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Protein

Trans-2-enoyl-CoA reductase, mitochondrial

Gene

MECR

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

Functioni

Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis.1 Publication

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.2 Publications

Kineticsi

  1. KM=37 µM for trans-2-hexenoyl-CoA2 Publications
  2. KM=7.1 µM for trans-2-decenoyl-CoA2 Publications
  3. KM=3.6 µM for trans-dodec-2-enoyl-CoA2 Publications
  4. KM=10.4 µM for trans-dec-2-enoyl-CoA2 Publications
  5. KM=10.2 µM for trans-oct-2-enoyl-CoA2 Publications
  6. KM=4.3 µM for trans-tetradec-2-enoyl-CoA2 Publications
  7. KM=6.6 µM for trans-hexadec-2-enoyl-CoA2 Publications
  8. KM=63.5 µM for trans-hex-2-enoyl-CoA2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671NADPBy similarity
    Binding sitei368 – 3681NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1964NADPBy similarity
    Nucleotide bindingi216 – 2183NADPBy similarity
    Nucleotide bindingi285 – 2884NADPBy similarity
    Nucleotide bindingi310 – 3123NADPBy similarity

    GO - Molecular functioni

    • trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • fatty acid biosynthetic process Source: UniProtKB-KW
    • fatty acid metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    SABIO-RKQ9BV79.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trans-2-enoyl-CoA reductase, mitochondrial (EC:1.3.1.38)
    Alternative name(s):
    Nuclear receptor-binding factor 1
    Short name:
    HsNrbf-1
    Short name:
    NRBF-1
    Gene namesi
    Name:MECR
    Synonyms:NBRF1
    ORF Names:CGI-63
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19691. MECR.

    Subcellular locationi

    Isoform 1 :
    Isoform 2 :

    GO - Cellular componenti

    • mitochondrion Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851S → A: Reduces catalytic activity by 68%. 1 Publication
    Mutagenesisi94 – 941Y → F: Reduces catalytic activity by 95%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication
    Mutagenesisi129 – 1291I → M: Strongly increases activity with trans-oct-2-enoyl-CoA. No effect on activity with trans-tetradec-2-enoyl-CoA. Decreases activity with trans-hexadec-2-enoyl-CoA by 20%. 1 Publication
    Mutagenesisi165 – 1651G → S: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 73%. Decreases activity with trans-hexadec-2-enoyl-CoA by 80%. 1 Publication
    Mutagenesisi170 – 1701T → A: Reduces catalytic activity by 69%. 1 Publication
    Mutagenesisi311 – 3111W → A: Reduces catalytic activity by 98%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication
    Mutagenesisi311 – 3111W → L: Reduces catalytic activity by 87%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication
    Mutagenesisi324 – 3241F → Y: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 25%. Decreases activity with trans-hexadec-2-enoyl-CoA by 68%. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671471.

    Polymorphism and mutation databases

    DMDMi334302832.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionSequence AnalysisAdd
    BLAST
    Chaini54 – 373320Trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000888Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611N6-acetyllysine; alternateBy similarity
    Modified residuei61 – 611N6-succinyllysine; alternateBy similarity
    Modified residuei252 – 2521N6-acetyllysine; alternateBy similarity
    Modified residuei252 – 2521N6-succinyllysine; alternateBy similarity
    Modified residuei267 – 2671N6-acetyllysine; alternateBy similarity
    Modified residuei267 – 2671N6-succinyllysine; alternateBy similarity
    Modified residuei316 – 3161N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BV79.
    PaxDbiQ9BV79.
    PRIDEiQ9BV79.

    PTM databases

    PhosphoSiteiQ9BV79.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung.1 Publication

    Gene expression databases

    BgeeiQ9BV79.
    CleanExiHS_MECR.
    ExpressionAtlasiQ9BV79. baseline and differential.
    GenevisibleiQ9BV79. HS.

    Organism-specific databases

    HPAiHPA022018.
    HPA022030.
    HPA028740.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 2 interacts with PPARA in the nucleus and increases its activity.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119291. 10 interactions.
    STRINGi9606.ENSP00000263702.

    Structurei

    Secondary structure

    1
    373
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 5210Combined sources
    Helixi54 – 574Combined sources
    Beta strandi58 – 636Combined sources
    Beta strandi72 – 8110Combined sources
    Helixi84 – 918Combined sources
    Beta strandi100 – 1034Combined sources
    Beta strandi109 – 1157Combined sources
    Beta strandi127 – 1337Combined sources
    Beta strandi138 – 1458Combined sources
    Helixi146 – 1483Combined sources
    Beta strandi149 – 1524Combined sources
    Beta strandi154 – 1563Combined sources
    Helixi158 – 1636Combined sources
    Helixi167 – 17711Combined sources
    Beta strandi186 – 1916Combined sources
    Helixi195 – 20713Combined sources
    Beta strandi210 – 2156Combined sources
    Helixi221 – 23010Combined sources
    Beta strandi234 – 2385Combined sources
    Helixi239 – 2435Combined sources
    Helixi245 – 2495Combined sources
    Beta strandi252 – 2543Combined sources
    Beta strandi258 – 2647Combined sources
    Helixi266 – 2738Combined sources
    Beta strandi281 – 2844Combined sources
    Beta strandi293 – 2953Combined sources
    Helixi297 – 3026Combined sources
    Beta strandi306 – 3094Combined sources
    Helixi312 – 3187Combined sources
    Helixi321 – 33616Combined sources
    Beta strandi345 – 3495Combined sources
    Helixi350 – 3523Combined sources
    Helixi353 – 3608Combined sources
    Beta strandi362 – 3643Combined sources
    Beta strandi366 – 3727Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZSYX-ray1.75A40-373[»]
    2VCYX-ray2.41A/B31-373[»]
    ProteinModelPortaliQ9BV79.
    SMRiQ9BV79. Positions 40-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BV79.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0604.
    GeneTreeiENSGT00740000115589.
    HOVERGENiHBG052446.
    InParanoidiQ9BV79.
    KOiK07512.
    OMAiCRAWGIN.
    OrthoDBiEOG78M024.
    PhylomeDBiQ9BV79.
    TreeFamiTF312886.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.

    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. AlignAdd to basket

    Isoform 1 (identifier: Q9BV79-1) [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

            10         20         30         40         50
    MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH
    60 70 80 90 100
    HGDPAKVVEL KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL
    110 120 130 140 150
    PAVGGNEGVA QVVAVGSNVT GLKPGDWVIP ANAGLGTWRT EAVFSEEALI
    160 170 180 190 200
    QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ LQPGDSVIQN ASNSGVGQAV
    210 220 230 240 250
    IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE ELRRPEMKNF
    260 270 280 290 300
    FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL
    310 320 330 340 350
    IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL
    360 370
    QDYQSALEAS MKPFISSKQI LTM
    Length:373
    Mass (Da):40,462
    Last modified:May 31, 2011 - v2
    Checksum:iDB13F6B0ED54A823
    GO
    Isoform 2 (identifier: Q9BV79-2) [UniParc]FASTAAdd to basket

    Also known as: cMECR

    The sequence of this isoform differs from the canonical sequence as follows:
         1-76: Missing.

    Show »
    Length:297
    Mass (Da):32,228
    Checksum:i1A27621E27728B76
    GO

    Sequence cautioni

    The sequence AAD34058.1 differs from that shown. Reason: Frameshift at positions 14 and 19. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 462AL → GV in AAD34058 (PubMed:10810093).Curated
    Sequence conflicti373 – 3731M → I in CAG32984 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961F → L.5 Publications
    Corresponds to variant rs1128400 [ dbSNP | Ensembl ].
    VAR_027935
    Natural varianti227 – 2271R → K.
    Corresponds to variant rs11544658 [ dbSNP | Ensembl ].
    VAR_055486
    Natural varianti258 – 2581R → L.
    Corresponds to variant rs34835902 [ dbSNP | Ensembl ].
    VAR_055487

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7676Missing in isoform 2. 1 PublicationVSP_041131Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF151821 mRNA. Translation: AAD34058.1. Frameshift.
    AK095099 mRNA. Translation: BAG52984.1.
    CR456703 mRNA. Translation: CAG32984.1.
    AL590729 Genomic DNA. Translation: CAI14329.1.
    AL590729 Genomic DNA. Translation: CAI14330.1.
    CH471059 Genomic DNA. Translation: EAX07655.1.
    BC001419 mRNA. Translation: AAH01419.1.
    CCDSiCCDS30659.1. [Q9BV79-1]
    CCDS30660.1. [Q9BV79-2]
    RefSeqiNP_001019903.2. NM_001024732.2.
    NP_057095.3. NM_016011.3.
    XP_005245944.1. XM_005245887.1. [Q9BV79-2]
    UniGeneiHs.183646.

    Genome annotation databases

    EnsembliENST00000263702; ENSP00000263702; ENSG00000116353. [Q9BV79-1]
    ENST00000373791; ENSP00000362896; ENSG00000116353. [Q9BV79-2]
    GeneIDi51102.
    KEGGihsa:51102.
    UCSCiuc001brp.1. human. [Q9BV79-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF151821 mRNA. Translation: AAD34058.1. Frameshift.
    AK095099 mRNA. Translation: BAG52984.1.
    CR456703 mRNA. Translation: CAG32984.1.
    AL590729 Genomic DNA. Translation: CAI14329.1.
    AL590729 Genomic DNA. Translation: CAI14330.1.
    CH471059 Genomic DNA. Translation: EAX07655.1.
    BC001419 mRNA. Translation: AAH01419.1.
    CCDSiCCDS30659.1. [Q9BV79-1]
    CCDS30660.1. [Q9BV79-2]
    RefSeqiNP_001019903.2. NM_001024732.2.
    NP_057095.3. NM_016011.3.
    XP_005245944.1. XM_005245887.1. [Q9BV79-2]
    UniGeneiHs.183646.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZSYX-ray1.75A40-373[»]
    2VCYX-ray2.41A/B31-373[»]
    ProteinModelPortaliQ9BV79.
    SMRiQ9BV79. Positions 40-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119291. 10 interactions.
    STRINGi9606.ENSP00000263702.

    PTM databases

    PhosphoSiteiQ9BV79.

    Polymorphism and mutation databases

    DMDMi334302832.

    Proteomic databases

    MaxQBiQ9BV79.
    PaxDbiQ9BV79.
    PRIDEiQ9BV79.

    Protocols and materials databases

    DNASUi51102.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000263702; ENSP00000263702; ENSG00000116353. [Q9BV79-1]
    ENST00000373791; ENSP00000362896; ENSG00000116353. [Q9BV79-2]
    GeneIDi51102.
    KEGGihsa:51102.
    UCSCiuc001brp.1. human. [Q9BV79-1]

    Organism-specific databases

    CTDi51102.
    GeneCardsiGC01M029519.
    HGNCiHGNC:19691. MECR.
    HPAiHPA022018.
    HPA022030.
    HPA028740.
    MIMi608205. gene.
    neXtProtiNX_Q9BV79.
    PharmGKBiPA142671471.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0604.
    GeneTreeiENSGT00740000115589.
    HOVERGENiHBG052446.
    InParanoidiQ9BV79.
    KOiK07512.
    OMAiCRAWGIN.
    OrthoDBiEOG78M024.
    PhylomeDBiQ9BV79.
    TreeFamiTF312886.

    Enzyme and pathway databases

    SABIO-RKQ9BV79.

    Miscellaneous databases

    EvolutionaryTraceiQ9BV79.
    GeneWikiiMECR.
    GenomeRNAii51102.
    NextBioi53817.
    PROiQ9BV79.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9BV79.
    CleanExiHS_MECR.
    ExpressionAtlasiQ9BV79. baseline and differential.
    GenevisibleiQ9BV79. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
    2. "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), VARIANT LEU-96.
      Tissue: Hippocampus.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-96.
    6. "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] (ISOFORM 1), VARIANT LEU-96.
      Tissue: Placenta.
    7. "Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II."
      Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.
      J. Biol. Chem. 278:20154-20161(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "A novel cytosolic isoform of mitochondrial Trans-2-Enoyl-CoA reductase enhances peroxisome proliferator-activated receptor alpha activity."
      Kim D.G., Yoo J.C., Kim E., Lee Y.S., Yarishkin O.V., Lee da Y., Lee K.H., Hong S.G., Hwang E.M., Park J.Y.
      Endocrinol. Metab. 29:185-194(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM 2).
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "The structure of human mitochondrial 2-enoyl thioester reductase (CGI-63)."
      Structural genomics consortium (SGC)
      Submitted (JUN-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 40-373.
    12. "Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties."
      Chen Z.J., Pudas R., Sharma S., Smart O.S., Juffer A.H., Hiltunen J.K., Wierenga R.K., Haapalainen A.M.
      J. Mol. Biol. 379:830-844(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 31-373, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-85; TYR-94; ILE-129; GLY-165; THR-170; TRP-311 AND PHE-324.

    Entry informationi

    Entry nameiMECR_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV79
    Secondary accession number(s): B3KT72
    , Q5SYU0, Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: May 31, 2011
    Last modified: June 24, 2015
    This is version 124 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

    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.