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Reviewed, UniProtKB/Swiss-Prot P23196 (APEX1_BOVIN)

Last modified February 9, 2010. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    DNA-(apurinic or apyrimidinic site) lyase
    EC=4.2.99.18
Alternative name(s):
    Apurinic-apyrimidinic endonuclease 1
      Short name=AP endonuclease 1
    APEX nuclease
      Short name=APEN
Gene names
Name: APEX1
Synonyms: APE, APEX, BAP1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Repairs oxidative DNA damages in vitro. May have a role in protection against cell lethality and suppression of mutations. Removes the blocking groups from the 3'-termini of the DNA strand breaks generated by ionizing radiations and bleomycin.

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

Subunit structure

Monomer. Component of the SET complex, which also contains SET, ANP32A, HMGB2 and NME1 By similarity.

Subcellular location

Nucleus.

Tissue specificity

Thymus.

Induction

By several DNA damaging agents.

Sequence similarities

Belongs to the DNA repair enzymes AP/exoA family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.3
Chain2 – 318317DNA-(apurinic or apyrimidinic site) lyase
PRO_0000200009

Sites

Active site3091Proton acceptor By similarity
Metal binding681Magnesium or manganese By similarity
Metal binding961Magnesium or manganese By similarity
Metal binding2101Magnesium or manganese By similarity
Metal binding2121Magnesium or manganese By similarity
Metal binding3081Magnesium or manganese By similarity
Metal binding3091Magnesium or manganese By similarity

Amino acid modifications

Modified residue1971N6-acetyllysine By similarity
Modified residue2621Phosphotyrosine By similarity

Experimental info

Sequence conflict21 – 222PE → LP AA sequence Ref.3
Sequence conflict2911V → L in AAI22611. Ref.2

Secondary structure

1 ...................................................... 318
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P23196-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 40C733FBA2EA738D

FASTA31835,570
        10         20         30         40         50         60 
MPKRGKKGAV VEDAEEPKTE PEAKKSKAGA KKNEKEAVGE GAVLYEDPPD QKTSPSGKSA 

        70         80         90        100        110        120 
TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS ENKLPVELQE LSGLSHQYWS 

       130        140        150        160        170        180 
APSDKEGYSG VGLLSRQCPL KVSYGIGEEE HDQEGRVIVA EYDAFVLVTA YVPNAGRGLV 

       190        200        210        220        230        240 
RLEYRQRWDE AFRKFLKGLA SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF 

       250        260        270        280        290        300 
GELLQAVPLT DSFRHLYPNT AYAYTFWTYM MNARSKNVGW RLDYFLLSQS VLPALCDSKI 

       310 
RSKALGSDHC PITLYLAL

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References

« Hide 'large scale' references
[1]"Isolation of cDNA clones encoding an enzyme from bovine cells that repairs oxidative DNA damage in vitro: homology with bacterial repair enzymes."
Robson C.N., Milne A.M., Pappin D.J.C., Hickson I.D.
Nucleic Acids Res. 19:1087-1092(1991) [PubMed: 1708495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-19.
Tissue: Thymus.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Basal ganglia.
[3]"Purification and amino-terminal amino acid sequence of an apurinic/apyrimidinic endonuclease from calf thymus."
Henner W.D., Kiker N.P., Jorgensen T.J., Munck J.-N.
Nucleic Acids Res. 15:5529-5544(1987) [PubMed: 2441359] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-23.
Tissue: Thymus.
[4]"Three-dimensional structure prediction of bovine AP lyase, BAP1: prediction of interaction with DNA and alterations as a result of Arg176->Ala, Asp282->Ala, and His308->Asn mutations."
Khurshid R., Salim A., Abbasi A.
Biochem. Biophys. Res. Commun. 326:711-717(2005) [PubMed: 15607727] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 40-318.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56685 mRNA. Translation: CAA40014.1.
BC122610 mRNA. Translation: AAI22611.1.
IPIIPI00715890.
PIRS26830.
RefSeqNP_788782.2.
UniGeneBt.1302

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LYRmodel-A40-318[»]
1XZRmodel-A40-318[»]
1XZSmodel-A40-318[»]
1XZTmodel-A40-318[»]
SMRP23196. Positions 40-318.
ModBaseSearch...

Protein-protein interaction databases

STRINGP23196.

Genome annotation databases

EnsemblENSBTAT00000003559; ENSBTAP00000003559; ENSBTAG00000002745; Bos taurus. [Genome view]
GeneID281630.
KEGGbta:281630.

Organism-specific databases

CTD281630.

Phylogenomic databases

eggNOGmaNOG08727.
HOVERGENP23196.
InParanoidP23196.
PhylomeDBP23196.

Enzyme and pathway databases

BRENDA4.2.99.18. 251.

Family and domain databases

InterProIPR000097. AP_endonuclease_F1.
IPR020847. AP_endonuclease_F1_BS.
IPR020848. AP_endonuclease_F1_CS.
IPR005135. Endo/exonuclease/phosphatase.
IPR004808. exoDNase_III.
[Graphical view]
PANTHERPTHR22748. ExoIII_xth. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
TIGRFAMsTIGR00195. exoDNase_III. 1 hit.
TIGR00633. xth. 1 hit.
PROSITEPS00726. AP_NUCLEASE_F1_1. 1 hit.
PS00727. AP_NUCLEASE_F1_2. 1 hit.
PS00728. AP_NUCLEASE_F1_3. 1 hit.
PS51435. AP_NUCLEASE_F1_4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAPEX1_BOVIN
AccessionPrimary (citable) accession number: P23196
Secondary accession number(s): Q0IIJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents