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Q13011 (ECH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

EC=5.3.3.-
Gene names
Name:ECH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homohexamer By similarity.

Subcellular location

Mitochondrion By similarity. Peroxisome By similarity.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
Peroxisome
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionIsomerase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisome

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionisomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Potential
Chain34 – 328295Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial
PRO_0000007417

Regions

Motif326 – 3283Microbody targeting signal Potential

Sites

Binding site1741Substrate; via amide nitrogen By similarity
Site1971Important for catalytic activity By similarity

Amino acid modifications

Modified residue2311N6-succinyllysine By similarity
Modified residue3271N6-acetyllysine Ref.8

Natural variations

Natural variant411E → A. Ref.3 Ref.4 Ref.5
Corresponds to variant rs9419 [ dbSNP | Ensembl ].
VAR_014927
Natural variant2171G → R.
Corresponds to variant rs2229259 [ dbSNP | Ensembl ].
VAR_033913

Experimental info

Sequence conflict2101Q → E in AAC50222. Ref.1
Sequence conflict2101Q → E in AAB86485. Ref.2
Sequence conflict2301R → H in AAC50222. Ref.1
Sequence conflict2301R → H in AAB86485. Ref.2
Sequence conflict2391G → D in AAC50222. Ref.1
Sequence conflict2391G → D in AAB86485. Ref.2
Sequence conflict2591A → P in AAC50222. Ref.1
Sequence conflict2591A → P in AAB86485. Ref.2
Sequence conflict2621A → P in AAC50222. Ref.1
Sequence conflict2621A → P in AAB86485. Ref.2
Sequence conflict268 – 2714SPVA → TTVL in AAC50222. Ref.1
Sequence conflict268 – 2714SPVA → TTVL in AAB86485. Ref.2
Sequence conflict3131A → P in AAC50222. Ref.1
Sequence conflict3131A → P in AAB86485. Ref.2

Secondary structure

............................................. 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13011 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 211E0FF40379E6DA

FASTA32835,816
        10         20         30         40         50         60 
MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA PDHSYESLRV 

        70         80         90        100        110        120 
TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA DCRAVVISGA GKMFTAGIDL 

       130        140        150        160        170        180 
MDMASDILQP KGDDVARISW YLRDIITRYQ ETFNVIERCP KPVIAAVHGG CIGGGVDLVT 

       190        200        210        220        230        240 
ACDIRYCAQD AFFQVKEVDV GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS 

       250        260        270        280        290        300 
GLVSRVFPDK EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS 

       310        320 
MLQTQDLVKS VQATTENKEL KTVTFSKL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16660 mRNA. Translation: AAC50222.1.
AF030249 expand/collapse EMBL AC list , 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.
PIRI38882.
RefSeqNP_001389.2. NM_001398.2.
UniGeneHs.196176.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VREX-ray1.95A/B/C50-322[»]
ProteinModelPortalQ13011.
SMRQ13011. Positions 50-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108220. 18 interactions.
IntActQ13011. 17 interactions.
MINTMINT-1393158.
STRING9606.ENSP00000221418.

PTM databases

PhosphoSiteQ13011.

Polymorphism databases

DMDM82654933.

2D gel databases

REPRODUCTION-2DPAGEIPI00011416.
UCD-2DPAGEQ13011.

Proteomic databases

PaxDbQ13011.
PeptideAtlasQ13011.
PRIDEQ13011.

Protocols and materials databases

DNASU1891.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221418; ENSP00000221418; ENSG00000104823.
GeneID1891.
KEGGhsa:1891.
UCSCuc002oji.3. human.

Organism-specific databases

CTD1891.
GeneCardsGC19M039306.
H-InvDBHIX0080117.
HGNCHGNC:3149. ECH1.
HPAHPA002907.
HPA005835.
MIM600696. gene.
neXtProtNX_Q13011.
PharmGKBPA27596.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1024.
HOGENOMHOG000027939.
HOVERGENHBG005556.
InParanoidQ13011.
KOK12663.
OMAEIDMGMA.
OrthoDBEOG7JHM64.
PhylomeDBQ13011.
TreeFamTF314317.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ13011.
BgeeQ13011.
CleanExHS_ECH1.
GenevestigatorQ13011.

Family and domain databases

Gene3D1.10.12.10. 1 hit.
InterProIPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSECH1. human.
EvolutionaryTraceQ13011.
GeneWikiECH1.
GenomeRNAi1891.
NextBio7711.
PROQ13011.
SOURCESearch...

Entry information

Entry nameECH1_HUMAN
AccessionPrimary (citable) accession number: Q13011
Secondary accession number(s): A8K745, Q8WVX0, Q96EZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM