiVAR_076195225C → R in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs769429279Ensembl.1
Natural variantiVAR_076196273K → E in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs565090080EnsemblClinVar.1
Natural variantiVAR_076480281E → G in ECHS1D; unknown pathological significance. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET

More...
DisGeNETi
1892

MalaCards human disease database

More...
MalaCardsi
ECHS1
MIMi616277 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000127884

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
255241 Leigh syndrome with leukodystrophy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27597

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03059 Acetoacetyl-Coenzyme A
DB02563 Hexanoyl-Coenzyme A
DB02910 Octanoyl-Coenzyme A

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ECHS1

Domain mapping of disease mutations (DMDM)

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DMDMi
62906863

<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 – 27MitochondrionCombined sources1 PublicationAdd BLAST27
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000741128 – 290Enoyl-CoA hydratase, mitochondrialAdd BLAST263

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 residuei46PhosphothreonineCombined sources1
Modified residuei101N6-acetyllysine; alternateBy similarity1
Modified residuei101N6-succinyllysine; alternateBy similarity1
Modified residuei114PhosphoserineCombined sources1
Modified residuei115N6-acetyllysine; alternateBy similarity1
Modified residuei115N6-succinyllysine; alternateBy similarity1
Modified residuei118N6-acetyllysineCombined sources1
Modified residuei204N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P30084

MaxQB - The MaxQuant DataBase

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MaxQBi
P30084

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

More...
PaxDbi
P30084

PeptideAtlas

More...
PeptideAtlasi
P30084

PRoteomics IDEntifications database

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PRIDEi
P30084

ProteomicsDB human proteome resource

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ProteomicsDBi
54632

Consortium for Top Down Proteomics

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TopDownProteomicsi
P30084

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P30084

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00024993
P30084

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P30084

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P30084

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P30084

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

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PhosphoSitePlusi
P30084

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P30084

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Liver, fibroblast, muscle. Barely detectable in spleen and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000127884 Expressed in 237 organ(s), highest expression level in cortex of kidney

CleanEx database of gene expression profiles

More...
CleanExi
HS_ECHS1

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P30084 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB003783
HPA021995
HPA022476

<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

Homohexamer; dimer of trimers.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108221, 68 interactors

Protein interaction database and analysis system

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IntActi
P30084, 35 interactors

Molecular INTeraction database

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MINTi
P30084

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000357535

<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

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P30084

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

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SMRi
P30084

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P30084

<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>Regioni98 – 101Substrate binding4

<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

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1680 Eukaryota
COG1024 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157609

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000027939

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG010157

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P30084

KEGG Orthology (KO)

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KOi
K07511

Identification of Orthologs from Complete Genome Data

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OMAi
IFKQTDA

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0MVQ

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P30084

TreeFam database of animal gene trees

More...
TreeFami
TF314497

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.12.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029045 ClpP/crotonase-like_dom_sf
IPR018376 Enoyl-CoA_hyd/isom_CS
IPR001753 Enoyl-CoA_hydra/iso
IPR014748 Enoyl-CoA_hydra_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00378 ECH_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52096 SSF52096, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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>.<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.

<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 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.

P30084-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAALRVLLSC VRGPLRPPVR CPAWRPFASG ANFEYIIAEK RGKNNTVGLI
60 70 80 90 100
QLNRPKALNA LCDGLIDELN QALKTFEEDP AVGAIVLTGG DKAFAAGADI
110 120 130 140 150
KEMQNLSFQD CYSSKFLKHW DHLTQVKKPV IAAVNGYAFG GGCELAMMCD
160 170 180 190 200
IIYAGEKAQF AQPEILIGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA
210 220 230 240 250
QDAKQAGLVS KICPVETLVE EAIQCAEKIA SNSKIVVAMA KESVNAAFEM
260 270 280 290
TLTEGSKLEK KLFYSTFATD DRKEGMTAFV EKRKANFKDQ
Length:290
Mass (Da):31,387
Last modified:April 26, 2005 - 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:i0CCD0C7F891B1704
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 conflicti84A → G in BAA03001 (PubMed:8012501).Curated1
Sequence conflicti121D → G in BAA03001 (PubMed:8012501).Curated1
Sequence conflicti138A → P in BAA03001 (PubMed:8012501).Curated1
Sequence conflicti188 – 189AM → EL in BAA03001 (PubMed:8012501).Curated2
Sequence conflicti197R → A in BAA03001 (PubMed:8012501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0733732A → V in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs587776498EnsemblClinVar.1
Natural variantiVAR_02227311V → A2 PublicationsCorresponds to variant dbSNP:rs10466126Ensembl.1
Natural variantiVAR_07618533F → S in ECHS1D. 2 Publications1
Natural variantiVAR_07618654R → H in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs375266808Ensembl.1
Natural variantiVAR_07618759N → S in ECHS1D; decreases significantly enoyl-CoA hydratase activity; decreases significantly protein expression. 3 PublicationsCorresponds to variant dbSNP:rs201865375EnsemblClinVar.1
Natural variantiVAR_07618866I → T in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs371063211Ensembl.1
Natural variantiVAR_02227475T → I5 PublicationsCorresponds to variant dbSNP:rs1049951EnsemblClinVar.1
Natural variantiVAR_07618977E → Q in ECHS1D. 1 Publication1
Natural variantiVAR_07619090G → R in ECHS1D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1085307550Ensembl.1
Natural variantiVAR_076191132A → T in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs770931871EnsemblClinVar.1
Natural variantiVAR_076479138A → V in ECHS1D; decreases enoyl-CoA hydratase activity of 70%; decreases significantly protein expression. 1 PublicationCorresponds to variant dbSNP:rs864309656EnsemblClinVar.1
Natural variantiVAR_076192150D → G in ECHS1D. 1 Publication1
Natural variantiVAR_073374158A → D in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs786204001EnsemblClinVar.1
Natural variantiVAR_076193159Q → R in ECHS1D. 2 PublicationsCorresponds to variant dbSNP:rs375032130EnsemblClinVar.1
Natural variantiVAR_076194195G → S in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs761989177Ensembl.1
Natural variantiVAR_076195225C → R in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs769429279Ensembl.1
Natural variantiVAR_076196273K → E in ECHS1D. 1 PublicationCorresponds to variant dbSNP:rs565090080EnsemblClinVar.1
Natural variantiVAR_076480281E → G in ECHS1D; unknown pathological significance. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D13900 mRNA Translation: BAA03001.1
X98126
, X98127, X98128, X98129 Genomic DNA Translation: CAA66808.1
BT007123 mRNA Translation: AAP35787.1
AL360181 Genomic DNA No translation available.
BC008906 mRNA Translation: AAH08906.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS7681.1

NCBI Reference Sequences

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RefSeqi
NP_004083.3, NM_004092.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.76394

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000368547; ENSP00000357535; ENSG00000127884

Database of genes from NCBI RefSeq genomes

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GeneIDi
1892

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1892

UCSC genome browser

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UCSCi
uc001lmu.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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
D13900 mRNA Translation: BAA03001.1
X98126
, X98127, X98128, X98129 Genomic DNA Translation: CAA66808.1
BT007123 mRNA Translation: AAP35787.1
AL360181 Genomic DNA No translation available.
BC008906 mRNA Translation: AAH08906.1
CCDSiCCDS7681.1
RefSeqiNP_004083.3, NM_004092.3
UniGeneiHs.76394

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HW5X-ray2.55A/B/C/D/E/F28-290[»]
ProteinModelPortaliP30084
SMRiP30084
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108221, 68 interactors
IntActiP30084, 35 interactors
MINTiP30084
STRINGi9606.ENSP00000357535

Chemistry databases

DrugBankiDB03059 Acetoacetyl-Coenzyme A
DB02563 Hexanoyl-Coenzyme A
DB02910 Octanoyl-Coenzyme A
SwissLipidsiSLP:000001471

PTM databases

iPTMnetiP30084
PhosphoSitePlusiP30084
SwissPalmiP30084

Polymorphism and mutation databases

BioMutaiECHS1
DMDMi62906863

2D gel databases

DOSAC-COBS-2DPAGEiP30084
REPRODUCTION-2DPAGEiIPI00024993
P30084
SWISS-2DPAGEiP30084
UCD-2DPAGEiP30084

Proteomic databases

EPDiP30084
MaxQBiP30084
PaxDbiP30084
PeptideAtlasiP30084
PRIDEiP30084
ProteomicsDBi54632
TopDownProteomicsiP30084

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1892
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368547; ENSP00000357535; ENSG00000127884
GeneIDi1892
KEGGihsa:1892
UCSCiuc001lmu.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1892
DisGeNETi1892
EuPathDBiHostDB:ENSG00000127884.4

GeneCards: human genes, protein and diseases

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GeneCardsi
ECHS1
HGNCiHGNC:3151 ECHS1
HPAiCAB003783
HPA021995
HPA022476
MalaCardsiECHS1
MIMi602292 gene
616277 phenotype
neXtProtiNX_P30084
OpenTargetsiENSG00000127884
Orphaneti255241 Leigh syndrome with leukodystrophy
PharmGKBiPA27597

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1680 Eukaryota
COG1024 LUCA
GeneTreeiENSGT00940000157609
HOGENOMiHOG000027939
HOVERGENiHBG010157
InParanoidiP30084
KOiK07511
OMAiIFKQTDA
OrthoDBiEOG091G0MVQ
PhylomeDBiP30084
TreeFamiTF314497

Enzyme and pathway databases

UniPathwayi
UPA00659

BioCyciMetaCyc:HS05132-MONOMER
BRENDAi4.2.1.17 2681
ReactomeiR-HSA-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-HSA-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-HSA-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-HSA-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA
R-HSA-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
SABIO-RKiP30084

Miscellaneous databases

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

More...
ChiTaRSi
ECHS1 human
EvolutionaryTraceiP30084

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ECHS1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1892

Protein Ontology

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PROi
PR:P30084

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000127884 Expressed in 237 organ(s), highest expression level in cortex of kidney
CleanExiHS_ECHS1
GenevisibleiP30084 HS

Family and domain databases

Gene3Di1.10.12.10, 1 hit
InterProiView protein in InterPro
IPR029045 ClpP/crotonase-like_dom_sf
IPR018376 Enoyl-CoA_hyd/isom_CS
IPR001753 Enoyl-CoA_hydra/iso
IPR014748 Enoyl-CoA_hydra_C
PfamiView protein in Pfam
PF00378 ECH_1, 1 hit
SUPFAMiSSF52096 SSF52096, 1 hit
PROSITEiView protein in PROSITE
PS00166 ENOYL_COA_HYDRATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiECHM_HUMAN
<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: P30084
Secondary accession number(s): O00739, Q5VWY1, Q96H54
<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: April 1, 1993
Last sequence update: April 26, 2005
Last modified: December 5, 2018
This is version 199 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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