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P30084

- ECHM_HUMAN

UniProt

P30084 - ECHM_HUMAN

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Protein

Enoyl-CoA hydratase, mitochondrial

Gene

ECHS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Substrate; via amide nitrogen
Sitei164 – 1641Important for catalytic activityBy similarity

GO - Molecular functioni

  1. enoyl-CoA hydratase activity Source: Reactome

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. fatty acid beta-oxidation Source: Reactome
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS05132-MONOMER.
ReactomeiREACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RKP30084.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.17)
Alternative name(s):
Enoyl-CoA hydratase 1
Short-chain enoyl-CoA hydratase
Short name:
SCEH
Gene namesi
Name:ECHS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:3151. ECHS1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27597.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727Mitochondrion1 PublicationAdd
BLAST
Chaini28 – 290263Enoyl-CoA hydratase, mitochondrialPRO_0000007411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-acetyllysine; alternateBy similarity
Modified residuei101 – 1011N6-succinyllysine; alternateBy similarity
Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei204 – 2041N6-succinyllysineBy similarity
Modified residuei211 – 2111N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP30084.
PaxDbiP30084.
PeptideAtlasiP30084.
PRIDEiP30084.

2D gel databases

DOSAC-COBS-2DPAGEP30084.
REPRODUCTION-2DPAGEIPI00024993.
P30084.
SWISS-2DPAGEP30084.
UCD-2DPAGEP30084.

PTM databases

PhosphoSiteiP30084.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP30084.
CleanExiHS_ECHS1.
GenevestigatoriP30084.

Organism-specific databases

HPAiCAB003783.
HPA021995.
HPA022476.

Interactioni

Subunit structurei

Homohexamer; dimer of trimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-719602,EBI-5323863
STAT3P407633EBI-719602,EBI-518675
Stat3P422273EBI-719602,EBI-602878From a different organism.

Protein-protein interaction databases

BioGridi108221. 39 interactions.
IntActiP30084. 18 interactions.
MINTiMINT-1401929.
STRINGi9606.ENSP00000357535.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 429Combined sources
Helixi43 – 453Combined sources
Beta strandi47 – 526Combined sources
Helixi55 – 573Combined sources
Helixi63 – 7816Combined sources
Beta strandi84 – 885Combined sources
Beta strandi91 – 955Combined sources
Helixi100 – 1034Combined sources
Helixi108 – 1136Combined sources
Turni114 – 1174Combined sources
Helixi119 – 1257Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi136 – 1394Combined sources
Helixi141 – 1477Combined sources
Beta strandi149 – 1557Combined sources
Beta strandi159 – 1613Combined sources
Helixi163 – 1675Combined sources
Beta strandi172 – 1743Combined sources
Turni175 – 1773Combined sources
Helixi178 – 1836Combined sources
Helixi185 – 19410Combined sources
Helixi200 – 2056Combined sources
Beta strandi210 – 2134Combined sources
Turni215 – 2173Combined sources
Helixi218 – 23114Combined sources
Helixi234 – 24512Combined sources
Helixi246 – 2483Combined sources
Helixi252 – 26615Combined sources
Helixi270 – 28011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HW5X-ray2.55A/B/C/D/E/F28-290[»]
ProteinModelPortaliP30084.
SMRiP30084. Positions 31-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30084.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1014Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiP30084.
KOiK07511.
OMAiHWDQLTR.
OrthoDBiEOG7N63NC.
PhylomeDBiP30084.
TreeFamiTF314497.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i0CCD0C7F891B1704
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841A → G in BAA03001. (PubMed:8012501)Curated
Sequence conflicti121 – 1211D → G in BAA03001. (PubMed:8012501)Curated
Sequence conflicti138 – 1381A → P in BAA03001. (PubMed:8012501)Curated
Sequence conflicti188 – 1892AM → EL in BAA03001. (PubMed:8012501)Curated
Sequence conflicti197 – 1971R → A in BAA03001. (PubMed:8012501)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111V → A.2 Publications
Corresponds to variant rs10466126 [ dbSNP | Ensembl ].
VAR_022273
Natural varianti75 – 751T → I.5 Publications
Corresponds to variant rs1049951 [ dbSNP | Ensembl ].
VAR_022274

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. Translation: CAH70286.1.
BC008906 mRNA. Translation: AAH08906.1.
CCDSiCCDS7681.1.
RefSeqiNP_004083.3. NM_004092.3.
UniGeneiHs.76394.

Genome annotation databases

EnsembliENST00000368547; ENSP00000357535; ENSG00000127884.
GeneIDi1892.
KEGGihsa:1892.
UCSCiuc001lmu.3. human.

Polymorphism databases

DMDMi62906863.

Keywords - Coding sequence diversityi

Polymorphism

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. Translation: CAH70286.1 .
BC008906 mRNA. Translation: AAH08906.1 .
CCDSi CCDS7681.1.
RefSeqi NP_004083.3. NM_004092.3.
UniGenei Hs.76394.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HW5 X-ray 2.55 A/B/C/D/E/F 28-290 [» ]
ProteinModelPortali P30084.
SMRi P30084. Positions 31-290.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108221. 39 interactions.
IntActi P30084. 18 interactions.
MINTi MINT-1401929.
STRINGi 9606.ENSP00000357535.

PTM databases

PhosphoSitei P30084.

Polymorphism databases

DMDMi 62906863.

2D gel databases

DOSAC-COBS-2DPAGE P30084.
REPRODUCTION-2DPAGE IPI00024993.
P30084.
SWISS-2DPAGE P30084.
UCD-2DPAGE P30084.

Proteomic databases

MaxQBi P30084.
PaxDbi P30084.
PeptideAtlasi P30084.
PRIDEi P30084.

Protocols and materials databases

DNASUi 1892.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368547 ; ENSP00000357535 ; ENSG00000127884 .
GeneIDi 1892.
KEGGi hsa:1892.
UCSCi uc001lmu.3. human.

Organism-specific databases

CTDi 1892.
GeneCardsi GC10M135175.
HGNCi HGNC:3151. ECHS1.
HPAi CAB003783.
HPA021995.
HPA022476.
MIMi 602292. gene.
neXtProti NX_P30084.
PharmGKBi PA27597.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1024.
GeneTreei ENSGT00760000119100.
HOGENOMi HOG000027939.
HOVERGENi HBG010157.
InParanoidi P30084.
KOi K07511.
OMAi HWDQLTR.
OrthoDBi EOG7N63NC.
PhylomeDBi P30084.
TreeFami TF314497.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:HS05132-MONOMER.
Reactomei REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RK P30084.

Miscellaneous databases

ChiTaRSi ECHS1. human.
EvolutionaryTracei P30084.
GeneWikii ECHS1.
GenomeRNAii 1892.
NextBioi 7715.
PROi P30084.
SOURCEi Search...

Gene expression databases

Bgeei P30084.
CleanExi HS_ECHS1.
Genevestigatori P30084.

Family and domain databases

Gene3Di 3.90.226.10. 1 hit.
InterProi IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view ]
Pfami PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 1 hit.
PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase."
    Kanazawa M., Ohtake A., Abe H., Yamamoto S., Satoh Y., Takayanagi M., Niimi H., Mori M., Hashimoto T.
    Enzyme Protein 47:9-13(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-11 AND ILE-75.
    Tissue: Liver.
  2. "Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3."
    Janssen U., Davis E.M., le Beau M.M., Stoffel W.
    Genomics 40:470-475(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-11 AND ILE-75.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-75.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-75.
    Tissue: Placenta.
  6. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-37.
    Tissue: Liver.
  7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-56; 102-115; 158-178; 186-197; 242-257 AND 262-273, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
    Hubbard M.J., McHugh N.J.
    Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-63; 75-92 AND 158-178, VARIANT ILE-75, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The crystal structure of human enoyl-coenzyme A (CoA) hydratase short chain 1, ECHS1."
    Structural genomics consortium (SGC)
    Submitted (AUG-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 24-290 IN COMPLEX WITH CROTONYL COENZYME A, SUBUNIT.

Entry informationi

Entry nameiECHM_HUMAN
AccessioniPrimary (citable) accession number: P30084
Secondary accession number(s): O00739, Q5VWY1, Q96H54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 26, 2005
Last modified: November 26, 2014
This is version 158 of the entry and version 4 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3