Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

C->U-editing enzyme APOBEC-1

Gene

APOBEC1

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

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

Zn2+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

  • AU-rich element binding Source: Ensembl
  • cytidine deaminase activity Source: ProtInc
  • RNA binding Source: ProtInc
  • zinc ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.36. 2681.
3.5.4.37. 2681.
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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:604. APOBEC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24889.

Polymorphism and mutation databases

BioMutaiAPOBEC1.
DMDMi152013530.

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.
GenevisibleiP41238. HS.

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

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 134125CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG41905.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033766.
HOVERGENiHBG050445.
KOiK16932.
OMAiNFVNYPP.
OrthoDBiEOG7NGQCB.
PhylomeDBiP41238.
TreeFamiTF331356.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41238-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSEKGPSTG DPTLRRRIEP WEFDVFYDPR ELRKEACLLY EIKWGMSRKI
60 70 80 90 100
WRSSGKNTTN HVEVNFIKKF TSERDFHPSM SCSITWFLSW SPCWECSQAI
110 120 130 140 150
REFLSRHPGV TLVIYVARLF WHMDQQNRQG LRDLVNSGVT IQIMRASEYY
160 170 180 190 200
HCWRNFVNYP PGDEAHWPQY PPLWMMLYAL ELHCIILSLP PCLKISRRWQ
210 220 230
NHLTFFRLHL QNCHYQTIPP HILLATGLIH PSVAWR
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 (Ref. 5) Curated
Sequence conflicti83 – 831S → T in AAD10701 (Ref. 5) Curated

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:
EMBLi
GenBanki
DDBJi
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_001644.4.
UniGeneiHs.560.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001644.4.
UniGeneiHs.560.

3D structure databases

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

Protein-protein interaction databases

BioGridi106836. 8 interactions.
STRINGi9606.ENSP00000229304.

PTM databases

PhosphoSiteiP41238.

Polymorphism and mutation databases

BioMutaiAPOBEC1.
DMDMi152013530.

Proteomic databases

PaxDbiP41238.
PRIDEiP41238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi339.
GeneCardsiGC12M007801.
HGNCiHGNC:604. APOBEC1.
MIMi600130. gene.
neXtProtiNX_P41238.
PharmGKBiPA24889.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41905.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033766.
HOVERGENiHBG050445.
KOiK16932.
OMAiNFVNYPP.
OrthoDBiEOG7NGQCB.
PhylomeDBiP41238.
TreeFamiTF331356.

Enzyme and pathway databases

BRENDAi3.5.4.36. 2681.
3.5.4.37. 2681.
ReactomeiREACT_1390. Formation of the Editosome.
REACT_167. mRNA Editing: C to U Conversion.

Miscellaneous databases

GeneWikiiAPOBEC1.
GenomeRNAii339.
NextBioi1403.
PROiP41238.
SOURCEiSearch...

Gene expression databases

BgeeiP41238.
CleanExiHS_APOBEC1.
GenevisibleiP41238. HS.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: June 24, 2015
This is version 144 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

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.