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P41238

- ABEC1_HUMAN

UniProt

P41238 - ABEC1_HUMAN

Protein

C->U-editing enzyme APOBEC-1

Gene

APOBEC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalytic component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.1 Publication

    Cofactori

    Zinc.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi61 – 611Zinc; catalyticBy similarity
    Active sitei63 – 631Proton donorBy similarity
    Metal bindingi93 – 931Zinc; catalyticBy similarity
    Metal bindingi96 – 961Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AU-rich element binding Source: Ensembl
    2. cytidine deaminase activity Source: ProtInc
    3. protein binding Source: UniProtKB
    4. RNA binding Source: ProtInc
    5. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cellular response to insulin stimulus Source: Ensembl
    2. cytidine deamination Source: GOC
    3. cytidine to uridine editing Source: Reactome
    4. defense response to virus Source: Ensembl
    5. DNA demethylation Source: UniProtKB
    6. gene expression Source: Reactome
    7. lipid metabolic process Source: ProtInc
    8. lipoprotein biosynthetic process Source: Ensembl
    9. lipoprotein transport Source: Ensembl
    10. mRNA modification Source: Reactome
    11. mRNA processing Source: UniProtKB-KW
    12. mRNA stabilization Source: Ensembl
    13. negative regulation of methylation-dependent chromatin silencing Source: UniProtKB
    14. regulation of cell proliferation Source: Ensembl
    15. response to calcium ion Source: Ensembl
    16. response to drug Source: Ensembl
    17. response to ethanol Source: Ensembl
    18. response to gamma radiation Source: Ensembl
    19. response to osmotic stress Source: Ensembl
    20. response to zinc ion Source: Ensembl
    21. RNA processing Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1390. Formation of the Editosome.
    REACT_167. mRNA Editing: C to U Conversion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C->U-editing enzyme APOBEC-1 (EC:3.5.4.-)
    Alternative name(s):
    Apolipoprotein B mRNA-editing enzyme 1
    HEPR
    Gene namesi
    Name:APOBEC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:604. APOBEC1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24889.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236C->U-editing enzyme APOBEC-1PRO_0000171742Add
    BLAST

    Proteomic databases

    PaxDbiP41238.
    PRIDEiP41238.

    PTM databases

    PhosphoSiteiP41238.

    Expressioni

    Tissue specificityi

    Expressed exclusively in the small intestine.

    Gene expression databases

    BgeeiP41238.
    CleanExiHS_APOBEC1.
    GenevestigatoriP41238.

    Interactioni

    Subunit structurei

    Homodimer. Part of the apolipoprotein B mRNA editing complex with A1CF. Found in a complex with CELF2/CUGBP2 and A1CF. Interacts with HNRPAB and SYNCRIP.2 Publications

    Protein-protein interaction databases

    BioGridi106836. 8 interactions.
    STRINGi9606.ENSP00000229304.

    Structurei

    3D structure databases

    ProteinModelPortaliP41238.
    SMRiP41238. Positions 37-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi180 – 19314Leu-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG41905.
    HOGENOMiHOG000033766.
    HOVERGENiHBG050445.
    InParanoidiP41238.
    KOiK16932.
    OMAiLQNCHYQ.
    OrthoDBiEOG7NGQCB.
    PhylomeDBiP41238.
    TreeFamiTF331356.

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR013158. APOBEC_N.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view]
    PfamiPF08210. APOBEC_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53927. SSF53927. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P41238-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSEKGPSTG DPTLRRRIEP WEFDVFYDPR ELRKEACLLY EIKWGMSRKI    50
    WRSSGKNTTN HVEVNFIKKF TSERDFHPSM SCSITWFLSW SPCWECSQAI 100
    REFLSRHPGV TLVIYVARLF WHMDQQNRQG LRDLVNSGVT IQIMRASEYY 150
    HCWRNFVNYP PGDEAHWPQY PPLWMMLYAL ELHCIILSLP PCLKISRRWQ 200
    NHLTFFRLHL QNCHYQTIPP HILLATGLIH PSVAWR 236
    Length:236
    Mass (Da):28,192
    Last modified:March 6, 2007 - v3
    Checksum:i28466B43F7FD82F7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531S → T in AAD10701. 1 PublicationCurated
    Sequence conflicti83 – 831S → T in AAD10701. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti80 – 801M → I.4 Publications
    Corresponds to variant rs2302515 [ dbSNP | Ensembl ].
    VAR_013779
    Natural varianti236 – 2361R → K.
    Corresponds to variant rs12820011 [ dbSNP | Ensembl ].
    VAR_048720

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25877 mRNA. Translation: AAA86766.1.
    L26234 mRNA. Translation: AAA64230.1.
    U72891 mRNA. Translation: AAD00185.1.
    AB009426 Genomic DNA. Translation: BAA23882.1.
    U78720 mRNA. Translation: AAD10701.1.
    CCDSiCCDS8579.1.
    PIRiI59323.
    RefSeqiNP_001635.2. NM_001644.3.
    XP_005253412.1. XM_005253355.2.
    UniGeneiHs.560.

    Genome annotation databases

    EnsembliENST00000229304; ENSP00000229304; ENSG00000111701.
    GeneIDi339.
    KEGGihsa:339.
    UCSCiuc001qtb.3. human.

    Polymorphism databases

    DMDMi152013530.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25877 mRNA. Translation: AAA86766.1 .
    L26234 mRNA. Translation: AAA64230.1 .
    U72891 mRNA. Translation: AAD00185.1 .
    AB009426 Genomic DNA. Translation: BAA23882.1 .
    U78720 mRNA. Translation: AAD10701.1 .
    CCDSi CCDS8579.1.
    PIRi I59323.
    RefSeqi NP_001635.2. NM_001644.3.
    XP_005253412.1. XM_005253355.2.
    UniGenei Hs.560.

    3D structure databases

    ProteinModelPortali P41238.
    SMRi P41238. Positions 37-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106836. 8 interactions.
    STRINGi 9606.ENSP00000229304.

    PTM databases

    PhosphoSitei P41238.

    Polymorphism databases

    DMDMi 152013530.

    Proteomic databases

    PaxDbi P41238.
    PRIDEi P41238.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229304 ; ENSP00000229304 ; ENSG00000111701 .
    GeneIDi 339.
    KEGGi hsa:339.
    UCSCi uc001qtb.3. human.

    Organism-specific databases

    CTDi 339.
    GeneCardsi GC12M007801.
    HGNCi HGNC:604. APOBEC1.
    MIMi 600130. gene.
    neXtProti NX_P41238.
    PharmGKBi PA24889.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41905.
    HOGENOMi HOG000033766.
    HOVERGENi HBG050445.
    InParanoidi P41238.
    KOi K16932.
    OMAi LQNCHYQ.
    OrthoDBi EOG7NGQCB.
    PhylomeDBi P41238.
    TreeFami TF331356.

    Enzyme and pathway databases

    Reactomei REACT_1390. Formation of the Editosome.
    REACT_167. mRNA Editing: C to U Conversion.

    Miscellaneous databases

    GeneWikii APOBEC1.
    GenomeRNAii 339.
    NextBioi 1403.
    PROi P41238.
    SOURCEi Search...

    Gene expression databases

    Bgeei P41238.
    CleanExi HS_APOBEC1.
    Genevestigatori P41238.

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR013158. APOBEC_N.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view ]
    Pfami PF08210. APOBEC_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53927. SSF53927. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a human small intestinal apolipoprotein B mRNA editing protein."
      Hadjiagapiou C., Giannoni F., Funahashi T., Skarosi S.F., Davidson N.O.
      Nucleic Acids Res. 22:1874-1879(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-80.
      Tissue: Intestine.
    2. "Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene."
      Lau P.P., Zhu H.-J., Baldini A., Charnsangavej C., Chan L.
      Proc. Natl. Acad. Sci. U.S.A. 91:8522-8526(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT ILE-80.
      Tissue: Small intestine.
    3. "Characterization of the human apobec-1 gene: expression in gastrointestinal tissues determined by alternative splicing with production of a novel truncated peptide."
      Hirano K., Min J., Funahashi T., Baunoch D.A., Davidson N.O.
      J. Lipid Res. 38:847-859(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-80.
      Tissue: Osteosarcoma.
    4. "Human apolipoprotein B RNA editing deaminase gene (APOBEC1)."
      Fujino T., Navaratnam N., Scott J.
      Genomics 47:266-275(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-80.
      Tissue: Peripheral blood leukocyte.
    5. "A novel mutation in exon 3 of the human apoB editing protein gene."
      Hong S.H., Kim J.Q., Lee C.C.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-147.
    6. "Cloning of an Apobec-1-binding protein that also interacts with apolipoprotein B mRNA and evidence for its involvement in RNA editing."
      Lau P.P., Zhu H.J., Nakamuta M., Chan L.
      J. Biol. Chem. 272:1452-1455(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRPAB.
    7. "Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome."
      Lau P.P., Chang B.-H., Chan L.
      Biochem. Biophys. Res. Commun. 282:977-983(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNCRIP.
    8. "C-->U editing of neurofibromatosis 1 mRNA occurs in tumors that express both the type II transcript and apobec-1, the catalytic subunit of the apolipoprotein B mRNA-editing enzyme."
      Mukhopadhyay D., Anant S., Lee R.M., Kennedy S., Viskochil D., Davidson N.O.
      Am. J. Hum. Genet. 70:38-50(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NF1 EDITING.
    9. "Proprotein convertase subtilisin/kexin type 9 interacts with apolipoprotein B and prevents its intracellular degradation, irrespective of the low-density lipoprotein receptor."
      Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.
      Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiABEC1_HUMAN
    AccessioniPrimary (citable) accession number: P41238
    Secondary accession number(s): Q9UE64, Q9UM71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3