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P41238 (ABEC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C->U-editing enzyme APOBEC-1

EC=3.5.4.-
Alternative name(s):
Apolipoprotein B mRNA-editing enzyme 1
HEPR
Gene names
Name:APOBEC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Cofactor

Zinc By similarity.

Subunit structure

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. Ref.6 Ref.7

Subcellular location

Cytoplasm Ref.9.

Tissue specificity

Expressed exclusively in the small intestine.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA demethylation

Inferred from sequence or structural similarity. Source: UniProtKB

RNA processing

Traceable author statement PubMed 7736571. Source: ProtInc

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

cytidine deamination

Traceable author statement PubMed 7736571. Source: GOC

cytidine to uridine editing

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

lipid metabolic process

Traceable author statement Ref.2. Source: ProtInc

lipoprotein biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein transport

Inferred from electronic annotation. Source: Ensembl

mRNA modification

Traceable author statement. Source: Reactome

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA stabilization

Inferred from electronic annotation. Source: Ensembl

negative regulation of methylation-dependent chromatin silencing

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionAU-rich element binding

Inferred from electronic annotation. Source: Ensembl

RNA binding

Traceable author statement PubMed 7736571. Source: ProtInc

cytidine deaminase activity

Traceable author statement PubMed 7736571. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 10669759. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 7736571. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236C->U-editing enzyme APOBEC-1
PRO_0000171742

Regions

Compositional bias180 – 19314Leu-rich

Sites

Active site631Proton donor By similarity
Metal binding611Zinc; catalytic By similarity
Metal binding931Zinc; catalytic By similarity
Metal binding961Zinc; catalytic By similarity

Natural variations

Natural variant801M → I. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs2302515 [ dbSNP | Ensembl ].
VAR_013779
Natural variant2361R → K.
Corresponds to variant rs12820011 [ dbSNP | Ensembl ].
VAR_048720

Experimental info

Sequence conflict531S → T in AAD10701. Ref.5
Sequence conflict831S → T in AAD10701. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P41238 [UniParc].

Last modified March 6, 2007. Version 3.
Checksum: 28466B43F7FD82F7

FASTA23628,192
        10         20         30         40         50         60 
MTSEKGPSTG DPTLRRRIEP WEFDVFYDPR ELRKEACLLY EIKWGMSRKI WRSSGKNTTN 

        70         80         90        100        110        120 
HVEVNFIKKF TSERDFHPSM SCSITWFLSW SPCWECSQAI REFLSRHPGV TLVIYVARLF 

       130        140        150        160        170        180 
WHMDQQNRQG LRDLVNSGVT IQIMRASEYY HCWRNFVNYP PGDEAHWPQY PPLWMMLYAL 

       190        200        210        220        230 
ELHCIILSLP PCLKISRRWQ NHLTFFRLHL QNCHYQTIPP HILLATGLIH PSVAWR 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8579.1.
PIRI59323.
RefSeqNP_001635.2. NM_001644.3.
XP_005253412.1. XM_005253355.2.
UniGeneHs.560.

3D structure databases

ProteinModelPortalP41238.
SMRP41238. Positions 37-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106836. 8 interactions.
STRING9606.ENSP00000229304.

PTM databases

PhosphoSiteP41238.

Polymorphism databases

DMDM152013530.

Proteomic databases

PaxDbP41238.
PRIDEP41238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229304; ENSP00000229304; ENSG00000111701.
GeneID339.
KEGGhsa:339.
UCSCuc001qtb.3. human.

Organism-specific databases

CTD339.
GeneCardsGC12M007801.
HGNCHGNC:604. APOBEC1.
MIM600130. gene.
neXtProtNX_P41238.
PharmGKBPA24889.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41905.
HOGENOMHOG000033766.
HOVERGENHBG050445.
InParanoidP41238.
KOK16932.
OMALQNCHYQ.
OrthoDBEOG7NGQCB.
PhylomeDBP41238.
TreeFamTF331356.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeP41238.
CleanExHS_APOBEC1.
GenevestigatorP41238.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF08210. APOBEC_N. 1 hit.
[Graphical view]
SUPFAMSSF53927. SSF53927. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAPOBEC1.
GenomeRNAi339.
NextBio1403.
PROP41238.
SOURCESearch...

Entry information

Entry nameABEC1_HUMAN
AccessionPrimary (citable) accession number: P41238
Secondary accession number(s): Q9UE64, Q9UM71
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM