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Q13011

- ECH1_HUMAN

UniProt

Q13011 - ECH1_HUMAN

Protein

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

Gene

ECH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (22 Nov 2005)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. receptor binding Source: UniProtKB

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway

    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: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3149. ECH1.

    Subcellular locationi

    Mitochondrion By similarity. Peroxisome By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion, Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27596.

    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 residuei327 – 3271N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13011.
    PaxDbiQ13011.
    PeptideAtlasiQ13011.
    PRIDEiQ13011.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00011416.
    UCD-2DPAGEQ13011.

    PTM databases

    PhosphoSiteiQ13011.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13011.
    BgeeiQ13011.
    CleanExiHS_ECH1.
    GenevestigatoriQ13011.

    Organism-specific databases

    HPAiHPA002907.
    HPA005835.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428582EBI-711968,EBI-466029
    STAT3P407632EBI-711968,EBI-518675

    Protein-protein interaction databases

    BioGridi108220. 19 interactions.
    IntActiQ13011. 17 interactions.
    MINTiMINT-1393158.
    STRINGi9606.ENSP00000221418.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000027939.
    HOVERGENiHBG005556.
    InParanoidiQ13011.
    KOiK12663.
    OMAiSWVKDVC.
    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

    MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA    50
    PDHSYESLRV TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA 100
    DCRAVVISGA GKMFTAGIDL MDMASDILQP KGDDVARISW YLRDIITRYQ 150
    ETFNVIERCP KPVIAAVHGG CIGGGVDLVT ACDIRYCAQD AFFQVKEVDV 200
    GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS GLVSRVFPDK 250
    EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS 300
    MLQTQDLVKS VQATTENKEL KTVTFSKL 328
    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. 1 PublicationCurated
    Sequence conflicti230 – 2301R → H in AAC50222. (PubMed:7558027)Curated
    Sequence conflicti230 – 2301R → H in AAB86485. 1 PublicationCurated
    Sequence conflicti239 – 2391G → D in AAC50222. (PubMed:7558027)Curated
    Sequence conflicti239 – 2391G → D in AAB86485. 1 PublicationCurated
    Sequence conflicti259 – 2591A → P in AAC50222. (PubMed:7558027)Curated
    Sequence conflicti259 – 2591A → P in AAB86485. 1 PublicationCurated
    Sequence conflicti262 – 2621A → P in AAC50222. (PubMed:7558027)Curated
    Sequence conflicti262 – 2621A → P in AAB86485. 1 PublicationCurated
    Sequence conflicti268 – 2714SPVA → TTVL in AAC50222. (PubMed:7558027)Curated
    Sequence conflicti268 – 2714SPVA → TTVL in AAB86485. 1 PublicationCurated
    Sequence conflicti313 – 3131A → P in AAC50222. (PubMed:7558027)Curated
    Sequence conflicti313 – 3131A → P in AAB86485. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411E → A.3 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:
    EMBL
    GenBank
    DDBJ
    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 databases

    DMDMi82654933.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS33014.1.
    PIRi I38882.
    RefSeqi NP_001389.2. NM_001398.2.
    UniGenei Hs.196176.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VRE X-ray 1.95 A/B/C 50-322 [» ]
    ProteinModelPortali Q13011.
    SMRi Q13011. Positions 50-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108220. 19 interactions.
    IntActi Q13011. 17 interactions.
    MINTi MINT-1393158.
    STRINGi 9606.ENSP00000221418.

    PTM databases

    PhosphoSitei Q13011.

    Polymorphism databases

    DMDMi 82654933.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00011416.
    UCD-2DPAGE Q13011.

    Proteomic databases

    MaxQBi Q13011.
    PaxDbi Q13011.
    PeptideAtlasi Q13011.
    PRIDEi Q13011.

    Protocols and materials databases

    DNASUi 1891.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221418 ; ENSP00000221418 ; ENSG00000104823 .
    GeneIDi 1891.
    KEGGi hsa:1891.
    UCSCi uc002oji.3. human.

    Organism-specific databases

    CTDi 1891.
    GeneCardsi GC19M039306.
    H-InvDB HIX0080117.
    HGNCi HGNC:3149. ECH1.
    HPAi HPA002907.
    HPA005835.
    MIMi 600696. gene.
    neXtProti NX_Q13011.
    PharmGKBi PA27596.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1024.
    HOGENOMi HOG000027939.
    HOVERGENi HBG005556.
    InParanoidi Q13011.
    KOi K12663.
    OMAi SWVKDVC.
    OrthoDBi EOG7JHM64.
    PhylomeDBi Q13011.
    TreeFami TF314317.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Miscellaneous databases

    ChiTaRSi ECH1. human.
    EvolutionaryTracei Q13011.
    GeneWikii ECH1.
    GenomeRNAii 1891.
    NextBioi 7711.
    PROi Q13011.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13011.
    Bgeei Q13011.
    CleanExi HS_ECH1.
    Genevestigatori Q13011.

    Family and domain databases

    Gene3Di 1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    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

    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. "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: October 1, 2014
    This is version 142 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