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Q53FV7

- Q53FV7_HUMAN

UniProt

Q53FV7 - Q53FV7_HUMAN

Protein
Submitted name:

Carnitine palmitoyltransferase 1B isoform a variant

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups Source: UniProtKB-KW

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotation, Transferase

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Carnitine palmitoyltransferase 1B isoform a variantImported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26848.

    PTM / Processingi

    Proteomic databases

    PRIDEiQ53FV7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the carnitine/choline acetyltransferase family.UniRule annotation

    Phylogenomic databases

    HOVERGENiHBG003458.
    KOiK08765.

    Family and domain databases

    InterProiIPR000542. Carn_acyl_trans.
    [Graphical view]
    PANTHERiPTHR22589. PTHR22589. 1 hit.
    PfamiPF00755. Carn_acyltransf. 1 hit.
    [Graphical view]
    PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q53FV7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEAHQAVAF QFTVTPDGVD FRLSREALKH VYLSGINSWK KRLIRIKNGI    50
    LRGVYPGSPT SWLVVIMATV GSSFCNVDIS LGLVSCIQRC LPQGCGPYQT 100
    PQTRALLSMA IFSTGVWVTG IFFFRQTLKL LLCYHGWMFE MHGKTSNLTR 150
    IWAMCIRLLS SRHPMLYSFQ TSLPKLPVPR VSATIQRYLE SVRPLLDDEE 200
    YYRMELLAKE FQDKTAPRLQ KYLVLKSWWA SNYVSDWWEE YIYLRGRSPL 250
    MVNSNYYVMD LVLIKNTDVQ AARLGNIIHA MIMYRRKLDR EEIKPVMALG 300
    IVPMCSYQME RMFNTTRIPG NDTDVLQHLS DSRHVAVYHK GRFFKLWLYE 350
    GARLLKPQDL EMQFQRILDD PSPPQPGEEK LAALTAGGRV EWAQARQAFF 400
    SSGKNKAALE AIERAAFFVA LDEESYSYDP EDEASLSLYG KALLHGNCYN 450
    RWFDKSFTLI SFKNGQLGLN AEHAWADAPI IGHLWEFVLG TDSFHLGYTE 500
    TGHCLGKPNP ALAPPTRLQW DIPKQCQAVI KSSYQVAKAL ADDVELYCFQ 550
    FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DRGKFCLTYE ASMTRMFREG 600
    RTETVRSCTS ESTAFVQAMM EGSHTKADLR DLFQKAAKKH QNMYRLAMTG 650
    AGIDRHLFCL YLVSKYLGVS SPFLAEVLSE PWRLSTSQIP QSQIRMFDPE 700
    QHPNHLGAGG GFGPVADDGY GVSYMIAGEN TIFFHISSKF SSSETNAQRF 750
    GNHIRKALLD IADLFQVPKA YS 772
    Length:772
    Mass (Da):87,786
    Last modified:May 24, 2005 - v1
    Checksum:i70B6F159BB023883
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK223174 mRNA. Translation: BAD96894.1.
    RefSeqiNP_001138607.1. NM_001145135.1.
    UniGeneiHs.439777.
    Hs.609867.

    Genome annotation databases

    GeneIDi1375.
    KEGGihsa:1375.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK223174 mRNA. Translation: BAD96894.1 .
    RefSeqi NP_001138607.1. NM_001145135.1.
    UniGenei Hs.439777.
    Hs.609867.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q53FV7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1375.
    KEGGi hsa:1375.

    Organism-specific databases

    CTDi 1375.
    H-InvDB HIX0041160.
    PharmGKBi PA26848.

    Phylogenomic databases

    HOVERGENi HBG003458.
    KOi K08765.

    Miscellaneous databases

    GenomeRNAii 1375.
    NextBioi 5575.

    Family and domain databases

    InterProi IPR000542. Carn_acyl_trans.
    [Graphical view ]
    PANTHERi PTHR22589. PTHR22589. 1 hit.
    Pfami PF00755. Carn_acyltransf. 1 hit.
    [Graphical view ]
    PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides."
      Maruyama K., Sugano S.
      Gene 138:171-174(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Human lungImported.
    2. "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library."
      Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.
      Gene 200:149-156(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Human lungImported.
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Human lungImported.

    Entry informationi

    Entry nameiQ53FV7_HUMAN
    AccessioniPrimary (citable) accession number: Q53FV7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 24, 2005
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 55 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.