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B4DJE7

- B4DJE7_HUMAN

UniProt

B4DJE7 - B4DJE7_HUMAN

Protein
Submitted name:

cDNA FLJ52595, highly similar to Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.99.3)

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. medium-chain-acyl-CoA dehydrogenase activity Source: Ensembl

    GO - Biological processi

    1. cardiac muscle cell differentiation Source: Ensembl
    2. carnitine metabolic process, CoA-linked Source: Ensembl
    3. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: Ensembl
    4. glycogen biosynthetic process Source: Ensembl
    5. liver development Source: Ensembl
    6. medium-chain fatty acid metabolic process Source: Ensembl
    7. post-embryonic development Source: Ensembl
    8. regulation of gluconeogenesis Source: Ensembl
    9. response to cold Source: Ensembl
    10. response to starvation Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    cDNA FLJ52595, highly similar to Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.99.3)Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl

    Family & Domainsi

    Phylogenomic databases

    HOVERGENiHBG000224.
    KOiK00249.

    Family and domain databases

    Gene3Di2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B4DJE7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWITNGGKAN WYFLLARSDP DPKAPANKAF TGFIVEADTP GIQIGRKELN    50
    MGQRCSDTRG IVFEDVKVPK ENVLIGDGAG FKVAMGAFDK TRPVVAAGAV 100
    GLAQRALDEA TKYALERKTF GKLLVEHQAI SFMLAEMAMK VELARMSYQR 150
    AAWEVDSGRR NTYYASIAKA FAGDIANQLA TDAVQILGGN GFNTEYPVEK 200
    LMRDAKIYQI YEGTSQIQRL IVAREHIDKY KN 232
    Length:232
    Mass (Da):25,663
    Last modified:September 23, 2008 - v1
    Checksum:iB903551ACCD1B68B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK296045 mRNA. Translation: BAG58809.1.
    RefSeqiNP_001272973.1. NM_001286044.1.
    UniGeneiHs.445040.

    Genome annotation databases

    GeneIDi34.
    KEGGihsa:34.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK296045 mRNA. Translation: BAG58809.1 .
    RefSeqi NP_001272973.1. NM_001286044.1.
    UniGenei Hs.445040.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 34.
    KEGGi hsa:34.

    Organism-specific databases

    CTDi 34.

    Phylogenomic databases

    HOVERGENi HBG000224.
    KOi K00249.

    Miscellaneous databases

    GenomeRNAii 34.
    NextBioi 35472513.

    Family and domain databases

    Gene3Di 2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NEDO human cDNA sequencing project focused on splicing variants."
      Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.
      , Sugano S., Nomura N., Isogai T.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Subthalamic nucleusImported.
    2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiB4DJE7_HUMAN
    AccessioniPrimary (citable) accession number: B4DJE7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 23, 2008
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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.