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Protein

Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

Gene

ECH1

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

Functioni

Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei174 – 1741Substrate; via amide nitrogenBy similarity
Sitei197 – 1971Important for catalytic activityBy similarity

GO - Molecular functioni

  1. isomerase activity Source: UniProtKB-KW
  2. receptor binding Source: UniProtKB

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC:5.3.3.-)
Gene namesi
Name:ECH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3149. ECH1.

Subcellular locationi

  1. Mitochondrion By similarity
  2. Peroxisome By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. membrane Source: UniProtKB
  3. mitochondrion Source: UniProtKB-SubCell
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27596.

Polymorphism and mutation databases

BioMutaiECH1.
DMDMi82654933.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 328295Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrialPRO_0000007417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311N6-succinyllysineBy similarity
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei327 – 3271N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13011.
PaxDbiQ13011.
PeptideAtlasiQ13011.
PRIDEiQ13011.

2D gel databases

REPRODUCTION-2DPAGEIPI00011416.
UCD-2DPAGEQ13011.

PTM databases

PhosphoSiteiQ13011.

Expressioni

Gene expression databases

BgeeiQ13011.
CleanExiHS_ECH1.
ExpressionAtlasiQ13011. baseline and differential.
GenevestigatoriQ13011.

Organism-specific databases

HPAiHPA002907.
HPA005835.

Interactioni

Subunit structurei

Homohexamer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-711968,EBI-10175124
HTTP428582EBI-711968,EBI-466029
STAT3P407632EBI-711968,EBI-518675
TRAF1Q130773EBI-711968,EBI-359224

Protein-protein interaction databases

BioGridi108220. 29 interactions.
IntActiQ13011. 19 interactions.
MINTiMINT-1393158.
STRINGi9606.ENSP00000221418.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 627Combined sources
Beta strandi64 – 729Combined sources
Helixi75 – 773Combined sources
Helixi83 – 9715Combined sources
Beta strandi104 – 1107Combined sources
Helixi120 – 1289Combined sources
Beta strandi132 – 1343Combined sources
Helixi135 – 15824Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi169 – 1724Combined sources
Helixi174 – 1796Combined sources
Beta strandi182 – 1887Combined sources
Beta strandi192 – 1943Combined sources
Helixi197 – 1993Combined sources
Helixi208 – 2158Combined sources
Helixi219 – 22810Combined sources
Beta strandi231 – 2333Combined sources
Helixi234 – 2396Combined sources
Beta strandi242 – 2498Combined sources
Helixi250 – 26516Combined sources
Helixi269 – 28416Combined sources
Helixi287 – 30115Combined sources
Helixi305 – 3139Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VREX-ray1.95A/B/C50-322[»]
ProteinModelPortaliQ13011.
SMRiQ13011. Positions 50-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13011.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi326 – 3283Microbody targeting signalSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG005556.
InParanoidiQ13011.
KOiK12663.
OMAiEIDMGMA.
OrthoDBiEOG7JHM64.
PhylomeDBiQ13011.
TreeFamiTF314317.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
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.

Q13011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA
60 70 80 90 100
PDHSYESLRV TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA
110 120 130 140 150
DCRAVVISGA GKMFTAGIDL MDMASDILQP KGDDVARISW YLRDIITRYQ
160 170 180 190 200
ETFNVIERCP KPVIAAVHGG CIGGGVDLVT ACDIRYCAQD AFFQVKEVDV
210 220 230 240 250
GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS GLVSRVFPDK
260 270 280 290 300
EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS
310 320
MLQTQDLVKS VQATTENKEL KTVTFSKL
Length:328
Mass (Da):35,816
Last modified:November 22, 2005 - v2
Checksum:i211E0FF40379E6DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101Q → E in AAC50222 (PubMed:7558027).Curated
Sequence conflicti210 – 2101Q → E in AAB86485 (Ref. 2) Curated
Sequence conflicti230 – 2301R → H in AAC50222 (PubMed:7558027).Curated
Sequence conflicti230 – 2301R → H in AAB86485 (Ref. 2) Curated
Sequence conflicti239 – 2391G → D in AAC50222 (PubMed:7558027).Curated
Sequence conflicti239 – 2391G → D in AAB86485 (Ref. 2) Curated
Sequence conflicti259 – 2591A → P in AAC50222 (PubMed:7558027).Curated
Sequence conflicti259 – 2591A → P in AAB86485 (Ref. 2) Curated
Sequence conflicti262 – 2621A → P in AAC50222 (PubMed:7558027).Curated
Sequence conflicti262 – 2621A → P in AAB86485 (Ref. 2) Curated
Sequence conflicti268 – 2714SPVA → TTVL in AAC50222 (PubMed:7558027).Curated
Sequence conflicti268 – 2714SPVA → TTVL in AAB86485 (Ref. 2) Curated
Sequence conflicti313 – 3131A → P in AAC50222 (PubMed:7558027).Curated
Sequence conflicti313 – 3131A → P in AAB86485 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411E → A.4 Publications
Corresponds to variant rs9419 [ dbSNP | Ensembl ].
VAR_014927
Natural varianti217 – 2171G → R.
Corresponds to variant rs2229259 [ dbSNP | Ensembl ].
VAR_033913

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16660 mRNA. Translation: AAC50222.1.
AF030249
, AF030246, AF030247, AF030248 Genomic DNA. Translation: AAB86485.1.
AK291860 mRNA. Translation: BAF84549.1.
CH471126 Genomic DNA. Translation: EAW56824.1.
BC011792 mRNA. Translation: AAH11792.1.
BC017408 mRNA. Translation: AAH17408.1.
CCDSiCCDS33014.1.
PIRiI38882.
RefSeqiNP_001389.2. NM_001398.2.
UniGeneiHs.196176.

Genome annotation databases

EnsembliENST00000221418; ENSP00000221418; ENSG00000104823.
GeneIDi1891.
KEGGihsa:1891.
UCSCiuc002oji.3. human.

Polymorphism and mutation databases

BioMutaiECH1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16660 mRNA. Translation: AAC50222.1.
AF030249
, AF030246, AF030247, AF030248 Genomic DNA. Translation: AAB86485.1.
AK291860 mRNA. Translation: BAF84549.1.
CH471126 Genomic DNA. Translation: EAW56824.1.
BC011792 mRNA. Translation: AAH11792.1.
BC017408 mRNA. Translation: AAH17408.1.
CCDSiCCDS33014.1.
PIRiI38882.
RefSeqiNP_001389.2. NM_001398.2.
UniGeneiHs.196176.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VREX-ray1.95A/B/C50-322[»]
ProteinModelPortaliQ13011.
SMRiQ13011. Positions 50-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108220. 29 interactions.
IntActiQ13011. 19 interactions.
MINTiMINT-1393158.
STRINGi9606.ENSP00000221418.

PTM databases

PhosphoSiteiQ13011.

Polymorphism and mutation databases

BioMutaiECH1.
DMDMi82654933.

2D gel databases

REPRODUCTION-2DPAGEIPI00011416.
UCD-2DPAGEQ13011.

Proteomic databases

MaxQBiQ13011.
PaxDbiQ13011.
PeptideAtlasiQ13011.
PRIDEiQ13011.

Protocols and materials databases

DNASUi1891.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221418; ENSP00000221418; ENSG00000104823.
GeneIDi1891.
KEGGihsa:1891.
UCSCiuc002oji.3. human.

Organism-specific databases

CTDi1891.
GeneCardsiGC19M039306.
H-InvDBHIX0080117.
HGNCiHGNC:3149. ECH1.
HPAiHPA002907.
HPA005835.
MIMi600696. gene.
neXtProtiNX_Q13011.
PharmGKBiPA27596.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG005556.
InParanoidiQ13011.
KOiK12663.
OMAiEIDMGMA.
OrthoDBiEOG7JHM64.
PhylomeDBiQ13011.
TreeFamiTF314317.

Enzyme and pathway databases

UniPathwayiUPA00659.

Miscellaneous databases

ChiTaRSiECH1. human.
EvolutionaryTraceiQ13011.
GeneWikiiECH1.
GenomeRNAii1891.
NextBioi7711.
PROiQ13011.
SOURCEiSearch...

Gene expression databases

BgeeiQ13011.
CleanExiHS_ECH1.
ExpressionAtlasiQ13011. baseline and differential.
GenevestigatoriQ13011.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase."
    Fitzpatrick D.R., Germain-Lee E., Valle D.
    Genomics 27:457-466(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Genomic structure of human ECH1."
    Fitzpatrick D.R., Valle D.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-41.
    Tissue: Skeletal muscle.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-41.
  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 ALA-41.
    Tissue: Melanoma and Pancreatic carcinoma.
  6. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 149-158 AND 215-230, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 66-77; 113-131; 149-211; 215-230 AND 232-245, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "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-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, VARIANT [LARGE SCALE ANALYSIS] ALA-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structure of human peroxisomal delta3,5,delta2,4-dienoyl CoA isomerase (ECH1)."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 50-322.

Entry informationi

Entry nameiECH1_HUMAN
AccessioniPrimary (citable) accession number: Q13011
Secondary accession number(s): A8K745, Q8WVX0, Q96EZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 22, 2005
Last modified: April 29, 2015
This is version 148 of the entry and version 2 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 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.