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O75521

- ECI2_HUMAN

UniProt

O75521 - ECI2_HUMAN

Protein

Enoyl-CoA delta isomerase 2, mitochondrial

Gene

ECI2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 4 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates By similarity.By similarity

    Catalytic activityi

    (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Acyl-CoABy similarity
    Binding sitei111 – 1111Acyl-CoABy similarity

    GO - Molecular functioni

    1. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
    2. fatty-acyl-CoA binding Source: InterPro
    3. receptor binding Source: UniProtKB

    GO - Biological processi

    1. fatty acid catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-CoA delta isomerase 2, mitochondrial (EC:5.3.3.8)
    Alternative name(s):
    DRS-1
    Delta(3),delta(2)-enoyl-CoA isomerase
    Short name:
    D3,D2-enoyl-CoA isomerase
    Diazepam-binding inhibitor-related protein 1
    Short name:
    DBI-related protein 1
    Dodecenoyl-CoA isomerase
    Hepatocellular carcinoma-associated antigen 88
    Peroxisomal 3,2-trans-enoyl-CoA isomerase
    Short name:
    pECI
    Renal carcinoma antigen NY-REN-1
    Gene namesi
    Name:ECI2
    Synonyms:DRS1, HCA88, PECI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14601. ECI2.

    Subcellular locationi

    Isoform 1 : Mitochondrion By similarity

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. membrane Source: UniProtKB
    3. mitochondrion Source: LIFEdb
    4. nucleus Source: HPA
    5. peroxisomal matrix Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion, Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33168.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3838MitochondrionSequence AnalysisAdd
    BLAST
    Chaini39 – 394356Enoyl-CoA delta isomerase 2, mitochondrialPRO_0000214027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-acetyllysine; alternate1 Publication
    Modified residuei51 – 511N6-succinyllysine; alternateBy similarity
    Modified residuei55 – 551N6-succinyllysineBy similarity
    Modified residuei62 – 621N6-acetyllysine; alternateBy similarity
    Modified residuei62 – 621N6-succinyllysine; alternateBy similarity
    Modified residuei70 – 701N6-succinyllysineBy similarity
    Modified residuei81 – 811N6-succinyllysineBy similarity
    Modified residuei90 – 901N6-succinyllysineBy similarity
    Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
    Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
    Modified residuei161 – 1611N6-succinyllysineBy similarity
    Modified residuei289 – 2891N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO75521.
    PaxDbiO75521.
    PRIDEiO75521.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00419263.
    UCD-2DPAGEO75521.

    PTM databases

    PhosphoSiteiO75521.

    Expressioni

    Tissue specificityi

    Abundant in heart, skeletal muscle and liver. Expressed in CD34+ T-cells and CD34+ bone marrow cells.1 Publication

    Gene expression databases

    ArrayExpressiO75521.
    BgeeiO75521.
    GenevestigatoriO75521.

    Organism-specific databases

    HPAiHPA022130.
    HPA031626.

    Interactioni

    Protein-protein interaction databases

    BioGridi115718. 12 interactions.
    IntActiO75521. 7 interactions.
    MINTiMINT-3001383.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 5213
    Helixi59 – 6911
    Turni70 – 745
    Helixi87 – 9913
    Helixi104 – 11815
    Beta strandi140 – 1478
    Beta strandi150 – 1556
    Helixi158 – 1603
    Helixi166 – 18116
    Beta strandi185 – 1928
    Helixi212 – 23221
    Beta strandi238 – 2425
    Helixi249 – 2524
    Helixi253 – 2564
    Beta strandi258 – 2636
    Beta strandi267 – 2693
    Helixi273 – 2753
    Helixi283 – 2919
    Helixi293 – 3008
    Helixi308 – 3136
    Beta strandi318 – 3214
    Turni323 – 3253
    Helixi326 – 33712
    Helixi342 – 35312
    Helixi354 – 3563
    Helixi357 – 37519
    Helixi378 – 3814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQUNMR-A31-133[»]
    2F6QX-ray1.95A/B/C138-394[»]
    ProteinModelPortaliO75521.
    SMRiO75521. Positions 31-133, 139-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75521.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 12486ACBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 705Acyl-CoA bindingBy similarity
    Regioni151 – 322172ECH-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi392 – 3943Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
    Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4281.
    HOVERGENiHBG006723.
    InParanoidiO75521.
    KOiK13239.
    OMAiRWLSDEC.
    OrthoDBiEOG72RN06.
    PhylomeDBiO75521.
    TreeFamiTF313375.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR022408. Acyl-CoA-binding_prot_CS.
    IPR000582. Acyl-CoA-binding_protein.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    [Graphical view]
    PfamiPF00887. ACBP. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    PRINTSiPR00689. ACOABINDINGP.
    SUPFAMiSSF47027. SSF47027. 1 hit.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00880. ACB_1. 1 hit.
    PS51228. ACB_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75521-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAMAYLAWRL ARRSCPSSLQ VTSFPVVQLH MNRTAMRASQ KDFENSMNQV    50
    KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG 100
    SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI 150
    TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN 200
    DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS 250
    VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML 300
    IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE 350
    VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL 394
    Length:394
    Mass (Da):43,585
    Last modified:September 1, 2009 - v4
    Checksum:i8AC633D43A320102
    GO
    Isoform 2 (identifier: O75521-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: Missing.

    Show »
    Length:359
    Mass (Da):39,609
    Checksum:iB9EC60A0D445C9F0
    GO

    Sequence cautioni

    The sequence AAC19317.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAD34173.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF66247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH02668.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH16781.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH17474.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH33841.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH34702.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAG52068.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191S → C in CAB66577. (PubMed:11230166)Curated
    Sequence conflicti195 – 1951Y → C in AAC19317. (PubMed:10354522)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471M → I.
    Corresponds to variant rs3177253 [ dbSNP | Ensembl ].
    VAR_058493
    Natural varianti344 – 3441A → V.2 Publications
    Corresponds to variant rs7166 [ dbSNP | Ensembl ].
    VAR_058494

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535Missing in isoform 2. 3 PublicationsVSP_037854Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF069301 mRNA. Translation: AAC19317.1. Different initiation.
    AL136642 mRNA. Translation: CAB66577.1.
    AK075108 mRNA. Translation: BAG52068.1. Different initiation.
    AL033383 Genomic DNA. Translation: CAI42125.1.
    AL033383 Genomic DNA. Translation: CAI42127.1.
    BC002668 mRNA. Translation: AAH02668.3. Different initiation.
    BC016781 mRNA. Translation: AAH16781.1. Different initiation.
    BC017474 mRNA. Translation: AAH17474.1. Different initiation.
    BC033841 mRNA. Translation: AAH33841.3. Different initiation.
    BC034702 mRNA. Translation: AAH34702.1. Different initiation.
    AF153612 mRNA. Translation: AAD34173.1. Different initiation.
    AF244138 mRNA. Translation: AAF66247.1. Different initiation.
    CCDSiCCDS43420.2. [O75521-1]
    RefSeqiNP_001159482.1. NM_001166010.1.
    NP_006108.2. NM_006117.2.
    NP_996667.2. NM_206836.2. [O75521-1]
    UniGeneiHs.15250.

    Genome annotation databases

    EnsembliENST00000361538; ENSP00000354737; ENSG00000198721.
    ENST00000380118; ENSP00000369461; ENSG00000198721. [O75521-1]
    ENST00000380125; ENSP00000369468; ENSG00000198721.
    ENST00000465828; ENSP00000420309; ENSG00000198721.
    GeneIDi10455.
    KEGGihsa:10455.
    UCSCiuc003mwc.3. human. [O75521-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF069301 mRNA. Translation: AAC19317.1 . Different initiation.
    AL136642 mRNA. Translation: CAB66577.1 .
    AK075108 mRNA. Translation: BAG52068.1 . Different initiation.
    AL033383 Genomic DNA. Translation: CAI42125.1 .
    AL033383 Genomic DNA. Translation: CAI42127.1 .
    BC002668 mRNA. Translation: AAH02668.3 . Different initiation.
    BC016781 mRNA. Translation: AAH16781.1 . Different initiation.
    BC017474 mRNA. Translation: AAH17474.1 . Different initiation.
    BC033841 mRNA. Translation: AAH33841.3 . Different initiation.
    BC034702 mRNA. Translation: AAH34702.1 . Different initiation.
    AF153612 mRNA. Translation: AAD34173.1 . Different initiation.
    AF244138 mRNA. Translation: AAF66247.1 . Different initiation.
    CCDSi CCDS43420.2. [O75521-1 ]
    RefSeqi NP_001159482.1. NM_001166010.1.
    NP_006108.2. NM_006117.2.
    NP_996667.2. NM_206836.2. [O75521-1 ]
    UniGenei Hs.15250.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQU NMR - A 31-133 [» ]
    2F6Q X-ray 1.95 A/B/C 138-394 [» ]
    ProteinModelPortali O75521.
    SMRi O75521. Positions 31-133, 139-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115718. 12 interactions.
    IntActi O75521. 7 interactions.
    MINTi MINT-3001383.

    PTM databases

    PhosphoSitei O75521.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00419263.
    UCD-2DPAGE O75521.

    Proteomic databases

    MaxQBi O75521.
    PaxDbi O75521.
    PRIDEi O75521.

    Protocols and materials databases

    DNASUi 10455.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361538 ; ENSP00000354737 ; ENSG00000198721 .
    ENST00000380118 ; ENSP00000369461 ; ENSG00000198721 . [O75521-1 ]
    ENST00000380125 ; ENSP00000369468 ; ENSG00000198721 .
    ENST00000465828 ; ENSP00000420309 ; ENSG00000198721 .
    GeneIDi 10455.
    KEGGi hsa:10455.
    UCSCi uc003mwc.3. human. [O75521-1 ]

    Organism-specific databases

    CTDi 10455.
    GeneCardsi GC06M004115.
    H-InvDB HIX0025043.
    HGNCi HGNC:14601. ECI2.
    HPAi HPA022130.
    HPA031626.
    MIMi 608024. gene.
    neXtProti NX_O75521.
    PharmGKBi PA33168.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4281.
    HOVERGENi HBG006723.
    InParanoidi O75521.
    KOi K13239.
    OMAi RWLSDEC.
    OrthoDBi EOG72RN06.
    PhylomeDBi O75521.
    TreeFami TF313375.

    Miscellaneous databases

    EvolutionaryTracei O75521.
    GeneWikii PECI_(gene).
    GenomeRNAii 10455.
    NextBioi 39633.
    PROi O75521.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75521.
    Bgeei O75521.
    Genevestigatori O75521.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR022408. Acyl-CoA-binding_prot_CS.
    IPR000582. Acyl-CoA-binding_protein.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    [Graphical view ]
    Pfami PF00887. ACBP. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    PRINTSi PR00689. ACOABINDINGP.
    SUPFAMi SSF47027. SSF47027. 1 hit.
    SSF52096. SSF52096. 1 hit.
    PROSITEi PS00880. ACB_1. 1 hit.
    PS51228. ACB_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor."
      Suk K., Kim Y.-H., Hwang D.-Y., Ihm S.-H., Yoo H.J., Lee M.-S.
      Biochim. Biophys. Acta 1454:126-131(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-344.
      Tissue: Pancreatic islet.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 2).
      Tissue: Placenta.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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] (ISOFORMS 1 AND 2).
      Tissue: Bone marrow, Skin and Uterus.
    6. "Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA isomerase of mammalian peroxisomes."
      Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.
      J. Biol. Chem. 274:21797-21803(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), SUBCELLULAR LOCATION.
    7. "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
      Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
      J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), VARIANT VAL-344.
      Tissue: Hepatoma.
    8. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    9. "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
      Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
      EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Diazepam-binding inhibitor-related protein 1: a candidate autoantigen in acquired aplastic anemia patients harboring a minor population of paroxysmal nocturnal hemoglobinuria-type cells."
      Feng X., Chuhjo T., Sugimori C., Kotani T., Lu X., Takami A., Takamatsu H., Yamazaki H., Nakao S.
      Blood 104:2425-2431(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "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-51 AND LYS-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Solution structure of RSGI RUH-045, a human acyl-CoA binding protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 36-133.
    14. "The crystal structure of human peroxisomal delta3, delta2 enoyl-CoA isomerase (pECI)."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 138-394.

    Entry informationi

    Entry nameiECI2_HUMAN
    AccessioniPrimary (citable) accession number: O75521
    Secondary accession number(s): Q5JYK5
    , Q5JYK7, Q7L124, Q8N0X0, Q9BUE9, Q9H0T9, Q9NQH1, Q9NYH7, Q9UN55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 150 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

    Caution

    It is uncertain whether Met-1 or Met-3 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3